|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-450 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 899.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 161 PYSEARYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLEPSEKMPWFKgwsverkegkaeGKCLIDALDAILPPQR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKEL 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 321 RRGYVAGDSKNNPPRGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 45553816 401 IIVLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKSVNFKETTSGK 450
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKEGSGTK 438
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-452 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 699.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 161 PYSEARYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLEPSEKMPWFKGwsverkegkaegKCLIDALDAILPPQR 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKEL 320
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 321 RRGYVAGDSKNNPPRGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAA 400
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 45553816 401 IIVLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKSVNFKETTSGKVT 452
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVT 440
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-445 |
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: 678.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 161 pYSEARYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLEPSEKMPWFKgwsverkegkaeGKCLIDALDAILPPQR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKEL 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 321 RRGYVAGDSkNNPPRGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAA 400
Cdd:COG5256 300 KRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 45553816 401 IIVLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKSVNFKE 445
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-445 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 668.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 3 KEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppY 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 163 SEARYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLEPSEKMPWFKgwsverkegkaeGKCLIDALDAILPPQRPT 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRR 322
Cdd:PRK12317 223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 323 GYVAGdSKNNPPRGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAAII 402
Cdd:PRK12317 303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 45553816 403 VLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKSVNFKE 445
Cdd:PRK12317 382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPAK 424
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-445 |
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: 665.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 161 pYSEARYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLEPSEKMPWFKgwsverkegkaeGKCLIDALDAILPPQR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKEL 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 321 RRGYVAGDSKnNPPRGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 45553816 401 IIVLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKSVNFKE 445
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-239 |
1.94e-160 |
|
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: 451.95 E-value: 1.94e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETSKYYVT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARYE 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553816 169 EIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLEPSEKMPWFKGWsverkegkaegkCLIDALDAILPPQ 239
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-441 |
6.20e-91 |
|
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: 282.75 E-value: 6.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETSKYY 86
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEAR 166
Cdd:COG2895 97 FIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 167 YEEIKKEVSSYIKKIGYnpASVAFVPISGWHGDNMLEPSEKMPWFKgwsverkegkaeGKCLIDALDAILPPQRPTDKPL 246
Cdd:COG2895 168 FEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAEDRNDAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 247 RLPLQDVYKiggigtvP-------VGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVK---NVS 316
Cdd:COG2895 234 RFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 317 vkelrRGYVAGDSkNNPPRGAADFTAQVIVLN-HPGQIANGYtpVLDCHTAHIACKFSEIKEKCDRRTGktTETEPKAIK 395
Cdd:COG2895 307 -----RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTL--EHEAADSLE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 45553816 396 SGDAAIIVLVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVIKSV 441
Cdd:COG2895 377 LNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGA 424
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-238 |
1.40e-76 |
|
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: 237.42 E-value: 1.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 5 KIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETSK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySE 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553816 165 ARYEEIKKEVSS-YIKKIGYNPASVAFVPISGWHGDNMLEpsekmpwfkgwsverkegkaegkcLIDALDAILPP 238
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
335-438 |
3.99e-69 |
|
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: 215.13 E-value: 3.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 335 RGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAAIIVLVPSKPLCVES 414
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 45553816 415 FQEFPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-235 |
4.34e-62 |
|
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: 200.49 E-value: 4.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAQEMGKgsFKYAWVLDKLKAERERGITIDIALWKFETSKY 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEA 165
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 166 RYEEIKKEVSSYIKKIGYNPasVAFVPISGWHGDNMLEPSEKMPWFKgwsverkegkaeGKCLIDALDAI 235
Cdd:cd04166 150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-438 |
1.81e-59 |
|
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: 200.29 E-value: 1.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGK--GSFKYAWVLDKLKAERERGITIDIALWKFETSKYYVTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 92 APGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARYEEIK 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 172 KEVSSYIKKIGynPASVAFVPISGWHGDNMLEPSEKMPWFkgwsverkegkaEGKCLIDALDAILPPQRPTDKPLRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 252 DVYKI-----GGIGTVPVGRVEtgllkPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSvkELRRG--Y 324
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGdlL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 325 VAGDsknNPPRGAADFTAQVIVLNHPGQIAnGYTPVLDCHTAHIACKFSEIKEKCDRRTGKttETEPKAIKSGDAAIIVL 404
Cdd:TIGR02034 297 AAAD---SAPEVADQFAATLVWMAEEPLLP-GRSYDLKLGTRKVRASVAAIKHKVDVNTLE--KGAAKSLELNEIGRVNL 370
|
410 420 430
....*....|....*....|....*....|....*.
gi 45553816 405 VPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 371 SLDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
242-332 |
7.68e-58 |
|
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: 185.47 E-value: 7.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELR 321
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 45553816 322 RGYVAGDSKNN 332
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-438 |
9.34e-57 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 198.23 E-value: 9.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMG--KGSFKYAWVLDKLKAERERGITIDIALWKFETSKYYVTIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 92 APGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARYEEIK 171
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 172 KEVSSYIKKIGYnpASVAFVPISGWHGDNMLEPSEKMPWFKGWSverkegkaegkcLIDALDAILPPQRPTDKPLRLPLQ 251
Cdd:PRK05506 182 ADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPS------------LLEHLETVEIASDRNLKDFRFPVQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 252 DVYKI-----GGIGTVPVGRVetgllKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKN---VSvkelrRG 323
Cdd:PRK05506 248 YVNRPnldfrGFAGTVASGVV-----RPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS-----RG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 324 YVAGDSkNNPPRGAADFTAQVIVLN----HPGqiaNGYtpVLDCHTAHIACKFSEIKEKCDRRTgkTTETEPKAIKSGDA 399
Cdd:PRK05506 318 DMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT--LERLAAKTLELNEI 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 45553816 400 AIIVLVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVI 438
Cdd:PRK05506 390 GRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMI 430
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-441 |
2.21e-56 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 194.06 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 3 KEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppy 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 163 SEARYEEIKKEVSSYIKKIGYNPASvafVPISGWHGDNMLEPSEKMPwfkgwSVERKEGKAEGKC--LIDALDAILP-PQ 239
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 240 RPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLV--TEVKSVEMHHEALTEAMPGDNVGFNVKNVSV 317
Cdd:PLN03126 284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 318 KELRRGYVAgdSKNNPPRGAADFTAQVIVLN------HPGQIAnGYTPVLDCHTAHIACKFSEIKEKCDRrtgkttetEP 391
Cdd:PLN03126 364 ADIQRGMVL--AKPGSITPHTKFEAIVYVLKkeeggrHSPFFA-GYRPQFYMRTTDVTGKVTSIMNDKDE--------ES 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 45553816 392 KAIKSGDAAIIVLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:PLN03126 433 KMVMPGDRVKMVVELIVPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-203 |
2.54e-55 |
|
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: 182.11 E-value: 2.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaqemgkgsfkyaWVLDKLKAERERGITIDIALWKFETSKYYVT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVKQLIVGVNKMDSTeppySEARYE 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFD 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 45553816 169 EIKKEVSSYIKKIGY---NPASVAFVPISGWHGDNMLE 203
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-359 |
2.44e-54 |
|
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: 186.51 E-value: 2.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKI-----HINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKfekeaqemGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEKFertkpHVNIGTIGHVDHGKTTLTA-------AITKVLAKK--------GGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 76 ALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 156 DSTEPPY-SEARYEEIKKEVSSYikkiGYNPASVAFVPISGWhgdNMLEPSEKMPWFKgwSVERkegkaegkcLIDALDA 234
Cdd:COG0050 139 DMVDDEElLELVEMEVRELLSKY----GFPGDDTPIIRGSAL---KALEGDPDPEWEK--KILE---------LMDAVDS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 235 ILP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGmvvnfAPVNLV-------TEVKSVEMHHEALTEAMPGD 306
Cdd:COG0050 201 YIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVG-----DEVEIVgirdtqkTVVTGVEMFRKLLDEGEAGD 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 307 NVGFNVKNVSVKELRRGYVAgdSKNNPPRGAADFTAQVIVLN-------HPgqIANGYTP 359
Cdd:COG0050 276 NVGLLLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVLSkeeggrhTP--FFNGYRP 331
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-440 |
1.80e-53 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 186.27 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 14 GHVDSGKSTTTGHLIYkcggiDKRTI-----EKFEKEAQEMGKGSFK--YAWVLDKLKAERERGITIDIALWKFETSKYY 86
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQIyedqlASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTEKRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEAR 166
Cdd:PRK05124 109 FIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 167 YEEIKKEVSSYIKKIGYNPaSVAFVPISGWHGDNMLEPSEKMPWFKGWSverkegkaegkcLIDALDAILPPQRPTDKPL 246
Cdd:PRK05124 180 FERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYSGPT------------LLEVLETVDIQRVVDAQPF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 247 RLPLQDVYKI-----GGIGTVPVGRVetgllKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKN---VSvk 318
Cdd:PRK05124 247 RFPVQYVNRPnldfrGYAGTLASGVV-----KVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDeidIS-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 319 elrRGYVAGDSKNNPPRGAAdFTAQVIVLNH----PGQ-----IANGYTPVldchtahiacKFSEIKEKCDRRTGKTTET 389
Cdd:PRK05124 320 ---RGDLLVAADEALQAVQH-ASADVVWMAEqplqPGQsydikIAGKKTRA----------RVDAIRYQVDINTLTQREA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 45553816 390 EpkAIKSGDAAIIVLVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVIKS 440
Cdd:PRK05124 386 E--NLPLNGIGLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-438 |
2.97e-53 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 184.01 E-value: 2.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDI 75
Cdd:CHL00071 1 MAREKFerkkpHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 76 ALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:CHL00071 66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 156 DSTEppySEARYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGdnmLEPSEKMPwfkgwSVERKEGKAEGKC--LIDALD 233
Cdd:CHL00071 139 DQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKIynLMDAVD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 234 AILP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNL--VTEVKSVEMHHEALTEAMPGDNVGF 310
Cdd:CHL00071 208 SYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLREtkTTTVTGLEMFQKTLDEGLAGDNVGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 311 NVKNVSVKELRRGYVAGDSKNNPPRgaADFTAQVIVLN------HPGQIAnGYTPVLDCHTAHIACKFSEIKEkcdrrtg 384
Cdd:CHL00071 288 LLRGIQKEDIERGMVLAKPGTITPH--TKFEAQVYILTkeeggrHTPFFP-GYRPQFYVRTTDVTGKIESFTA------- 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 45553816 385 kTTETEPKAIKSGDAAIIVLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:CHL00071 358 -DDGSKTEMVMPGDRIKMTVELIYPIAIEKGM------RFAIREGGRTVGAGVV 404
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-441 |
4.09e-53 |
|
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: 183.05 E-value: 4.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:TIGR00485 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 76 ALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:TIGR00485 66 AHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 156 D-STEPPYSEARYEEIKKEVSSYikkigynpasvafvpisGWHGDNmlepsekMPWFKGWSVERKEGKAEGKC----LID 230
Cdd:TIGR00485 139 DmVDDEELLELVEMEVRELLSQY-----------------DFPGDD-------TPIIRGSALKALEGDAEWEAkileLMD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 231 ALDAILP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPV--NLVTEVKSVEMHHEALTEAMPGDN 307
Cdd:TIGR00485 195 AVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLkdTRKTTVTGVEMFRKELDEGRAGDN 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 308 VGFNVKNVSVKELRRGYVAgdSKNNPPRGAADFTAQVIVLN------HPGqIANGYTPVLDCHTAHIackfseikekcdr 381
Cdd:TIGR00485 275 VGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVLSkeeggrHTP-FFSGYRPQFYFRTTDV------------- 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553816 382 rTGKTTETEP-KAIKSGDAAIIVLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:TIGR00485 339 -TGTIELPEGvEMVMPGDNVKMTVELISPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-347 |
1.33e-52 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 181.68 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKE-----KIHINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTA-------AITKVLAERGLNQAK-------DYDSI-DAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 76 ALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 156 DSTE-PPYSEARYEEIKKEVSSYikkigynpasvafvpisGWHGDNmlepsekMPWFKGWSVERKEGKAEG----KCLID 230
Cdd:PRK12736 139 DLVDdEELLELVEMEVRELLSEY-----------------DFPGDD-------IPVIRGSALKALEGDPKWedaiMELMD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 231 ALDAILP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPG---MVVNFAPVnLVTEVKSVEMHHEALTEAMPGD 306
Cdd:PRK12736 195 AVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGD 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 45553816 307 NVGFNVKNVSVKELRRGYVAGDSKNNPPRgaADFTAQVIVL 347
Cdd:PRK12736 274 NVGVLLRGVDRDEVERGQVLAKPGSIKPH--TKFKAEVYIL 312
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-441 |
1.87e-52 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 182.72 E-value: 1.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 3 KEKIHINIVVIGHVDSGKSTTTGhliykcggidkrTIEKFEKEAQEMGKGSFKYawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTA------------AITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPY 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 163 SEARYEEIKKEVSSYIKkigynpasvaFvpisgwhgdnmlePSEKMPWFKGWSVERKEGKAE--GKC----LIDALDAIL 236
Cdd:PLN03127 195 LLELVEMELRELLSFYK----------F-------------PGDEIPIIRGSALSALQGTNDeiGKNailkLMDAVDEYI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 237 P-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPG---MVVNFAP-VNLVTEVKSVEMHHEALTEAMPGDNVGFN 311
Cdd:PLN03127 252 PePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 312 VKNVSVKELRRGYVAgdSKNNPPRGAADFTAQVIVLN------HPGQIANgYTPVLDCHTAHIackfseikekcdrrTGK 385
Cdd:PLN03127 332 LRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADV--------------TGK 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 45553816 386 TTETE-PKAIKSGDAAIIVLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:PLN03127 395 VELPEgVKMVMPGDNVTAVFELISPVPLEPGQ------RFALREGGRTVGAGVVSKV 445
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-347 |
2.21e-52 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 181.16 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKI-----HINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK00049 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGAEAK-------AYDQI-DKAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 76 ALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK00049 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 156 DSTE-PPYSEARYEEIKKEVSSYikkiGYNPASVAFVPISGWHGdnmLEPSEKMPWFKgwSVERkegkaegkcLIDALDA 234
Cdd:PRK00049 139 DMVDdEELLELVEMEVRELLSKY----DFPGDDTPIIRGSALKA---LEGDDDEEWEK--KILE---------LMDAVDS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 235 ILP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPG---MVVNFAPVNLVTeVKSVEMHHEALTEAMPGDNVGF 310
Cdd:PRK00049 201 YIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGA 279
|
330 340 350
....*....|....*....|....*....|....*..
gi 45553816 311 NVKNVSVKELRRGYVAGDSKNNPPRgaADFTAQVIVL 347
Cdd:PRK00049 280 LLRGIKREDVERGQVLAKPGSITPH--TKFEAEVYVL 314
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-347 |
3.30e-51 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 178.11 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 76 ALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 156 DSTEPP-YSEARYEEIKKEVSSYikkigynpasvafvpisGWHGDNmlepsekMPWFKGWSVERKEGKAEGKC------L 228
Cdd:PRK12735 139 DMVDDEeLLELVEMEVRELLSKY-----------------DFPGDD-------TPIIRGSALKALEGDDDEEWeakileL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 229 IDALDAILP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPG---MVVNFAPvNLVTEVKSVEMHHEALTEAMP 304
Cdd:PRK12735 195 MDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKE-TQKTTVTGVEMFRKLLDEGQA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 45553816 305 GDNVGFNVKNVSVKELRRGYVAGDSKNNPPRgaADFTAQVIVL 347
Cdd:PRK12735 274 GDNVGVLLRGTKREDVERGQVLAKPGSIKPH--TKFEAEVYVL 314
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-438 |
2.62e-41 |
|
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: 155.84 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFEtSKY 85
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLgfAYLPLP-DGR 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtLGVKQLIVGVNKMDSTEPpyse 164
Cdd:COG3276 52 RLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-LGIKRGIVVLTKADLVDE---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 165 ARYEEIKKEVSSYIKkiGYNPASVAFVPISgwhgdnmlepsekmpwfkgwSVErKEGKAEgkcLIDALDAIL--PPQRPT 242
Cdd:COG3276 120 EWLELVEEEIRELLA--GTFLEDAPIVPVS--------------------AVT-GEGIDE---LRAALDALAaaVPARDA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRR 322
Cdd:COG3276 174 DGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIER 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 323 GYVAgdSKNNPPRGAADFTAQVIVLNHPGQ-IANGyTPVLdCH--TAHIackfseikekcdrrTGKTTETEPKAIKSGDA 399
Cdd:COG3276 254 GDVL--AAPGALRPTDRIDVRLRLLPSAPRpLKHW-QRVH-LHhgTAEV--------------LARVVLLDREELAPGEE 315
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 45553816 400 AIIVLVPSKPLCVESFQefpplgRFAVRDM--RQTVAVGVI 438
Cdd:COG3276 316 ALAQLRLEEPLVAARGD------RFILRDYspRRTIGGGRV 350
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
333-441 |
3.47e-35 |
|
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: 126.23 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 333 PPRGAADFTAQVIVLNH-----PGQIANGYTPVLDCHTAHIACKFSEIKEKCDrrTGKTTEtEPKAIKSGDAAIIVLVPS 407
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 45553816 408 KPLCVESFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-357 |
6.05e-34 |
|
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: 134.23 E-value: 6.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETSKYYV 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppysEARY 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 168 EEIKKEVSSYIKKIGYNPASVAFVpISGWHGDNMlepsekmpwfkgwsverKEGKAEGKCLIDALDAilppqRPTDKPLR 247
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGI-----------------GELKKELKNLLESLDI-----KRIQKPLR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 248 LPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGYVAG 327
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLIL 258
|
330 340 350
....*....|....*....|....*....|
gi 45553816 328 DSKNNPPRGAADFTAQVIVLnhPGQIANGY 357
Cdd:TIGR00475 259 TPEDPKLRVVVKFIAEVPLL--ELQPYHIA 286
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-238 |
3.52e-33 |
|
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: 123.85 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 6 IHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETSKY 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySEA 165
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD---DEE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553816 166 RYEEIKKEVSSYIKKIGYNPASVAFVPISGWhgdNMLEPSEKMPWFKgwSVERkegkaegkcLIDALDAILPP 238
Cdd:cd01884 136 LLELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVD--KILE---------LLDALDSYIPT 194
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
340-438 |
1.34e-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: 105.94 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 340 FTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKttETEPKAIKSGDAAIIVLVPSKPLCVESFQEFP 419
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 45553816 420 PLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-177 |
3.98e-25 |
|
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: 101.14 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETSKYyV 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARY 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDEDRLELVE 125
|
170
....*....|
gi 45553816 168 EEIKKEVSSY 177
Cdd:cd04171 126 EEILELLAGT 135
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
340-438 |
5.90e-22 |
|
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: 90.31 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 340 FTAQVIVLNHPGQI-ANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAAIIVLVPSKPLCVESFQEF 418
Cdd:cd03704 6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
|
90 100
....*....|....*....|
gi 45553816 419 PPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03704 86 PQLGRFTLRDEGKTIAIGKV 105
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
340-441 |
3.86e-19 |
|
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: 82.59 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 340 FTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDRRTGKTTETEPKAIKSGDAAIIVLVPSKPLCVESFQEFP 419
Cdd:cd04093 8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKDNK 87
|
90 100
....*....|....*....|..
gi 45553816 420 PLGRFAVRDMRQTVAVGVIKSV 441
Cdd:cd04093 88 ELGRFVLRRGGETIAAGIVTEI 109
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-191 |
6.01e-18 |
|
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: 81.43 E-value: 6.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFETSK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 85 YYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD--STE 159
Cdd:cd01890 66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDlpAAD 135
|
170 180 190
....*....|....*....|....*....|..
gi 45553816 160 PpysearyEEIKKEVSSYikkIGYNPASVAFV 191
Cdd:cd01890 136 P-------DRVKQEIEDV---LGLDASEAILV 157
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
246-325 |
1.42e-17 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 77.30 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 246 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNvsVKELRRGYV 325
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-309 |
1.67e-16 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 81.05 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWK--- 79
Cdd:PRK04000 10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKcpd 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 80 FETSKYYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAgiskngQTREHaLLAF 141
Cdd:PRK04000 62 CEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 142 T-LGVKQLIVGVNKMDSTEPPYSEARYEEIKKEVSSYIkkigynpASVA-FVPISGWHGDNMlepsekmpwfkgwsverk 219
Cdd:PRK04000 135 DiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-------AENApIIPVSALHKVNI------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 220 egkaegKCLIDALDAILP-PQRPTDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---LLKPGMVVNFAP 282
Cdd:PRK04000 190 ------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEEGG 263
|
330 340 350
....*....|....*....|....*....|.
gi 45553816 283 ----VNLVTEVKSVEMHHEALTEAMPGDNVG 309
Cdd:PRK04000 264 ktkwEPITTKIVSLRAGGEKVEEARPGGLVG 294
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-316 |
2.05e-16 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 81.60 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 82 TSKYYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVN 153
Cdd:COG0481 69 DGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA------QTLANVYLALENDLEIIPV-IN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 154 KMD--STEPpysearyEEIKKEVssyIKKIGYNPASVafVPISGwhgdnmlepsekmpwfkgwsverKEGkaEGkclIDA 231
Cdd:COG0481 134 KIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSA-----------------------KTG--IG---IEE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 232 -LDAI---LPPqrPTDKPLRlPLQ--------DVYKiggiGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSV---EMHH 296
Cdd:COG0481 174 iLEAIverIPP--PKGDPDA-PLQalifdswyDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvfTPKM 246
|
330 340
....*....|....*....|...
gi 45553816 297 EALTEAMPGDnVGF---NVKNVS 316
Cdd:COG0481 247 TPVDELSAGE-VGYiiaGIKDVR 268
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-178 |
4.01e-16 |
|
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: 77.66 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaqemgkGSfkyawV------LDKLKAERERGITIDIALWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgvKQL----IVGVNKMDsT 158
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKID-R 128
|
170 180
....*....|....*....|
gi 45553816 159 EPPYSEARYEEIKKEVSSYI 178
Cdd:cd04168 129 AGADLEKVYQEIKEKLSPDI 148
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
246-325 |
4.05e-15 |
|
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: 70.25 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 246 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-194 |
4.40e-15 |
|
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: 73.55 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTttghliykcggIDKRTIEKFEKEAqemgkgsfkyawvLDKLKAERERGITIDIALWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTS-----------LAKALSEIASTAA-------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 81 -------ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGvKQLIVGVN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45553816 154 KMDSTEPPYSEARYEEIKKEVSSYIKKIgyNPASVAFVPIS 194
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVS 167
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
248-325 |
1.08e-14 |
|
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: 69.08 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 248 LPLQDVYKIGGIGTVPVGRVETGLLKPGM---VVNFAPvNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81
|
.
gi 45553816 325 V 325
Cdd:cd03697 82 V 82
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-201 |
2.30e-14 |
|
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: 71.53 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTTTGHLiykcGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 83 SKYY----------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTRE 135
Cdd:cd01888 53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553816 136 HALLAFTLGVKQLIVGVNKMDSTEPPYSEARYEEIKKevssYIKkiGYNPASVAFVPISGWHGDNM 201
Cdd:cd01888 122 HLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVK--GTIAENAPIIPISAQLKYNI 181
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-323 |
2.91e-14 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 75.09 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETSKYyV 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTlGVKQLIVGVNKMDSTEppysEAR 166
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVD----EAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 167 YEEIKKEVSSYIKKIGYNPASVaFVPisgwhgdnmlepsekmpwfkgwSVERKEGKAEgkcLIDALDAILPPQRPTDKPL 246
Cdd:PRK10512 122 IAEVRRQVKAVLREYGFAEAKL-FVT----------------------AATEGRGIDA---LREHLLQLPEREHAAQHRF 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553816 247 RLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVK-NVSVKELRRG 323
Cdd:PRK10512 176 RLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINRG 253
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-212 |
7.48e-14 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 69.93 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAQEMGKGsfkyawVLDKLKAERERGITIdiaLWKfETSKYY-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR---EHALLAftlGVKqLIVGVNKM 155
Cdd:cd01891 65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553816 156 DSteppySEARYEEIKKEVSSYIKKIGYNPASVAFvPI------SGWHGDNMLEPSEKM-PWFK 212
Cdd:cd01891 128 DR-----PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLdPLFE 185
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
260-325 |
7.83e-14 |
|
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: 66.13 E-value: 7.83e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553816 260 GTVPVGRVETGLLKPGMVVNFAPV-----NLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGYV 325
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-156 |
2.97e-13 |
|
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: 68.80 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAqemgkGSFKYawvLDKLKAERERGITID---IALwKFETSK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 85 ------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgeFEaGISKngQTreHALL--AFTLGVKQLIVgVNKMD 156
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----VE-GVCV--QT--ETVLrqALEERVKPVLV-INKID 135
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-274 |
7.07e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 70.51 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekEAQEMgkgsfkyawVLDKLKAERERGITIDIALWKFETSKYYVT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA------ETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVgVNKMD--STEPPYSEAR 166
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDrpGARPDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 167 YEEIKKEVSSYIKKIGYnPA--SVAFVPISGWHGDNMLEpsEKMPWFKGwsverkegkaegkclidALDAILPPQRPTDK 244
Cdd:PRK10218 144 VFDLFVNLDATDEQLDF-PIvyASALNGIAGLDHEDMAE--DMTPLYQA-----------------IVDHVPAPDVDLDG 203
|
250 260 270
....*....|....*....|....*....|
gi 45553816 245 PLRLPLQDVYKIGGIGTVPVGRVETGLLKP 274
Cdd:PRK10218 204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKP 233
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-121 |
1.38e-12 |
|
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: 69.69 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtiekfekeaqeMGK---GSFkyawVLDKLKAERERGITIDIALWKFETSKY 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR------------IGEvhdGNT----VMDWMPEEQERGITITSAATTCEWKGH 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 45553816 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTG 121
Cdd:COG0480 75 KINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG 110
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
4.03e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 68.44 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAqemgkgsfkyawvlDKLKAERERGITIDIAL----WKfets 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553816 84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD 156
Cdd:PRK13351 72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWRQADRYGIPRLIF-INKMD 136
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-156 |
8.55e-12 |
|
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: 65.31 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaqemgkGSFkyawVLDKLKAERERGITIDIALWKFETSKYYV 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553816 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKQLIVgVNKMD 156
Cdd:cd04170 67 NLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMD 127
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
245-328 |
8.88e-12 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 60.99 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 245 PLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 45553816 325 VAGD 328
Cdd:cd16267 81 ILCD 84
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-156 |
1.04e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 67.07 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETSKYYVTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553816 92 APGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAFT--LGVKQLIVgVNKMD 156
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMD 123
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
1.36e-11 |
|
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: 64.82 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETSKYYVT 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIG-EVHGGGA------------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90
....*....|
gi 45553816 89 IIDAPGHRDF 98
Cdd:cd01886 68 IIDTPGHVDF 77
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-278 |
6.34e-11 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 64.27 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKIhINIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAQEMgkgsfkyawVLDKLKAERERGITIdiaLWKf 80
Cdd:COG1217 1 MMREDI-RNIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 81 ETSKYY----VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG---QTR---EHALlafTLG 144
Cdd:COG1217 61 NTAVRYkgvkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 145 VKqLIVGVNKMDSteppySEARYEEIKKEVSSYIKKIGYNPASVAFvPI------SGWHGDNMLEPSEKMpwfkgwsver 218
Cdd:COG1217 122 LK-PIVVINKIDR-----PDARPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDL---------- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553816 219 kegkaegKCLIDA-LDAILPPQRPTDKPLRlpLQ------DVYkIGGIGtvpVGRVETGLLKPGMVV 278
Cdd:COG1217 185 -------TPLFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQV 238
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
245-325 |
1.95e-10 |
|
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: 57.11 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 245 PLRLPLQDVYKigGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 45553816 325 V 325
Cdd:cd04089 79 V 79
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-201 |
2.19e-10 |
|
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: 59.41 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaqemgkgsfkyawVLDKLK----AERE-RGITIDIALWKFETSK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 85 YY--VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVGVNKMDst 158
Cdd:cd01887 47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID-- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45553816 159 EPPYSEARYEEIKKEVSSY---IKKIGynpASVAFVPISGWHGDNM 201
Cdd:cd01887 113 KPYGTEADPERVKNELSELglvGEEWG---GDVSIVPISAKTGEGI 155
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-211 |
2.54e-10 |
|
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: 59.97 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKcggIDKRTIEKFEKEAQEmgkgsfKYawvLDKLKAERERGITID---IALwKFETSK- 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ---THKRTPSVKLGWKPL------RY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 85 --YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--REhallAFTLGVKQLIVgVNKMDS--T 158
Cdd:cd04167 69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH----AIQEGLPMVLV-INKIDRliL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45553816 159 E---PPYsEARYE--EIKKEVSSYIKKIGyNPASVAFVPISGwhgdNMLEPSEKMPWF 211
Cdd:cd04167 139 ElklPPT-DAYYKlrHTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
9-182 |
5.81e-10 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 59.23 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaqemGKGSFKYAwvLDKLKAERERGIT---------------- 72
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTssvsndilgfdsdgev 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 73 ----IDIALWK----FETSKYYVTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFT 142
Cdd:cd04165 64 vnypDNHLGELdveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALA 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45553816 143 LGVKQLIVgVNKMDSTeppySEARYEEIKKEVSSYIKKIG 182
Cdd:cd04165 137 LKVPVFVV-VTKIDMT----PANVLQETLKDLKRLLKSPG 171
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
6.85e-10 |
|
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: 59.53 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAQEM-GKGSFKYAwVLDKLKAERERGITIDIALWKFETSKYYVTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 45553816 91 DAPGHRDFIKNMITGTSQADCAVLIVAAGTG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
245-328 |
1.22e-09 |
|
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: 54.81 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 245 PLRLPLQDVYKiGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMH-HEALTEAMPGDNVGFNVKNVSVKELRRG 323
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 45553816 324 YVAGD 328
Cdd:cd03698 80 DILSS 84
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
252-325 |
3.90e-09 |
|
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: 53.38 E-value: 3.90e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553816 252 DVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVN----LVTEVKSVEMHHEALTEAMPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-98 |
4.51e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 55.64 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeaqeMGKgsfkyAWVLDKLKAERERGITIDIA----LWKFETSK 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGE-----QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
|
90
....*....|....
gi 45553816 85 YYVTIIDAPGHRDF 98
Cdd:PRK07560 87 YLINLIDTPGHVDF 100
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-194 |
1.01e-07 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 54.24 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaqemgkgsfkyawvldKLKAERERGITIDIA-----LWKFE- 81
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLGyanakIYKCPk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 82 ---------------------------TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagiSKNGQTR 134
Cdd:PTZ00327 87 cprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 135 EHALLAFTLGVKQLIVGVNKMDSTEPPYSEARYEEIKKEVSSYIKKigynpaSVAFVPIS 194
Cdd:PTZ00327 161 EHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPIS 214
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
1.64e-07 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 53.90 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAqemGKGSFkyawvLDKLKAERERGITID---IAL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNA---GDARF-----TDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*...
gi 45553816 78 ---WKFETSK----YYVTIIDAPGHRDF 98
Cdd:PTZ00416 78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-98 |
2.91e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 53.19 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfekeAQEMGKGsfkyAWVLDKLKAERERGITID---IALW------- 78
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGII-----------AQEVAGD----VRMTDTRADEAERGITIKstgISLYyemtdes 85
|
90 100
....*....|....*....|....*.
gi 45553816 79 ------KFETSKYYVTIIDAPGHRDF 98
Cdd:PLN00116 86 lkdfkgERDGNEYLINLIDSPGHVDF 111
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
246-310 |
2.94e-07 |
|
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: 47.95 E-value: 2.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553816 246 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVNFAPVNLVTEVKSVEMHHEALTEAMPGDNVGF 310
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-201 |
1.68e-06 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 50.60 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 10 IVVIGHVDSGKSTTtghliykcggIDKrtIEKFEKEAQEMGkgsfkyawvldklkaererGITIDIA----LWKFETSKY 85
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDK--IRKTQIAQKEAG-------------------GITQKIGayevEFEYKDENQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREhALLAFTLGVKQLIVGVNKMDSTeppysEA 165
Cdd:CHL00189 296 KIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKA-----NA 362
|
170 180 190
....*....|....*....|....*....|....*....
gi 45553816 166 RYEEIKKEVSSY---IKKIGynpASVAFVPISGWHGDNM 201
Cdd:CHL00189 363 NTERIKQQLAKYnliPEKWG---GDTPMIPISASQGTNI 398
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-208 |
9.64e-06 |
|
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: 45.53 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIAL--WKFETSKYYVT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 89 IIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHALLAFTLGVKQLIVGvNKMDSTEPpys 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKIDLLEE--- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45553816 164 earYEEIKKEVSSYIKKIGYNPasvaFVPISGWHGDNMLEPSEKM 208
Cdd:cd00882 122 ---REVEELLRLEELAKILGVP----VFEVSAKTGEGVDELFEKL 159
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-203 |
2.41e-04 |
|
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: 41.59 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 8 INIVVIGHVDSGKSTTTGHLIYKcggidkrtiEKFEKEAQEmgkGSFKYAWVLdklkAERERGITIDIALWkfetskyyv 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---------KGSITEYYP---GTTRNYVTT----VIEEDGKTYKFNLL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 88 tiiDAPGHRDFIKNMITGTSQADcAVLIVAAGTG---EFEAGISKNGQTREHALlafTLGVKQLIVGvNKMDSteppyse 164
Cdd:TIGR00231 57 ---DTAGQEDYDAIRRLYYPQVE-RSLRVFDIVIlvlDVEEILEKQTKEIIHHA---DSGVPIILVG-NKIDL------- 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 45553816 165 aRYEEIKKEVSSYIKKIGYNPasvaFVPISGWHGDNMLE 203
Cdd:TIGR00231 122 -KDADLKTHVASEFAKLNGEP----IIPLSAETGKNIDS 155
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-194 |
5.28e-04 |
|
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: 42.31 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 10 IVVI-GHVDSGKSTttghliykcggidkrtiekfekeaqemgkgsfkyawVLDKLK----AERE-RGITIDIALWKFETS 83
Cdd:COG0532 6 VVTVmGHVDHGKTS------------------------------------LLDAIRktnvAAGEaGGITQHIGAYQVETN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagisKNG---QTRE---HALLAftlGVKqLIVGVNKMDS 157
Cdd:COG0532 50 GGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA---GVP-IIVAINKIDK 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45553816 158 teppySEARYEEIKKEVSSYikkiGYNPAS----VAFVPIS 194
Cdd:COG0532 116 -----PGANPDRVKQELAEH----GLVPEEwggdTIFVPVS 147
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
5-203 |
1.07e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 39.96 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 5 KIHINIVVIGHVDSGKSTttghLIYKcggidkrtiekfekeaqemgkgsFKYAWVlDKLKAERERGITIDIALWKFETSK 84
Cdd:COG1100 1 MGEKKIVVVGTGGVGKTS----LVNR-----------------------LVGDIF-SLEKYLSTNGVTIDKKELKLDGLD 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 85 YYVTIIDAPGHRDFIK---NMITGTSQADcAVLIVAAGTgefeagISKNGQT-REHALLAFTLG--VKQLIVGvNKMDst 158
Cdd:COG1100 53 VDLVIWDTPGQDEFREtrqFYARQLTGAS-LYLFVVDGT------REETLQSlYELLESLRRLGkkSPIILVL-NKID-- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45553816 159 eppyseaRYEEIKKEVSSYIKKIGYNPASVAFVPISGWHGDNMLE 203
Cdd:COG1100 123 -------LYDEEEIEDEERLKEALSEDNIVEVVATSAKTGEGVEE 160
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
340-385 |
1.74e-03 |
|
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: 37.50 E-value: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 45553816 340 FTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFSEIKEKCDrRTGK 385
Cdd:cd03708 6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVL-RTGD 50
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
340-438 |
3.98e-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: 36.44 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553816 340 FTAQVIVLN------HPGqIANGYTPVLDCHTAHIACKFSEIKEKcdrrtgkttetepKAIKSGDAAIIVLVPSKPLCVE 413
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRIDLPEGK-------------EMVMPGEDTSVKLTLLKPMVLE 71
|
90 100
....*....|....*....|....*
gi 45553816 414 SFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:cd03706 72 KGQ------RFTLREGGRTIGTGVV 90
|
|
| |
