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Conserved domains on  [gi|187251827|ref|YP_001876309|]
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elongation factor Tu [Elusimicrobium minutum Pei191]

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List of domain hits

Name Accession Description Interval E-value
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
11-206 4.11e-114

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  Cd Length: 195  Bit Score: 334.17  E-value: 4.11e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  11 PHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGgvVRDASKIVTVAVSHVEYESDKRHYAHIDCPGHADY 90
Cdd:cd01884    1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKA--PEEKARGITINTAHVEYETANRHYAHVDCPGHADY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  91 IKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL-ADAELLDLVEMEIRDLLSKYEFDGDNT 169
Cdd:cd01884   79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMvDDEELLELVEMEVRELLSKYGFDGDDT 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 187251827 170 PIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEP 206
Cdd:cd01884  159 PIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
EFTU_III cd03707
Domain III of elongation factor (EF) Tu. Ef-Tu consists of three structural domains, ...
303-390 1.77e-53

Domain III of elongation factor (EF) Tu. Ef-Tu consists of three structural domains, designated I, II and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and binding to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


:

Pssm-ID: 239678  Cd Length: 90  Bit Score: 174.27  E-value: 1.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 303 KPHTKFKGQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGELKFAGD--MIMPGDNAEIEVTLITPVAMEEGLRFAIRE 380
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYIRTTDVTGSITLPEGteMVMPGDNVKMTVELIHPIALEKGLRFAIRE 80
                         90
                 ....*....|
gi 187251827 381 GGRTVGAGVV 390
Cdd:cd03707   81 GGRTVGAGVI 90
EFTU_II cd03697
EFTU_II: Elongation factor Tu domain II. Elongation factors Tu (EF-Tu) are three-domain ...
214-299 7.78e-48

EFTU_II: Elongation factor Tu domain II. Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven a-helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Either non-catalytic domain is composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: in a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA, and in an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


:

Pssm-ID: 239668  Cd Length: 87  Bit Score: 159.21  E-value: 7.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERG 293
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGTIKVGDEVEIVGFGETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKREDVERG 80

                 ....*.
gi 187251827 294 QVLAAP 299
Cdd:cd03697   81 MVLAKP 86
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-395 0e+00

elongation factor Tu; Reviewed


:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 763.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRDASkiVTVAVSHVEYESDKRHYA 80
Cdd:PRK00049   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARG--ITINTAHVEYETEKRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:PRK00049  79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:PRK00049 159 SKYDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:PRK00049 239 IKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTGELKFAGD--MIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PRK00049 319 GGRHTPFFNGYRPQFYFRTTDVTGVIELPEGveMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
 
Name Accession Description Interval E-value
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
11-206 4.11e-114

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  Cd Length: 195  Bit Score: 334.17  E-value: 4.11e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  11 PHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGgvVRDASKIVTVAVSHVEYESDKRHYAHIDCPGHADY 90
Cdd:cd01884    1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKA--PEEKARGITINTAHVEYETANRHYAHVDCPGHADY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  91 IKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL-ADAELLDLVEMEIRDLLSKYEFDGDNT 169
Cdd:cd01884   79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMvDDEELLELVEMEVRELLSKYGFDGDDT 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 187251827 170 PIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEP 206
Cdd:cd01884  159 PIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
EFTU_III cd03707
Domain III of elongation factor (EF) Tu. Ef-Tu consists of three structural domains, ...
303-390 1.77e-53

Domain III of elongation factor (EF) Tu. Ef-Tu consists of three structural domains, designated I, II and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and binding to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 239678  Cd Length: 90  Bit Score: 174.27  E-value: 1.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 303 KPHTKFKGQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGELKFAGD--MIMPGDNAEIEVTLITPVAMEEGLRFAIRE 380
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYIRTTDVTGSITLPEGteMVMPGDNVKMTVELIHPIALEKGLRFAIRE 80
                         90
                 ....*....|
gi 187251827 381 GGRTVGAGVV 390
Cdd:cd03707   81 GGRTVGAGVI 90
EFTU_II cd03697
EFTU_II: Elongation factor Tu domain II. Elongation factors Tu (EF-Tu) are three-domain ...
214-299 7.78e-48

EFTU_II: Elongation factor Tu domain II. Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven a-helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Either non-catalytic domain is composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: in a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA, and in an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 239668  Cd Length: 87  Bit Score: 159.21  E-value: 7.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERG 293
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGTIKVGDEVEIVGFGETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKREDVERG 80

                 ....*.
gi 187251827 294 QVLAAP 299
Cdd:cd03697   81 MVLAKP 86
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
10-204 6.08e-63

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: 249504  Cd Length: 185  Bit Score: 202.35  E-value: 6.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   10 KPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIakggvvrDASKI-----VTVAVSHVEYESDKRHYAHIDC 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYVTGAISKESAKGARVL-------DKLKEerergITIKIAAVSFETKKRHINIIDT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   85 PGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLAD-AELLDLVEMEIRDLLSKYE 163
Cdd:pfam00009  74 PGHVDFTKEMIRGASQADGAILVVDAVEGVMPQTREHLLLAKTLGVP-IIVFINKIDRVDdAELEEIVEEISRELLKKYG 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 187251827  164 FDGDNT-PIIRGSALKAIegdsspigepSIKALLEALDTWIP 204
Cdd:pfam00009 153 EGGEETvPVVPGSALTGE----------GIDELLEALDLYLP 184
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
301-394 8.22e-41

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 251756  Cd Length: 97  Bit Score: 141.12  E-value: 8.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  301 SIKPHTKFKGQVYILKKdeggrHTPLTPGYKPQFYFRTTDVTG---ELKFAGD-----MIMPGDNAEIEVTLITPVAMEE 372
Cdd:pfam03143   1 PIKPHTKFEAQVYILNH-----PTPIFAGYRPVFYCHTADVTGkfiELLSKIDpgkveMVKPGDNVIVTVELIKPIAVEK 75
                          90       100
                  ....*....|....*....|..
gi 187251827  373 GLRFAIREGGRTVGAGVVTKVI 394
Cdd:pfam03143  76 GQRFAIREGGRTVAVGVVTEVL 97
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
228-297 3.14e-18

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 251757  Cd Length: 70  Bit Score: 78.44  E-value: 3.14e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  228 GTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLA 297
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVVIGPNGTGKKGRVTSLEMFHGDLREAVAGANAGIILAGIGLKDIKRGDTLT 70
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
13-148 8.62e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model [Unknown function, General].


Pssm-ID: 232886  Cd Length: 162  Bit Score: 41.20  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   13 VNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEmgyadiakgGVVRDaskivtVAVSHVEYESDKRHYAHIDCPGHADYIK 92
Cdd:TIGR00231   2 IKIVIVGDPNVGKSTLLNRLLGNKISITEYKP---------GTTRN------YVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187251827   93 ------NMITGAAQM-DGAILVVSAQDGPMPQTREHVLLAKQvNVPkLVVFLNKVDLADAELL 148
Cdd:TIGR00231  67 irrlyyRAVESSLRVfDIVILVLDVEEILEKQTKEIIHHAES-GVP-IILVGNKIDLRDAKLK 127
COG2229 COG2229
Predicted GTPase [General function prediction only]
64-184 1.02e-03

Predicted GTPase [General function prediction only]


Pssm-ID: 225138  Cd Length: 187  Bit Score: 38.60  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  64 TVAVSHVEYESDKRHYAHI-DCPGHaDYIKNMITGAAQ-MDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVD 141
Cdd:COG2229   54 TVAMDFGSIELDEDTGVHLfGTPGQ-ERFKFMWEILSRgAVGAIVLVDSSRPITFHAEEIIDFLTSRNPIPVVVAINKQD 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 187251827 142 LADAELLDlvemEIRDLLskyEFDGDNTPIIRGSalkAIEGDS 184
Cdd:COG2229  133 LFDALPPE----KIREAL---KLELLSVPVIEID---ATEGEG 165
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-395 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 763.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRDASkiVTVAVSHVEYESDKRHYA 80
Cdd:PRK00049   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARG--ITINTAHVEYETEKRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:PRK00049  79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:PRK00049 159 SKYDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:PRK00049 239 IKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTGELKFAGD--MIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PRK00049 319 GGRHTPFFNGYRPQFYFRTTDVTGVIELPEGveMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
TufB COG0050
GTPases - translation elongation factors [Translation, ribosomal structure and biogenesis]
1-395 0e+00

GTPases - translation elongation factors [Translation, ribosomal structure and biogenesis]


Pssm-ID: 223128 [Multi-domain]  Cd Length: 394  Bit Score: 648.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRDASkiVTVAVSHVEYESDKRHYA 80
Cdd:COG0050    1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKKGGAEAKAYDQIDNAPEEKARG--ITINTAHVEYETANRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:COG0050   79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYIVVFLNKVDMVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDSSpiGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:COG0050  159 SEYGFPGDDTPIIRGSALKALEGDAK--WEAKIEELMDAVDSYIPTPERDIDKPFLMPVEDVFSISGRGTVVTGRVERGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:COG0050  237 LKVGEEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGVKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEE 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:COG0050  317 GGRHTPFFHGYRPQFYFRTTDVTGaiTLPEGVEMVMPGDNVKMVVELIHPIAMEEGLRFAIREGGRTVGAGVVTKIIE 394
tufA CHL00071
elongation factor Tu
1-395 0e+00

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 648.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADI-------AKGgvvrdaskiVTVAVSHVEYE 73
Cdd:CHL00071   1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIdsapeekARG---------ITINTAHVEYE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  74 SDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVD-LADAELLDLVE 152
Cdd:CHL00071  72 TENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDqVDDEELLELVE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 153 MEIRDLLSKYEFDGDNTPIIRGSALKAIEgdsSPIGEPSIK-----------ALLEALDTWIPEPKRETDKPFLMAVEDV 221
Cdd:CHL00071 152 LEVRELLSKYDFPGDDIPIVSGSALLALE---ALTENPKIKrgenkwvdkiyNLMDAVDSYIPTPERDTDKPFLMAIEDV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 222 FSITGRGTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKS 301
Cdd:CHL00071 229 FSITGRGTVATGRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGT 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 302 IKPHTKFKGQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGELKF-------AGDMIMPGDNAEIEVTLITPVAMEEGL 374
Cdd:CHL00071 309 ITPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddgsKTEMVMPGDRIKMTVELIYPIAIEKGM 388
                        410       420
                 ....*....|....*....|.
gi 187251827 375 RFAIREGGRTVGAGVVTKVIE 395
Cdd:CHL00071 389 RFAIREGGRTVGAGVVSKILK 409
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
1-395 0e+00

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: 624.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827    1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGvvRDASKIVTVAVSHVEYESDKRHYA 80
Cdd:TIGR00485   1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAP--EEKARGITINTAHVEYETENRHYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:TIGR00485  79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  160 SKYEFDGDNTPIIRGSALKAIEGDssPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:TIGR00485 159 SEYDFPGDDTPIIRGSALKALEGD--AEWEAKILELMDAVDEYIPTPERETDKPFLMPIEDVFSITGRGTVVTGRVERGI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:TIGR00485 237 VKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLKKEE 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827  320 GGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:TIGR00485 317 GGRHTPFFSGYRPQFYFRTTDVTGsiTLPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKIIE 394
PLN03127 PLN03127
Elongation factor Tu; Provisional
2-395 0e+00

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 597.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   2 AKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGvvRDASKIVTVAVSHVEYESDKRHYAH 81
Cdd:PLN03127  51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAP--EEKARGITIATAHVEYETAKRHYAH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLLS 160
Cdd:PLN03127 129 VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVdDEELLELVEMELRELLS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 161 KYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVV 240
Cdd:PLN03127 209 FYKFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTI 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 241 KVGDTIEIIGFRD--TMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKD 318
Cdd:PLN03127 289 KVGEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKD 368
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827 319 EGGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PLN03127 369 EGGRHTPFFSNYRPQFYLRTADVTGkvELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-393 3.99e-50

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 176.09  E-value: 3.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKfvrtkPHVNVGTIGHVDHGKTTLTT--------ALTKVLAK-EGKAKEMGYADIaKGGVVRDASKI-----VTVA 66
Cdd:PTZ00141   1 MGKEK-----THINLVVIGHVDSGKSTTTGhliykcggIDKRTIEKfEKEAAEMGKGSF-KYAWVLDKLKAerergITID 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  67 VSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMP-------QTREHVLLAKQVNVPKLVVFLNK 139
Cdd:PTZ00141  75 IALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 140 VDLADA----ELLDLVEMEIRDLLSKYEFDGDNTPIIrgsALKAIEGDSspIGEPSIK-------ALLEALDTWIPePKR 208
Cdd:PTZ00141 155 MDDKTVnysqERYDEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDN--MIEKSDNmpwykgpTLLEALDTLEP-PKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 209 ETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDtieIIGFRDT-MNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEK 287
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSgVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSV 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 288 NQIERGQVLAAPKS--IKPHTKFKGQVYILkkDEGGRhtpLTPGYKPQFYFRTTDV--------------TG-ELKFAGD 350
Cdd:PTZ00141 306 KDIKRGYVASDSKNdpAKECADFTAQVIVL--NHPGQ---IKNGYTPVLDCHTAHIackfaeieskidrrSGkVLEENPK 380
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 187251827 351 MIMPGDNAEIEVTLITPVAMEE-------GlRFAIREGGRTVGAGVVTKV 393
Cdd:PTZ00141 381 AIKSGDAAIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
 
Name Accession Description Interval E-value
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
11-206 4.11e-114

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  Cd Length: 195  Bit Score: 334.17  E-value: 4.11e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  11 PHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGgvVRDASKIVTVAVSHVEYESDKRHYAHIDCPGHADY 90
Cdd:cd01884    1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKA--PEEKARGITINTAHVEYETANRHYAHVDCPGHADY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  91 IKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL-ADAELLDLVEMEIRDLLSKYEFDGDNT 169
Cdd:cd01884   79 IKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMvDDEELLELVEMEVRELLSKYGFDGDDT 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 187251827 170 PIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEP 206
Cdd:cd01884  159 PIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
EFTU_III cd03707
Domain III of elongation factor (EF) Tu. Ef-Tu consists of three structural domains, ...
303-390 1.77e-53

Domain III of elongation factor (EF) Tu. Ef-Tu consists of three structural domains, designated I, II and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and binding to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 239678  Cd Length: 90  Bit Score: 174.27  E-value: 1.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 303 KPHTKFKGQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGELKFAGD--MIMPGDNAEIEVTLITPVAMEEGLRFAIRE 380
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYIRTTDVTGSITLPEGteMVMPGDNVKMTVELIHPIALEKGLRFAIRE 80
                         90
                 ....*....|
gi 187251827 381 GGRTVGAGVV 390
Cdd:cd03707   81 GGRTVGAGVI 90
EFTU_II cd03697
EFTU_II: Elongation factor Tu domain II. Elongation factors Tu (EF-Tu) are three-domain ...
214-299 7.78e-48

EFTU_II: Elongation factor Tu domain II. Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven a-helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Either non-catalytic domain is composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: in a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA, and in an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 239668  Cd Length: 87  Bit Score: 159.21  E-value: 7.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERG 293
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGTIKVGDEVEIVGFGETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKREDVERG 80

                 ....*.
gi 187251827 294 QVLAAP 299
Cdd:cd03697   81 MVLAKP 86
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
10-204 6.08e-63

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: 249504  Cd Length: 185  Bit Score: 202.35  E-value: 6.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   10 KPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIakggvvrDASKI-----VTVAVSHVEYESDKRHYAHIDC 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYVTGAISKESAKGARVL-------DKLKEerergITIKIAAVSFETKKRHINIIDT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   85 PGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLAD-AELLDLVEMEIRDLLSKYE 163
Cdd:pfam00009  74 PGHVDFTKEMIRGASQADGAILVVDAVEGVMPQTREHLLLAKTLGVP-IIVFINKIDRVDdAELEEIVEEISRELLKKYG 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 187251827  164 FDGDNT-PIIRGSALKAIegdsspigepSIKALLEALDTWIP 204
Cdd:pfam00009 153 EGGEETvPVVPGSALTGE----------GIDELLEALDLYLP 184
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
14-206 2.60e-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: 150.52  E-value: 2.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGKTTLTTALTKVLAKEGKAK--EMGYADIAKggvVRDASKIvTVAVSHVEYESDKRHYAHIDCPGHADYI 91
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGtrKETFLDTLK---EERERGI-TIKTGVVEFEWPKRRINFIDTPGHEDFS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  92 KNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLADAELLDLVEMEIRDLLSKYEF---DGDN 168
Cdd:cd00881   77 KETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRVGEEDFDEVLREIKELLKLIGFtflKGKD 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 187251827 169 TPIIRGSALKAIEGDSspigepsikaLLEALDTWIPEP 206
Cdd:cd00881  156 VPIIPISALTGEGIEE----------LLDAIVEHLPPP 183
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
301-394 8.22e-41

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 251756  Cd Length: 97  Bit Score: 141.12  E-value: 8.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  301 SIKPHTKFKGQVYILKKdeggrHTPLTPGYKPQFYFRTTDVTG---ELKFAGD-----MIMPGDNAEIEVTLITPVAMEE 372
Cdd:pfam03143   1 PIKPHTKFEAQVYILNH-----PTPIFAGYRPVFYCHTADVTGkfiELLSKIDpgkveMVKPGDNVIVTVELIKPIAVEK 75
                          90       100
                  ....*....|....*....|..
gi 187251827  373 GLRFAIREGGRTVGAGVVTKVI 394
Cdd:pfam03143  76 GQRFAIREGGRTVAVGVVTEVL 97
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
14-207 8.51e-32

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670  Cd Length: 219  Bit Score: 120.29  E-value: 8.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGKTTLT--------TALTKVLAK-EGKAKEMGyadiaKGG----VVRDASKI-----VTVAVSHVEYESD 75
Cdd:cd01883    1 NLVVIGHVDAGKSTLTghllyklgGVDKRTIEKyEKEAKEMG-----KESfkyaWVLDKLKEerergVTIDVGLAKFETE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  76 KRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDG-------PMPQTREHVLLAKQVNVPKLVVFLNKVDLA----D 144
Cdd:cd01883   76 KYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVtvnwS 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 145 AELLDLVEMEIRDLLSKYEFDGDNTPIIRGSALkaiEGDSspIGEPSIKA-------LLEALDTwIPEPK 207
Cdd:cd01883  156 QERYDEIKKKVSPFLKKVGYNPKDVPFIPISGF---TGDN--LIEKSENMpwykgptLLEALDS-LEPPE 219
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU). mtEF-TU is highly conserved and is 55-60% ...
303-393 5.43e-30

Domain III of mitochondrial EF-TU (mtEF-TU). mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU the nucleotide-binding domain (domain I) of EF-TUmt is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 239677  Cd Length: 93  Bit Score: 111.28  E-value: 5.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 303 KPHTKFKGQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGELKFAG--DMIMPGDNAEIEVTLITPVAMEEGLRFAIRE 380
Cdd:cd03706    1 KPHDKVEAQVYILSKAEGGRHKPFVSNFQPQMFSLTWDCAARIDLPPgkEMVMPGEDTKVTLILRRPMVLEKGQRFTLRD 80
                         90
                 ....*....|...
gi 187251827 381 GGRTVGAGVVTKV 393
Cdd:cd03706   81 GNRTIGTGLVTDT 93
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
15-209 9.81e-28

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  Cd Length: 170  Bit Score: 107.31  E-value: 9.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  15 VGTIGHVDHGKTTLttaltkVLA---------KEGKAK----EMGYAdiakggvvrdaskivtvavsHVEYESDKRhYAH 81
Cdd:cd04171    2 IGTAGHIDHGKTTL------IKAltgietdrlPEEKKRgitiDLGFA--------------------YLDLPDGKR-LGF 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAELLDLVEMEIRDLLSK 161
Cdd:cd04171   55 IDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAG 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 187251827 162 YEFdgDNTPIIRGSalkAIEGDsspigepSIKALLEALDTwIPEPKRE 209
Cdd:cd04171  135 TFL--ADAPIFPVS---SVTGE-------GIEELKNYLDE-LAEPQSK 169
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
13-208 5.53e-24

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  Cd Length: 197  Bit Score: 97.34  E-value: 5.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  13 VNVGTIGHVDHGKTTLTTALTKVL-------AKEGKAKEMGYADIakgGVVRDASKIVTVAVSHVEYESDK--------R 77
Cdd:cd01888    1 INIGTIGHVAHGKTTLVKALSGVWtvrhkeeLKRNITIKLGYANA---KIYKCPNCGCPRPYDTPECECPGcggetklvR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  78 HYAHIDCPGHADYIKNMITGAAQMDGAILVVSA-QDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAElldlvemeir 156
Cdd:cd01888   78 HVSFVDCPGHEILMATMLSGAAVMDGALLLIAAnEPCPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE---------- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 157 DLLSKYEF--------DGDNTPIIRGSALKAIegdsspigepSIKALLEALDTWIPEPKR 208
Cdd:cd01888  148 QALENYEQikefvkgtIAENAPIIPISAQLKY----------NIDVLCEYIVKKIPTPPR 197
EF1_alpha_II cd03693
EF1_alpha_II: this family represents the domain II of elongation factor 1-alpha (EF-1a) that ...
210-300 1.78e-18

EF1_alpha_II: this family represents the domain II of elongation factor 1-alpha (EF-1a) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 239664  Cd Length: 91  Bit Score: 79.52  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 210 TDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIigfrdtMNTVATG----IEMFRKLLDQGEAGDNVGVLLRGV 285
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGVLKPGMVVTF------APAGVTGevksVEMHHEPLEEALPGDNVGFNVKNV 74
                         90
                 ....*....|....*
gi 187251827 286 EKNQIERGQVLAAPK 300
Cdd:cd03693   75 SKKDIKRGDVAGDSK 89
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
63-201 2.37e-18

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  Cd Length: 209  Bit Score: 81.85  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  63 VTVAVSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL 142
Cdd:cd04166   64 ITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827 143 AD--AELLDLVEMEIRDLLSKYEF-DGDNTPIirgSALkaiEGDSspIGEPSIK-------ALLEALDT 201
Cdd:cd04166  144 VDydEEVFEEIKADYLAFAASLGIeDITFIPI---SAL---EGDN--VVSRSENmpwykgpTLLEHLET 204
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
228-297 3.14e-18

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 251757  Cd Length: 70  Bit Score: 78.44  E-value: 3.14e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  228 GTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLA 297
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVVIGPNGTGKKGRVTSLEMFHGDLREAVAGANAGIILAGIGLKDIKRGDTLT 70
Translation_Factor_II_like cd01342
Translation_Factor_II_like: Elongation factor Tu (EF-Tu) domain II-like proteins. Elongation ...
214-298 9.23e-18

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


Pssm-ID: 238652  Cd Length: 83  Bit Score: 77.36  E-value: 9.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRgvEKNQIERG 293
Cdd:cd01342    1 LRALVFKVFKDKGRGTVATGRVESGTLKKGDKVRVGPGGGGVKGKVKSLKRFKGEVDEAVAGDIVGIVLK--DKDDIKIG 78

                 ....*
gi 187251827 294 QVLAA 298
Cdd:cd01342   79 DTLTD 83
selB_II cd03696
selB_II: this subfamily represents the domain of elongation factor SelB, homologous to domain ...
214-298 1.37e-17

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


Pssm-ID: 239667  Cd Length: 83  Bit Score: 76.75  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEI--IGfrdtMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIE 291
Cdd:cd03696    1 FRLPIDRVFTVKGQGTVVTGTVLSGSVKVGDKVEIlpLG----EETRVRSIQVHGKDVEEAKAGDRVALNLTGVDAKDLE 76

                 ....*..
gi 187251827 292 RGQVLAA 298
Cdd:cd03696   77 RGDVLSS 83
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
13-190 3.47e-17

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  Cd Length: 192  Bit Score: 78.18  E-value: 3.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  13 VNVGTIGHVDHGKTTLTTALTKVLA-----KEGKAKEMGYA-DIAKGGVVRDASKIvtvAVSHVEYESDKRHYAHIDCPG 86
Cdd:cd01889    1 VNVGLLGHVDSGKTSLAKALSEIAStaafdKNPQSQERGITlDLGFSSFEVDKPKH---LEDNENPQIENYQITLVDCPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  87 HADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNvPKLVVFLNKVDLADAELLDLVEMEIRDLLSK--YEF 164
Cdd:cd01889   78 HASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLC-KPLIVVLNKIDLIPEEERKRKIEKMKKRLQKtlEKT 156
                        170       180
                 ....*....|....*....|....*.
gi 187251827 165 DGDNTPIIRGSAlkAIEGDSSPIGEP 190
Cdd:cd01889  157 RLKDSPIIPVSA--KPGEGEAELGGE 180
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and EF-G. Elongation factors (EF) EF-Tu and ...
303-390 5.97e-16

Domain III of Elongation factor (EF) Tu (EF-TU) and EF-G. Elongation factors (EF) EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental data showed that: (1) intrinsic GTPase activity of EF-G is influenced by excision of its domain III; (2) that EF-G lacking domain III has a 1,000-fold decreased GTPase activity on the ribosome and, a slightly decreased affinity for GTP; and (3) EF-G lacking domain III does not stimulate translocation, despite the physical presence of domain IV which is also very important for translocation. These findings indicate an essential contribution of domain III to activation of GTP hydrolysis. Domains III and V of EF-G have the same fold (although they are not completely superimposable), the double split beta-alpha-beta fold. This fold is observed in a large number of ribonucleotide binding proteins and is also referred to as the ribonucleoprotein (RNP) or RNA recognition (RRM) motif. This domain III is found in several elongation factors, as well as in peptide chain release factors and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 238771  Cd Length: 102  Bit Score: 72.83  E-value: 5.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 303 KPHTKFKGQVYILKKDEggrhtPLTPGYKPQFYFRTTDVTG-------------ELKFAGDMIMPGDNAEIEVTLITPVA 369
Cdd:cd01513    1 QAVDKFVAEIYVLDHPE-----PLSPGYKPVLNVGTAHVPGriakllskvdgktEEKKPPEFLKSGERGIVEVELQKPVA 75
                         90       100
                 ....*....|....*....|....*..
gi 187251827 370 ME------EGLRFAIREGGRTVGAGVV 390
Cdd:cd01513   76 LEtfsenqEGGRFALRDGGRTVGAGLI 102
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
82-206 1.19e-14

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  Cd Length: 194  Bit Score: 71.09  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADY------IKNMItgaaqmDGAILVVSAQDGPMPQTReHVL---LAKQVnvpKLVVFLNKVDLADAELLDLVE 152
Cdd:cd01891   70 IDTPGHADFggeverVLSMV------DGVLLLVDASEGPMPQTR-FVLkkaLEAGL---KPIVVINKIDRPDARPEEVVD 139
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 187251827 153 mEIRDLLSKYEFDGD--NTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEP 206
Cdd:cd01891  140 -EVFDLFLELNATDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
68-200 4.44e-14

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: 69.04  E-value: 4.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  68 SHVEYESDKRHYAHIDCPGHADYiKNMITGAAQM-DGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLADAE 146
Cdd:cd01887   40 YQVPIDVKIPGITFIDTPGHEAF-TNMRARGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGT 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 147 LLDlvEMEIRDLLSKYEFDGDN----TPIIRGSALKaiegdsspiGEpSIKALLEALD 200
Cdd:cd01887  118 EAD--PERVKNELSELGLVGEEwggdVSIVPISAKT---------GE-GIDDLLEAIL 163
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
82-160 2.07e-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: 64.95  E-value: 2.07e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKlVVFLNKVDLADAElLDLVEMEIRDLLS 160
Cdd:cd04168   69 IDTPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPT-IIFVNKIDRAGAD-LEKVYQEIKEKLS 145
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
63-161 1.22e-10

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: 60.30  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  63 VTVAVSHVEYEsDKRHYAhIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLvVFLNKVDL 142
Cdd:cd04170   52 IETSVAPLEWN-GHKINL-IDTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMDR 128
                         90
                 ....*....|....*....
gi 187251827 143 ADAELLDLVEmEIRDLLSK 161
Cdd:cd04170  129 ARADFDKTLA-ALREAFGR 146
eRF3_II_like cd03698
eRF3_II_like: domain similar to domain II of the eukaryotic class II release factor (eRF3). In ...
213-297 1.84e-10

eRF3_II_like: domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribsome. eRF3 is a GTPase, which enhances the termination efficiency by stimulating the eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and, to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 239669  Cd Length: 83  Bit Score: 56.76  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 213 PFLMAVEDVFSITGrGTVATGRIERGVVKVGDTIEIIGFRDTMntVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIER 292
Cdd:cd03698    1 PFRLPISDKYKDQG-GTVVSGKVESGSIQKGDTLLVMPSKESV--EVKSIYVDDEEVDYAVAGENVRLKLKGIDEEDISP 77

                 ....*
gi 187251827 293 GQVLA 297
Cdd:cd03698   78 GDVLC 82
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
14-156 6.74e-10

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  Cd Length: 218  Bit Score: 57.24  E-value: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGKTTLTTAltkVLAK--------EGKAKEMGYADIAKggvvRDASKIVTVAVS-HVEYESDKRHYAH--- 81
Cdd:cd01885    2 NICIIAHVDHGKTTLSDS---LLASagiiseklAGKARYLDTREDEQ----ERGITIKSSAISlYFEYEEEKMDGNDyli 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 --IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTrEHVL---LAKQVnvpKLVVFLNKVDLADAEL-LDLVEMEI 155
Cdd:cd01885   75 nlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT-ETVLrqaLEERV---KPVLVINKIDRLILELkLSPEEAYQ 150

                 .
gi 187251827 156 R 156
Cdd:cd01885  151 R 151
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
82-206 3.56e-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  Cd Length: 179  Bit Score: 54.46  E-value: 3.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVpKLVVFLNKVDLADAElLDLVEMEIRDLLsk 161
Cdd:cd01890   72 IDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAAD-PDRVKQEIEDVL-- 147
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 187251827 162 yEFDGDNtpIIRGSAlKAIEGdsspigepsIKALLEALDTWIPEP 206
Cdd:cd01890  148 -GLDASE--AILVSA-KTGLG---------VEDLLEAIVERIPPP 179
EF1_alpha_III cd03705
Domain III of EF-1. Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent ...
308-390 1.67e-07

Domain III of EF-1. Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This family is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 239676  Cd Length: 104  Bit Score: 48.73  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 308 FKGQVYILkkdegGRHTPLTPGYKPQFYFRTTDVTGelKFAG-----------------DMIMPGDNAEIEVTLITPVAM 370
Cdd:cd03705    6 FTAQVIVL-----NHPGQIKPGYTPVLDCHTAHVAC--RFAEilskidprtgkkleenpKFLKSGDAAIVKIVPQKPLVV 78
                         90       100
                 ....*....|....*....|....*.
gi 187251827 371 E-----EGL-RFAIREGGRTVGAGVV 390
Cdd:cd03705   79 EtfseyPPLgRFAVRDMGQTVAVGIV 104
eRF3_II cd04089
eRF3_II: domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, ...
213-296 2.65e-07

eRF3_II: domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribsome. eRF3 is a GTPase, which enhances the termination efficiency by stimulating the eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 239756  Cd Length: 82  Bit Score: 47.93  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 213 PFLMAVEDVFSitGRGTVATGRIERGVVKVGDTIEIIGFRDTMntVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIER 292
Cdd:cd04089    1 PLRLPIIDKYK--DMGTVVLGKVESGTIKKGDKLLVMPNKTQV--EVLSIYNEDVEVRYARPGENVRLRLKGIEEEDISP 76

                 ....
gi 187251827 293 GQVL 296
Cdd:cd04089   77 GFVL 80
GTPBP_II cd03694
Domain II of the GP-1 family of GTPase. This group includes proteins similar to GTPBP1 and ...
214-298 5.19e-07

Domain II of the GP-1 family of GTPase. This group includes proteins similar to GTPBP1 and GTPBP2. GTPB1 is structurally, related to elongation factor 1 alpha, a key component of protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 239665  Cd Length: 87  Bit Score: 46.83  E-value: 5.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDT--MNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIE 291
Cdd:cd03694    1 AEFQIDEIYSVPGVGTVVGGTVSKGVIRLGDTLLLGPDQDGsfRPVTVKSIHRNRSPVRVVRAGQSASLALKKIDRSLLR 80

                 ....*..
gi 187251827 292 RGQVLAA 298
Cdd:cd03694   81 KGMVLVS 87
HBS1_C cd04093
HBS1_C: this family represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1) ...
306-393 2.00e-05

HBS1_C: this family represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1) which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and, to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 239760  Cd Length: 107  Bit Score: 42.59  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 306 TKFKGQVYILKKDeggrhTPLTPGYKPQFYFRTTDV--------------TGE-LKFAGDMIMPGDNAEIEVTLITPVAM 370
Cdd:cd04093    4 TRFEARILTFNVD-----KPILPGTPFELFRHSLKEpatitklvsildksTGEvSKKKPRCLTKGQTAIVEIELERPIPL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 187251827 371 EE-------GlRFAIREGGRTVGAGVVTKV 393
Cdd:cd04093   79 ELfkdnkelG-RVVLRRDGETIAAGLVTEI 107
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
82-199 3.23e-05

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 42.92  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPG-------HADYIKNMItgaAQMDGAILVVSAqDGPMPQT-REHVLLAKQVNVPKLVVFLNKVDLADAELLDLVEM 153
Cdd:cd09912   51 VDTPGlnstiehHTEITESFL---PRADAVIFVLSA-DQPLTESeREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLE 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 187251827 154 EIRDLLSKYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEAL 199
Cdd:cd09912  127 YSREELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQSGFEEL 172
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
82-141 3.69e-05

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  Cd Length: 213  Bit Score: 43.03  E-value: 3.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVD 141
Cdd:cd04167   76 IDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
55-148 3.86e-05

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728  Cd Length: 224  Bit Score: 43.43  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  55 VVRDASKIVTVavshveyesdkrhyahIDCPGHADYIKNMITG--AAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPK 132
Cdd:cd04165   78 ICEKSSKVVTF----------------IDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPV 141
                         90
                 ....*....|....*.
gi 187251827 133 LVVfLNKVDLADAELL 148
Cdd:cd04165  142 FVV-VTKIDMTPANVL 156
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
13-148 8.62e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model [Unknown function, General].


Pssm-ID: 232886  Cd Length: 162  Bit Score: 41.20  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   13 VNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEmgyadiakgGVVRDaskivtVAVSHVEYESDKRHYAHIDCPGHADYIK 92
Cdd:TIGR00231   2 IKIVIVGDPNVGKSTLLNRLLGNKISITEYKP---------GTTRN------YVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187251827   93 ------NMITGAAQM-DGAILVVSAQDGPMPQTREHVLLAKQvNVPkLVVFLNKVDLADAELL 148
Cdd:TIGR00231  67 irrlyyRAVESSLRVfDIVILVLDVEEILEKQTKEIIHHAES-GVP-IILVGNKIDLRDAKLK 127
CysN_NodQ_II cd03695
CysN_NodQ_II: This subfamily represents the domain II of the large subunit of ATP sulfurylase ...
214-298 1.62e-04

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


Pssm-ID: 239666  Cd Length: 81  Bit Score: 39.40  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDV--FSITGRGtvATGRIERGVVKVGDTIEII--GFRdtmnTVATGIEMFRKLLDQGEAGDNVGVLLrgvEKN- 288
Cdd:cd03695    1 FRFPVQYVirPNADFRG--YAGTIASGSIRVGDEVVVLpsGKT----SRVKSIETFDGELDEAGAGESVTLTL---EDEi 71
                         90
                 ....*....|
gi 187251827 289 QIERGQVLAA 298
Cdd:cd03695   72 DVSRGDVIVA 81
COG2229 COG2229
Predicted GTPase [General function prediction only]
64-184 1.02e-03

Predicted GTPase [General function prediction only]


Pssm-ID: 225138  Cd Length: 187  Bit Score: 38.60  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  64 TVAVSHVEYESDKRHYAHI-DCPGHaDYIKNMITGAAQ-MDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVD 141
Cdd:COG2229   54 TVAMDFGSIELDEDTGVHLfGTPGQ-ERFKFMWEILSRgAVGAIVLVDSSRPITFHAEEIIDFLTSRNPIPVVVAINKQD 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 187251827 142 LADAELLDlvemEIRDLLskyEFDGDNTPIIRGSalkAIEGDS 184
Cdd:COG2229  133 LFDALPPE----KIREAL---KLELLSVPVIEID---ATEGEG 165
selB_III cd04094
This family represents the domain of elongation factor SelB, homologous to domain III of EF-Tu. ...
293-390 1.58e-03

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


Pssm-ID: 239761  Cd Length: 97  Bit Score: 36.39  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 293 GQVLAAPKSIKPHTKFKGQVYILKKDEggrhTPLTPGYKPQFYFRTTDVTGELK-FAGDMIMPGDNAEIEVTLITPVAME 371
Cdd:cd04094    1 GDVLADPGSLLPTRRLDVRLTVLLSAP----RPLKHRQRVHLHHGTSEVLARVVlLDRDELAPGEEALAQLRLEEPLVAL 76
                         90       100
                 ....*....|....*....|.
gi 187251827 372 EGLRFAIREGG--RTVGAGVV 390
Cdd:cd04094   77 RGDRFILRSYSplRTLGGGRV 97
GTPBP_III cd03708
Domain III of the GP-1 family of GTPase. This group includes proteins similar to GTPBP1 and ...
308-393 1.72e-03

Domain III of the GP-1 family of GTPase. This group includes proteins similar to GTPBP1 and GTPBP2. GTPB1 is structurally, related to elongation factor 1 alpha, a key component of protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 239679  Cd Length: 87  Bit Score: 36.45  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 308 FKGQVYILKkdeggrH-TPLTPGYKPQFYFRTTDVTGELKFA-GDMIMPGDNAEIEVTLI-TPVAMEEGLRFAIREGgRT 384
Cdd:cd03708    6 FEAEILVLH------HpTTISPGYQATVHIGSIRQTARIVSIdKDVLRTGDRALVRFRFLyHPEYLREGQRLIFREG-RT 78

                 ....*....
gi 187251827 385 VGAGVVTKV 393
Cdd:cd03708   79 KGVGEVTKV 87
BipA_TypA_II cd03691
BipA_TypA_II: domain II of BipA (also called TypA) having homology to domain II of the ...
228-280 3.34e-03

BipA_TypA_II: domain II of BipA (also called TypA) having homology to domain II of the elongation factors (EFs) EF-G and EF-Tu. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.


Pssm-ID: 239662  Cd Length: 86  Bit Score: 35.54  E-value: 3.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 228 GTVATGRIERGVVKVGDTIEIIGFRDTMNTV-ATGIEMFRKL----LDQGEAGDNVGV 280
Cdd:cd03691   15 GRIAIGRIFRGTVKVGQQVAVVKRDGKIEKAkITKLFGFEGLkrveVEEAEAGDIVAI 72
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
102-178 6.90e-03

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 35.90  E-value: 6.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187251827 102 DGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVfLNKVDLADAEllDLVEMEIRDLLSKYEFDgDNTPIirgSALK 178
Cdd:cd04163   84 DLVLFVVDASEWIGEGDEFILELLKKSKTPVILV-LNKIDLVKDK--EDLLPLLEKLKELHPFA-EIFPI---SALK 153
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-395 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 763.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRDASkiVTVAVSHVEYESDKRHYA 80
Cdd:PRK00049   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARG--ITINTAHVEYETEKRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:PRK00049  79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:PRK00049 159 SKYDFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:PRK00049 239 IKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTGELKFAGD--MIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PRK00049 319 GGRHTPFFNGYRPQFYFRTTDVTGVIELPEGveMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
PRK12735 PRK12735
elongation factor Tu; Reviewed
1-395 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 751.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKggVVRDASKIVTVAVSHVEYESDKRHYA 80
Cdd:PRK12735   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDN--APEEKARGITINTSHVEYETANRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:PRK12735  79 HVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:PRK12735 159 SKYDFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:PRK12735 239 VKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PRK12735 319 GGRHTPFFNGYRPQFYFRTTDVTGtiELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
1-395 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 690.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGvvRDASKIVTVAVSHVEYESDKRHYA 80
Cdd:PRK12736   1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAP--EEKERGITINTAHVEYETEKRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:PRK12736  79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDssPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:PRK12736 159 SEYDFPGDDIPVIRGSALKALEGD--PKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:PRK12736 237 VKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEE 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTGELKFA--GDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PRK12736 317 GGRHTPFFNNYRPQFYFRTTDVTGSIELPegTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
TufB COG0050
GTPases - translation elongation factors [Translation, ribosomal structure and biogenesis]
1-395 0e+00

GTPases - translation elongation factors [Translation, ribosomal structure and biogenesis]


Pssm-ID: 223128 [Multi-domain]  Cd Length: 394  Bit Score: 648.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRDASkiVTVAVSHVEYESDKRHYA 80
Cdd:COG0050    1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKKGGAEAKAYDQIDNAPEEKARG--ITINTAHVEYETANRHYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:COG0050   79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYIVVFLNKVDMVdDEELLELVEMEVRELL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 160 SKYEFDGDNTPIIRGSALKAIEGDSSpiGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:COG0050  159 SEYGFPGDDTPIIRGSALKALEGDAK--WEAKIEELMDAVDSYIPTPERDIDKPFLMPVEDVFSISGRGTVVTGRVERGI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:COG0050  237 LKVGEEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGVKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEE 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827 320 GGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:COG0050  317 GGRHTPFFHGYRPQFYFRTTDVTGaiTLPEGVEMVMPGDNVKMVVELIHPIAMEEGLRFAIREGGRTVGAGVVTKIIE 394
tufA CHL00071
elongation factor Tu
1-395 0e+00

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 648.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADI-------AKGgvvrdaskiVTVAVSHVEYE 73
Cdd:CHL00071   1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIdsapeekARG---------ITINTAHVEYE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  74 SDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVD-LADAELLDLVE 152
Cdd:CHL00071  72 TENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDqVDDEELLELVE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 153 MEIRDLLSKYEFDGDNTPIIRGSALKAIEgdsSPIGEPSIK-----------ALLEALDTWIPEPKRETDKPFLMAVEDV 221
Cdd:CHL00071 152 LEVRELLSKYDFPGDDIPIVSGSALLALE---ALTENPKIKrgenkwvdkiyNLMDAVDSYIPTPERDTDKPFLMAIEDV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 222 FSITGRGTVATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKS 301
Cdd:CHL00071 229 FSITGRGTVATGRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGT 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 302 IKPHTKFKGQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGELKF-------AGDMIMPGDNAEIEVTLITPVAMEEGL 374
Cdd:CHL00071 309 ITPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddgsKTEMVMPGDRIKMTVELIYPIAIEKGM 388
                        410       420
                 ....*....|....*....|.
gi 187251827 375 RFAIREGGRTVGAGVVTKVIE 395
Cdd:CHL00071 389 RFAIREGGRTVGAGVVSKILK 409
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
1-395 0e+00

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: 624.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827    1 MAKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGvvRDASKIVTVAVSHVEYESDKRHYA 80
Cdd:TIGR00485   1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAP--EEKARGITINTAHVEYETENRHYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   81 HIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLL 159
Cdd:TIGR00485  79 HVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  160 SKYEFDGDNTPIIRGSALKAIEGDssPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGV 239
Cdd:TIGR00485 159 SEYDFPGDDTPIIRGSALKALEGD--AEWEAKILELMDAVDEYIPTPERETDKPFLMPIEDVFSITGRGTVVTGRVERGI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  240 VKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDE 319
Cdd:TIGR00485 237 VKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLKKEE 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827  320 GGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:TIGR00485 317 GGRHTPFFSGYRPQFYFRTTDVTGsiTLPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKIIE 394
PLN03127 PLN03127
Elongation factor Tu; Provisional
2-395 0e+00

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 597.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   2 AKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGvvRDASKIVTVAVSHVEYESDKRHYAH 81
Cdd:PLN03127  51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAP--EEKARGITIATAHVEYETAKRHYAH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA-DAELLDLVEMEIRDLLS 160
Cdd:PLN03127 129 VDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVdDEELLELVEMELRELLS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 161 KYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVV 240
Cdd:PLN03127 209 FYKFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTI 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 241 KVGDTIEIIGFRD--TMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKD 318
Cdd:PLN03127 289 KVGEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKD 368
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827 319 EGGRHTPLTPGYKPQFYFRTTDVTG--ELKFAGDMIMPGDNAEIEVTLITPVAMEEGLRFAIREGGRTVGAGVVTKVIE 395
Cdd:PLN03127 369 EGGRHTPFFSNYRPQFYLRTADVTGkvELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
PLN03126 PLN03126
Elongation factor Tu; Provisional
2-395 0e+00

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 538.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   2 AKEKFVRTKPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRdaSKIVTVAVSHVEYESDKRHYAH 81
Cdd:PLN03126  71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEER--ARGITINTATVEYETENRHYAH 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLAD-AELLDLVEMEIRDLLS 160
Cdd:PLN03126 149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDdEELLELVELEVRELLS 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 161 KYEFDGDNTPIIRGSALKAIEgdsSPIGEPSIK-----------ALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGT 229
Cdd:PLN03126 229 SYEFPGDDIPIISGSALLALE---ALMENPNIKrgdnkwvdkiyELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGT 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 230 VATGRIERGVVKVGDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFK 309
Cdd:PLN03126 306 VATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFE 385
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 310 GQVYILKKDEGGRHTPLTPGYKPQFYFRTTDVTGE-LKFAGD------MIMPGDNAEIEVTLITPVAMEEGLRFAIREGG 382
Cdd:PLN03126 386 AIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKvTSIMNDkdeeskMVMPGDRVKMVVELIVPVACEQGMRFAIREGG 465
                        410
                 ....*....|...
gi 187251827 383 RTVGAGVVTKVIE 395
Cdd:PLN03126 466 KTVGAGVIQSIIE 478
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
8-393 1.09e-83

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 264.10  E-value: 1.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   8 RTKPHVNVGTIGHVDHGKT--------TLTTALTKVLAK-EGKAKEMGYADiAKGGVVRDASKI-----VTVAVSHVEYE 73
Cdd:PRK12317   2 KEKPHLNLAVIGHVDHGKStlvgrllyETGAIDEHIIEElREEAKEKGKES-FKFAWVMDRLKEerergVTIDLAHKKFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  74 SDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQD--GPMPQTREHVLLAKQVNVPKLVVFLNKVDLA--DAELLD 149
Cdd:PRK12317  81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVnyDEKRYE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 150 LVEMEIRDLLSKYEFDGDNTPIIRGSALkaiEGDSspIGEPSIK-------ALLEALDTwIPEPKRETDKPFLMAVEDVF 222
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPDDIPFIPVSAF---EGDN--VVKKSENmpwyngpTLLEALDN-LKPPEKPTDKPLRIPIQDVY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 223 SITGRGTVATGRIERGVVKVGDTIEIigfrdtMNTVATG----IEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAA 298
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVVF------MPAGVVGevksIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGH 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 299 PKsiKPHT---KFKGQVYILKkdeggrH-TPLTPGYKPQFYFRTTDV--------------TGELKFAG-DMIMPGDNAE 359
Cdd:PRK12317 309 PD--NPPTvaeEFTAQIVVLQ------HpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQVAEENpQFIKTGDAAI 380
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 187251827 360 IEVTLITPVAMEE-------GlRFAIREGGRTVGAGVVTKV 393
Cdd:PRK12317 381 VKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
10-393 8.68e-80

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]


Pssm-ID: 227581 [Multi-domain]  Cd Length: 428  Bit Score: 254.15  E-value: 8.68e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  10 KPHVNVGTIGHVDHGKTTLT--------TALTKVLAK-EGKAKEMGyadiaKGG----VVRDASKI-----VTVAVSHVE 71
Cdd:COG5256    5 KPHLNLVFIGHVDAGKSTLVgrllydlgEIDKRTMEKlEKEAKELG-----KESfkfaWVLDKTKEerergVTIDVAHSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  72 YESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDG-------PMPQTREHVLLAKQVNVPKLVVFLNKVDLA- 143
Cdd:COG5256   80 FETDKYNFTIIDAPGHRDFVKNMITGASQADVAVLVVDARDGefeagfgVGGQTREHAFLARTLGIKQLIVAVNKMDLVs 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 144 -DAELLDLVEMEIRDLLSKYEFDGDNTPIIRGSALKaieGDSspIGEPS-------IKALLEALDTwIPEPKRETDKPFL 215
Cdd:COG5256  160 wDEERFEEIVSEVSKLLKMVGYNPKDVPFIPISGFK---GDN--LTKKSenmpwykGPTLLEALDQ-LEPPERPLDKPLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 216 MAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDTmnTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQV 295
Cdd:COG5256  234 LPIQDVYSISGIGTVPVGRVESGVIKPGQKVTFMPAGVV--GEVKSIEMHHEEISQAEPGDNVGFNVRGVEKNDIRRGDV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 296 LAAPKSIKPH-TKFKGQVYILkkdegGRHTPLTPGYKPQFYFRTTDVTG---------------ELKFAGDMIMPGDNAE 359
Cdd:COG5256  312 IGHSDNPPTVsPEFTAQIIVL-----WHPGIITSGYTPVLHAHTAQVACriaellskldprtgkKLEENPQFLKRGDAAI 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 187251827 360 IEVTLITPVAME-------EGlRFAIREGGRTVGAGVVTKV 393
Cdd:COG5256  387 VKIEPEKPLCLEkvseipqLG-RFALRDMGQTIAAGKVLEV 426
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-393 4.15e-60

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: 202.40  E-value: 4.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827    1 MAKEKfvrtkPHVNVGTIGHVDHGKTTLT--------TALTKVLAK-EGKAKEMGYADIAKGGVV----RDASKIVTVAV 67
Cdd:TIGR00483   1 MAKEK-----EHINVAFIGHVDHGKSTTVghllykcgAIDEQTIEKfEKEAQEKGKASFEFAWVMdrlkEERERGVTIDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   68 SHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGP---MPQTREHVLLAKQVNVPKLVVFLNKVDLA- 143
Cdd:TIGR00483  76 AHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEfevQPQTREHAFLARTLGINQLIVAINKMDSVn 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  144 -DAELLDLVEMEIRDLLSKYEFDGDNTPIIRGSALKAIEGDSSPIGEPSIKA--LLEALDTwIPEPKRETDKPFLMAVED 220
Cdd:TIGR00483 156 yDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGktLLEALDA-LEPPEKPTDKPLRIPIQD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  221 VFSITGRGTVATGRIERGVVKVGD--TIEIIGfrdtMNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAA 298
Cdd:TIGR00483 235 VYSITGVGTVPVGRVETGVLKPGDkvVFEPAG----VSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGH 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  299 PKS-IKPHTKFKGQVYILKKDeggrhTPLTPGYKPQFYFRTTDV--------------TGELKFAG-DMIMPGDNAEIEV 362
Cdd:TIGR00483 311 PDNpPKVAKEFTAQIVVLQHP-----GAITVGYTPVFHCHTAQIacrfdellkkndprTGQVLEENpQFLKTGDAAIVKF 385
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 187251827  363 TLITPVAMEEGL------RFAIREGGRTVGAGVVTKV 393
Cdd:TIGR00483 386 KPTKPMVIEAVKeipplgRFAIRDMGQTVAAGMIIDV 422
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-393 3.99e-50

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 176.09  E-value: 3.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKfvrtkPHVNVGTIGHVDHGKTTLTT--------ALTKVLAK-EGKAKEMGYADIaKGGVVRDASKI-----VTVA 66
Cdd:PTZ00141   1 MGKEK-----THINLVVIGHVDSGKSTTTGhliykcggIDKRTIEKfEKEAAEMGKGSF-KYAWVLDKLKAerergITID 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  67 VSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMP-------QTREHVLLAKQVNVPKLVVFLNK 139
Cdd:PTZ00141  75 IALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 140 VDLADA----ELLDLVEMEIRDLLSKYEFDGDNTPIIrgsALKAIEGDSspIGEPSIK-------ALLEALDTWIPePKR 208
Cdd:PTZ00141 155 MDDKTVnysqERYDEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDN--MIEKSDNmpwykgpTLLEALDTLEP-PKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 209 ETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDtieIIGFRDT-MNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEK 287
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSgVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSV 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 288 NQIERGQVLAAPKS--IKPHTKFKGQVYILkkDEGGRhtpLTPGYKPQFYFRTTDV--------------TG-ELKFAGD 350
Cdd:PTZ00141 306 KDIKRGYVASDSKNdpAKECADFTAQVIVL--NHPGQ---IKNGYTPVLDCHTAHIackfaeieskidrrSGkVLEENPK 380
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 187251827 351 MIMPGDNAEIEVTLITPVAMEE-------GlRFAIREGGRTVGAGVVTKV 393
Cdd:PTZ00141 381 AIKSGDAAIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
13-388 5.01e-49

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: 175.45  E-value: 5.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   13 VNVGTIGHVDHGKTTLTTALTKVLA-------KEGKAKEMGYADIakggvvrdaskivtvavshveyESDKRHYAHIDCP 85
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAAdrlpeekKRGMTIDLGFAYF----------------------PLPDYRLGFIDVP 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   86 GHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAELLDLVEMEIRDLLSKYEFD 165
Cdd:TIGR00475  59 GHEKFISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  166 gDNTPIIRGSAlKAIEGdsspIGE--PSIKALLEALDTwipepkRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVG 243
Cdd:TIGR00475 139 -KNAKIFKTSA-KTGQG----IGElkKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVG 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  244 DTIEIIGFRDTMNTVAtgIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLaapksIKPHTKFKGQVYILKKdeggrH 323
Cdd:TIGR00475 207 DNLRLLPINHEVRVKA--IQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI-----LTPEDPKLRVVVKFIA-----E 274
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187251827  324 TPLTPGYKPQFYFRTTDVTGELKFAGDMIMpgdnaeiEVTLITPVAMEEGLRFAIREGGRTVGAG 388
Cdd:TIGR00475 275 VPLLELQPYHIAHGMSVTTGKISLLDKGIA-------LLTLDAPLILAKGDKLVLRDSSGNFLAG 332
GTPBP1 COG5258
GTPase [General function prediction only]
10-394 4.38e-47

GTPase [General function prediction only]


Pssm-ID: 227583 [Multi-domain]  Cd Length: 527  Bit Score: 169.19  E-value: 4.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  10 KPHVNVGTIGHVDHGKTTLTTALTKVLAKEGKAKEMGYADIAKGGVVRDASKIVTVAV--------------------SH 69
Cdd:COG5258  115 PEHVLVGVAGHVDHGKSTLVGVLVTGRLDDGDGATRSYLDVQKHEVERGLSADISLRVygfddgkvvrlknpldeaekAA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  70 VEYESDKRhYAHIDCPGHADYIKNMITG--AAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVfLNKVDLADAEL 147
Cdd:COG5258  195 VVKRADKL-VSFVDTVGHEPWLRTTIRGllGQKVDYGLLVVAADDGVTKMTKEHLGIALAMELPVIVV-VTKIDMVPDDR 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 148 LDLVEMEIRDLLSKYEfdgdNTPII---RGSALKAIEGDSS-----PIGEPS------IKALLEALDTWIPEPKRETDKP 213
Cdd:COG5258  273 FQGVVEEISALLKRVG----RIPLIvkdTDDVVLAAKAMKAgrgvvPIFYTSsvtgegLDLLDEFFLLLPKRRRWDDEGP 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFRDT--MNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIE 291
Cdd:COG5258  349 FLMYIDKIYSVTGVGTVVSGSVKSGILHVGDTVLLGPFKDGkfREVVVKSIEMHHYRVDSAKAGSIIGIALKGVEKEELE 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 292 RGQVLAAPKSIKPHTKFKGQVYILkkdeggRH-TPLTPGYKPQFYFRTTDVTGELKFA-GDMIMPGDNAEIEVTL-ITPV 368
Cdd:COG5258  429 RGMVLSAGADPKAVREFDAEVLVL------RHpTTIRAGYEPVFHYETIREAVYFEEIdKGFLMPGDRGVVRMRFkYRPH 502
                        410       420
                 ....*....|....*....|....*.
gi 187251827 369 AMEEGLRFAIREgGRTVGAGVVTKVI 394
Cdd:COG5258  503 HVEEGQKFVFRE-GRSKGVGRVIRVD 527
SelB COG3276
Selenocysteine-specific translation elongation factor [Translation, ribosomal structure and ...
13-376 4.67e-43

Selenocysteine-specific translation elongation factor [Translation, ribosomal structure and biogenesis]


Pssm-ID: 225815 [Multi-domain]  Cd Length: 447  Bit Score: 156.79  E-value: 4.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  13 VNVGTIGHVDHGKTTLTTALTKVLakEGKAKEMGyadiaKGGVVRDaskivtVAVSHVEYESDKRHYahIDCPGHADYIK 92
Cdd:COG3276    1 MIIGTAGHIDHGKTTLLKALTGGV--TDRLPEEK-----KRGITID------LGFYYRKLEDGVMGF--IDVPGHPDFIS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  93 NMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAELLDLVEMEIRDLLSKyefdgDNTPII 172
Cdd:COG3276   66 NLLAGLGGIDYALLVVAADEGLMAQTGEHLLILDLLGIKNGIIVLTKADRVDEARIEQKIKQILADLSL-----ANAKIF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 173 RGSAlKAIEGdsspigepsIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDTIEIIGFR 252
Cdd:COG3276  141 KTSA-KTGRG---------IEELKNELIDLLEEIERDEQKPFRIAIDRAFTVKGVGTVVTGTVLSGEVKVGDKLYLSPIN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 253 DTMNTvaTGIEMFRKLLDQGEAGDNVGVLLRGVEKNQIERGQVLAAPKSIKPHTKFKGQVYILKKDEggrhTPLTPGYKP 332
Cdd:COG3276  211 KEVRV--RSIQAHDVDVEEAKAGQRVGLALKGVEKEEIERGDWLLKPEPLEVTTRLIVELEIDPLFK----KTLKQGQPV 284
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 187251827 333 QFYFRTTDVTG---ELKFAGDMIM-----PGDNAEIEVTLITPVAMEEGLRF 376
Cdd:COG3276  285 HIHVGLRSVTGrivPLEKNAELNLvkpiaLGDNDRLVLRDNSAVIKLAGARV 336
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
11-390 3.90e-38

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 211860 [Multi-domain]  Cd Length: 406  Bit Score: 142.12  E-value: 3.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   11 PHVNVGTIGHVDHGKTTLTTALTKVLA-------KEGKAKEMGYADIakggVVR-----DASKIVTVAVSHVEYESDK-- 76
Cdd:TIGR03680   3 PEVNIGMVGHVDHGKTTLTKALTGVWTdthseelKRGISIRLGYADA----EIYkcpecDGPECYTTEPVCPNCGSETel 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   77 -RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDG-PMPQTREHVLLAKQVNVPKLVVFLNKVDLADAE-LLDLVEm 153
Cdd:TIGR03680  79 lRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTREHLMALEIIGIKNIVIVQNKIDLVSKEkALENYE- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  154 EIRDLLSKYEfdGDNTPIIRGSALKAIegdsspigepSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGT---- 229
Cdd:TIGR03680 158 EIKEFVKGTI--AENAPIIPVSALHNA----------NIDALLEAIEKFIPTPERDLDKPPLMYVARSFDVNKPGTppek 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  230 ----VATGRIERGVVKVGDTIEII-GFRDT---------MNTVATGIEMFRKLLDQGEAGDNVGV---LLRGVEKNQIER 292
Cdd:TIGR03680 226 lkggVIGGSLIQGKLKVGDEIEIRpGIKVEkggktkwepIYTEITSLRAGGYKVEEARPGGLVGVgtkLDPALTKADALA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  293 GQVLAAPKSIKP-HTKFKGQVYILKK----DEGGRHTPLTPGYKPQFYFRTTDVTGELKFAGDmimpgdnAEIEVTLITP 367
Cdd:TIGR03680 306 GQVVGKPGTLPPvWESLELEVHLLERvvgtEEELKVEPIKTGEVLMLNVGTATTVGVVTSARK-------DEIEVKLKRP 378
                         410       420
                  ....*....|....*....|....*..
gi 187251827  368 VAMEEGLRFAI--REGGR--TVGAGVV 390
Cdd:TIGR03680 379 VCAEEGDRVAIsrRVGGRwrLIGYGII 405
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
1-393 7.84e-38

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 142.15  E-value: 7.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFvrtkpHVNVGTIGHVDHGKTTLTTALTKVLAK---------EGKAKEMGYADIAKGGVV----RDASKIVTVAV 67
Cdd:PLN00043   1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGidkrvierfEKEAAEMNKRSFKYAWVLdklkAERERGITIDI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  68 SHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMP-------QTREHVLLAKQVNVPKLVVFLNKV 140
Cdd:PLN00043  76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 141 DLADAEL----LDLVEMEIRDLLSKYEFDGDNTPIIrgsALKAIEGD-----SSPIGEPSIKALLEALDTwIPEPKRETD 211
Cdd:PLN00043 156 DATTPKYskarYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGDnmierSTNLDWYKGPTLLEALDQ-INEPKRPSD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 212 KPFLMAVEDVFSITGRGTVATGRIERGVVKVGdtiEIIGFRDT-MNTVATGIEMFRKLLDQGEAGDNVGVLLRGVEKNQI 290
Cdd:PLN00043 232 KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTgLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 291 ERGQVLAAPKS--IKPHTKFKGQVYILKK--DEGGRHTPLTPGYKPQFYFRTTDVT--------GELKFAGDMIMPGDNA 358
Cdd:PLN00043 309 KRGYVASNSKDdpAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILtkidrrsgKELEKEPKFLKNGDAG 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 187251827 359 EIEVTLITPVAMEEGL------RFAIREGGRTVGAGVVTKV 393
Cdd:PLN00043 389 FVKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
1-392 2.11e-35

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]


Pssm-ID: 227582 [Multi-domain]  Cd Length: 415  Bit Score: 134.78  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVrtKPHVNVGTIGHVDHGKTTLTTALTKVLA-------KEGKAKEMGYAD--IAKGGVVRDASKIVTVAVSHVE 71
Cdd:COG5257    1 MADPKHI--QPEVNIGMVGHVDHGKTTLTKALSGVWTdrhseelKRGITIKLGYADakIYKCPECYRPECYTTEPKCPNC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  72 YESDK--RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSA-QDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAELL 148
Cdd:COG5257   79 GAETElvRRVSFVDAPGHETLMATMLSGAALMDGALLVIAAnEPCPQPQTREHLMALEIIGIKNIIIVQNKIDLVSRERA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 149 DLVEMEIRDLLSkyEFDGDNTPIIRGSALKAIegdsspigepSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRG 228
Cdd:COG5257  159 LENYEQIKEFVK--GTVAENAPIIPISAQHKA----------NIDALIEAIEKYIPTPERDLDKPPRMYVARSFDVNKPG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 229 T--------VATGRIERGVVKVGDTIEI-----------IGFRDTMNTVaTGIEMFRKLLDQGEAGDNVGV---LLRGVE 286
Cdd:COG5257  227 TppeelkggVIGGSLVQGVLRVGDEIEIrpgivvekggkTVWEPITTEI-VSLQAGGEDVEEARPGGLVGVgtkLDPTLT 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 287 KNQIERGQVLAAPKSIKP-HTKFKGQVYILKK----DEGGRHTPLTPGYKPQFYFRTTDVTGELKFAGDmimpgdnAEIE 361
Cdd:COG5257  306 KADALVGQVVGKPGTLPPvWTSIRIEYHLLERvvgtKEELKVEPIKTNEVLMLNVGTATTVGVVTSAKK-------DEIE 378
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 187251827 362 VTLITPVAMEEGLRFAI--REGG--RTVGAGVVTK 392
Cdd:COG5257  379 VKLKRPVCAEIGERVAIsrRIGNrwRLIGYGTIKE 413
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
11-390 4.53e-34

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 130.74  E-value: 4.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  11 PHVNVGTIGHVDHGKTTLttaltkVLAKEGK-----AKEM--------GYAD--IAKGGVVRDASKIVTVAVSHVEYESD 75
Cdd:PRK04000   8 PEVNIGMVGHVDHGKTTL------VQALTGVwtdrhSEELkrgitirlGYADatIRKCPDCEEPEAYTTEPKCPNCGSET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  76 K--RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSA-QDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAEllDLVE 152
Cdd:PRK04000  82 EllRRVSFVDAPGHETLMATMLSGAALMDGAILVIAAnEPCPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKE--RALE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 153 --MEIRDLLSKYEFdgDNTPIIRGSALKAIegdsspigepSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGT- 229
Cdd:PRK04000 160 nyEQIKEFVKGTVA--ENAPIIPVSALHKV----------NIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTp 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 230 -------VATGRIERGVVKVGDTIEI-------IGFRDTMNTVATGIEMFR---KLLDQGEAGDNVGV---LLRGVEKNQ 289
Cdd:PRK04000 228 peklkggVIGGSLIQGVLKVGDEIEIrpgikveEGGKTKWEPITTKIVSLRaggEKVEEARPGGLVGVgtkLDPSLTKAD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 290 IERGQVLAAPKSIKP-HTKFKGQVYILKK----DEGGRHTPLTPGYKPQFYFRTTDVTGELKFAGDmimpgdnAEIEVTL 364
Cdd:PRK04000 308 ALAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVTSARK-------DEAEVKL 380
                        410       420       430
                 ....*....|....*....|....*....|
gi 187251827 365 ITPVAMEEGLRFAI--REGGR--TVGAGVV 390
Cdd:PRK04000 381 KRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
CysN COG2895
GTPases - Sulfate adenylate transferase subunit 1 [Inorganic ion transport and metabolism]
63-392 4.92e-30

GTPases - Sulfate adenylate transferase subunit 1 [Inorganic ion transport and metabolism]


Pssm-ID: 225448 [Multi-domain]  Cd Length: 431  Bit Score: 118.94  E-value: 4.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  63 VTVAVSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL 142
Cdd:COG2895   72 ITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTADLAILLVDARKGVLEQTRRHSFIASLLGIRHVVVAVNKMDL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 143 AD--AELLDLVEMEIRDLLSKYEFDgDNTPIirgsALKAIEGDSspIGEPSIK-------ALLEALDTWIPEPKRETdKP 213
Cdd:COG2895  152 VDysEEVFEAIVADYLAFAAQLGLK-DVRFI----PISALLGDN--VVSKSENmpwykgpTLLEILETVEIADDRSA-KA 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDV--FSITGRGTvaTGRIERGVVKVGDTIEIIgfRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLrgveKNQIE 291
Cdd:COG2895  224 FRFPVQYVnrPNLDFRGY--AGTIASGSVKVGDEVVVL--PSGKTSRVKRIVTFDGELAQASAGEAVTLVL----ADEID 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 292 --RGQVLAAPKSI--------------KPHTKFKGQVYILKkdeggRHTPLTPGYKPQFYFRtTDVTGELKFAGDMIMPG 355
Cdd:COG2895  296 isRGDLIVAADAPpavadafdadvvwmDEEPLLPGRSYDLK-----IATRTVRARVEEIKHQ-LDVNTLEQEGAESLPLN 369
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 187251827 356 DNAEIEVTLITPVAMEE--------GLRFAIREGGRTVGAGVVTK 392
Cdd:COG2895  370 EIGRVRISFDKPIAFDAyaenratgSFILIDRLTNGTVGAGMILA 414
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
17-307 8.94e-30

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 120.16  E-value: 8.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  17 TIGHVDHGKTTLTTALTKVLA-------KEGKAKEMGYAdiakggvvrdaskivtvavshveY--ESDKRHYAHIDCPGH 87
Cdd:PRK10512   5 TAGHVDHGKTTLLQAITGVNAdrlpeekKRGMTIDLGYA-----------------------YwpQPDGRVLGFIDVPGH 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  88 ADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLADAELLDLVEMEIRDLLSKYEFDGd 167
Cdd:PRK10512  62 EKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLREYGFAE- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 168 nTPIIRGSALKAIegdsspigepSIKALLEALDTwIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDTIE 247
Cdd:PRK10512 141 -AKLFVTAATEGR----------GIDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLW 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187251827 248 IIGFRDTMNTvaTGIEMFRKLLDQGEAGDNVGVLLRG-VEKNQIERGQVLAAPKSIKPHTK 307
Cdd:PRK10512 209 LTGVNKPMRV--RGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDWLLADAPPEPFTR 267
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
13-249 4.11e-25

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 104.70  E-value: 4.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  13 VNVGTIGHVDHGKTTLTTALTKVLAKEGKA-KEM------GYADiakggvvrdaSKIVT-----VAVSHVEYESDK---- 76
Cdd:PTZ00327  35 INIGTIGHVAHGKSTVVKALSGVKTVRFKReKVRnitiklGYAN----------AKIYKcpkcpRPTCYQSYGSSKpdnp 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  77 ------------RHYAHIDCPGHADYIKNMITGAAQMDGAILVVSA-QDGPMPQTREHVLLAKQVNVPKLVVFLNKVDLA 143
Cdd:PTZ00327 105 pcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAAnESCPQPQTSEHLAAVEIMKLKHIIILQNKIDLV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 144 DAELLDLVEMEIRDLLSKYEfdGDNTPIIRGSALKAIegdsspigepSIKALLEALDTWIPEPKRETDKPFLMAV----- 218
Cdd:PTZ00327 185 KEAQAQDQYEEIRNFVKGTI--ADNAPIIPISAQLKY----------NIDVVLEYICTQIPIPKRDLTSPPRMIVirsfd 252
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 187251827 219 -----EDVFSItgRGTVATGRIERGVVKVGDTIEII 249
Cdd:PTZ00327 253 vnkpgEDIENL--KGGVAGGSILQGVLKVGDEIEIR 286
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
82-304 4.93e-25

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors].


Pssm-ID: 233394 [Multi-domain]  Cd Length: 594  Bit Score: 105.85  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   82 IDCPGHADY------IKNMItgaaqmDGAILVVSAQDGPMPQTRehVLLAKQVNVP-KLVVFLNKVDLADAElLDLVEME 154
Cdd:TIGR01394  69 VDTPGHADFggeverVLGMV------DGVLLLVDASEGPMPQTR--FVLKKALELGlKPIVVINKIDRPSAR-PDEVVDE 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  155 IRDLLskYEFDGDNT----PIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVE--DVFSITGRg 228
Cdd:TIGR01394 140 VFDLF--AELGADDEqldfPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR- 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  229 tVATGRIERGVVKVGDTIEIIGFRDTMNTV-ATGIEMFRKL----LDQGEAGDNVGVLlrGVEKNQIerGQVLAAPKSIK 303
Cdd:TIGR01394 217 -IAIGRVHRGTVKKGQQVALMKRDGTIENGrISKLLGFEGLerveIDEAGAGDIVAVA--GLEDINI--GETIADPEVPE 291

                  .
gi 187251827  304 P 304
Cdd:TIGR01394 292 A 292
TypA COG1217
Predicted membrane GTPase involved in stress response [Signal transduction mechanisms]
82-304 1.81e-23

Predicted membrane GTPase involved in stress response [Signal transduction mechanisms]


Pssm-ID: 224138 [Multi-domain]  Cd Length: 603  Bit Score: 101.16  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADY------IKNMItgaaqmDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVfLNKVDLADAELLDLVEmEI 155
Cdd:COG1217   73 VDTPGHADFggeverVLSMV------DGVLLLVDASEGPMPQTRFVLKKALALGLKPIVV-INKIDRPDARPDEVVD-EV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 156 RDLLSKYEFDGD--NTPIIRGSALKAIEGDSSPIGEPSIKALLEALDTWIPEPKRETDKPFLMAVE--DVFSITGRgtVA 231
Cdd:COG1217  145 FDLFVELGATDEqlDFPIVYASARNGTASLDPEDEADDMAPLFETILDHVPAPKGDLDEPLQMQVTqlDYNSYVGR--IG 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 232 TGRIERGVVKVGDTIEIIG-------FRDTMNTVATGIEmfRKLLDQGEAGDNVGVllRGVEKNQIerGQVLAAPKSIKP 304
Cdd:COG1217  223 IGRIFRGTVKPNQQVALIKsdgttenGRITKLLGFLGLE--RIEIEEAEAGDIVAI--AGLEDINI--GDTICDPDNPEA 296
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
63-390 4.03e-22

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: 95.52  E-value: 4.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   63 VTVAVSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL 142
Cdd:TIGR02034  66 ITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  143 A--DAELLDLVEMEIRDLLSKYEFDgDNTPIirgsALKAIEGDSspIGEPSIK-------ALLEALDTWIPEPKREtDKP 213
Cdd:TIGR02034 146 VdyDEEVFENIKKDYLAFAEQLGFR-DVTFI----PLSALKGDN--VVSRSESmpwysgpTLLEILETVEVERDAQ-DLP 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  214 FLMAVEDV---------FSitgrGTVATGRiergvVKVGDTIEIIgfRDTMNTVATGIEMFRKLLDQGEAGDNVGVLLRg 284
Cdd:TIGR02034 218 LRFPVQYVnrpnldfrgYA----GTIASGS-----VHVGDEVVVL--PSGRSSRVARIVTFDGDLEQARAGQAVTLTLD- 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  285 vEKNQIERGQVLAAPKSIKP--------------HTKFKGQVYILKkdeggRHTPLTPGYKPQFYFRtTDVTGELKFAGD 350
Cdd:TIGR02034 286 -DEIDISRGDLLAAADSAPEvadqfaatlvwmaeEPLLPGRSYDLK-----LGTRKVRASVAAIKHK-VDVNTLEKGAAK 358
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 187251827  351 MIMPGDNAEIEVTLITPVAMEE--------GLRFAIREGGRTVGAGVV 390
Cdd:TIGR02034 359 SLELNEIGRVNLSLDEPIAFDPyaenrttgAFILIDRLSNRTVGAGMI 406
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
9-246 2.99e-19

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU [Protein synthesis, Translation factors].


Pssm-ID: 232995 [Multi-domain]  Cd Length: 587  Bit Score: 88.28  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827    9 TKPHVnVGTIGHVDHGKTTLTTALTKVLAKEGKAkemgyadiakGGVVRDaskivtVAVSHVEYEsDKRHYAHIDCPGHA 88
Cdd:TIGR00487  85 ERPPV-VTIMGHVDHGKTSLLDSIRKTKVAQGEA----------GGITQH------IGAYHVENE-DGKMITFLDTPGHE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   89 DYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLADAElLDLVEMEIRDL-LSKYEFDGD 167
Cdd:TIGR00487 147 AFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEAN-PDRVKQELSEYgLVPEDWGGD 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  168 nTPIIRGSALKAIegdsspigepSIKALLEA--LDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDT 245
Cdd:TIGR00487 225 -TIFVPVSALTGD----------GIDELLDMilLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDI 293

                  .
gi 187251827  246 I 246
Cdd:TIGR00487 294 V 294
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
63-299 7.44e-18

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 84.21  E-value: 7.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  63 VTVAVSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL 142
Cdd:PRK05506  90 ITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 143 AD--AELLDLVEMEIRDLLSKYEFdGDNTPIirgsALKAIEGDSspIGEPSIK-------ALLEALDTWIPEPKREtDKP 213
Cdd:PRK05506 170 VDydQEVFDEIVADYRAFAAKLGL-HDVTFI----PISALKGDN--VVTRSARmpwyegpSLLEHLETVEIASDRN-LKD 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDV---------FSitgrGTVATgrierGVVKVGDTIEII--GFRDTMNTVATgiemFRKLLDQGEAGDNVGVLL 282
Cdd:PRK05506 242 FRFPVQYVnrpnldfrgFA----GTVAS-----GVVRPGDEVVVLpsGKTSRVKRIVT----PDGDLDEAFAGQAVTLTL 308
                        250
                 ....*....|....*....
gi 187251827 283 RgvekNQIE--RGQVLAAP 299
Cdd:PRK05506 309 A----DEIDisRGDMLARA 323
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
63-349 3.15e-17

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 81.88  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  63 VTVAVSHVEYESDKRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVFLNKVDL 142
Cdd:PRK05124  93 ITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 143 AD--AELLDLVEMEIRDLLSKYEFDGDntpiIRGSALKAIEGDSspIGEPSIK-------ALLEALDTwIPEPKRETDKP 213
Cdd:PRK05124 173 VDysEEVFERIREDYLTFAEQLPGNLD----IRFVPLSALEGDN--VVSQSESmpwysgpTLLEVLET-VDIQRVVDAQP 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 214 FLMAVEDV---------FSitgrGTVATgrierGVVKVGDTIEII--GFRDTMNTVATgiemFRKLLDQGEAGDNVGVLL 282
Cdd:PRK05124 246 FRFPVQYVnrpnldfrgYA----GTLAS-----GVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL 312
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827 283 rgveKNQIE--RGQVLAAPKSiKPHTKFKGQVYILKKDEggrhTPLTPGykpQFYFrttdvtgeLKFAG 349
Cdd:PRK05124 313 ----EDEIDisRGDLLVAADE-ALQAVQHASADVVWMAE----QPLQPG---QSYD--------IKIAG 361
FusA COG0480
Translation elongation factors (GTPases) [Translation, ribosomal structure and biogenesis]
14-161 5.77e-16

Translation elongation factors (GTPases) [Translation, ribosomal structure and biogenesis]


Pssm-ID: 223556 [Multi-domain]  Cd Length: 697  Bit Score: 78.44  E-value: 5.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGKTTLTTAltkVLAKEGKAKEMGyaDIAKGGVVRDASKI-------VTVAVSHVEYESDKRHYAhIDCPG 86
Cdd:COG0480   12 NIGIVAHIDAGKTTLTER---ILFYTGIISKIG--EVHDGAATMDWMEQeqergitITSAATTLFWKGDYRINL-IDTPG 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187251827  87 HADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKlVVFLNKVDLADAELLDLVEmEIRDLLSK 161
Cdd:COG0480   86 HVDFTIEVERSLRVLDGAVVVVDAVEGVEPQTETVWRQADKYGVPR-ILFVNKMDRLGADFYLVVE-QLKERLGA 158
PRK10218 PRK10218
GTP-binding protein; Provisional
14-280 9.49e-16

GTP-binding protein; Provisional


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 77.83  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGKTTLTTALTKVLAK-----EGKAKEMGYADIAKggvvrdaSKIVTVAVSHVEYESDKRHYAHIDCPGHA 88
Cdd:PRK10218   7 NIAIIAHVDHGKTTLVDKLLQQSGTfdsraETQERVMDSNDLEK-------ERGITILAKNTAIKWNDYRINIVDTPGHA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  89 DYIKNMITGAAQMDGAILVVSAQDGPMPQTReHVLLAKQVNVPKLVVFLNKVDLADAElLDLVEMEIRDLLSKYEFDGD- 167
Cdd:PRK10218  80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTR-FVTKKAFAYGLKPIVVINKVDRPGAR-PDWVVDQVFDLFVNLDATDEq 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 168 -NTPIIRGSALKAIEG-DSSPIGEpSIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDT 245
Cdd:PRK10218 158 lDFPIVYASALNGIAGlDHEDMAE-DMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 187251827 246 IEIIGFR-----DTMNTVATGIEMFRKLLDQGEAGDNVGV 280
Cdd:PRK10218 237 VTIIDSEgktrnAKVGKVLGHLGLERIETDLAEAGDIVAI 276
InfB COG0532
Translation initiation factor 2 (IF-2; GTPase) [Translation, ribosomal structure and ...
19-246 3.29e-15

Translation initiation factor 2 (IF-2; GTPase) [Translation, ribosomal structure and biogenesis]


Pssm-ID: 223606 [Multi-domain]  Cd Length: 509  Bit Score: 75.66  E-value: 3.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  19 GHVDHGkttlttaltkvlakegKAKEMGYadIAKGGVV-RDASKIvT--VAVSHVEYESDKRH-YAHIDCPGHAdYIKNM 94
Cdd:COG0532   12 GHVDHG----------------KTTLLDK--IRKTNVAaGEAGGI-TqhIGAYQVPLDVIKIPgITFIDTPGHE-AFTAM 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  95 IT-GAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLADAELldlvEMEIRDLLSK----YEFDGDnT 169
Cdd:COG0532   72 RArGASVTDIAILVVAADDGVMPQTIEAINHAKAAGVP-IVVAINKIDKPEANP----DKVKQELQEYglvpEEWGGD-V 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827 170 PIIRGSALKAiEGdsspigepsIKALLEA--LDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDTI 246
Cdd:COG0532  146 IFVPVSAKTG-EG---------IDELLELilLLAEVLELKANPEGPARGTVIEVKLDKGLGPVATVIVQDGTLKKGDII 214
infB CHL00189
translation initiation factor 2; Provisional
15-248 1.79e-14

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 73.71  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  15 VGTIGHVDHGKTTlttaltkVLAKEGKA----KEMGyadiakgGVVRdasKIVTVAVShVEYESDKRHYAHIDCPGHADY 90
Cdd:CHL00189 247 VTILGHVDHGKTT-------LLDKIRKTqiaqKEAG-------GITQ---KIGAYEVE-FEYKDENQKIVFLDTPGHEAF 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  91 IKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLADAELldlveMEIRDLLSKYEFD----G 166
Cdd:CHL00189 309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANT-----ERIKQQLAKYNLIpekwG 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 167 DNTPIIRGSALKaiegdsspigEPSIKALLEA------LDTWIPEPKRETDKPFLMAVEDVFsitgRGTVATGRIERGVV 240
Cdd:CHL00189 383 GDTPMIPISASQ----------GTNIDKLLETilllaeIEDLKADPTQLAQGIILEAHLDKT----KGPVATILVQNGTL 448

                 ....*...
gi 187251827 241 KVGDTIEI 248
Cdd:CHL00189 449 HIGDIIVI 456
lepA TIGR01393
GTP-binding protein LepA; LepA (GUF1 in Saccaromyces) is a GTP-binding membrane protein ...
14-287 4.62e-13

GTP-binding protein LepA; LepA (GUF1 in Saccaromyces) is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown [Unknown function, General].


Pssm-ID: 130460 [Multi-domain]  Cd Length: 595  Bit Score: 69.27  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   14 NVGTIGHVDHGKTTLT----TALTKVLAKEGKAKEMGYADIAK--GGVVrdasKIVTVAVSHVEYESDKRHYAHIDCPGH 87
Cdd:TIGR01393   5 NFSIIAHIDHGKSTLAdrllEYTGAISEREMREQVLDSMDLERerGITI----KAQAVRLNYKAKDGETYVLNLIDTPGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   88 ADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVpKLVVFLNKVDLADAElLDLVEMEIRDLLSKyefdgD 167
Cdd:TIGR01393  81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDL-EIIPVINKIDLPSAD-PERVKKEIEEVIGL-----D 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  168 NTPIIRGSAlKAIEGdsspigepsIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVKVGDTIE 247
Cdd:TIGR01393 154 ASEAILASA-KTGIG---------IEEILEAIVKRVPPPKGDPDAPLKALIFDSHYDNYRGVVALVRVFEGTIKPGDKIR 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 187251827  248 IIGFRDTMNTVATGIEMFRKLLDQG-EAGDnVGVLLRGVEK 287
Cdd:TIGR01393 224 FMSTGKEYEVDEVGVFTPKLTKTDElSAGE-VGYIIAGIKD 263
LepA COG0481
Membrane GTPase LepA [Cell envelope biogenesis, outer membrane]
82-246 5.37e-12

Membrane GTPase LepA [Cell envelope biogenesis, outer membrane]


Pssm-ID: 223557 [Multi-domain]  Cd Length: 603  Bit Score: 66.05  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVpKLVVFLNKVDLADAELlDLVEMEIRDLlsk 161
Cdd:COG0481   81 IDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENNL-EIIPVLNKIDLPAADP-ERVKQEIEDI--- 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 162 yeFDGDNTPIIRGSAlKAIEGdsspigepsIKALLEALDTWIPEPKRETDKPFLMAVEDVFSITGRGTVATGRIERGVVK 241
Cdd:COG0481  156 --IGIDASDAVLVSA-KTGIG---------IEDVLEAIVEKIPPPKGDPDAPLKALIFDSWYDNYLGVVVLVRIFDGTLK 223

                 ....*
gi 187251827 242 VGDTI 246
Cdd:COG0481  224 KGDKI 228
infB PRK05306
translation initiation factor IF-2; Validated
82-246 3.81e-11

translation initiation factor IF-2; Validated


Pssm-ID: 235401 [Multi-domain]  Cd Length: 746  Bit Score: 63.33  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYiknmiT-----GAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDLADAElLDLVEMEir 156
Cdd:PRK05306 301 LDTPGHEAF-----TamrarGAQVTDIVVLVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGAN-PDRVKQE-- 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 157 dlLSKY-----EFDGDnTPIIRGSALKaiegdsspiGEpSIKALLEA-------LDtwipepkretdkpfLMAVEDVFSI 224
Cdd:PRK05306 372 --LSEYglvpeEWGGD-TIFVPVSAKT---------GE-GIDELLEAillqaevLE--------------LKANPDRPAR 424
                        170       180       190
                 ....*....|....*....|....*....|.
gi 187251827 225 ---------TGRGTVATGRIERGVVKVGDTI 246
Cdd:PRK05306 425 gtvieakldKGRGPVATVLVQNGTLKVGDIV 455
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
1-156 4.88e-11

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD [Protein synthesis, Translation factors].


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 62.99  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827    1 MAKEKFVRtkphvNVGTIGHVDHGKTTLTTAltkVLAKEGK-AKEMGYADIAKGGVVRDASKIVTVAVSHV----EYESD 75
Cdd:TIGR00490  13 MWKPKFIR-----NIGIVAHIDHGKTTLSDN---LLAGAGMiSEELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   76 KRHYAHIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVpKLVVFLNKVDLADAEL-LDLVEME 154
Cdd:TIGR00490  85 EYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENV-KPVLFINKVDRLINELkLTPQELQ 163

                  ..
gi 187251827  155 IR 156
Cdd:TIGR00490 164 ER 165
PRK12740 PRK12740
elongation factor G; Reviewed
63-160 3.94e-10

elongation factor G; Reviewed


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 60.14  E-value: 3.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  63 VTVAVSHVEYEsDKRHYAhIDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLvVFLNKVDL 142
Cdd:PRK12740  48 ITSAATTCEWK-GHKINL-IDTPGHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMDR 124
                         90
                 ....*....|....*...
gi 187251827 143 ADAELLDLVEmEIRDLLS 160
Cdd:PRK12740 125 AGADFFRVLA-QLQEKLG 141
PRK07560 PRK07560
elongation factor EF-2; Reviewed
14-156 3.34e-09

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 57.18  E-value: 3.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGKTTLT---TALTKVLAKE--GKAKEMGYADI-AKGGVVRDASkivtvAVSHV-EYEsDKRHYAH-IDCP 85
Cdd:PRK07560  22 NIGIIAHIDHGKTTLSdnlLAGAGMISEElaGEQLALDFDEEeQARGITIKAA-----NVSMVhEYE-GKEYLINlIDTP 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187251827  86 GHADYIKNMITGAAQMDGAILVVSAQDGPMPQTrEHVL---LAKQVnvpKLVVFLNKVDLADAEL-LDLVEMEIR 156
Cdd:PRK07560  96 GHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVLrqaLRERV---KPVLFINKVDRLIKELkLTPQEMQQR 166
PRK05433 PRK05433
GTP-binding protein LepA; Provisional
82-246 4.69e-09

GTP-binding protein LepA; Provisional


Pssm-ID: 235462 [Multi-domain]  Cd Length: 600  Bit Score: 56.58  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVpKLVVFLNKVDLADAELlDLVEMEIRDLLSk 161
Cdd:PRK05433  79 IDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDL-EIIPVLNKIDLPAADP-ERVKQEIEDVIG- 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 162 yeFDGDNtpIIRGSAlKAIEGdsspigepsIKALLEALDTWIPEPKRETDKPfLMA-----VEDVFsitgRGTVATGRIE 236
Cdd:PRK05433 156 --IDASD--AVLVSA-KTGIG---------IEEVLEAIVERIPPPKGDPDAP-LKAlifdsWYDNY----RGVVVLVRVV 216
                        170
                 ....*....|
gi 187251827 237 RGVVKVGDTI 246
Cdd:PRK05433 217 DGTLKKGDKI 226
PRK13351 PRK13351
elongation factor G; Reviewed
14-161 1.29e-08

elongation factor G; Reviewed


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 55.34  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  14 NVGTIGHVDHGkttLTTALTKVLAKEGKAKEMGyaDIAKGGVV-------RDASKIVTVAVSHVEYesDKRHYAHIDCPG 86
Cdd:PRK13351  10 NIGILAHIDAG---KTTLTERILFYTGKIHKMG--EVEDGTTVtdwmpqeQERGITIESAATSCDW--DNHRINLIDTPG 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187251827  87 HADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLvVFLNKVDLADAELLDLVEmEIRDLLSK 161
Cdd:PRK13351  83 HIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMDRVGADLFKVLE-DIEERFGK 155
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-147 8.24e-06

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 46.58  E-value: 8.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRtkphvNVGTIGHVDHGkttLTTALTKVLAKEG--KAKEMGYA-------DIAKGGVVrdaskIVTVAVS--- 68
Cdd:PTZ00416  13 MDNPDQIR-----NMSVIAHVDHG---KSTLTDSLVCKAGiiSSKNAGDArftdtraDEQERGIT-----IKSTGISlyy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  69 --HVEYESDKRHYA--HIDCPGHADYiKNMITGAAQM-DGAILVVSAQDGPMPQTrEHVL---LAKQVnvpKLVVFLNKV 140
Cdd:PTZ00416  80 ehDLEDGDDKQPFLinLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI---RPVLFINKV 154

                 ....*..
gi 187251827 141 DLADAEL 147
Cdd:PTZ00416 155 DRAILEL 161
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
14-159 3.16e-05

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G [Protein synthesis, Translation factors].


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 44.80  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   14 NVGTIGHVDHGkttLTTALTKVLAKEGKAKEMGyaDIAKGGVVRDASK-------IVTVAVSHVEYesdKRHYAH-IDCP 85
Cdd:TIGR00484  12 NIGISAHIDAG---KTTTTERILFYTGRIHKIG--EVHDGAATMDWMEqekergiTITSAATTVFW---KGHRINiIDTP 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187251827   86 GHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPKlVVFLNKVDLADAELLDLVEmEIRDLL 159
Cdd:TIGR00484  84 GHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPR-IAFVNKMDKTGANFLRVVN-QIKQRL 155
PRK12739 PRK12739
elongation factor G; Reviewed
82-159 5.00e-05

elongation factor G; Reviewed


Pssm-ID: 237185 [Multi-domain]  Cd Length: 691  Bit Score: 44.05  E-value: 5.00e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTrEHVL-LAKQVNVPKlVVFLNKVDLADAELLDLVEMeIRDLL 159
Cdd:PRK12739  78 IDTPGHVDFTIEVERSLRVLDGAVAVFDAVSGVEPQS-ETVWrQADKYGVPR-IVFVNKMDRIGADFFRSVEQ-IKDRL 153
PRK09419 PRK09419
bifunctional 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase ...
98-279 1.43e-04

bifunctional 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase precursor protein; Reviewed


Pssm-ID: 236505 [Multi-domain]  Cd Length: 1163  Bit Score: 42.50  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   98 AAQMDGAILVVSAQDgpmpqtreHVLLAKQVNvPKLVV-------FLNKVDLADAELLDLVEMEIRDLLSKYEFDGDNTP 170
Cdd:PRK09419  865 AKKVKGVDAIISAHT--------HTLVDKVVN-GTPVVqaykygrALGRVDVKFDKKGVVVVKTSRIDLSKIDDDLPEDP 935
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  171 IIRgSALKAIEGDSSPIGEPSIKALLEALDTWiPEPKRETDKPFLMAVEDV--------FSITGRGTVATGrIERGVVKV 242
Cdd:PRK09419  936 EMK-EILDKYEKELAPIKNEKVGYTSVDLDGQ-PEHVRTGVSNLGNFIADGmkkivgadIAITNGGGVRAP-IDKGDITV 1012
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 187251827  243 GDTIEIIGFRDTMNTVATGIEMFRKLLDQGEAGDNVG 279
Cdd:PRK09419 1013 GDLYTVMPFGNTLYTMDLTGADIKKALEHGISPVEFG 1049
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
82-142 1.77e-04

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 42.18  E-value: 1.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187251827   82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDL 142
Cdd:PRK14845  531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDL 590
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
82-142 3.80e-04

translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by This model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region [Protein synthesis, Translation factors].


Pssm-ID: 129582 [Multi-domain]  Cd Length: 590  Bit Score: 40.96  E-value: 3.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187251827   82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVDL 142
Cdd:TIGR00491  74 IDTPGHEAFTNLRKRGGALADLAILIVDINEGFKPQTQEALNILRMYKTP-FVVAANKIDR 133
prfC TIGR00503
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ...
82-156 5.27e-04

peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally described as stop codon-independent, in contrast to peptide chain release factor 1 (RF-1, prfA) and RF-2 (prfB). RF-1 and RF-2 are closely related to each other, while RF-3 is similar to elongation factors EF-Tu and EF-G; RF-1 is active at UAA and UAG and RF-2 is active at UAA and UGA. More recently, RF-3 was shown to be active primarily at UGA stop codons in E. coli. All bacteria and organelles have RF-1. The Mycoplasmas and organelles, which translate UGA as Trp rather than as a stop codon, lack RF-2. RF-3, in contrast, seems to be rare among bacteria and is found so far only in Escherichia coli and some other gamma subdivision Proteobacteria, in Synechocystis PCC6803, and in Staphylococcus aureus [Protein synthesis, Translation factors].


Pssm-ID: 129594 [Multi-domain]  Cd Length: 527  Bit Score: 40.66  E-value: 5.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187251827   82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVD---LADAELLDLVEMEIR 156
Cdd:TIGR00503  85 LDTPGHEDFSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTP-IFTFMNKLDrdiRDPLELLDEVENELK 161
PRK04004 PRK04004
translation initiation factor IF-2; Validated
82-141 9.50e-04

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 39.78  E-value: 9.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPGHADYIKNMITGAAQMDGAILVVSAQDGPMPQTREHVLLAKQVNVPkLVVFLNKVD 141
Cdd:PRK04004  76 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
era PRK00089
GTPase Era; Reviewed
102-217 3.32e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 37.72  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827 102 DGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVfLNKVDLAD--AELLDLVEmeirDLLSKYEFDgdntPIIRGSALKA 179
Cdd:PRK00089  86 DLVLFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKdkEELLPLLE----ELSELMDFA----EIVPISALKG 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 187251827 180 IegdsspigepSIKALLEALDTWIPE-----PKRE-TDKP--FLMA 217
Cdd:PRK00089 157 D----------NVDELLDVIAKYLPEgppyyPEDQiTDRPerFLAA 192
Era COG1159
GTPase [General function prediction only]
82-217 3.48e-03

GTPase [General function prediction only]


Pssm-ID: 224081 [Multi-domain]  Cd Length: 298  Bit Score: 37.56  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  82 IDCPG-----HA--DYIKNMITGAAQ-MDGAILVVSAQDGPMPQTREHVLLAKQVNVPKLVVfLNKVDLA--DAELLDLV 151
Cdd:COG1159   59 VDTPGihkpkHAlgELMNKAARSALKdVDLILFVVDADEGWGPGDEFILEQLKKTKTPVILV-VNKIDKVkpKTVLLKLI 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187251827 152 EmeirdllsKYEFDGDNTPIIRGSALKAIegdsspigepSIKALLEALDTWIPE-----PKRE-TDKP--FLMA 217
Cdd:COG1159  138 A--------FLKKLLPFKEIVPISALKGD----------NVDTLLEIIKEYLPEgpwyyPEDQiTDRPerFLAA 193
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
1-147 9.11e-03

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 37.01  E-value: 9.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827   1 MAKEKFVRtkphvNVGTIGHVDHGKTTLT---TALTKVLAKE--GKAKEMGY-ADIAKGGVVRDASKI------VTVAVS 68
Cdd:PLN00116  13 MDKKHNIR-----NMSVIAHVDHGKSTLTdslVAAAGIIAQEvaGDVRMTDTrADEAERGITIKSTGIslyyemTDESLK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187251827  69 HVEYESDKRHYA--HIDCPGHADYiKNMITGAAQM-DGAILVVSAQDGPMPQTrEHVL---LAKQVnvpKLVVFLNKVDL 142
Cdd:PLN00116  88 DFKGERDGNEYLinLIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI---RPVLTVNKMDR 162

                 ....*
gi 187251827 143 ADAEL 147
Cdd:PLN00116 163 CFLEL 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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