|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
1-432 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 840.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 1 MSQKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFE 80
Cdd:PRK12317 1 AKEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 81 TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagMSVEGQTREHIILAKTMGLDQLIVAVNKMDLTEpp 160
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDA-----GGVMPQTREHVFLARTLGINQLIVAINKMDAVN-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 161 YDEKRYKEIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDV 240
Cdd:PRK12317 154 YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 241 YSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHPNNPP 320
Cdd:PRK12317 234 YSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 321 TVADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEK 400
Cdd:PRK12317 314 TVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEK 393
|
410 420 430
....*....|....*....|....*....|..
1JNY_A 401 YNEFPPLGRFAMRDMGKTVGVGIIVDVKPAKV 432
Cdd:PRK12317 394 VKEIPQLGRFAIRDMGQTIAAGMVIDVKPAKV 425
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-431 |
0e+00 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 830.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 1 MSQKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFE 80
Cdd:COG5256 2 ASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 81 TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEpp 160
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDAVN-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 161 YDEKRYKEIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDV 240
Cdd:COG5256 153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 241 YSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHPNNPP 320
Cdd:COG5256 233 YSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 321 TVADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEK 400
Cdd:COG5256 313 TVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEK 392
|
410 420 430
....*....|....*....|....*....|.
1JNY_A 401 YNEFPPLGRFAMRDMGKTVGVGIIVDVKPAK 431
Cdd:COG5256 393 FKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
3-431 |
0e+00 |
|
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: 605.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFETK 82
Cdd:TIGR00483 4 EKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEppYD 162
Cdd:TIGR00483 84 KYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN--YD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 163 EKRYKEIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDVYS 242
Cdd:TIGR00483 158 EEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQDVYS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 243 ISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHPNNPPTV 322
Cdd:TIGR00483 238 ITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDNPPKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 323 ADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEKYN 402
Cdd:TIGR00483 318 AKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVK 397
|
410 420
....*....|....*....|....*....
1JNY_A 403 EFPPLGRFAMRDMGKTVGVGIIVDVKPAK 431
Cdd:TIGR00483 398 EIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
3-429 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 600.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFETK 82
Cdd:PTZ00141 4 EKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEAGMSVEGQTREHIILAKTMGLDQLIVAVNKMDLTEPPYD 162
Cdd:PTZ00141 84 KYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 163 EKRYKEIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDVYS 242
Cdd:PTZ00141 164 QERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 243 ISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHP-NNPPT 321
Cdd:PTZ00141 244 IGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSkNDPAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 322 VADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEKY 401
Cdd:PTZ00141 324 ECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVF 403
|
410 420
....*....|....*....|....*...
1JNY_A 402 NEFPPLGRFAMRDMGKTVGVGIIVDVKP 429
Cdd:PTZ00141 404 NEYPPLGRFAVRDMKQTVAVGVIKSVEK 431
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
3-428 |
4.95e-164 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 469.19 E-value: 4.95e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFETK 82
Cdd:PLN00043 4 EKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEAGMSVEGQTREHIILAKTMGLDQLIVAVNKMDLTEPPYD 162
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 163 EKRYKEIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDVYS 242
Cdd:PLN00043 164 KARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 243 ISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHP-NNPPT 321
Cdd:PLN00043 244 IGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSkDDPAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 322 VADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEKY 401
Cdd:PLN00043 324 EAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETF 403
|
410 420
....*....|....*....|....*..
1JNY_A 402 NEFPPLGRFAMRDMGKTVGVGIIVDVK 428
Cdd:PLN00043 404 SEYPPLGRFAVRDMRQTVAVGVIKSVE 430
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
8-226 |
4.06e-136 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 389.16 E-value: 4.06e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEAGMSVEGQTREHIILAKTMGLDQLIVAVNKMDLTEPPYDEKRYK 167
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1JNY_A 168 EIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPP 226
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
2-427 |
3.03e-128 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 377.12 E-value: 3.03e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 2 SQKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFET 81
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 82 KKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEppY 161
Cdd:COG2895 93 PKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKG-------VLEQTRRHSYIASLLGIRHVVVAVNKMDLVD--Y 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 162 DEKRYKEIVDQVSKFMRSYGFNTnkVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDVY 241
Cdd:COG2895 164 SEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 242 ----SISGVgtvpVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGF----NVrgvekkDIKRGDVV 313
Cdd:COG2895 242 rpnlDFRGY----AGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtledEI------DISRGDVI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 314 GHPNNPPTVADEFTARIivVW-HPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPqfLKQGDVAIVKFKP 392
Cdd:COG2895 312 VAADAPPEVADQFEATL--VWmDEEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAADS--LELNDIGRVTLRL 387
|
410 420 430
....*....|....*....|....*....|....*..
1JNY_A 393 IKPLCVEKYNEFPPLGRFAM--RDMGKTVGVGIIVDV 427
Cdd:COG2895 388 AEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGA 424
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
7-424 |
1.87e-90 |
|
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: 279.64 E-value: 1.87e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 7 LNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEK--FAFLLDRLKEERERGVTINLTFMRFETKKY 84
Cdd:TIGR02034 1 LRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEidLALLVDGLQAEREQGITIDVAYRYFSTDKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 85 FFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEppYDEK 164
Cdd:TIGR02034 81 KFIVADTPGHEQYTRNMATGASTADLAVLLVDARKG-------VLEQTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 165 RYKEIVDQVSKFMRSYGFNTnkVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDV---- 240
Cdd:TIGR02034 152 VFENIKKDYLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVnrpn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 241 -----YSisgvgtvpvGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIgfNVRGVEKKDIKRGDVVGH 315
Cdd:TIGR02034 230 ldfrgYA---------GTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAV--TLTLDDEIDISRGDLLAA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 316 PNNPPTVADEFTARIivVW-HPTALANGYTPVLHVHTASVACRVSELVSKLDPRTG-QEAEKNpqfLKQGDVAIVKFKPI 393
Cdd:TIGR02034 299 ADSAPEVADQFAATL--VWmAEEPLLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLeKGAAKS---LELNEIGRVNLSLD 373
|
410 420 430
....*....|....*....|....*....|...
1JNY_A 394 KPLCVEKYNEFPPLGRFAM--RDMGKTVGVGII 424
Cdd:TIGR02034 374 EPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
3-426 |
1.27e-87 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 279.12 E-value: 1.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEK--FAFLLDRLKEERERGVTINLTFMRFE 80
Cdd:PRK05506 21 RKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQGDEidLALLVDGLAAEREQGITIDVAYRYFA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 81 TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEpp 160
Cdd:PRK05506 101 TPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKG-------VLTQTRRHSFIASLLGIRHVVLAVNKMDLVD-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 161 YDEKRYKEIVDQVSKFMRSYGFNTnkVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDV 240
Cdd:PRK05506 172 YDQEVFDEIVADYRAFAAKLGLHD--VTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 241 ---------YSisgvgtvpvGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIgfNVRGVEKKDIKRGD 311
Cdd:PRK05506 250 nrpnldfrgFA---------GTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV--TLTLADEIDISRGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 312 VVGHPNNPPTVADEFTAriIVVW-HPTALANGYTPVLHVHTASVACRVSELVSKLDPRTgQEAEKNPQfLKQGDVAIVKF 390
Cdd:PRK05506 319 MLARADNRPEVADQFDA--TVVWmAEEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNT-LERLAAKT-LELNEIGRCNL 394
|
410 420 430
....*....|....*....|....*....|....*...
1JNY_A 391 KPIKPLCVEKYNEFPPLGRFAM--RDMGKTVGVGIIVD 426
Cdd:PRK05506 395 STDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIDF 432
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
3-426 |
7.33e-84 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 264.85 E-value: 7.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKKLGKESEK--FAFLLDRLKEERERGVTINLTFMRFE 80
Cdd:PRK05124 24 HKSLLRFLTCGSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 81 TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEpp 160
Cdd:PRK05124 104 TEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKG-------VLDQTRRHSFIATLLGIKHLVVAVNKMDLVD-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 161 YDEKRYKEIVDQVSKFMRSYGFNTNkVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDV 240
Cdd:PRK05124 175 YSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 241 ---------YSisgvgtvpvGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRgvEKKDIKRGD 311
Cdd:PRK05124 254 nrpnldfrgYA---------GTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLE--DEIDISRGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 312 VVGHPNNPPTVADEFTARiiVVW-HPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGqeAEKNPQFLKQGDVAIVKF 390
Cdd:PRK05124 323 LLVAADEALQAVQHASAD--VVWmAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTL--TQREAENLPLNGIGLVEL 398
|
410 420 430
....*....|....*....|....*....|....*...
1JNY_A 391 KPIKPLCVEKYNEFPPLGRFAM--RDMGKTVGVGIIVD 426
Cdd:PRK05124 399 TFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
4-427 |
3.97e-79 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 250.07 E-value: 3.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLvgrllmdrgfidekTVKEAEEAAKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKK 83
Cdd:COG0050 10 KPHVNIGTIGHVDHGKTTL--------------TAAITKVLAKKGGAKAKAYD-QIDKAPEEKERGITINTSHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEppyDE 163
Cdd:COG0050 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-------PMPQTREHILLARQVGVPYIVVFLNKCDMVD---DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 164 krykEIVDQVSKFMR----SYGFNTNKvrfVPVVAPSGdnithksenMKWYNGPTLEEYLDQ-LEL----------PPKP 228
Cdd:COG0050 145 ----ELLELVEMEVRellsKYGFPGDD---TPIIRGSA---------LKALEGDPDPEWEKKiLELmdavdsyipePERD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 229 VDKPLRIPIQDVYSISGVGTVPVGRVESGVLKVGDK--IVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKD 306
Cdd:COG0050 209 TDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEveIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKRED 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 307 IKRGDVVGHPN--NPPTvadEFTARIIVV------WHpTALANGYTPVLHVHTASV--ACRVSELVSKLDPrtgqeaekn 376
Cdd:COG0050 289 VERGQVLAKPGsiTPHT---KFEAEVYVLskeeggRH-TPFFNGYRPQFYFRTTDVtgVITLPEGVEMVMP--------- 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
1JNY_A 377 pqflkqGDVAIVKFKPIKPLCVEKynefpplG-RFAMRDMGKTVGVGIIVDV 427
Cdd:COG0050 356 ------GDNVTMTVELITPIAMEE-------GlRFAIREGGRTVGAGVVTKI 394
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
8-226 |
5.43e-78 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 240.93 E-value: 5.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVkEAEEAAKKLGKESEK--FAFLLDRLKEERERGVTINLTFMRFETKKYF 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQL-AALERSKSSGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 86 FTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEppYDEKR 165
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKG-------VLEQTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1JNY_A 166 YKEIVDQVSKFMRSYGFNTnkVRFVPVVAPSGDNITHKSENMKWYNGPTLEEYLDQLELPP 226
Cdd:cd04166 151 FEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIAS 209
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
4-427 |
3.22e-77 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 245.24 E-value: 3.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLvgrllmdrgfidekTVKEAEEAAKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKK 83
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTTL--------------TAAITKVLAERGLNQAKDYD-SIDAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEyeagMSvegQTREHIILAKTMGLDQLIVAVNKMDLTEppyDE 163
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGP----MP---QTREHILLARQVGVPYLVVFLNKVDLVD---DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 164 krykEIVD----QVSKFMRSYGFNTNKvrfVPVVAPS------GDNITHKS--ENMKwyngpTLEEYLDQlelPPKPVDK 231
Cdd:PRK12736 145 ----ELLElvemEVRELLSEYDFPGDD---IPVIRGSalkaleGDPKWEDAimELMD-----AVDEYIPT---PERDTDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 232 PLRIPIQDVYSISGVGTVPVGRVESGVLKVGD--KIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKR 309
Cdd:PRK12736 210 PFLMPVEDVFTITGRGTVVTGRVERGTVKVGDevEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVER 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 310 GDVVGHPN--NPPTvadEFTARIIVV------WHpTALANGYTPVLHVHTASVacrvselvskldprTGQ-EAEKNPQFL 380
Cdd:PRK12736 290 GQVLAKPGsiKPHT---KFKAEVYILtkeeggRH-TPFFNNYRPQFYFRTTDV--------------TGSiELPEGTEMV 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1JNY_A 381 KQGDVAIVKFKPIKPLCVEKynefpplG-RFAMRDMGKTVGVGIIVDV 427
Cdd:PRK12736 352 MPGDNVTITVELIHPIAMEQ-------GlKFAIREGGRTVGAGTVTEI 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-427 |
3.57e-75 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 240.63 E-value: 3.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMdrgfidektvkeaeEAAKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETK 82
Cdd:CHL00071 9 KKPHVNIGTIGHVDHGKTTLTAAITM--------------TLAAKGGAKAKKYD-EIDSAPEEKARGITINTAHVEYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEyeagMSvegQTREHIILAKTMGLDQLIVAVNKMDLTeppyD 162
Cdd:CHL00071 74 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGP----MP---QTKEHILLAKQVGVPNIVVFLNKEDQV----D 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 163 EKRYKEIVD-QVSKFMRSYGFNTNKVRFVP------VVAPSGDNITHKSENmKW----YNgptLEEYLDQ-LELPPKPVD 230
Cdd:CHL00071 143 DEELLELVElEVRELLSKYDFPGDDIPIVSgsallaLEALTENPKIKRGEN-KWvdkiYN---LMDAVDSyIPTPERDTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 231 KPLRIPIQDVYSISGVGTVPVGRVESGVLKVGDK--IVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIK 308
Cdd:CHL00071 219 KPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTveIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 309 RGDVVGHPN--NPPTvadEFTARIIVVW------HpTALANGYTPVLHVHTASVACRVSELVSKldprTGQEAEknpqFL 380
Cdd:CHL00071 299 RGMVLAKPGtiTPHT---KFEAQVYILTkeeggrH-TPFFPGYRPQFYVRTTDVTGKIESFTAD----DGSKTE----MV 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
1JNY_A 381 KQGDVAIVKFKPIKPLCVEKynefpplG-RFAMRDMGKTVGVGIIVDV 427
Cdd:CHL00071 367 MPGDRIKMTVELIYPIAIEK-------GmRFAIREGGRTVGAGVVSKI 407
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
4-427 |
5.19e-74 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 237.01 E-value: 5.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLVGRLLMdrgfidektvkeaeEAAKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKK 83
Cdd:PRK00049 10 KPHVNVGTIGHVDHGKTTLTAAITK--------------VLAKKGGAEAKAYD-QIDKAPEEKARGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTeppyDE 163
Cdd:PRK00049 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADG-------PMPQTREHILLARQVGVPYIVVFLNKCDMV----DD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 164 KRYKEIVD-QVSKFMRSYGFNTNKvrfVPVVAPSGDNITHKSENMKWYngPTLEEYLDQLE----LPPKPVDKPLRIPIQ 238
Cdd:PRK00049 144 EELLELVEmEVRELLSKYDFPGDD---TPIIRGSALKALEGDDDEEWE--KKILELMDAVDsyipTPERAIDKPFLMPIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 239 DVYSISGVGTVPVGRVESGVLKVGDK--IVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHP 316
Cdd:PRK00049 219 DVFSISGRGTVVTGRVERGIIKVGEEveIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 317 N--NPPTvadEFTARIIVV------WHpTALANGYTPVLHVHTASV--ACRVSELVSKLDPrtgqeaeknpqflkqGDVA 386
Cdd:PRK00049 299 GsiTPHT---KFEAEVYVLskeeggRH-TPFFNGYRPQFYFRTTDVtgVIELPEGVEMVMP---------------GDNV 359
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1JNY_A 387 IVKFKPIKPLCVEKynefpplG-RFAMRDMGKTVGVGIIVDV 427
Cdd:PRK00049 360 EMTVELIAPIAMEE-------GlRFAIREGGRTVGAGVVTKI 394
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
4-201 |
2.73e-73 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 227.79 E-value: 2.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEAAKklgkesekfaflLDRLKEERERGVTINLTFMRFETKK 83
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAG------------LDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNKMDLTeppyDE 163
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGV-PIIVFINKMDRV----DG 136
|
170 180 190
....*....|....*....|....*....|....*....
1JNY_A 164 KRYKEIVDQVS-KFMRSYGFNTNKVRFVPVVAPSGDNIT 201
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGVQ 175
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
4-424 |
2.59e-72 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 232.42 E-value: 2.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLVGRLLmdrgfidekTVkeaeeAAKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKK 83
Cdd:PRK12735 10 KPHVNVGTIGHVDHGKTTLTAAIT---------KV-----LAKKGGGEAKAYD-QIDNAPEEKARGITINTSHVEYETAN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEyeagMSvegQTREHIILAKTMGLDQLIVAVNKMDLTeppyDE 163
Cdd:PRK12735 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGP----MP---QTREHILLARQVGVPYIVVFLNKCDMV----DD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 164 KRYKEIVD-QVSKFMRSYGFNTNKvrfVPVVAPSGDNITHKSENMKWYngPTLEEYLDQLE----LPPKPVDKPLRIPIQ 238
Cdd:PRK12735 144 EELLELVEmEVRELLSKYDFPGDD---TPIIRGSALKALEGDDDEEWE--AKILELMDAVDsyipEPERAIDKPFLMPIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 239 DVYSISGVGTVPVGRVESGVLKVGDK--IVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHP 316
Cdd:PRK12735 219 DVFSISGRGTVVTGRVERGIVKVGDEveIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 317 N--NPPTvadEFTARIIVV------WHpTALANGYTPVLHVHTASV--ACRVSELVSKLDPrtgqeaeknpqflkqGDVA 386
Cdd:PRK12735 299 GsiKPHT---KFEAEVYVLskeeggRH-TPFFNGYRPQFYFRTTDVtgTIELPEGVEMVMP---------------GDNV 359
|
410 420 430
....*....|....*....|....*....|....*....
1JNY_A 387 IVKFKPIKPLCVEKynefpplG-RFAMRDMGKTVGVGII 424
Cdd:PRK12735 360 KMTVELIAPIAMEE-------GlRFAIREGGRTVGAGVV 391
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-431 |
3.67e-71 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 235.96 E-value: 3.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 13 GHVDHGKSTLVGRLlmdrgfidekTvkeaeeaakklGKESekfafllDRLKEERERGVTINLTFMRFE-TKKYFFTIIDA 91
Cdd:COG3276 7 GHIDHGKTTLVKAL----------T-----------GIDT-------DRLKEEKKRGITIDLGFAYLPlPDGRRLGFVDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 92 PGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHI-ILaKTMGLDQLIVAVNKMDLTeppyDEKRYKEIV 170
Cdd:COG3276 59 PGHEKFIKNMLAGAGGIDLVLLVVAADEG-------VMPQTREHLaIL-DLLGIKRGIVVLTKADLV----DEEWLELVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 171 DQVSKFMRSYGFNTNKVrfVPVVAPSGDNIthksenmkwyngPTLEEYLDQL--ELPPKPVDKPLRIPIQDVYSISGVGT 248
Cdd:COG3276 127 EEIRELLAGTFLEDAPI--VPVSAVTGEGI------------DELRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 249 VPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHPnNPPTVADEFTA 328
Cdd:COG3276 193 VVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAP-GALRPTDRIDV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 329 RIIVVWH-PTALANGyTPV-LHVHTASVACRVSELvskldprtGQEAeknpqfLKQGDVAIVKFKPIKPLCVEKynefpp 406
Cdd:COG3276 272 RLRLLPSaPRPLKHW-QRVhLHHGTAEVLARVVLL--------DREE------LAPGEEALAQLRLEEPLVAAR------ 330
|
410 420
....*....|....*....|....*...
1JNY_A 407 lG-RFAMRDMG--KTVGVGIIVDVKPAK 431
Cdd:COG3276 331 -GdRFILRDYSprRTIGGGRVLDPNPPK 357
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-427 |
2.36e-68 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 224.88 E-value: 2.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEEaakklgkesekfaflLDRLKEERERGVTINLTFMRFETK 82
Cdd:PLN03126 78 KKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYETE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEagmsvegQTREHIILAKTMGLDQLIVAVNKMDLTEppyD 162
Cdd:PLN03126 143 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD---D 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 163 EKRYKEIVDQVSKFMRSYGFNTNKvrfVPVVAPSG--------DNITHKSENMKWYNgpTLEEYLDQLE----LPPKPVD 230
Cdd:PLN03126 213 EELLELVELEVRELLSSYEFPGDD---IPIISGSAllalealmENPNIKRGDNKWVD--KIYELMDAVDsyipIPQRQTD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 231 KPLRIPIQDVYSISGVGTVPVGRVESGVLKVGD--KIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIK 308
Cdd:PLN03126 288 LPFLLAVEDVFSITGRGTVATGRVERGTVKVGEtvDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 309 RGDVVGHPNNpPTVADEFTARIIVV------WHPTALAnGYTPVLHVHTASVACRVSELVSKLDprtgQEAeknpQFLKQ 382
Cdd:PLN03126 368 RGMVLAKPGS-ITPHTKFEAIVYVLkkeeggRHSPFFA-GYRPQFYMRTTDVTGKVTSIMNDKD----EES----KMVMP 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
1JNY_A 383 GDVAIVKFKPIKPLCVEKYNefpplgRFAMRDMGKTVGVGIIVDV 427
Cdd:PLN03126 438 GDRVKMVVELIVPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
4-427 |
6.54e-67 |
|
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: 218.49 E-value: 6.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLVGRLLMdrgfidektvkeaeeAAKKLGKESEKFAFLLDRLKEERERGVTINLTFMRFETKK 83
Cdd:TIGR00485 10 KPHVNVGTIGHVDHGKTTLTAAITT---------------VLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTeppyDE 163
Cdd:TIGR00485 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDG-------PMPQTREHILLARQVGVPYIVVFLNKCDMV----DD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 164 KRYKEIVD-QVSKFMRSYGF---NTNKVRFVPVVAPSGDNITHKS--ENMKwyngpTLEEYLDQlelPPKPVDKPLRIPI 237
Cdd:TIGR00485 144 EELLELVEmEVRELLSQYDFpgdDTPIIRGSALKALEGDAEWEAKilELMD-----AVDEYIPT---PEREIDKPFLLPI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 238 QDVYSISGVGTVPVGRVESGVLKVGDK--IVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGH 315
Cdd:TIGR00485 216 EDVFSITGRGTVVTGRVERGIIKVGEEveIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 316 PNNpPTVADEFTARIIVVWHP-----TALANGYTPVLHVHTASVACRVSElvskldprtgqeaEKNPQFLKQGDVAIVKF 390
Cdd:TIGR00485 296 PGS-IKPHTKFEAEVYVLSKEeggrhTPFFSGYRPQFYFRTTDVTGTIEL-------------PEGVEMVMPGDNVKMTV 361
|
410 420 430
....*....|....*....|....*....|....*..
1JNY_A 391 KPIKPLCVEKYNefpplgRFAMRDMGKTVGVGIIVDV 427
Cdd:TIGR00485 362 ELISPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
4-427 |
8.31e-67 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 219.70 E-value: 8.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 4 KPHLNLIVIGHVDHGKSTLVGRLlmdrgfidekTVKEAEEAAKKLGKESEkfaflLDRLKEERERGVTINLTFMRFETKK 83
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTLTAAI----------TKVLAEEGKAKAVAFDE-----IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEagmsvegQTREHIILAKTMGLDQLIVAVNKMDLTeppyDE 163
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVV----DD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 164 KRYKEIVD-QVSKFMRSYGFNTNKvrfVPVVAPSG-------DNITHKSENMKWYNGptLEEYLDQlelPPKPVDKPLRI 235
Cdd:PLN03127 193 EELLELVEmELRELLSFYKFPGDE---IPIIRGSAlsalqgtNDEIGKNAILKLMDA--VDEYIPE---PVRVLDKPFLM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 236 PIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRS----IETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGD 311
Cdd:PLN03127 265 PIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPGGPLKTtvtgVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 312 VVGHPNNPPTvADEFTARIIVVWHP-----TALANGYTPVLHVHTASVacrvselvskldprTGQ-EAEKNPQFLKQGDV 385
Cdd:PLN03127 345 VICKPGSIKT-YKKFEAEIYVLTKDeggrhTPFFSNYRPQFYLRTADV--------------TGKvELPEGVKMVMPGDN 409
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1JNY_A 386 AIVKFKPIKPLCVEkynefpPLGRFAMRDMGKTVGVGIIVDV 427
Cdd:PLN03127 410 VTAVFELISPVPLE------PGQRFALREGGRTVGAGVVSKV 445
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
321-424 |
2.75e-57 |
|
Domain III of Elongation Factor 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 model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).
Pssm-ID: 294004 [Multi-domain] Cd Length: 104 Bit Score: 183.55 E-value: 2.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 321 TVADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEK 400
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
1JNY_A 401 YNEFPPLGRFAMRDMGKTVGVGII 424
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
7-389 |
7.40e-54 |
|
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: 188.93 E-value: 7.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 7 LNLIVIGHVDHGKSTLVgrllmdrgfideKTVKEAEEaakklgkesekfafllDRLKEERERGVTINLTFMRFETKKYFF 86
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLL------------KALTGIAA----------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 87 TIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTeppyDEKRY 166
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-------VMTQTGEHLAVLDLLGIPHTIVVITKADRV----NEEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 167 KEIVDQVSKFMRSYGFNTNkVRFVPVVAPSGDNITHksenmkwyngptLEEYLDQL--ELPPKPVDKPLRIPIQDVYSIS 244
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFLKN-AKIFKTSAKTGQGIGE------------LKKELKNLleSLDIKRIQKPLRMAIDRAFKVK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 245 GVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHPNNPPT-VA 323
Cdd:TIGR00475 189 GAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLrVV 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1JNY_A 324 DEFTARI-IVVWHPtalangytpvLHVHTAsvACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVK 389
Cdd:TIGR00475 269 VKFIAEVpLLELQP----------YHIAHG--MSVTTGKISLLDKGIALLTLDAPLILAKGDKLVLR 323
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
229-319 |
1.13e-52 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 171.22 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 229 VDKPLRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIK 308
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
1JNY_A 309 RGDVVGHPNNP 319
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
8-226 |
9.31e-51 |
|
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: 169.40 E-value: 9.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLmdrgfidektvkeaEEAAKKLGKESEKFAFLlDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLL--------------YQTGAIDRRGTRKETFL-DTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNKMDLTeppyDEKRYK 167
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEG-------VEPQTREHLNIALAGGL-PIIVAVNKIDRV----GEEDFD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1JNY_A 168 EIVDQVSKFMRSYGFNTNKVRFVPVVAPSGdnithksenMKWYNGPTLEEYLDQLELPP 226
Cdd:cd00881 134 EVLREIKELLKLIGFTFLKGKDVPIIPISA---------LTGEGIEELLDAIVEHLPPP 183
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
6-427 |
1.14e-49 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 176.28 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 6 HLNLIVIGHVDHGKSTLVGRLLmdrgfidektvkeaeeaakkLGK----ESEKFAFlLDRLKEERERGVTINLTF----- 76
Cdd:COG5258 122 HIVVGVAGHVDHGKSTLVGTLV--------------------TGKlddgNGGTRSF-LDVQPHEVERGLSADLSYavygf 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 77 -------MR-----------FETKKYFFTIIDAPGHRDFVKNMITG--ASQADAAILVVSAKKGeyeagmsVEGQTREHI 136
Cdd:COG5258 181 dddgpvrMKnplrktdrarvVEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDG-------PTHTTREHL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 137 ILAKTMGLdQLIVAVNKMDLteppYDEKRYKEIVDQVSKFMRsygfntnKVRFVPVVAPSGDNITHKSENMKWYNGPTLE 216
Cdd:COG5258 254 GILLAMDL-PVIVAITKIDK----VDDERVEEVEREIENLLR-------IVGRTPLEVESRHDVDAAIEEINGRVVPILK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 217 ------EYLDQLE-----LPPKPV--DKPLRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAG-----KVgEVRS 278
Cdd:COG5258 322 tsavtgEGLDLLDelferLPKRATdeDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKdgsfrEV-EVKS 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 279 IETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVGHPNNPPTVADEFTARIIVVWHPTALANGYTPVLHVHTASVACRV 358
Cdd:COG5258 401 IEMHYHRVDKAEAGRIVGIALKGVEEEELERGMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRF 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1JNY_A 359 SELVSKldprtgqeaeknpqFLKQGDVAIV--KFKpIKPLCVEKYNefpplgRFAMRDmGKTVGVGIIVDV 427
Cdd:COG5258 481 EPIDKG--------------YLLPGDSGRVrlRFK-YRPYYVEEGQ------RFVFRE-GRSKGVGTVTDI 529
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
5-228 |
1.98e-42 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 148.12 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 5 PHLNLIVIGHVDHGKSTLVGRLLMdrgfidektvkeaeEAAKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKKY 84
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITK--------------VLAKKGGAKAKKYD-EIDKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 85 FFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEPPydek 164
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-------PMPQTREHLLLARQVGVPYIVVFLNKADMVDDE---- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1JNY_A 165 rykEIVDQVSKFMR----SYGFNTNKvrfVPVVAPSGDNITHKSENMKWYNgpTLEEYLDQL-ELPPKP 228
Cdd:cd01884 135 ---ELLELVEMEVRellsKYGFDGDD---TPIVRGSALKALEGDDPNKWVD--KILELLDALdSYIPTP 195
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
13-365 |
1.40e-35 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 138.65 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 13 GHVDHGKSTLVGRLlmdrgfidekTVKEAeeaakklgkesekfafllDRLKEERERGVTINLTFMRF-ETKKYFFTIIDA 91
Cdd:PRK10512 7 GHVDHGKTTLLQAI----------TGVNA------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 92 PGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTeppyDEKRYKEIVD 171
Cdd:PRK10512 59 PGHEKFLSNMLAGVGGIDHALLVVACDDG-------VMAQTREHLAILQLTGNPMLTVALTKADRV----DEARIAEVRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 172 QVSKFMRSYGFntNKVRFVPVVAPSGDNIthksenmkwyngPTLEEYLDQLELPPKPVDKPLRIPIQDVYSISGVGTVPV 251
Cdd:PRK10512 128 QVKAVLREYGF--AEAKLFVTAATEGRGI------------DALREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLVVT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 252 GRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRG-VEKKDIKRGD-VVGHPnnPPTVADeftaR 329
Cdd:PRK10512 194 GTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDwLLADA--PPEPFT----R 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
1JNY_A 330 IIVV---------WHPtalangytpvLHVHTAS--VACRVSELVSKL 365
Cdd:PRK10512 268 VIVElqthtpltqWQP----------LHIHHAAshVTGRVSLLEDNL 304
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
13-225 |
1.08e-32 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 121.56 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 13 GHVDHGKSTLVGRLLmdrgfidektvkeaeeaakklGKESekfafllDRLKEERERGVTINLTFMRFETKKYFFT-IIDA 91
Cdd:cd04171 6 GHIDHGKTTLIKALT---------------------GIET-------DRLPEEKKRGITIDLGFAYLDLPDGKRLgFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 92 PGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVAVNKMDLTEPPydekRYKEIVD 171
Cdd:cd04171 58 PGHEKFVKNMLAGAGGIDAVLLVVAADEG-------IMPQTREHLEILELLGIKKGLVVLTKADLVDED----RLELVEE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1JNY_A 172 QVSKFMRSYGFntNKVRFVPVVAPSGDNITHksenmkwyngptLEEYLDQLELP 225
Cdd:cd04171 127 EILELLAGTFL--ADAPIFPVSSVTGEGIEE------------LKNYLDELAEP 166
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
322-427 |
1.13e-32 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. 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: 294003 [Multi-domain] Cd Length: 108 Bit Score: 119.20 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 322 VADEFTARIIVV-WHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCVEK 400
Cdd:cd03704 2 VVTEFEAQIVILdLLKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLET 81
|
90 100
....*....|....*....|....*..
1JNY_A 401 YNEFPPLGRFAMRDMGKTVGVGIIVDV 427
Cdd:cd03704 82 FKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
319-427 |
3.19e-32 |
|
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: 397314 [Multi-domain] Cd Length: 105 Bit Score: 118.14 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 319 PPTVADEFTARIIVVWH-----PTALANGYTPVLHVHTASVACRVSELVSKLDPrtgQEAEKNPQFLKQGDVAIVKFKPI 393
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLDP---GGVSENPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
1JNY_A 394 KPLCVEKYNefpplgRFAMRDMGKTVGVGIIVDV 427
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
3-327 |
8.77e-29 |
|
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: 274720 [Multi-domain] Cd Length: 406 Bit Score: 116.69 E-value: 8.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLLmdrgfidektvkeaeeaakklgkesekfAFLLDRLKEERERGVTINL-----TFM 77
Cdd:TIGR03680 1 RQPEVNIGMVGHVDHGKTTLTKALT----------------------------GVWTDTHSEELKRGISIRLgyadaEIY 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 78 RFETKKYF---------------------FTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEAgmsvegQTREHI 136
Cdd:TIGR03680 53 KCPECDGPecyttepvcpncgsetellrrVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPCPQP------QTKEHL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 137 ILAKTMGLDQLIVAVNKMDLTEPPYDEKRYKEIVdqvsKFMRsyGFNTNKVRFVPVVAPSGDNIThksenmkwyngpTLE 216
Cdd:TIGR03680 127 MALEIIGIKNIVIVQNKIDLVSKEKALENYEEIK----EFVK--GTVAENAPIIPVSALHNANID------------ALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 217 EYL-DQLELPPKPVDKPLRIPIQDVYSISGVGTVPV--------GRVESGVLKVGDKIVFMPA------GKVG------E 275
Cdd:TIGR03680 189 EAIeKFIPTPERDLDKPPLMYVARSFDVNKPGTPPEklkggvigGSLIQGKLKVGDEIEIRPGikvekgGKTKwepiytE 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
1JNY_A 276 VRSIETHHTKMDKAEPGDNIGFNVR---GVEKKDIKRGDVVGHPNNPPTVADEFT 327
Cdd:TIGR03680 269 ITSLRAGGYKVEEARPGGLVGVGTKldpALTKADALAGQVVGKPGTLPPVWESLE 323
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
322-424 |
4.95e-27 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its 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 findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 104.01 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 322 VADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTgqEAEKNPQFLKQGDVAIVKFKPIKPLCVEKY 401
Cdd:cd01513 2 AVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKT--KEKKPPDSLQPGENGTVEVELQKPVVLERG 79
|
90 100
....*....|....*....|...
1JNY_A 402 NEFPPLGRFAMRDMGKTVGVGII 424
Cdd:cd01513 80 KEFPTLGRFALRDGGRTVGAGLI 102
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
319-427 |
6.16e-26 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model 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, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 101.08 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 319 PPTVADEFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNPQFLKQGDVAIVKFKPIKPLCV 398
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
1JNY_A 399 EKYNEFPPLGRFAMRDMGKTVGVGIIVDV 427
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
8-327 |
7.45e-26 |
|
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: 273597 [Multi-domain] Cd Length: 594 Bit Score: 110.08 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKtvkeaeeaakklGKESEKFaflLDRLKEERERGVTI---NLTFMRFETKky 84
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALLKQSGTFRAN------------EAVAERV---MDSNDLERERGITIlakNTAIRYNGTK-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 85 fFTIIDAPGHRDFVKNMITGASQADAAILVVSAkkgeYEAGMSvegQTRehIILAKT--MGLdQLIVAVNKMDlteppYD 162
Cdd:TIGR01394 66 -INIVDTPGHADFGGEVERVLGMVDGVLLLVDA----SEGPMP---QTR--FVLKKAleLGL-KPIVVINKID-----RP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 163 EKRYKEIVDQVSKFMRSYGFNTNKVRFvPVVAPSGDN------ITHKSENMKwyngPTLEEYLDQLELPPKPVDKPLRIP 236
Cdd:TIGR01394 130 SARPDEVVDEVFDLFAELGADDEQLDF-PIVYASGRAgwasldLDDPSDNMA----PLFDAIVRHVPAPKGDLDEPLQML 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 237 IQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPA------GKVGEVRSIE-THHTKMDKAEPGDNIGfnVRGVEkkDIKR 309
Cdd:TIGR01394 205 VTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRdgtienGRISKLLGFEgLERVEIDEAGAGDIVA--VAGLE--DINI 280
|
330 340
....*....|....*....|..
1JNY_A 310 GDVVGHPNNP---PTVA-DEFT 327
Cdd:TIGR01394 281 GETIADPEVPealPTITvDEPT 302
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
12-319 |
1.24e-24 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 106.26 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 12 IGHVDHGKSTLVGRLLMDRGFIDEKTVKEAeeaakklgkesekfafLLDRLKEERERGVTINLTFMRFETK-----KYFF 86
Cdd:COG0481 12 IAHIDHGKSTLADRLLELTGTLSEREMKEQ----------------VLDSMDLERERGITIKAQAVRLNYKakdgeTYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 87 TIIDAPGHRDF---VknmitgaSQADAA----ILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDqLIVAVNKMDL--T 157
Cdd:COG0481 76 NLIDTPGHVDFsyeV-------SRSLAAcegaLLVVDASQG-------VEAQTLANVYLALENDLE-IIPVINKIDLpsA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 158 EPpydEKRYKEIVDQVskfmrsyGFNTNKVrfVPVVAPSGDNIthksenmkwyngptlEEYLDQL--ELPPkPV---DKP 232
Cdd:COG0481 141 DP---ERVKQEIEDII-------GIDASDA--ILVSAKTGIGI---------------EEILEAIveRIPP-PKgdpDAP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 233 LRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIET---HHTKMDKAEPGDnIGFNVRGVEK-KDIK 308
Cdd:COG0481 193 LQALIFDSWYDSYRGVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVGVftpKMTPVDELSAGE-VGYIIAGIKDvRDAR 271
|
330
....*....|.
1JNY_A 309 RGDVVGHPNNP 319
Cdd:COG0481 272 VGDTITLAKNP 282
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-327 |
2.89e-24 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 103.78 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 1 MSQKPHLNLIVIGHVDHGKSTLVGRLlmdrgfIDEKTvkeaeeaakklgkesekfafllDRLKEERERGVTINL-----T 75
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQAL------TGVWT----------------------DRHSEELKRGITIRLgyadaT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 76 FMRFETKK---YFFT------------------IIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEAgmsvegQTRE 134
Cdd:PRK04000 56 IRKCPDCEepeAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 135 HIILAKTMGLDQLIVAVNKMDLTEPPYDEKRYKEIVDQVSkfmrsyGFNTNKVRFVPVVAPSGDNIThksenmkwyngpT 214
Cdd:PRK04000 130 HLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVK------GTVAENAPIIPVSALHKVNID------------A 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 215 LEEYLDQ-LELPPKPVDKPLRIPIQDVYSISGVGTVP---VGRV-----ESGVLKVGDKIVFMPAGKVG----------- 274
Cdd:PRK04000 192 LIEAIEEeIPTPERDLDKPPRMYVARSFDVNKPGTPPeklKGGViggslIQGVLKVGDEIEIRPGIKVEeggktkwepit 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
1JNY_A 275 -EVRSIETHHTKMDKAEPGDNIGFNVR---GVEKKDIKRGDVVGHPNNPPTVADEFT 327
Cdd:PRK04000 272 tKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPPVWESLT 328
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
233-314 |
4.14e-24 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 95.02 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 233 LRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVekKDIKRGDV 312
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTGDT 78
|
..
1JNY_A 313 VG 314
Cdd:cd01342 79 LT 80
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
233-313 |
1.36e-22 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 91.05 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 233 LRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDV 312
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
.
1JNY_A 313 V 313
Cdd:cd03696 81 L 81
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-197 |
1.73e-22 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 94.35 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLvgrllmdrgfidektvkeaeeaAKKLGKESEKFAFllDRLKEERERGVTINLTFMRFETKK---- 83
Cdd:cd01889 2 NVGLLGHVDSGKTSL----------------------AKALSEIASTAAF--DKNPQSQERGITLDLGFSSFEVDKpkhl 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 84 ----------YFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDqLIVAVNK 153
Cdd:cd01889 58 ednenpqienYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLCKP-LIVVLNK 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
1JNY_A 154 MDLteppYDEKRYKEIVDQVSKFMRSYGFNTNK--VRFVPVVAPSG 197
Cdd:cd01889 130 IDL----IPEEERKRKIEKMKKRLQKTLEKTRLkdSPIIPVSAKPG 171
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
8-200 |
5.47e-22 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 92.60 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAeeaakklgkesekfafLLDRLKEERERGVTIN-----LTFMRFETK 82
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMKEQ----------------VLDSMDLERERGITIKaqavrLFYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNKMDLtePPYD 162
Cdd:cd01890 66 EYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-------VEAQTLANFYLALENNL-EIIPVINKIDL--PAAD 135
|
170 180 190
....*....|....*....|....*....|....*....
1JNY_A 163 EKRYK-EIVDqvskfmrSYGFNTNKVrfVPVVAPSGDNI 200
Cdd:cd01890 136 PDRVKqEIED-------VLGLDASEA--ILVSAKTGLGV 165
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
3-327 |
6.45e-22 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 96.83 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 3 QKPHLNLIVIGHVDHGKSTLVGRLlmdrgfidektvkeaeeaakkLGKESekfafllDRLKEERERGVTINL-----TFM 77
Cdd:COG5257 2 KQPEVNIGVVGHVDHGKTTLVQAL---------------------TGVWT-------DRHSEELKRGITIRLgyadaTFY 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 78 RFE--TKKYFFTI-------------------IDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEAgmsvegQTREHI 136
Cdd:COG5257 54 KCPncEPPEAYTTepkcpncgsetellrrvsfVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 137 ILAKTMGLDQLIVAVNKMDLTEPPYDEKRYKEIVDQVSkfmrsyGFNTNKVRFVPVVAPSGDNIthksenmkwynGPTLE 216
Cdd:COG5257 128 MALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVK------GTVAENAPIIPVSAQHKVNI-----------DALIE 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 217 EYLDQLELPPKPVDKPLRIPIQDVYSISGVGTVP------V--GRVESGVLKVGDKIVFMP------AGKVG------EV 276
Cdd:COG5257 191 AIEEEIPTPERDLSKPPRMLVARSFDVNKPGTPPkdlkggVigGSLIQGVLKVGDEIEIRPgikvekGGKTKyepittTV 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
1JNY_A 277 RSIETHHTKMDKAEPGDNIGFNVR---GVEKKDIKRGDVVGHPNNPPTVADEFT 327
Cdd:COG5257 271 VSLRAGGEEVEEAKPGGLVAVGTKldpSLTKSDSLVGSVAGKPGTLPPVLDSLT 324
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
235-317 |
3.37e-21 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 87.19 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 235 IPIQDVYSISGVGTVPVGRVESGVLKVGDK--IVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDV 312
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEveIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
....*
1JNY_A 313 VGHPN 317
Cdd:cd03697 83 LAKPG 87
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
8-327 |
1.07e-20 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 94.70 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGfidekTVKEAEEAAKKLgkesekfaflLDRLKEERERGVTI---NLTFMRFETKky 84
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSG-----TFRENQEVAERV----------MDSNDLERERGITIlakNTAVRYKGVK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 85 fFTIIDAPGHRDF------VKNMitgasqADAAILVVSAkkgeyeagmsVEG---QTRehIILAKT--MGLdQLIVAVNK 153
Cdd:COG1217 71 -INIVDTPGHADFggeverVLSM------VDGVLLLVDA----------FEGpmpQTR--FVLKKAleLGL-KPIVVINK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 154 MDlteppYDEKRYKEIVDQVSKFMRSYGFNTNKVRFvPVVAPSG------DNITHKSENMKwyngPTLEEYLDQLELPPK 227
Cdd:COG1217 131 ID-----RPDARPDEVVDEVFDLFIELGATDEQLDF-PVVYASArngwasLDLDDPGEDLT----PLFDTILEHVPAPEV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 228 PVDKPLRIPIQDV-YSiSGVGTVPVGRVESGVLKVGDKIVFM-PAGKV--GEVRSIETHH----TKMDKAEPGDNIGFNv 299
Cdd:COG1217 201 DPDGPLQMLVTNLdYS-DYVGRIAIGRIFRGTIKKGQQVALIkRDGKVekGKITKLFGFEglerVEVEEAEAGDIVAIA- 278
|
330 340 350
....*....|....*....|....*....|....*...
1JNY_A 300 rGVEKKDIkrGDVVGHPNNP----------PTVADEFT 327
Cdd:COG1217 279 -GIEDINI--GDTICDPENPealppikidePTLSMTFS 313
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
7-200 |
2.39e-20 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 88.48 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 7 LNLIVIGHVDHGKSTLVgrllmdRGFIDEKTVKEAEEAAK----KLG--------KESEKFAFLLDRLKEERERGVTiNL 74
Cdd:cd01888 1 INIGTIGHVAHGKTTLV------KALSGVWTVRHKEELKRnitiKLGyanakiykCPNCGCPRPYDTPECECPGCGG-ET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 75 TFMRFetkkyfFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmSVEGQTREHIILAKTMGLDQLIVAVNKM 154
Cdd:cd01888 74 KLVRH------VSFVDCPGHEILMATMLSGAAVMDGALLLIAANEP------CPQPQTSEHLAALEIMGLKHIIILQNKI 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
1JNY_A 155 DLTEPPYDEKRYKEIVdqvsKFMRsyGFNTNKVRFVPVVAPSGDNI 200
Cdd:cd01888 142 DLVKEEQALENYEQIK----EFVK--GTIAENAPIIPISAQLKYNI 181
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
8-330 |
5.60e-19 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 89.38 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTvkEAEEAakklgkesekfafLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA--ETQER-------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGEYEagmsvegQTREHIILAKTMGLdQLIVAVNKMDltEPpydEKRYK 167
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGL-KPIVVINKVD--RP---GARPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 168 EIVDQVSKFMRSYGFNTNKVRFVPVVAPSGDNITH-KSENMKWYNGPTLEEYLDQLELPPKPVDKPLRIPIQDVYSISGV 246
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGlDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 247 GTVPVGRVESGVLKVGDKIVFMPA------GKVGEVRS-IETHHTKMDKAEPGDNIGFNVRGvekkDIKRGDVVGHPNN- 318
Cdd:PRK10218 219 GVIGIGRIKRGKVKPNQQVTIIDSegktrnAKVGKVLGhLGLERIETDLAEAGDIVAITGLG----ELNISDTVCDTQNv 294
|
330
....*....|....*
1JNY_A 319 ---PPTVADEFTARI 330
Cdd:PRK10218 295 ealPALSVDEPTVSM 309
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
247-314 |
7.21e-19 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 80.39 E-value: 7.21e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1JNY_A 247 GTVPVGRVESGVLKVGDKIVFMPAGK-----VGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGDVVG 314
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
8-208 |
5.98e-18 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 81.49 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGfidekTVKEAEEAAKKlgkesekfafLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSG-----TFRENEEVGER----------VMDSNDLERERGITILAKNTAITYKDTKIN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTRehIILAKTM--GLdQLIVAVNKMDlteppYDEKR 165
Cdd:cd01891 69 IIDTPGHADFGGEVERVLSMVDGVLLLVDASEG-------PMPQTR--FVLKKALeaGL-KPIVVINKID-----RPDAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1JNY_A 166 YKEIVDQVSKFMRSYGFNTNKVRFvPVVAPSG------DNITHKSENMK 208
Cdd:cd01891 134 PEEVVDEVFDLFLELNATDEQLDF-PIVYASAkngwasLNLDDPSEDLD 181
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
8-174 |
1.57e-17 |
|
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: 81.51 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEktvkeaeeaakkLGKESEKFAFLlDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRE------------LGSVDKGTTRT-DSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTRehiILAKTmgLDQL----IVAVNKMDlTEPPYDE 163
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRL--LRKLniptIIFVNKID-RAGADLE 134
|
170
....*....|.
1JNY_A 164 KRYKEIVDQVS 174
Cdd:cd04168 135 KVYQEIKEKLS 145
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
8-209 |
1.62e-17 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 80.78 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDrgfidekTVKEaeeaaKKLGKESEKFAFLLDRLKEERERGVTINLTFMRF-----ETK 82
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ-------THKR-----TPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLvledsKGK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAkkgeyeagmsVEG---QTREHIILAKTMGLdQLIVAVNKMD---- 155
Cdd:cd04167 70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDV----------VEGltsVTERLIRHAIQEGL-PMVLVINKIDrlil 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1JNY_A 156 -LTEPPYDEKR-YKEIVDQVSKFMRSYGFNTNkvrfvPVVAPSGDNITHKSENMKW 209
Cdd:cd04167 139 eLKLPPTDAYYkLRHTIDEINNYIASFSTTEG-----FLVSPELGNVLFASSKFGF 189
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
232-312 |
2.39e-17 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 76.37 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 232 PLRIPIQDVYSisGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGD 311
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
1JNY_A 312 V 312
Cdd:cd04089 79 V 79
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
11-200 |
2.77e-17 |
|
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: 79.05 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLVGRLlmdrgfidEKTVKEAEEAakklgkesekfaflldrlkeereRGVT--INLTFMRFETKKYFFTI 88
Cdd:cd01887 5 VMGHVDHGKTTLLDKI--------RKTNVAAGEA-----------------------GGITqhIGAYQVPIDVKIPGITF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 89 IDAPGHRDFvKNMIT-GASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGlDQLIVAVNKMDLtePPYDEkryk 167
Cdd:cd01887 54 IDTPGHEAF-TNMRArGASVTDIAILVVAADDG-------VMPQTIEAINHAKAAN-VPIIVAINKIDK--PYGTE---- 118
|
170 180 190
....*....|....*....|....*....|....*..
1JNY_A 168 EIVDQVSKFMRSYGF----NTNKVRFVPVVAPSGDNI 200
Cdd:cd01887 119 ADPERVKNELSELGLvgeeWGGDVSIVPISAKTGEGI 155
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
1-325 |
4.83e-16 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 79.66 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 1 MSQKPHLNLIVIGHVDHGKSTLVgrllmdRGFIDEKTVkeaeeaakklgkesekfaflldRLKEERERGVTINLTFMRFE 80
Cdd:PTZ00327 29 ISRQATINIGTIGHVAHGKSTVV------KALSGVKTV----------------------RFKREKVRNITIKLGYANAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 81 ---------------------------------TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKkgeyeagMS 127
Cdd:PTZ00327 81 iykcpkcprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAAN-------ES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 128 V-EGQTREHIILAKTMGLDQLIVAVNKMDLTEPPYDEKRYKEIVDQVSkfmrsyGFNTNKVRFVPVVAPSGdnithksen 206
Cdd:PTZ00327 154 CpQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVK------GTIADNAPIIPISAQLK--------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 207 mkwYNGPTLEEYL--------DQLELPPK-------PVDKPLripiQDVYSISgvGTVPVGRVESGVLKVGDKIVFMP-- 269
Cdd:PTZ00327 219 ---YNIDVVLEYIctqipipkRDLTSPPRmivirsfDVNKPG----EDIENLK--GGVAGGSILQGVLKVGDEIEIRPgi 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 270 -----AGKV------GEVRSIETHHTKMDKAEPGDNIGFNVR---GVEKKDIKRGDVVGHPNNPPTVADE 325
Cdd:PTZ00327 290 iskdsGGEFtcrpirTRIVSLFAENNELQYAVPGGLIGVGTTidpTLTRADRLVGQVLGYPGKLPEVYAE 359
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
12-155 |
5.15e-16 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 80.17 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 12 IGHVDHGKSTLVGRLLMDRGFIDektvkeaeeaakKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKKYFFTIIDA 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIH------------RIGEVEDGTT-TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
1JNY_A 92 PGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVaVNKMD 155
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTETVWRQAEKYGVPRIIF-VNKMD 123
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
8-180 |
1.14e-15 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 75.73 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVkeaeeaakklGKesekfAFLLDRLKEERERGVTINLT--FMRFET---- 81
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIISEKLA----------GK-----ARYLDTREDEQERGITIKSSaiSLYFEYeeek 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 82 ---KKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAkkgeyeagmsVEG---QTreHIILAKTMGlDQL--IVAVNK 153
Cdd:cd01885 67 mdgNDYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----------VEGvcvQT--ETVLRQALE-ERVkpVLVINK 133
|
170 180 190
....*....|....*....|....*....|...
1JNY_A 154 MD-----LTEPPYD-EKRYKEIVDQVSKFMRSY 180
Cdd:cd01885 134 IDrlileLKLSPEEaYQRLLRIVEDVNAIIETY 166
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
11-155 |
1.28e-15 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 76.48 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLVGRLLMDRGFIDEK-TVKeaeeaakklGKESEKFAfLLDRLKEERERGVTINLTFMRFETKKYFFTII 89
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAIQEAgAVK---------ARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1JNY_A 90 DAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNKMD 155
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-------VEPQTRKLFEVCRLRGI-PIITFINKLD 134
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
232-313 |
2.97e-15 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 70.62 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 232 PLRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGD 311
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
..
1JNY_A 312 VV 313
Cdd:cd16267 81 IL 82
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
8-155 |
3.21e-15 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 77.78 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDektvkeaeeaakKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIH------------RIGEVHDGNT-VMDWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQT----REhiilaktmgLDQL----IVAVNKMD 155
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQTetvwRQ---------ADKYgvprIVFVNKMD 137
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
8-234 |
5.43e-15 |
|
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: 74.55 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDektvkeaeeaakKLGKeSEKFAFLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAID------------RLGR-VEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVaVNKMD------------ 155
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMDraradfdktlaa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 156 LTE-----------PPYDEKRYKEIVDQVSkfMRSYGFNTNKVRFVPVVAPS------------GDNITHKSENMkwyng 212
Cdd:cd04170 140 LREafgrpvvpiqlPIGEGDEFTGVVDLLS--EKAYRYDPGEPSVEIEIPEElkekvaeareelLEAVAETDEEL----- 212
|
250 260
....*....|....*....|..
1JNY_A 213 ptLEEYLDQLELPPKPVDKPLR 234
Cdd:cd04170 213 --MEKYLEEGELTEEELRAGLR 232
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
233-312 |
3.79e-13 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 64.51 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 233 LRIPIQDVY----SISGVgtvpVGRVESGVLKVGDKIVFMPAGKVGEVRSIETHHTKMDKAEPGDNIGfnVRGVEKKDIK 308
Cdd:cd03695 1 FRFPVQYVNrpnlDFRGY----AGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVT--LTLEDEIDVS 74
|
....
1JNY_A 309 RGDV 312
Cdd:cd03695 75 RGDL 78
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
8-322 |
4.41e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 71.14 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLmdrgFIDEKTvkeaeeaaKKLGkESEKFAFLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIL----FYTGKI--------HKMG-EVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLDQLIVaVNKMD------------ 155
Cdd:PRK13351 77 LIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-------VQPQTETVWRQADRYGIPRLIF-INKMDrvgadlfkvled 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 156 -----------LTEPPYDEKRYKEIVDQVskFMRSYGFNTNKVRFVPVVAPSGDNITHKSENMKW--------YNGPTLE 216
Cdd:PRK13351 149 ieerfgkrplpLQLPIGSEDGFEGVVDLI--TEPELHFSEGDGGSTVEEGPIPEELLEEVEEAREkliealaeFDDELLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 217 EYLDQLELP------------------------------------------PKPVDKPLRIPIQD--------------- 239
Cdd:PRK13351 227 LYLEGEELSaeqlraplregtrsghlvpvlfgsalknigieplldavvdylPSPLEVPPPRGSKDngkpvkvdpdpekpl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 240 ------VYSISGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSI---ETH-HTKMDKAEPGDnIGfNVRGVekKDIKR 309
Cdd:PRK13351 307 lalvfkVQYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLfrlQGNkREEVDRAKAGD-IV-AVAGL--KELET 382
|
410
....*....|...
1JNY_A 310 GDVVGHPNNPPTV 322
Cdd:PRK13351 383 GDTLHDSADPVLL 395
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
8-181 |
8.26e-13 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 70.28 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTvkeaeeAAKKLGkesekfaflLDRLKEERERGVTIN-----LTFmRFETK 82
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL------AGEQLA---------LDFDEEEQARGITIKaanvsMVH-EYEGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 83 KYFFTIIDAPGHRDFvKNMITGASQA-DAAILVVSAkkgeyeagmsVEG---QT--------REHIilaktmgldQLIVA 150
Cdd:PRK07560 86 EYLINLIDTPGHVDF-GGDVTRAMRAvDGAIVVVDA----------VEGvmpQTetvlrqalRERV---------KPVLF 145
|
170 180 190
....*....|....*....|....*....|....*..
1JNY_A 151 VNKMD-----LTEPPYD-EKRYKEIVDQVSKFMRSYG 181
Cdd:PRK07560 146 INKVDrlikeLKLTPQEmQQRLLKIIKDVNKLIKGMA 182
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
237-313 |
3.27e-11 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 59.16 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 237 IQDVYSISGVGTVPVGRVESGVLKVGDKIVFMPAgKVGE-----VRSIETHHTKMDKAEPGDNIGFNVRGVEKKDIKRGD 311
Cdd:cd03694 5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPD-ADGKfrpvtVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGM 83
|
..
1JNY_A 312 VV 313
Cdd:cd03694 84 VL 85
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
8-120 |
1.83e-10 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 63.14 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIdektvkeaeeAAKKLGKesekfAFLLDRLKEERERGVTINLT--FMRFE----- 80
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTDSLVCKAGII----------SSKNAGD-----ARFTDTRADEQERGITIKSTgiSLYYEhdled 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
1JNY_A 81 ---TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKG 120
Cdd:PTZ00416 86 gddKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEG 128
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
232-312 |
2.18e-10 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 56.74 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 232 PLRIPIQDVYSiSGVGTVPVGRVESGVLKVGDKIVFMPAGKVGEVRSIETH-HTKMDKAEPGDNIGFNVRGVEKKDIKRG 310
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
..
1JNY_A 311 DV 312
Cdd:cd03698 80 DI 81
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-155 |
1.76e-09 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 60.12 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 1 MSQKPHL-NLIVIGHVDHGKSTLVGRLLMDRGFIDEKTVKEAEeaakklgkesekfafLLDRLKEERERGVTINLT--FM 77
Cdd:PLN00116 13 MDKKHNIrNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVR---------------MTDTRADEAERGITIKSTgiSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 78 RFE--------------TKKYFFTIIDAPGHRDFVKNMITGASQADAAILVVSAKKgeyeaGMSVEGQTrehiILAKTMG 143
Cdd:PLN00116 78 YYEmtdeslkdfkgerdGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIE-----GVCVQTET----VLRQALG 148
|
170
....*....|...
1JNY_A 144 LD-QLIVAVNKMD 155
Cdd:PLN00116 149 ERiRPVLTVNKMD 161
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
321-424 |
2.67e-09 |
|
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III 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 sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N- and C-termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 294010 [Multi-domain] Cd Length: 103 Bit Score: 54.36 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 321 TVADEFTARIivVW-HPTALANGYTPVLHVHTASVACRVSELVSKLDPRTGQEAEKNpqFLKQGDVAIVKFKPIKPLCVE 399
Cdd:cd04095 1 EVSDQFEATL--VWmDEKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLEREPAD--TLALNDIGRVTLRLAEPLAFD 76
|
90 100
....*....|....*....|....*..
1JNY_A 400 KYNEFPPLGRFAM--RDMGKTVGVGII 424
Cdd:cd04095 77 PYAENRATGSFILidRLTNATVAAGMI 103
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-202 |
3.15e-09 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 55.54 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLVGRLLmdrgfidektvkeaeeaakklGKEsekfaflldRLKEERERGVTINLTF--MRFETKKYFFTI 88
Cdd:cd00882 2 VVGRGGVGKSSLLNALL---------------------GGE---------VGEVSDVPGTTRDPDVyvKELDKGKVKLVL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 89 IDAPGHRDFVKNMITG-----ASQADAAILVVSAKKGEYEagmsvEGQTREHIILAKTMGLDqLIVAVNKMDLTEPpyDE 163
Cdd:cd00882 52 VDTPGLDEFGGLGREElarllLRGADLILLVVDSTDRESE-----EDAKLLILRRLRKEGIP-IILVGNKIDLLEE--RE 123
|
170 180 190
....*....|....*....|....*....|....*....
1JNY_A 164 KRYKEIVDQVSKFmrsygfntNKVRFVPVVAPSGDNITH 202
Cdd:cd00882 124 VEELLRLEELAKI--------LGVPVFEVSAKTGEGVDE 154
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
11-268 |
1.14e-08 |
|
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: 273104 [Multi-domain] Cd Length: 591 Bit Score: 57.13 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLVGRLlmdRGFIDEKtvKEAEEAAKKLGKeSEKFAFLLDRLKEERERGVTINLTFmrfetKKYFFtiID 90
Cdd:TIGR00491 9 VLGHVDHGKTTLLDKI---RGTAVVK--KEAGGITQHIGA-SEVPTDVIEKICGDLLKSFKIKLKI-----PGLLF--ID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 91 APGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNKMDLT-------EPPY-- 161
Cdd:TIGR00491 76 TPGHEAFTNLRKRGGALADIAILVVDINEG-------FKPQTLEALNILRSRKT-PFVVAANKIDRIpgwksheGYPFle 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 162 -------------DEKRYKEIVD------QVSKFMRSYGFnTNKVRFVPVVAPSGDNIthkSENMKWYNGPTLEEYLDQL 222
Cdd:TIGR00491 148 sinkqeqrvrqnlDKQVYNLVIQlaeqgfNAERFDRIRDF-TKTVAIIPVSAKTGEGI---PELLAILAGLAQNYLENKL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
1JNY_A 223 ELppkPVDKPLRIPIQDVYSISGVGTVPVGRVESGVLKVGDKIVFM 268
Cdd:TIGR00491 224 KL---AIEGPAKGTILEVKEEQGLGYTIDAVIYDGILRKGDIIVLA 266
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-201 |
1.63e-08 |
|
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: 272973 [Multi-domain] Cd Length: 162 Bit Score: 53.53 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIDektvkeaeeaakklgkESEKFAFLLDRLKEERERGvtinltfmrfetKKYFFT 87
Cdd:TIGR00231 3 KIVIVGHPNVGKSTLLNSLLGNKGSIT----------------EYYPGTTRNYVTTVIEEDG------------KTYKFN 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 88 IIDAPGHRDF-------VKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREhIILAKTMGLdQLIVAVNKMDLTEPP 160
Cdd:TIGR00231 55 LLDTAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEI-------LEKQTKE-IIHHADSGV-PIILVGNKIDLKDAD 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
1JNY_A 161 YDEKrYKEIVDqvskfmrsygfNTNKVRFVPVVAPSGDNIT 201
Cdd:TIGR00231 126 LKTH-VASEFA-----------KLNGEPIIPLSAETGKNID 154
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
237-312 |
2.13e-08 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 51.14 E-value: 2.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1JNY_A 237 IQDVYSISGvGTVPVGRVESGVLKVGDKIVfmPAGKVGEVRSIETHHTKMDKAEPGDNIGFNVRGVEKkdIKRGDV 312
Cdd:cd16265 5 VEKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDV 75
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
8-155 |
5.59e-08 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 53.65 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 8 NLIVIGHVDHGKSTLVGRLLMDRGFIdektvkeaeeaaKKLGKESEKFAfLLDRLKEERERGVTINLTFMRFETKKYFFT 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRI------------HKIGEVHGGGA-TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1JNY_A 88 IIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQT----REhiilAKTMGLDQlIVAVNKMD 155
Cdd:cd01886 68 IIDTPGHVDFTIEVERSLRVLDGAVAVFDAVAG-------VQPQTetvwRQ----ADRYGVPR-IAFVNKMD 127
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
325-427 |
6.33e-08 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the 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: 294007 [Multi-domain] Cd Length: 87 Bit Score: 49.82 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 325 EFTARIIVVWHPTALANGYTPVLHVHTASVACRVSELvskldprtgqeaekNPQFLKQGDVAIVKFKPIkplcveKYNEF 404
Cdd:cd03708 5 EFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISI--------------DKEVLRTGDRALVRFRFL------YRPEY 64
|
90 100
....*....|....*....|....
1JNY_A 405 PPLG-RFAMRDmGKTVGVGIIVDV 427
Cdd:cd03708 65 LREGqRLIFRE-GRTKGIGTVTKV 87
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
11-266 |
2.73e-07 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 52.91 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLVGRllmdrgfidektVKEAEEAAKKLGKESEKFAflldrlkeererGVTINLTFmRFETKKYFFtiID 90
Cdd:CHL00189 249 ILGHVDHGKTTLLDK------------IRKTQIAQKEAGGITQKIG------------AYEVEFEY-KDENQKIVF--LD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 91 APGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNKMDLTEPpyDEKRYKEIV 170
Cdd:CHL00189 302 TPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAINYIQAANV-PIIVAINKIDKANA--NTERIKQQL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 171 DQVSKFMRSYGfntNKVRFVPVVAPSGDNITHKSENMKwyngpTLEEYLDqleLPPKPVDKPLRIpIQDVYSISGVGTVP 250
Cdd:CHL00189 372 AKYNLIPEKWG---GDTPMIPISASQGTNIDKLLETIL-----LLAEIED---LKADPTQLAQGI-ILEAHLDKTKGPVA 439
|
250
....*....|....*.
1JNY_A 251 VGRVESGVLKVGDKIV 266
Cdd:CHL00189 440 TILVQNGTLHIGDIIV 455
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
11-133 |
5.61e-07 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 51.67 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLVGRLLMDRGFIDEK-TVKeaeeaakklGKESEKFAfLLDRLKEERERGVTINLTFMRFETKKYFFTII 89
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAIQEAgTVK---------GRKSGRHA-TSDWMEMEKQRGISVTSSVMQFPYRDCLINLL 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
1JNY_A 90 DAPGHRDFvknmitgaSQ--------ADAAILVVSAKKGeyeagmsVEGQTR 133
Cdd:PRK00741 85 DTPGHEDF--------SEdtyrtltaVDSALMVIDAAKG-------VEPQTR 121
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
11-291 |
6.70e-07 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 51.55 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 11 VIGHVDHGKSTLvgrllmdrgfidektvkeaeeaakklgkesekfaflLDRLKE----ERERG----------VTIN--- 73
Cdd:COG0532 9 VMGHVDHGKTSL------------------------------------LDAIRKtnvaAGEAGgitqhigayqVETNggk 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 74 LTFmrfetkkyfftiIDAPGHRDFVKNMITGASQADAAILVVSAKKGeyeagmsVEGQTREHIILAKTMGLdQLIVAVNK 153
Cdd:COG0532 53 ITF------------LDTPGHEAFTAMRARGAQVTDIVILVVAADDG-------VMPQTIEAINHAKAAGV-PIIVAINK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 154 MDlteppydekryKEivdqvskfmrsyGFNTNKVR------------------FVPVVAPSGDNIthksenmkwyngPTL 215
Cdd:COG0532 113 ID-----------KP------------GANPDRVKqelaehglvpeewggdtiFVPVSAKTGEGI------------DEL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 216 EEYL----DQLELppK-PVDKPlripiqdvysisGVGTV-----PVGR-------VESGVLKVGDKIVfmpAGKV-GEVR 277
Cdd:COG0532 158 LEMIllqaEVLEL--KaNPDRP------------ARGTVieaklDKGRgpvatvlVQNGTLKVGDIVV---AGTAyGRVR 220
|
330
....*....|....*
1JNY_A 278 SIETHHTK-MDKAEP 291
Cdd:COG0532 221 AMFDDRGKrVKEAGP 235
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
86-170 |
4.81e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 40.69 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 86 FTIIDAPG-------HRDFVKNMITGASQADAAILVVSAKKGEYEagmsvegqTREHIILAKTMGLDQLIVAvNKMDLTE 158
Cdd:cd00880 48 VVLIDTPGldeegglGRERVEEARQVADRADLVLLVVDSDLTPVE--------EEAKLGLLRERGKPVLLVL-NKIDLVP 118
|
90
....*....|..
1JNY_A 159 PPYDEKRYKEIV 170
Cdd:cd00880 119 ESEEEELLRERK 130
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
337-427 |
1.18e-03 |
|
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 mtEF-TU 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: 294005 [Multi-domain] Cd Length: 93 Bit Score: 37.98 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 337 TALANGYTPVLHVHTASVACRVsELVskldprtgqeAEKNpqFLKQGDVAIVKFKPIKPLCVEKynefpplG-RFAMRDM 415
Cdd:cd03706 22 KPFTSGFQQQMFSKTWDCACRI-DLP----------EGKE--MVMPGEDTSVKLTLLKPMVLEK-------GqRFTLREG 81
|
90
....*....|..
1JNY_A 416 GKTVGVGIIVDV 427
Cdd:cd03706 82 GRTIGTGVVTKL 93
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
246-319 |
1.19e-03 |
|
Domain II of BipA; BipA (also called TypA) 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. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 37.94 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 246 VGTVPVGRVESGVLKVGDKIVFMPAGKV---GEVRSIETHH----TKMDKAEPGDNIGFNvrGVEKKDIkrGDVVGHPNN 318
Cdd:cd03691 14 LGRIAIGRIFSGTVKVGQQVTVVDEDGKiekGRVTKLFGFEglerVEVEEAEAGDIVAIA--GLEDITI--GDTICDPEV 89
|
.
1JNY_A 319 P 319
Cdd:cd03691 90 P 90
|
|
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
6-100 |
8.89e-03 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 37.91 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JNY_A 6 HLNLIVIGHVDHGKSTLVGRLLmDRGFIDEKTVKEAEEAAKKLGKESEKFAFLldrlkeeRERGVTINLTfmrfetkkyf 85
Cdd:cd01850 4 QFNIMVVGESGLGKSTFINTLF-GTKLYPSKYPPAPGEHITKTVEIKISKAEL-------EENGVKLKLT---------- 65
|
90
....*....|....*
1JNY_A 86 ftIIDAPGHRDFVKN 100
Cdd:cd01850 66 --VIDTPGFGDNINN 78
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