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Conserved domains on  [gi|1440910973|gb|AXJ14399|]
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elongation factor 1a, partial [Hortaea werneckii]

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 ...
 1-192 2.32e-127

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: 365.61  E-value: 2.32e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAG 80
Cdd:PTZ00141   47 AEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 ISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEAST 158
Cdd:PTZ00141  127 ISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSD 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1440910973 159 NCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:PTZ00141  207 NMPWYK-----------GPTLLEALDTLEPPKRP 229
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-192 2.32e-127

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 365.61  E-value: 2.32e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAG 80
Cdd:PTZ00141   47 AEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 ISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEAST 158
Cdd:PTZ00141  127 ISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSD 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1440910973 159 NCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:PTZ00141  207 NMPWYK-----------GPTLLEALDTLEPPKRP 229
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-189 4.92e-127

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: 356.42  E-value: 4.92e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAG 80
Cdd:cd01883    39 KEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 ISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEAST 158
Cdd:cd01883   119 FEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSE 198

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1440910973 159 NCPWYKGWeketkakvtgkTLLEAIDNIDPP 189
Cdd:cd01883   199 NMPWYKGP-----------TLLEALDSLEPP 218
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-192 1.00e-101

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: 299.54  E-value: 1.00e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   2 ELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEfeagi 81
Cdd:COG5256    48 KKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV----- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  82 skDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCP 161
Cdd:COG5256   123 --MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMP 200

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1440910973 162 WYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:COG5256   201 WYN-----------GPTLLEALDNLKEPEKP 220
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-192 1.15e-100

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: 297.16  E-value: 1.15e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEag 80
Cdd:TIGR00483  47 QEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE-- 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 isKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNC 160
Cdd:TIGR00483 125 --VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENT 202

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1440910973 161 PWYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:TIGR00483 203 PWYK-----------GKTLLEALDALEPPEKP 223
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-189 2.32e-59

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: 183.88  E-value: 2.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   2 ELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagi 81
Cdd:pfam00009  32 KRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  82 sKDGQTREHALLAYTLGVKqLIVAINKMDTTkwSEERYGEIIKETS-AFIKKVGFNPKHVPFVPISGFNGDNMieastnc 160
Cdd:pfam00009 106 -VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------- 174

                         170       180
                  ....*....|....*....|....*....
gi 1440910973 161 pwykgweketkakvtgKTLLEAIDNIDPP 189
Cdd:pfam00009 175 ----------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-192 2.32e-127

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 365.61  E-value: 2.32e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAG 80
Cdd:PTZ00141   47 AEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 ISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEAST 158
Cdd:PTZ00141  127 ISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSD 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1440910973 159 NCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:PTZ00141  207 NMPWYK-----------GPTLLEALDTLEPPKRP 229
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-189 4.92e-127

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: 356.42  E-value: 4.92e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAG 80
Cdd:cd01883    39 KEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 ISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEAST 158
Cdd:cd01883   119 FEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSE 198

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1440910973 159 NCPWYKGWeketkakvtgkTLLEAIDNIDPP 189
Cdd:cd01883   199 NMPWYKGP-----------TLLEALDSLEPP 218
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-192 1.00e-101

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: 299.54  E-value: 1.00e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   2 ELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEfeagi 81
Cdd:COG5256    48 KKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV----- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  82 skDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCP 161
Cdd:COG5256   123 --MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMP 200

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1440910973 162 WYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:COG5256   201 WYN-----------GPTLLEALDNLKEPEKP 220
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-192 1.15e-100

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: 297.16  E-value: 1.15e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEag 80
Cdd:TIGR00483  47 QEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE-- 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 isKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNC 160
Cdd:TIGR00483 125 --VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENT 202

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1440910973 161 PWYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:TIGR00483 203 PWYK-----------GKTLLEALDALEPPEKP 223
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-192 5.23e-99

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 292.60  E-value: 5.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   2 ELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefEAGI 81
Cdd:PRK12317   47 EKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  82 SKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEASTNCP 161
Cdd:PRK12317  122 GVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMP 201

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1440910973 162 WYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:PRK12317  202 WYN-----------GPTLLEALDNLKPPEKP 221
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-192 1.17e-96

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 287.76  E-value: 1.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEAG 80
Cdd:PLN00043   47 AEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 ISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGDNMIEAST 158
Cdd:PLN00043  127 ISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERST 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1440910973 159 NCPWYKgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:PLN00043  207 NLDWYK-----------GPTLLEALDQINEPKRP 229
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 4-190 4.54e-60

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: 186.24  E-value: 4.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   4 GKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagisk 83
Cdd:cd04166    43 QGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE----- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  84 dgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHvpFVPISGFNGDNMIEASTNCPWY 163
Cdd:cd04166   118 --QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWY 193

                         170       180
                  ....*....|....*....|....*..
gi 1440910973 164 KgweketkakvtGKTLLEAIDNIDPPS 190
Cdd:cd04166   194 K-----------GPTLLEHLETVEIAS 209
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-189 2.32e-59

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: 183.88  E-value: 2.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   2 ELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagi 81
Cdd:pfam00009  32 KRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  82 sKDGQTREHALLAYTLGVKqLIVAINKMDTTkwSEERYGEIIKETS-AFIKKVGFNPKHVPFVPISGFNGDNMieastnc 160
Cdd:pfam00009 106 -VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------- 174

                         170       180
                  ....*....|....*....|....*....
gi 1440910973 161 pwykgweketkakvtgKTLLEAIDNIDPP 189
Cdd:pfam00009 175 ----------------QTLLDALDEYLPS 187
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 4-192 3.61e-59

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: 190.68  E-value: 3.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   4 GKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagisk 83
Cdd:COG2895    60 GTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE----- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  84 dgQTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHvpFVPISGFNGDNMIEASTNCPWY 163
Cdd:COG2895   135 --QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWY 210

                         170       180
                  ....*....|....*....|....*....
gi 1440910973 164 KgweketkakvtGKTLLEAIDNIDPPSRP 192
Cdd:COG2895   211 D-----------GPTLLEHLETVEVAEDR 228
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 10-187 5.66e-48

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 162.39  E-value: 5.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  10 YAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTRE 89
Cdd:PRK05124   78 LALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  90 HALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPkHVPFVPISGFNGDNMIEASTNCPWYKgweke 169
Cdd:PRK05124  151 HSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYS----- 224

                         170
                  ....*....|....*...
gi 1440910973 170 tkakvtGKTLLEAIDNID 187
Cdd:PRK05124  225 ------GPTLLEVLETVD 236
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 6-165 3.55e-46

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 160.09  E-value: 3.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   6 GSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdg 85
Cdd:PRK05506   71 DEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT------- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  86 QTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNpkHVPFVPISGFNGDNMIEASTNCPWYKG 165
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEG 221
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 6-186 2.65e-45

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: 154.07  E-value: 2.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   6 GSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdg 85
Cdd:TIGR02034  47 GEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  86 QTREHALLAYTLGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGFNPKHvpFVPISGFNGDNMIEASTNCPWYkg 165
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLGFRDVT--FIPLSALKGDNVVSRSESMPWY-- 195

                         170       180
                  ....*....|....*....|.
gi 1440910973 166 weketkakvTGKTLLEAIDNI 186
Cdd:TIGR02034 196 ---------SGPTLLEILETV 207
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 12-190 3.43e-43

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: 142.43  E-value: 3.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  12 WVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEfeagiskDGQTREHA 91
Cdd:cd00881    35 TFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  92 LLAyTLGVKQLIVAINKMDTTKwsEERYGEIIKETSAFIKKVGF---NPKHVPFVPISGFNGDNMieastncpwykgwek 168
Cdd:cd00881   108 NIA-LAGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGI--------------- 169

                         170       180
                  ....*....|....*....|..
gi 1440910973 169 etkakvtgKTLLEAIDNIDPPS 190
Cdd:cd00881   170 --------EELLDAIVEHLPPP 183
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-189 2.54e-32

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: 114.99  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEag 80
Cdd:cd01884    27 AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 iskdgQTREHALLAYTLGVKQLIVAINKMDTTKwSEERYGEIIKETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNC 160
Cdd:cd01884   105 -----QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPN 175

                         170       180
                  ....*....|....*....|....*....
gi 1440910973 161 PWYKGWEKetkakvtgktLLEAIDNIDPP 189
Cdd:cd01884   176 KWVDKILE----------LLDALDSYIPT 194
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-192 6.17e-31

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: 116.02  E-value: 6.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeag 80
Cdd:COG0050    37 AKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSA-------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 isKDG---QTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEIIK-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEA 156
Cdd:COG0050   109 --TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSKYGFPGDDTPIIRGSALKA---LEG 181

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1440910973 157 STNCPWYKG-WEketkakvtgktLLEAIDN-IDPPSRP 192
Cdd:COG0050   182 DPDPEWEKKiLE-----------LMDAVDSyIPEPERD 208
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-192 4.10e-28

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 108.49  E-value: 4.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFK-YAWVlDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefea 79
Cdd:PRK12736   37 AERGLNQAKdYDSI-DAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAA------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  80 gisKDG---QTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEIIK-ETSAFIKKVGFNPKHVPFVPISGF---NGDN 152
Cdd:PRK12736  109 ---TDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDDIPVIRGSALkalEGDP 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1440910973 153 mieastncPWYKGWEKetkakvtgktLLEAIDN-IDPPSRP 192
Cdd:PRK12736  184 --------KWEDAIME----------LMDAVDEyIPTPERD 206
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-192 2.27e-27

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 106.43  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFK-YAWVlDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGtgefea 79
Cdd:PRK00049   37 AKKGGAEAKaYDQI-DKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAA------ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  80 giskDG---QTREHALLAYTLGVKQLIVAINKMDTTKwsEERYGEIIK-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIE 155
Cdd:PRK00049  110 ----DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD--DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LE 180

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1440910973 156 ASTNCPWYKGWEKetkakvtgktLLEAIDN-IDPPSRP 192
Cdd:PRK00049  181 GDDDEEWEKKILE----------LMDAVDSyIPTPERA 208
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 15-151 5.83e-26

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: 97.68  E-value: 5.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  15 DKLKSERERGITIDIALWKFETPKYYVT-VIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefEAGISKdgQTREHALL 93
Cdd:cd04171    25 DRLPEEKKRGITIDLGFAYLDLPDGKRLgFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEI 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1440910973  94 AYTLGVKQLIVAINKMDTTkwSEERYGEIIKETSAFIKKVGFNPkhVPFVPISGFNGD 151
Cdd:cd04171    98 LELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFLAD--APIFPVSSVTGE 151
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 15-150 3.84e-25

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: 101.53  E-value: 3.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  15 DKLKSERERGITIDIALWKFETPKYY-VTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREH 90
Cdd:COG3276    26 DRLKEEKKRGITIDLGFAYLPLPDGRrLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA----------DEGvmpQTREH 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440910973  91 -ALLAyTLGVKQLIVAINKMDTTkwSEERYGEIIKETSAFIKKVGFnpKHVPFVPISGFNG 150
Cdd:COG3276    96 lAILD-LLGIKRGIVVLTKADLV--DEEWLELVEEEIRELLAGTFL--EDAPIVPVSAVTG 151
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-110 7.86e-25

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 99.53  E-value: 7.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGtgefeag 80
Cdd:PRK12735   37 AKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAA------- 109

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1440910973  81 iskDG---QTREHALLAYTLGVKQLIVAINKMD 110
Cdd:PRK12735  110 ---DGpmpQTREHILLARQVGVPYIVVFLNKCD 139
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-156 1.34e-24

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: 98.70  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEag 80
Cdd:TIGR00485  37 AKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 iskdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEIIK-ETSAFIKKVGFNPKHVPFV---PISGFNGDNMIEA 156
Cdd:TIGR00485 115 -----QTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSQYDFPGDDTPIIrgsALKALEGDAEWEA 187
tufA CHL00071
elongation factor Tu
 14-191 4.24e-24

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 97.72  E-value: 4.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  14 LDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALL 93
Cdd:CHL00071   50 IDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  94 AYTLGVKQLIVAINKMDttKWSEERYGEIIK-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTNCPWYKGWEKETKA 172
Cdd:CHL00071  123 AKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENPKIKRGENKWVD 197

                         170       180
                  ....*....|....*....|
gi 1440910973 173 KVtgKTLLEAIDN-IDPPSR 191
Cdd:CHL00071  198 KI--YNLMDAVDSyIPTPER 215
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 15-155 8.53e-23

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: 94.94  E-value: 8.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  15 DKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREHA 91
Cdd:TIGR00475  26 DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVDA----------DEGvmtQTGEHL 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1440910973  92 LLAYTLGVKQLIVAINKMDTTkwSEERYGEIIKETSAFIKKVGFNpKHVPFVPISGFNGDNMIE 155
Cdd:TIGR00475  96 AVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFL-KNAKIFKTSAKTGQGIGE 156
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-191 1.26e-22

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 93.91  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   1 AELGKGSFKYAWVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEag 80
Cdd:PLN03126  106 ASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  81 iskdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEIIK-ETSAFIKKVGFNPKHVPFVPISGFNGdnmIEASTN 159
Cdd:PLN03126  184 -----QTKEHILLAKQVGVPNMVVFLNKQDQV--DDEELLELVElEVRELLSSYEFPGDDIPIISGSALLA---LEALME 253

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1440910973 160 CPWYKGWEKETKAKVTgkTLLEAIDNIDP-PSR 191
Cdd:PLN03126  254 NPNIKRGDNKWVDKIY--ELMDAVDSYIPiPQR 284
PLN03127 PLN03127
Elongation factor Tu; Provisional
 14-116 3.10e-22

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 92.58  E-value: 3.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  14 LDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHALL 93
Cdd:PLN03127   99 IDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILL 171

                          90       100
                  ....*....|....*....|...
gi 1440910973  94 AYTLGVKQLIVAINKMDTTKWSE 116
Cdd:PLN03127  172 ARQVGVPSLVVFLNKVDVVDDEE 194
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 4-156 3.55e-15

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 70.37  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   4 GKGSFKYA----WVlDKLKSERERGITI-----DIALWKFETPKYY----------------------VTVIDAPGHRDF 52
Cdd:cd01888    12 GKTTLVKAlsgvWT-VRHKEELKRNITIklgyaNAKIYKCPNCGCPrpydtpececpgcggetklvrhVSFVDCPGHEIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  53 IKNMITGTSQADCAVLIIAAGTGefeagiSKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSE--ERYGEI---IKETS 127
Cdd:cd01888    91 MATMLSGAAVMDGALLLIAANEP------CPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQalENYEQIkefVKGTI 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1440910973 128 AFikkvgfnpkHVPFVPIS---GFNGDNMIEA 156
Cdd:cd01888   165 AE---------NAPIIPISaqlKYNIDVLCEY 187
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 14-146 3.06e-14

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 eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 67.78  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  14 LDKLKSERERGITIDIALWKFETPK--------------YYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefea 79
Cdd:cd01889    29 FDKNPQSQERGITLDLGFSSFEVDKpkhlednenpqienYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG---- 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440910973  80 gisKDGQTREHALLAYTLGvKQLIVAINKMDTTKWSEerygeiIKETSAFIKKV------GFNPKHVPFVPIS 146
Cdd:cd01889   105 ---IQTQTAECLVIGELLC-KPLIVVLNKIDLIPEEE------RKRKIEKMKKRlqktleKTRLKDSPIIPVS 167
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 4-156 1.46e-13

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 67.95  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973   4 GKGSFKYA----WVlDKLKSERERGITI-----DIALWK---FETPKYYVT------------------VIDAPGHRDFI 53
Cdd:PRK04000   21 GKTTLVQAltgvWT-DRHSEELKRGITIrlgyaDATIRKcpdCEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLM 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  54 KNMITGTSQADCAVLIIAAGTGEFEAgiskdgQTREHALLAYTLGVKQLIVAINKMDTTkwSEERYGEIIKETSAFIKkv 133
Cdd:PRK04000  100 ATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALDIIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK-- 169

                         170       180
                  ....*....|....*....|....*.
gi 1440910973 134 GFNPKHVPFVPIS---GFNGDNMIEA 156
Cdd:PRK04000  170 GTVAENAPIIPVSalhKVNIDALIEA 195
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 15-135 8.32e-13

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 65.84  E-value: 8.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  15 DKLKSERERGITIDI--ALWKFETPKYyVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTRE 89
Cdd:PRK10512   26 DRLPEEKKRGMTIDLgyAYWPQPDGRV-LGFIDVPGHEKFLSNMLAGVGGIDHALLVVAC----------DDGvmaQTRE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1440910973  90 H-ALLAYTlGVKQLIVAINKMDTTkwSEERYGEIIKETSAFIKKVGF 135
Cdd:PRK10512   95 HlAILQLT-GNPMLTVALTKADRV--DEARIAEVRRQVKAVLREYGF 138
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 14-153 8.44e-12

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 60.56  E-value: 8.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  14 LDKLKS----ERE-RGITIDIALWKFETPKYY--VTVIDAPGHRDFiKNMIT-GTSQADCAVLIIAAGTGeFEAgiskdg 85
Cdd:cd01887    17 LDKIRKtnvaAGEaGGITQHIGAYQVPIDVKIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------ 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1440910973  86 QTRE---HALLAYTlgvkQLIVAINKMDTTKWSE---ERYGEIIKETSAFIKKVGfnpKHVPFVPISGFNGDNM 153
Cdd:cd01887    89 QTIEainHAKAANV----PIIVAINKIDKPYGTEadpERVKNELSELGLVGEEWG---GDVSIVPISAKTGEGI 155
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 14-122 2.80e-11

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 60.33  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  14 LDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTRE- 89
Cdd:cd04168    39 TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISA----------VEGvqaQTRIl 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1440910973  90 -HALLAYTLGVkqlIVAINKMDTTKWSEER-YGEI 122
Cdd:cd04168   109 fRLLRKLNIPT---IIFVNKIDRAGADLEKvYQEI 140
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 13-110 1.67e-09

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 54.46  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITID---IAL-WKFETPKYYV-TVIDAPGHRDFikNMITGTSQADC--AVLIIAAGTGeFEAgiskdg 85
Cdd:cd01890    36 VLDSMDLERERGITIKaqaVRLfYKAKDGEEYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------ 106

                          90       100
                  ....*....|....*....|....*
gi 1440910973  86 QTREHALLAYTLGVKqLIVAINKMD 110
Cdd:cd01890   107 QTLANFYLALENNLE-IIPVINKID 130
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
20-110 1.23e-08

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 53.59  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  20 ERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagisKDGQTRehALLAYT--L 97
Cdd:PRK12740   41 ERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekY 111

                          90
                  ....*....|...
gi 1440910973  98 GVKQLIVaINKMD 110
Cdd:PRK12740  112 GVPRIIF-VNKMD 123
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 36-155 1.90e-08

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 53.08  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  36 TPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagiSKDGQTREHALLAYTLGVKQLIVAINKMDTTKWS 115
Cdd:PTZ00327  114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEA 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1440910973 116 E--ERYGEIIKetsaFIKkvGFNPKHVPFVPIS---GFNGDNMIE 155
Cdd:PTZ00327  188 QaqDQYEEIRN----FVK--GTIADNAPIIPISaqlKYNIDVVLE 226
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 13-110 1.34e-07

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 49.51  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITIdiaLWK---FETPKYYVTVIDAPGHRDF------IKNMitgtsqADCAVLIIAAGTGEFEagisk 83
Cdd:cd01891    39 VMDSNDLERERGITI---LAKntaITYKDTKINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP----- 104

                          90       100       110
                  ....*....|....*....|....*....|
gi 1440910973  84 dgQTR---EHALLAytlGVKqLIVAINKMD 110
Cdd:cd01891   105 --QTRfvlKKALEA---GLK-PIVVINKID 128
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 20-110 1.00e-06

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 48.09  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  20 ERERGITI---DIAL-WKfetpKYYVTVIDAPGHRDF------IKNMitgtsqADCAVLIIAAgtgeFEagiskdG---Q 86
Cdd:COG1217    50 ERERGITIlakNTAVrYK----GVKINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQ 109

                          90       100
                  ....*....|....*....|....*..
gi 1440910973  87 TR---EHALlayTLGVKqLIVAINKMD 110
Cdd:COG1217   110 TRfvlKKAL---ELGLK-PIVVINKID 132
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 13-110 1.02e-06

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 48.12  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITIDIAL----WKfetpKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagisKDGQTr 88
Cdd:COG0480    48 VMDWMPEEQERGITITSAAttceWK----GHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQT- 115

                          90       100
                  ....*....|....*....|....*....
gi 1440910973  89 EHALlaytlgvKQL-------IVAINKMD 110
Cdd:COG0480   116 ETVW-------RQAdkygvprIVFVNKMD 137
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 4-75 1.49e-06

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 47.21  E-value: 1.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440910973   4 GKGSFKYAwVLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTG 75
Cdd:cd04169    37 ARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
PRK13351 PRK13351
elongation factor G-like protein;
13-110 3.40e-06

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 46.48  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGeFEAgiskdgQTREHAL 92
Cdd:PRK13351   47 VTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWR 119

                          90
                  ....*....|....*...
gi 1440910973  93 LAYTLGVKQLIVaINKMD 110
Cdd:PRK13351  120 QADRYGIPRLIF-INKMD 136
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 24-110 4.25e-06

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 46.16  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  24 GITIDIALWKFETPKYYVTVIDAPGHRDFiknmiT-----GTSQADCAVLIIAAgtgefeagisKDG---QTRE---HAL 92
Cdd:COG0532    36 GITQHIGAYQVETNGGKITFLDTPGHEAF-----TamrarGAQVTDIVILVVAA----------DDGvmpQTIEainHAK 100

                          90
                  ....*....|....*...
gi 1440910973  93 LAytlGVKqLIVAINKMD 110
Cdd:COG0532   101 AA---GVP-IIVAINKID 114
infB CHL00189
translation initiation factor 2; Provisional
 24-153 4.74e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 45.98  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  24 GITIDIALWKFETP----KYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagisKDG---QTREhALLAYT 96
Cdd:CHL00189  276 GITQKIGAYEVEFEykdeNQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA----------DDGvkpQTIE-AINYIQ 344

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1440910973  97 LGVKQLIVAINKMDTTKWSEERYGEIIKETSAFIKKVGfnpKHVPFVPISGFNGDNM 153
Cdd:CHL00189  345 AANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKWG---GDTPMIPISASQGTNI 398
PRK10218 PRK10218
translational GTPase TypA;
13-110 6.18e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 45.86  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGEFEagiskdgQTREHAL 92
Cdd:PRK10218   42 VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTK 114

                          90
                  ....*....|....*...
gi 1440910973  93 LAYTLGVKQLIVaINKMD 110
Cdd:PRK10218  115 KAFAYGLKPIVV-INKVD 131
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 13-110 1.62e-05

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 43.76  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITID---IALwKFETPK-------YYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAgtgefeagis 82
Cdd:cd01885    37 YLDTREDEQERGITIKssaISL-YFEYEEekmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA---------- 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1440910973  83 KDG---QTreHALL--AYTLGVKQLIVaINKMD 110
Cdd:cd01885   106 VEGvcvQT--ETVLrqALEERVKPVLV-INKID 135
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 13-110 2.07e-05

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 43.74  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDFIKNMITGTSQADCAVLIIAAGTGefeagisKDGQTREHAL 92
Cdd:cd04170    38 VSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWE 110

                          90
                  ....*....|....*...
gi 1440910973  93 LAYTLGVKQLIVaINKMD 110
Cdd:cd04170   111 FLDDAKLPRIIF-INKMD 127
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 13-52 3.72e-05

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 42.86  E-value: 3.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITIDIALWKFETPKYYVTVIDAPGHRDF 52
Cdd:cd01886    38 TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDF 77
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 13-110 4.78e-05

Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 43.08  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440910973  13 VLDKLKSERERGITID---IAL-WKFETPKYYV-TVIDAPGHRDFiknmitgT-----SQADC--AVLIIAAGTGeFEAg 80
Cdd:COG0481    42 VLDSMDLERERGITIKaqaVRLnYKAKDGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA- 112

                          90       100       110
                  ....*....|....*....|....*....|
gi 1440910973  81 iskdgQTREHALLAYTLGVKqLIVAINKMD 110
Cdd:COG0481   113 -----QTLANVYLALENDLE-IIPVINKID 136
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 13-52 1.18e-04

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 41.77  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1440910973  13 VLDKLKSERERGITIDIA----LWKFETPKYYVTVIDAPGHRDF 52
Cdd:PRK07560   57 ALDFDEEEQARGITIKAAnvsmVHEYEGKEYLINLIDTPGHVDF 100
 
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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