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Conserved domains on  [gi|16304373|gb|AAL15032|]
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Sup35p, partial [Saccharomyces cerevisiae]

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 ...
 260-429 1.51e-99

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 cd01883:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 219  Bit Score: 295.94  E-value: 1.51e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 260 SLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEKRRYT 339
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 340 ILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYD 419
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160

                       170
                ....*....|
gi 16304373 420 QCVSNVSNFL 429
Cdd:cd01883 161 EIKKKVSPFL 170
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 28-197 4.75e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373    28 QGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGG----YQQYNPQGGYQQQFNPQGGRGNYKNFN 103
Cdd:PRK10263  378 EGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEqpaqQPYYAPAPEQPVAGNAWQAEEQQSTFA 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   104 YNNNLQGYQAGFQPQSQgmslnDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVDTKPAESDKKEEEKSAETKEPTKE 183
Cdd:PRK10263  458 PQSTYQTEQTYQQPAAQ-----EPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPE 532

                         170
                  ....*....|....
gi 16304373   184 PTKVEEPVKKEEKP 197
Cdd:PRK10263  533 PVKEPEPIKSSLKA 546
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 260-429 1.51e-99

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: 295.94  E-value: 1.51e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 260 SLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEKRRYT 339
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 340 ILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYD 419
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160

                       170
                ....*....|
gi 16304373 420 QCVSNVSNFL 429
Cdd:cd01883 161 EIKKKVSPFL 170
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 252-429 1.98e-57

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 194.97  E-value: 1.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  252 MFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYF 331
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  332 ETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTV 411
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160

                        170
                 ....*....|....*...
gi 16304373  412 NWSKERYDQCVSNVSNFL 429
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYL 178
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 252-429 1.24e-55

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: 189.76  E-value: 1.24e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 252 MFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYF 331
Cdd:COG5256   1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 332 ETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEyetgferGGQTREHALLAKTQGVNKMVVVVNKMDDptV 411
Cdd:COG5256  81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDA--V 151

                       170
                ....*....|....*...
gi 16304373 412 NWSKERYDQCVSNVSNFL 429
Cdd:COG5256 152 NYSEKRYEEVKEEVSKLL 169
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 256-395 1.03e-46

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: 158.84  E-value: 1.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   256 KDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREakdagrqgwylsRVMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGE------------AGLDNLPEERERGITIKSAAVSFETKD 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGeyetgfeRGGQTREHALLAKTQG 395
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLG 121
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 261-420 2.25e-24

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: 103.99  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   261 LIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWY--LSRVMDTNKEERNDGKTIEVGKAYFETEKRRY 338
Cdd:TIGR02034   3 FLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEidLALLVDGLQAEREQGITIDVAYRYFSTDKRKF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   339 TILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQGVNKMVVVVNKMDdpTVNWSKERY 418
Cdd:TIGR02034  83 IVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVF 153


                  ..
gi 16304373   419 DQ 420
Cdd:TIGR02034 154 EN 155
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 28-197 4.75e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373    28 QGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGG----YQQYNPQGGYQQQFNPQGGRGNYKNFN 103
Cdd:PRK10263  378 EGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEqpaqQPYYAPAPEQPVAGNAWQAEEQQSTFA 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   104 YNNNLQGYQAGFQPQSQgmslnDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVDTKPAESDKKEEEKSAETKEPTKE 183
Cdd:PRK10263  458 PQSTYQTEQTYQQPAAQ-----EPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPE 532

                         170
                  ....*....|....
gi 16304373   184 PTKVEEPVKKEEKP 197
Cdd:PRK10263  533 PVKEPEPIKSSLKA 546
 
Name Accession Description Interval E-value
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 260-429 1.51e-99

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: 295.94  E-value: 1.51e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 260 SLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEKRRYT 339
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 340 ILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYD 419
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160

                       170
                ....*....|
gi 16304373 420 QCVSNVSNFL 429
Cdd:cd01883 161 EIKKKVSPFL 170
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 252-429 1.98e-57

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 194.97  E-value: 1.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  252 MFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYF 331
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  332 ETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTV 411
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160

                        170
                 ....*....|....*...
gi 16304373  412 NWSKERYDQCVSNVSNFL 429
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYL 178
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 252-429 1.24e-55

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: 189.76  E-value: 1.24e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 252 MFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYF 331
Cdd:COG5256   1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 332 ETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEyetgferGGQTREHALLAKTQGVNKMVVVVNKMDDptV 411
Cdd:COG5256  81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDA--V 151

                       170
                ....*....|....*...
gi 16304373 412 NWSKERYDQCVSNVSNFL 429
Cdd:COG5256 152 NYSEKRYEEVKEEVSKLL 169
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 256-429 2.55e-53

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 183.59  E-value: 2.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:PRK12317   4 KPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEyetGFErgGQTREHALLAKTQGVNKMVVVVNKMDdpTVNWSK 415
Cdd:PRK12317  84 YYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMD--AVNYDE 156

                        170
                 ....*....|....
gi 16304373  416 ERYDQCVSNVSNFL 429
Cdd:PRK12317 157 KRYEEVKEEVSKLL 170
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 256-395 1.03e-46

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: 158.84  E-value: 1.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   256 KDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREakdagrqgwylsRVMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGE------------AGLDNLPEERERGITIKSAAVSFETKD 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGeyetgfeRGGQTREHALLAKTQG 395
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLG 121
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 256-429 1.52e-39

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 147.16  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:PLN00043   5 KVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSK 415
Cdd:PLN00043  85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSK 164

                        170
                 ....*....|....
gi 16304373  416 ERYDQCVSNVSNFL 429
Cdd:PLN00043 165 ARYDEIVKEVSSYL 178
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 263-395 1.50e-31

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: 118.55  E-value: 1.50e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 263 FMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYereakdagrqgwylsRVMDTNKEERNDGKTIEVGKAYFETEKRRYTILD 342
Cdd:cd00881   4 VIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRINFID 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16304373 343 APGHKMYVSEMIGGASQADVGVLVISARKGEyetgferGGQTREHALLAKTQG 395
Cdd:cd00881  69 TPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIALAGG 114
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 261-429 1.79e-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: 119.21  E-value: 1.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 261 LIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKdAGRQGWY--LSRVMDTNKEERNDGKTIEVGKAYFETEKRRY 338
Cdd:cd04166   2 FITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERSKS-SGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTPKRKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 339 TILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQGVNKMVVVVNKMDdpTVNWSKERY 418
Cdd:cd04166  81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD--LVDYDEEVF 151

                       170
                ....*....|.
gi 16304373 419 DQCVSNVSNFL 429
Cdd:cd04166 152 EEIKADYLAFA 162
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 265-391 2.96e-25

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: 106.71  E-value: 2.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 265 GHVDAGKSTMGGNLLYLTGSV--DKrtIEKYEREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTILD 342
Cdd:COG2895  24 GSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRKFIIAD 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16304373 343 APGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLA 391
Cdd:COG2895 102 TPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIA 143
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 261-420 2.25e-24

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: 103.99  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   261 LIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWY--LSRVMDTNKEERNDGKTIEVGKAYFETEKRRY 338
Cdd:TIGR02034   3 FLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEidLALLVDGLQAEREQGITIDVAYRYFSTDKRKF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   339 TILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQGVNKMVVVVNKMDdpTVNWSKERY 418
Cdd:TIGR02034  83 IVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVF 153


                  ..
gi 16304373   419 DQ 420
Cdd:TIGR02034 154 EN 155
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 265-428 3.19e-23

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 102.31  E-value: 3.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  265 GHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWY--LSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTILD 342
Cdd:PRK05506  31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQGDEidLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  343 APGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQGVNKMVVVVNKMDdpTVNWSKERYDQCV 422
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMD--LVDYDQEVFDEIV 181


                 ....*.
gi 16304373  423 SNVSNF 428
Cdd:PRK05506 182 ADYRAF 187
PRK12736 PRK12736
elongation factor Tu; Reviewed
 256-395 5.69e-21

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 93.86  E-value: 5.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTmggnllyLTGSVDKRTIEKYEREAKDAGRqgwylsrvMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:PRK12736  10 KPHVNIGTIGHVDHGKTT-------LTAAITKVLAERGLNQAKDYDS--------IDAAPEEKERGITINTAHVEYETEK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQG 395
Cdd:PRK12736  75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVG 127
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 258-392 1.05e-20

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: 89.18  E-value: 1.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 258 HVSLIFMGHVDAGKSTmggnllyLTGSVDKRTIEKYEREAKDAGRqgwylsrvMDTNKEERNDGKTIEVGKAYFETEKRR 337
Cdd:cd01884   2 HVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGAKAKKYDE--------IDKAPEEKARGITINTAHVEYETANRH 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16304373 338 YTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAK 392
Cdd:cd01884  67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLAR 114
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 265-391 7.26e-20

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 91.51  E-value: 7.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  265 GHVDAGKSTMGGNLLYltgsvDKRTIekYEREA----KDAGRQGWYLSRV-----MDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:PRK05124  34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLaslhNDSKRHGTQGEKLdlallVDGLQAEREQGITIDVAYRYFSTEK 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLA 391
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIA 155
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 256-392 2.84e-19

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 89.05  E-value: 2.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 256 KDHVSLIFMGHVDAGKSTmggnllyLTGSVDKRTIEKYEREAKDAGRqgwylsrvMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:COG0050  10 KPHVNIGTIGHVDHGKTT-------LTAAITKVLAKKGGAKAKAYDQ--------IDKAPEEKERGITINTSHVEYETEK 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16304373 336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAK 392
Cdd:COG0050  75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLAR 124
PLN03126 PLN03126
Elongation factor Tu; Provisional
 256-395 2.64e-18

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 86.59  E-value: 2.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEReakdagrqgwylsrvMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:PLN03126  79 KPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYETEN 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQG 395
Cdd:PLN03126 144 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVG 196
tufA CHL00071
elongation factor Tu
 256-395 3.01e-18

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 86.16  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEReakdagrqgwylsrvMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:CHL00071  10 KPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHVEYETEN 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQG 395
Cdd:CHL00071  75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVG 127
PRK00049 PRK00049
elongation factor Tu; Reviewed
 256-392 4.00e-18

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 85.63  E-value: 4.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTmggnllyLTGSVDKRTIEKYEREAKDagrqgwYLSrvMDTNKEERNDGKTIEVGKAYFETEK 335
Cdd:PRK00049  10 KPHVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGAEAKA------YDQ--IDKAPEEKARGITINTAHVEYETEK 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16304373  336 RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAK 392
Cdd:PRK00049  75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLAR 124
PLN03127 PLN03127
Elongation factor Tu; Provisional
 256-395 7.13e-18

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 85.26  E-value: 7.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  256 KDHVSLIFMGHVDAGKSTmggnllyLTGSVDKRTIEKyereakdagrqGWylSRVM-----DTNKEERNDGKTIEVGKAY 330
Cdd:PLN03127  59 KPHVNVGTIGHVDHGKTT-------LTAAITKVLAEE-----------GK--AKAVafdeiDKAPEEKARGITIATAHVE 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16304373  331 FETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQG 395
Cdd:PLN03127 119 YETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVG 176
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 265-387 1.49e-12

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: 65.32  E-value: 1.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 265 GHVDAGKSTMggnLLYLTGsvdkrtiekyereakdagrqgwylsrvMDTN--KEERNDGKTIEVGKAYFETEK-RRYTIL 341
Cdd:cd04171   6 GHIDHGKTTL---IKALTG---------------------------IETDrlPEEKKRGITIDLGFAYLDLPDgKRLGFI 55

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 16304373 342 DAPGHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREH 387
Cdd:cd04171  56 DVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREH 94
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 266-372 1.99e-12

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: 66.49  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 266 HVDAGKSTMGGNLLYLTGSVDkrtiekyEREAKDAGrqgwylSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPG 345
Cdd:cd04168   7 HVDAGKTTLTESLLYTSGAIR-------ELGSVDKG------TTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPG 73

                        90       100
                ....*....|....*....|....*..
gi 16304373 346 HKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:cd04168  74 HMDFIAEVERSLSVLDGAILVISAVEG 100
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 265-395 8.65e-11

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: 63.74  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   265 GHVDAGKSTMggnLLYLTGSvdkrtiekyereakDAGRQgwylsrvmdtnKEERNDGKTIEVGKAYFETEKRRYTILDAP 344
Cdd:TIGR00475   7 GHVDHGKTTL---LKALTGI--------------AADRL-----------PEEKKRGMTIDLGFAYFPLPDYRLGFIDVP 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16304373   345 GHKMYVSEMIGGASQADVGVLVISARKGEYEtgferggQTREHALLAKTQG 395
Cdd:TIGR00475  59 GHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLG 102
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 264-372 3.15e-09

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: 58.90  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 264 MGHVDAGKSTMGGNLLYLTGSVDKRtiekyereakdaGR--QGwylSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTIL 341
Cdd:COG0480  15 VAHIDAGKTTLTERILFYTGAIHRI------------GEvhDG---NTVMDWMPEEQERGITITSAATTCEWKGHKINII 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 16304373 342 DAPGHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:COG0480  80 DTPGHVDFTGEVERSLRVLDGAVVVFDAVAG 110
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 265-387 3.17e-09

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: 58.77  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 265 GHVDAGKSTmggnLLY-LTGsvdkrtiekyereakdagrqgwylsrvMDTN--KEERNDGKTIEVGKAYFETEK-RRYTI 340
Cdd:COG3276   7 GHIDHGKTT----LVKaLTG---------------------------IDTDrlKEEKKRGITIDLGFAYLPLPDgRRLGF 55

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 16304373 341 LDAPGHKMYVSEMIGGASQADVGVLVISARkgEyetgfergG---QTREH 387
Cdd:COG3276  56 VDVPGHEKFIKNMLAGAGGIDLVLLVVAAD--E--------GvmpQTREH 95
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
264-369 7.23e-09

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 57.83  E-value: 7.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  264 MGHVDAGKSTMGGNLLYLTGSVDKRTiekyEREAKDAgrqgwylsrVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDA 343
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIG----EVEDGTT---------TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67

                         90       100
                 ....*....|....*....|....*.
gi 16304373  344 PGHKMYVSEMIGGASQADVGVLVISA 369
Cdd:PRK12740  68 PGHVDFTGEVERALRVLDGAVVVVCA 93
PRK13351 PRK13351
elongation factor G-like protein;
263-372 9.49e-08

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 54.19  E-value: 9.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  263 FMGHVDAGKSTMGGNLLYLTGSVDKR-TIEKyereakdaGrqgwylSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTIL 341
Cdd:PRK13351  13 ILAHIDAGKTTLTERILFYTGKIHKMgEVED--------G------TTVTDWMPQEQERGITIESAATSCDWDNHRINLI 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 16304373  342 DAPGHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:PRK13351  79 DTPGHIDFTGEVERSLRVLDGAVVVFDAVTG 109
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 259-391 3.85e-07

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 51.78  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  259 VSLIFMGHVDAGKSTmggnLLY-LTGSvdkrtiekyereakdagrqgWylsrvMDTNKEERNDGKTIEVGKA-------- 329
Cdd:PRK04000  10 VNIGMVGHVDHGKTT----LVQaLTGV--------------------W-----TDRHSEELKRGITIRLGYAdatirkcp 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  330 ------YFETEK------------RRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETgferggQTREHaLLA 391
Cdd:PRK04000  61 dceepeAYTTEPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMA 133
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 265-372 7.02e-07

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: 50.28  E-value: 7.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 265 GHVDAGKSTMGGNLLYLTGSVDKRtiekyerEAKDAGrqgwylSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAP 344
Cdd:cd04170   6 GHSGSGKTTLAEALLYATGAIDRL-------GRVEDG------NTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTP 72

                        90       100
                ....*....|....*....|....*...
gi 16304373 345 GHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:cd04170  73 GYADFVGETLSALRAVDAALIVVEAQSG 100
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 266-372 1.32e-05

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: 45.66  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 266 HVDAGKSTMGGNLLYLTGSvdkrtiekyEREAKDAGrqgwylSRVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPG 345
Cdd:cd01891  10 HVDHGKTTLVDALLKQSGT---------FRENEEVG------ERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPG 74

                        90       100
                ....*....|....*....|....*..
gi 16304373 346 HKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:cd01891  75 HADFGGEVERVLSMVDGVLLLVDASEG 101
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 263-393 1.92e-05

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: 44.77  E-value: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 263 FMGHVDAGKSTmggnLLyltgsvDKrtIEKYEREAKDAGrqgwylsrvmdtnkeerndGKTIEVGkAYF---ETEKRRYT 339
Cdd:cd01887   5 VMGHVDHGKTT----LL------DK--IRKTNVAAGEAG-------------------GITQHIG-AYQvpiDVKIPGIT 52

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16304373 340 ILDAPGHKMYvSEM-IGGASQADVGVLVISArkgeyETGFERggQTRE---HALLAKT 393
Cdd:cd01887  53 FIDTPGHEAF-TNMrARGASVTDIAILVVAA-----DDGVMP--QTIEainHAKAANV 102
PRK10218 PRK10218
translational GTPase TypA;
260-372 2.24e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 46.63  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  260 SLIFMGHVDAGKSTMGGNLLYLTGSVDKRTiEKYEReakdagrqgwylsrVMDTNKEERNDGKTIEVGKAYFETEKRRYT 339
Cdd:PRK10218   7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 16304373  340 ILDAPGHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:PRK10218  72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDG 104
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 264-390 2.40e-05

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: 45.05  E-value: 2.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 264 MGHVDAGKSTMGGNLLYL--TGSVDKrtiekyereakdagrqgwylsrvmdtNKEERNDGKTIEVGKAYF---------- 331
Cdd:cd01889   6 LGHVDSGKTSLAKALSEIasTAAFDK--------------------------NPQSQERGITLDLGFSSFevdkpkhled 59

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16304373 332 ----ETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGeYETgferggQTREHALL 390
Cdd:cd01889  60 nenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQT------QTAECLVI 115
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 265-390 3.97e-05

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 45.81  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  265 GHVDAGKSTMggnLLYLTGsVDKrtiekyereakdagrqgwylsrvmDTNKEERNDGKTIEVGKAYF-ETEKRRYTILDA 343
Cdd:PRK10512   7 GHVDHGKTTL---LQAITG-VNA------------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 16304373  344 PGHKMYVSEMIGGASQADVGVLVISARKGEYetgfergGQTREH-ALL 390
Cdd:PRK10512  59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAIL 99
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 265-387 1.13e-04

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: 43.03  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 265 GHVDAGKSTMGGNLlylTG-SVDKrtiEKYEREAKDAGRQGWYLSRVMD-TNKEERNDGKTIEVGKAYFETE---KRRYT 339
Cdd:cd01888   7 GHVAHGKTTLVKAL---SGvWTVR---HKEELKRNITIKLGYANAKIYKcPNCGCPRPYDTPECECPGCGGEtklVRHVS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16304373 340 ILDAPGHKMYVSEMIGGASQADVGVLVISArkgeyETGFERgGQTREH 387
Cdd:cd01888  81 FVDCPGHEILMATMLSGAAVMDGALLLIAA-----NEPCPQ-PQTSEH 122
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 259-372 1.67e-04

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 42.64  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 259 VSLIfmGHVDAGKSTMGGNLLYLTgsvdkrtiekyeREAKDAGRQGWYLSRVMDTNKEERNDGKTIEVGKAYFETEKRRY 338
Cdd:cd04167   3 VCIA--GHLHHGKTSLLDMLIEQT------------HKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKG 68

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16304373 339 -----TILDAPGHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:cd04167  69 ksyliNIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEG 107
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 264-346 6.89e-04

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: 41.32  E-value: 6.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 264 MGHVDAGKSTMGGNLLYLTGSVDKRtiekYEREAKDAgrqgwylsrVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDA 343
Cdd:cd01886   5 IAHIDAGKTTTTERILYYTGRIHKI----GEVHGGGA---------TMDWMEQERERGITIQSAATTCFWKDHRINIIDT 71


                ...
gi 16304373 344 PGH 346
Cdd:cd01886  72 PGH 74
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 266-346 8.28e-04

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 41.77  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  266 HVDAGKSTMGGNLLYLTGSVDKRTiekyereakdAGRQgwylsRVMDTNKEERNDGKTIevgKA-----YFETEKRRYTI 340
Cdd:PRK07560  28 HIDHGKTTLSDNLLAGAGMISEEL----------AGEQ-----LALDFDEEEQARGITI---KAanvsmVHEYEGKEYLI 89


                 ....*...
gi 16304373  341 --LDAPGH 346
Cdd:PRK07560  90 nlIDTPGH 97
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 266-372 1.08e-03

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: 40.29  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 266 HVDAGKSTMGGNLLYLTGSVDKRTiekyereakdAGRQgwylsRVMDTNKEERNDGKTIevgKA-----YFETEKRRYT- 339
Cdd:cd01885   8 HVDHGKTTLSDSLLASAGIISEKL----------AGKA-----RYLDTREDEQERGITI---KSsaislYFEYEEEKMDg 69

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16304373 340 ------ILDAPGHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:cd01885  70 ndylinLIDSPGHVDFSSEVTAALRLTDGALVVVDAVEG 108
infB CHL00189
translation initiation factor 2; Provisional
 264-372 1.88e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 40.59  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373  264 MGHVDAGKSTMggnllyltgsVDKrtIEKYEREAKDAGrqgwylsrvmdtnkeerndGKTIEVGkAY-----FETEKRRY 338
Cdd:CHL00189 250 LGHVDHGKTTL----------LDK--IRKTQIAQKEAG-------------------GITQKIG-AYevefeYKDENQKI 297

                         90       100       110
                 ....*....|....*....|....*....|....
gi 16304373  339 TILDAPGHKMYVSEMIGGASQADVGVLVISARKG 372
Cdd:CHL00189 298 VFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG 331
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 28-197 4.75e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373    28 QGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGG----YQQYNPQGGYQQQFNPQGGRGNYKNFN 103
Cdd:PRK10263  378 EGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEqpaqQPYYAPAPEQPVAGNAWQAEEQQSTFA 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373   104 YNNNLQGYQAGFQPQSQgmslnDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVDTKPAESDKKEEEKSAETKEPTKE 183
Cdd:PRK10263  458 PQSTYQTEQTYQQPAAQ-----EPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPIPE 532

                         170
                  ....*....|....
gi 16304373   184 PTKVEEPVKKEEKP 197
Cdd:PRK10263  533 PVKEPEPIKSSLKA 546
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 266-346 5.64e-03

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: 37.51  E-value: 5.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16304373 266 HVDAGKSTMGGNLLYLTGSVDKrtiekyeREAKDagrqgwylsRVMDTNKEERNDGKTIevgKA------YFETEKRRYT 339
Cdd:cd01890   8 HIDHGKSTLADRLLELTGTVSE-------REMKE---------QVLDSMDLERERGITI---KAqavrlfYKAKDGEEYL 68


                ....*....
gi 16304373 340 I--LDAPGH 346
Cdd:cd01890  69 LnlIDTPGH 77
 
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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