|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-444 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 914.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 81 ETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEAGFAKEGQTREHALLAFTLGVKQMIVAVNKMDDAG- 159
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 160 -WAEARYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQD 238
Cdd:PTZ00141 161 nYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 239 VYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVASDSKND 318
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 319 PAMGAADFLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVV 398
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 677286257 399 ESFQEYPPLGRFAVRDMRSTVAVGVIKEVNKKEATAGKVTKAAQKK 444
Cdd:PTZ00141 401 EVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKEGSGTKAAAKAKKK 446
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-445 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 726.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 81 ETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEAGFAKEGQTREHALLAFTLGVKQMIVAVNKMDDA-- 158
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 159 GWAEARYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQD 238
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 239 VYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVASDSKND 318
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 319 PAMGAADFLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVV 398
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 677286257 399 ESFQEYPPLGRFAVRDMRSTVAVGVIKEVNKKEATAGKVTKAAQKKK 445
Cdd:PLN00043 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAKKK 447
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-431 |
0e+00 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 683.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 81 ETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEfeagfakEGQTREHALLAFTLGVKQMIVAVNKMDDAGW 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 161 AEARYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVY 240
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 241 KIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVASDSKNDPA 320
Cdd:COG5256 234 SISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 321 MgAADFLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVVES 400
Cdd:COG5256 314 V-AEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEK 392
|
410 420 430
....*....|....*....|....*....|.
gi 677286257 401 FQEYPPLGRFAVRDMRSTVAVGVIKEVNKKE 431
Cdd:COG5256 393 FKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-431 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 676.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 3 KEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 EKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEfeagfAKEGQTREHALLAFTLGVKQMIVAVNKMDDAGWAE 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG-----GVMPQTREHVFLARTLGINQLIVAINKMDAVNYDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 163 ARYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVYKI 242
Cdd:PRK12317 157 KRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYSI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 243 GGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVASDSKNDPAMg 322
Cdd:PRK12317 237 SGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTV- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 323 AADFLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVVESFQ 402
Cdd:PRK12317 316 AEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVK 395
|
410 420
....*....|....*....|....*....
gi 677286257 403 EYPPLGRFAVRDMRSTVAVGVIKEVNKKE 431
Cdd:PRK12317 396 EIPQLGRFAIRDMGQTIAAGMVIDVKPAK 424
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-431 |
0e+00 |
|
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]
Pssm-ID: 129574 [Multi-domain] Cd Length: 426 Bit Score: 667.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 81 ETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfaKEGQTREHALLAFTLGVKQMIVAVNKMDDAGW 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 161 AEARYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVY 240
Cdd:TIGR00483 157 DEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQDVY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 241 KIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVASDSKNdPA 320
Cdd:TIGR00483 237 SITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 321 MGAADFLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVVES 400
Cdd:TIGR00483 316 KVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEA 395
|
410 420 430
....*....|....*....|....*....|.
gi 677286257 401 FQEYPPLGRFAVRDMRSTVAVGVIKEVNKKE 431
Cdd:TIGR00483 396 VKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-225 |
7.31e-154 |
|
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: 434.61 E-value: 7.31e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETEKFYCT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 89 IIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEAGFAKEGQTREHALLAFTLGVKQMIVAVNKMDD--AGWAEARYN 166
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDvtVNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 677286257 167 EIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPK 225
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-427 |
1.79e-99 |
|
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: 303.93 E-value: 1.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGI--DKrtIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETE--K 84
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPkrK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 85 FycTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKQMIVAVNKMDDAGWA 161
Cdd:COG2895 97 F--IIADTPGHEQYTRNMVTGASTADLAILLID----------ARKGvleQTRRHSYIASLLGIRHVVVAVNKMDLVDYS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 162 EARYNEIQTEVKRFLKTVGYNPdkVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVYK 241
Cdd:COG2895 165 EEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 242 iggigtvP-------VGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVK---NVSvkelkRGFV 311
Cdd:COG2895 243 -------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS-----RGDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 312 ASDSkNDPAMGAADFLAQVIVLN----HPGE---IKNGyapvldchTAHIACKFAEIRSKMDRRTGKELEkdPKTIKSGD 384
Cdd:COG2895 311 IVAA-DAPPEVADQFEATLVWMDeeplLPGRkylLKHG--------TRTVRATVTAIKYRIDVNTLEHEA--ADSLELND 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 677286257 385 AAMVLMQPSKPMVVESFQEYPPLGRFAV--RDMRSTVAVGVIKEV 427
Cdd:COG2895 380 IGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGA 424
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-224 |
1.50e-78 |
|
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: 241.66 E-value: 1.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 5 KVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDIALWKFETEK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 85 FYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTREHALLAFTLGVKqMIVAVNKMDDAgwAEAR 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677286257 165 YNEIQTEVKR-FLKTVGYNPDKVPFIPISGFRGDNMLErsdnlkwykgpiLVEAINLCEPP 224
Cdd:pfam00009 139 LEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------LLDALDEYLPS 187
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
321-424 |
3.09e-67 |
|
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: 209.74 E-value: 3.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 321 MGAADFLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVVES 400
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 677286257 401 FQEYPPLGRFAVRDMRSTVAVGVI 424
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-225 |
6.10e-67 |
|
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: 212.82 E-value: 6.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAAEMGKgsFKYAWVLDKLKAERERGITIDIALWKFETEKF 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 86 YCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKQMIVAVNKMDDAGWAE 162
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVD----------ARKGvleQTRRHSYIASLLGIRHVVVAVNKMDLVDYDE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677286257 163 ARYNEIQTEVKRFLKTVGYNPdkVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPK 225
Cdd:cd04166 149 EVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIAS 209
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-434 |
5.46e-64 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 213.62 E-value: 5.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 14 GHVDAGKSTTTGHLIYkcggiDKRTIekFEKEAAEMGKGSFK---------YAWVLDKLKAERERGITIDIALWKFETEK 84
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 85 FYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKMDDAGWAEAR 164
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 165 YNEIQTEVKRFLKTVGYNPDkVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVYKI-- 242
Cdd:PRK05124 180 FERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 243 ---GGIGTvpvgrVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKN---VSvkelkRGFVASDSK 316
Cdd:PRK05124 259 dfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDeidIS-----RGDLLVAAD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 317 NDPAMGAAdFLAQV-------IVLNHPGEIKngyapvldchtahIACKF-----AEIRSKMDRRTGKELEKDpkTIKSGD 384
Cdd:PRK05124 329 EALQAVQH-ASADVvwmaeqpLQPGQSYDIK-------------IAGKKtrarvDAIRYQVDINTLTQREAE--NLPLNG 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 677286257 385 AAMVLMQPSKPMVVESFQEYPPLGRFAV--RDMRSTVAVGVIKEVNKKEATA 434
Cdd:PRK05124 393 IGLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVREPLAQATAA 444
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-424 |
1.81e-63 |
|
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: 210.31 E-value: 1.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 14 GHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGK--GSFKYAWVLDKLKAERERGITIDIALWKFETEKFYCTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 92 APGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKMDDAGWAEARYNEIQTE 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 172 VKRFLKTVGYNPdkVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVYKI-----GGIG 246
Cdd:TIGR02034 160 YLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 247 TVPVGRVEtgvlkPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSvkELKRG--FVASDSkndPAMGAA 324
Cdd:TIGR02034 238 TIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGdlLAAADS---APEVAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 325 DFLAQVIVL-NHPgeIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKdpKTIKSGDAAMVLMQPSKPMVVESFQE 403
Cdd:TIGR02034 308 QFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA--KSLELNEIGRVNLSLDEPIAFDPYAE 383
|
410 420
....*....|....*....|...
gi 677286257 404 YPPLGRFAVRDMRS--TVAVGVI 424
Cdd:TIGR02034 384 NRTTGAFILIDRLSnrTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-424 |
2.57e-62 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 212.87 E-value: 2.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 14 GHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMG--KGSFKYAWVLDKLKAERERGITIDIALWKFETEKFYCTIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 92 APGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKMDDAGWAEARYNEIQTE 171
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 172 VKRFLKTVGYNpdKVPFIPISGFRGDNMLERSDNLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVYKI-----GGIG 246
Cdd:PRK05506 184 YRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 247 TvpvgrVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKN---VSvkelkRGFVASDSKNDPAMgA 323
Cdd:PRK05506 262 T-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS-----RGDMLARADNRPEV-A 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 324 ADFLAQVIVLN----HPGeikNGYapVLDCHTAHIACKFAEIRSKMDRRTgkeLEKDP-KTIKSGDAAMVLMQPSKPMVV 398
Cdd:PRK05506 331 DQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAaKTLELNEIGRCNLSTDAPIAF 402
|
410 420
....*....|....*....|....*...
gi 677286257 399 ESFQEYPPLGRFAV--RDMRSTVAVGVI 424
Cdd:PRK05506 403 DPYARNRTTGSFILidRLTNATVGAGMI 430
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
228-318 |
1.99e-60 |
|
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: 191.63 E-value: 1.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 228 NDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELK 307
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 677286257 308 RGFVASDSKND 318
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-311 |
9.92e-59 |
|
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: 197.30 E-value: 9.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKE-----KVHINLVVIGHVDAGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 76 ALWKFETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKQMIVAV 152
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVS----------ATDGpmpQTREHILLARQVGVPYIVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 153 NKMD---DAGWAEAryneIQTEVKRFLKTVGYNPDKVPFIPISGFRGdnmLERSDNLKWYKgPI--LVEAINLCEP-PKR 226
Cdd:COG0050 136 NKCDmvdDEELLEL----VEMEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEK-KIleLMDAVDSYIPePER 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 227 PNDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAgVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSV 303
Cdd:COG0050 208 DTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKR 286
|
....*...
gi 677286257 304 KELKRGFV 311
Cdd:COG0050 287 EDVERGQV 294
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-311 |
2.68e-57 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 193.87 E-value: 2.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKE-----KVHINLVVIGHVDAGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFK-YAWVlDKLKAERERGITID 74
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITIN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 75 IALWKFETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKQMIVA 151
Cdd:PRK00049 65 TAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVS----------AADGpmpQTREHILLARQVGVPYIVVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 152 VNK---MDDAGWAEAryneIQTEVKRFLKTVGYNPDKVPFIPISGFRGdnmLERSDNLKWYKGPI-LVEAINLCEP-PKR 226
Cdd:PRK00049 135 LNKcdmVDDEELLEL----VEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKILeLMDAVDSYIPtPER 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 227 PNDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAGVTTeVKSVEMHHEQLPEANPGDNVGFNVKNVSV 303
Cdd:PRK00049 208 AIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGALLRGIKR 286
|
....*...
gi 677286257 304 KELKRGFV 311
Cdd:PRK00049 287 EDVERGQV 294
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-224 |
7.24e-57 |
|
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: 185.58 E-value: 7.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFekeaaemgkgsfkyaWVLDKLKAERERGITIDIALWKFETEKFYCT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 89 IIDAPGHRDFIKNMITGTSQADLAILVIASGTGEfeagfakEGQTREHALLAFtLGVKQMIVAVNKMDDAGwaEARYNEI 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 677286257 169 QTEVKRFLKTVGY---NPDKVPFIPISGFRGDNMLErsdnlkwykgpiLVEAINLCEPP 224
Cdd:cd00881 136 LREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------------LLDAIVEHLPP 182
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-429 |
8.16e-55 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 187.07 E-value: 8.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKE-----KVHINLVVIGHVDAGKSTTTGHLiykcggidkrtiekfEKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 76 ALWKFETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 156 DDAGWAEArYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGdnmLERSDnlKWYKGPI-LVEAINLCEP-PKRPNDKPLR 233
Cdd:PRK12736 139 DLVDDEEL-LELVEMEVRELLSEYDFPGDDIPVIRGSALKA---LEGDP--KWEDAIMeLMDAVDEYIPtPERDTDKPFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 234 LPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAgVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGF 310
Cdd:PRK12736 213 MPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 311 VAsdSKNDPAMGAADFLAQVIVLN------HPGEIKNgYAPVLDCHTAHIackfaeirskmdrrTGK-ELEKDPKTIKSG 383
Cdd:PRK12736 292 VL--AKPGSIKPHTKFKAEVYILTkeeggrHTPFFNN-YRPQFYFRTTDV--------------TGSiELPEGTEMVMPG 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 677286257 384 DAAMVLMQPSKPMVVEsfqeypPLGRFAVRDMRSTVAVGVIKEVNK 429
Cdd:PRK12736 355 DNVTITVELIHPIAME------QGLKFAIREGGRTVGAGTVTEILD 394
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-427 |
1.18e-54 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 189.06 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 3 KEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 EKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKMDDAGWAE 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVDDEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 163 ArYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRG------DNMLERSDNlKWY-KGPILVEAINLCEP-PKRPNDKPLRL 234
Cdd:PLN03126 215 L-LELVELEVRELLSSYEFPGDDIPIISGSALLAlealmeNPNIKRGDN-KWVdKIYELMDAVDSYIPiPQRQTDLPFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 235 PLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVT--TEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVA 312
Cdd:PLN03126 293 AVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 313 sdSKNDPAMGAADFLAQVIVLNHPGEIKN-----GYAPVLDCHTAHIACKFAEIRSKMDrrtgkeleKDPKTIKSGDAAM 387
Cdd:PLN03126 373 --AKPGSITPHTKFEAIVYVLKKEEGGRHspffaGYRPQFYMRTTDVTGKVTSIMNDKD--------EESKMVMPGDRVK 442
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 677286257 388 VLMQPSKPMVVESFQeypplgRFAVRDMRSTVAVGVIKEV 427
Cdd:PLN03126 443 MVVELIVPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-311 |
3.69e-54 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 185.43 E-value: 3.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKV-----HINLVVIGHVDAGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 76 ALWKFETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNK- 154
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKc 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 155 --MDDAGWAEAryneIQTEVKRFLKTVGYNPDKVPFIPISGFRGdnmLERSDNLKWYKGPI-LVEAINLCEP-PKRPNDK 230
Cdd:PRK12735 139 dmVDDEELLEL----VEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKILeLMDAVDSYIPePERAIDK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 231 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAGVTTeVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELK 307
Cdd:PRK12735 212 PFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVE 290
|
....
gi 677286257 308 RGFV 311
Cdd:PRK12735 291 RGQV 294
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-427 |
3.32e-52 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 180.54 E-value: 3.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 3 KEKVHINLVVIGHVDAGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAWVlDKLKAERERGITIDIALWKFET 82
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 EKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNK---MDDAG 159
Cdd:CHL00071 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKedqVDDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 160 WAEAryneIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLERSDNL-----KWYKGPI-LVEAINLCEP-PKRPNDKPL 232
Cdd:CHL00071 146 LLEL----VELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgenKWVDKIYnLMDAVDSYIPtPERDTDKPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 233 RLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVT---FAPAGVTTeVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRG 309
Cdd:CHL00071 222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 310 FVASDSKN-DPamgAADFLAQVIVLN------HPGeIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTgkelekdpKTIKS 382
Cdd:CHL00071 301 MVLAKPGTiTP---HTKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKIESFTADDGSKT--------EMVMP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 677286257 383 GDAAMVLMQPSKPMVVESFQeypplgRFAVRDMRSTVAVGVIKEV 427
Cdd:CHL00071 369 GDRIKMTVELIYPIAIEKGM------RFAIREGGRTVGAGVVSKI 407
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-427 |
1.52e-49 |
|
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: 173.42 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKV-----HINLVVIGHVDAGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:TIGR00485 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 76 ALWKFETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKM 155
Cdd:TIGR00485 66 AHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 156 DDAGwAEARYNEIQTEVKRFLKTVGYNPDKVPFIPISGFR---GDNMLERsdnlKWYKgpiLVEAINLCEP-PKRPNDKP 231
Cdd:TIGR00485 139 DMVD-DEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKaleGDAEWEA----KILE---LMDAVDEYIPtPEREIDKP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAGVTTeVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKR 308
Cdd:TIGR00485 211 FLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDNVGLLLRGIKREEIER 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 309 GFVAsdSKNDPAMGAADFLAQVIVLN------HPGEIkNGYAPVLDCHTAHIackfaeirskmdrrTGK-ELEKDPKTIK 381
Cdd:TIGR00485 290 GMVL--AKPGSIKPHTKFEAEVYVLSkeeggrHTPFF-SGYRPQFYFRTTDV--------------TGTiELPEGVEMVM 352
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 677286257 382 SGDAAMVLMQPSKPMVVESFQeypplgRFAVRDMRSTVAVGVIKEV 427
Cdd:TIGR00485 353 PGDNVKMTVELISPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-427 |
1.77e-49 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 174.24 E-value: 1.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 3 KEKVHINLVVIGHVDAGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 EKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKMD---DAG 159
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDvvdDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 160 WAEAryneIQTEVKRFLKTVGYNPDKVPFI---PISGFRGDN-MLERSDNLKwykgpiLVEAINLCEP-PKRPNDKPLRL 234
Cdd:PLN03127 195 LLEL----VEMELRELLSFYKFPGDEIPIIrgsALSALQGTNdEIGKNAILK------LMDAVDEYIPePVRVLDKPFLM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 235 PLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAG-VTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGF 310
Cdd:PLN03127 265 PIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 311 VAsdSKNDPAMGAADFLAQVIVLN------HPGEIKNgYAPVLDCHTAHIackfaeirskmdrrTGK-ELEKDPKTIKSG 383
Cdd:PLN03127 345 VI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADV--------------TGKvELPEGVKMVMPG 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 677286257 384 DAAMVLMQPSKPMVVESFQeypplgRFAVRDMRSTVAVGVIKEV 427
Cdd:PLN03127 408 DNVTAVFELISPVPLEPGQ------RFALREGGRTVGAGVVSKV 445
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
14-314 |
4.92e-45 |
|
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: 165.86 E-value: 4.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 14 GHVDAGKSTttghLIYKCGGIDkrTiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETEKFyCTIID 91
Cdd:COG3276 7 GHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLgfAYLPLPDGRR-LGFVD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 92 APGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREH-ALLAFtLGVKQMIVAVNKMD--DAGWAEary 165
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADlvDEEWLE--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 166 nEIQTEVKRFLKTVGYnpDKVPFIPISGFRGDNMLErsdnlkwykgpiLVEAI-NLCE-PPKRPNDKPLRLPLQDVYKIG 243
Cdd:COG3276 124 -LVEEEIRELLAGTFL--EDAPIVPVSAVTGEGIDE------------LRAALdALAAaVPARDADGPFRLPIDRVFSIK 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677286257 244 GIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVASD 314
Cdd:COG3276 189 GFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAA 259
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-210 |
1.08e-36 |
|
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: 133.09 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 7 HINLVVIGHVDAGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETEKFY 86
Cdd:cd01884 2 HVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 87 CTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQMIVAVNKMD---DAGWAEA 163
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADmvdDEELLEL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 677286257 164 ryneIQTEVKRFLKTVGYNPDKVPFIPISGFRGdnmLERSDNLKWYK 210
Cdd:cd01884 140 ----VEMEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPNKWVD 179
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-312 |
3.26e-36 |
|
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: 140.39 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 8 INLVVIGHVDAGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDIALWKFETEKFYC 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 88 TIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKQMIVAVNKMDDAGwaEAR 164
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRVN--EEE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 165 YNEIQTEVKRFLKTVGYNPDKVPFIpISGFRGDNMLERSDNLKwykgpILVEAINLceppKRPNdKPLRLPLQDVYKIGG 244
Cdd:TIGR00475 121 IKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKELK-----NLLESLDI----KRIQ-KPLRMAIDRAFKVKG 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677286257 245 IGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFVA 312
Cdd:TIGR00475 190 AGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI 257
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
319-427 |
4.63e-32 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 117.75 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 319 PAMGAADFLAQVIVLNH-----PGEIKNGYAPVLDCHTAHIACKFAEIRSKMDrrTGKELEKdPKTIKSGDAAMVLMQPS 393
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 677286257 394 KPMVVESFQeypplgRFAVRDMRSTVAVGVIKEV 427
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
326-424 |
1.32e-26 |
|
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: 102.86 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 326 FLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKEleKDPKTIKSGDAAMVLMQPSKPMVVESFQEYP 405
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 677286257 406 PLGRFAVRDMRSTVAVGVI 424
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-192 |
5.17e-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: 100.76 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 14 GHVDAGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETEKfYCTIID 91
Cdd:cd04171 6 GHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGK-RLGFID 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 92 APGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKQMIVAVNKMD--DAGWAEaryn 166
Cdd:cd04171 57 VPGHEKFVKNMLAGAGGIDAVLLVVA----------ADEGimpQTREHLEILELLGIKKGLVVLTKADlvDEDRLE---- 122
|
170 180
....*....|....*....|....*.
gi 677286257 167 EIQTEVKRFLKTVGYNPdkVPFIPIS 192
Cdd:cd04171 123 LVEEEILELLAGTFLAD--APIFPVS 146
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-388 |
2.89e-23 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 101.08 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKVH--INLVVIGHVDAGKSTttghLIYKCGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI----- 73
Cdd:PRK04000 1 MMWEKVQpeVNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgya 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 74 DIALWK---FETEKFYCT------------------IIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG- 131
Cdd:PRK04000 53 DATIRKcpdCEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIA----------ANEPc 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 132 ---QTREHaLLAFT-LGVKQMIVAVNKMD--DAGWAEARYNEIqtevKRFLKtvGYNPDKVPFIPISGFRGDNMlersDn 205
Cdd:PRK04000 123 pqpQTKEH-LMALDiIGIKNIVIVQNKIDlvSKERALENYEQI----KEFVK--GTVAENAPIIPVSALHKVNI----D- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 206 lkwykgpILVEAI-NLCEPPKRPNDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKPGMVVTFAP 268
Cdd:PRK04000 191 -------ALIEAIeEEIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEEGG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 269 AG----VTTEVKSVEMHHEQLPEANPGdnvgfnvknvsvkelkrGFVASDSKNDPAMGAADFLAQVIVlNHPGEIkngyA 344
Cdd:PRK04000 264 KTkwepITTKIVSLRAGGEKVEEARPG-----------------GLVGVGTKLDPSLTKADALAGSVA-GKPGTL----P 321
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 677286257 345 PVLDchtahiacKFaEIRSK-MDRRTGKELEKDPKTIKSGDAAMV 388
Cdd:PRK04000 322 PVWE--------SL-TIEVHlLERVVGTKEELKVEPIKTGEPLML 357
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
326-427 |
6.66e-21 |
|
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: 87.23 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 326 FLAQVIVLNHPGEI-KNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVVESFQEY 404
Cdd:cd03704 6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
|
90 100
....*....|....*....|...
gi 677286257 405 PPLGRFAVRDMRSTVAVGVIKEV 427
Cdd:cd03704 86 PQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-176 |
1.55e-19 |
|
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: 87.29 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRtiekfekeaaemgkGSfkyawV------LDKLKAERERGITIDIALWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 EKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTRehaLLAFTLgvKQM----IVAVNKM 155
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVIS----------AVEGvqaQTR---ILFRLL--RKLniptIIFVNKI 126
|
170 180
....*....|....*....|.
gi 677286257 156 DDAGwaeARYNEIQTEVKRFL 176
Cdd:cd04168 127 DRAG---ADLEKVYQEIKEKL 144
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
326-427 |
8.68e-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: 81.44 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 326 FLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIRSKMDRRTGKELEKDPKTIKSGDAAMVLMQPSKPMVVESFQEYP 405
Cdd:cd04093 8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKDNK 87
|
90 100
....*....|....*....|..
gi 677286257 406 PLGRFAVRDMRSTVAVGVIKEV 427
Cdd:cd04093 88 ELGRFVLRRGGETIAAGIVTEI 109
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
232-311 |
2.36e-18 |
|
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: 79.23 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNvsVKELKRGFV 311
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-226 |
7.15e-17 |
|
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: 78.46 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 8 INLVVIGHVDAGKSTTTGHLiykcGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 EKFY------------C----------TIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG----QTREH 136
Cdd:cd01888 53 CGCPrpydtpececpgCggetklvrhvSFVDCPGHEILMATMLSGAAVMDGALLLIA----------ANEPcpqpQTSEH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 137 aLLAF-TLGVKQMIVAVNKMDDAGWAEARYNeiQTEVKRFLKTVGYnpDKVPFIPISGFRGDNMlersdnlkwykgPILV 215
Cdd:cd01888 123 -LAALeIMGLKHIIILQNKIDLVKEEQALEN--YEQIKEFVKGTIA--ENAPIIPISAQLKYNI------------DVLC 185
|
250
....*....|..
gi 677286257 216 EAI-NLCEPPKR 226
Cdd:cd01888 186 EYIvKKIPTPPR 197
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
232-311 |
1.28e-16 |
|
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: 74.49 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFV 311
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-207 |
3.97e-16 |
|
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: 76.25 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 8 INLVVIGHVDAGKSTTTghliykcggidkRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDIALWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTSLA------------KALSEIASTAA------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 81 -------ETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGvKQMIV 150
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVD----------AKKGiqtQTAECLVIGELLC-KPLIV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 677286257 151 AVNKMDDAGWAEaRYNEIQTEVKRFLKTVGYNPDK-VPFIPISGFRGDNMLERSDNLK 207
Cdd:cd01889 126 VLNKIDLIPEEE-RKRKIEKMKKRLQKTLEKTRLKdSPIIPVSAKPGEGEAELGGELK 182
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
234-313 |
5.25e-16 |
|
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: 72.94 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 234 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFA--PAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFV 311
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
..
gi 677286257 312 AS 313
Cdd:cd03697 83 LA 84
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-156 |
7.08e-15 |
|
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: 72.57 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRtiekfekeaaEMgkgsfkYAWVLDKLKAERERGITID---IAL-WKFETEK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EM------KEQVLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677286257 85 FYC-TIIDAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTREHALLAFTLGVKqMIVAVNKMD 156
Cdd:cd01890 66 EYLlNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-------VEAQTLANFYLALENNLE-IIPVINKID 130
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
246-311 |
1.55e-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: 68.06 E-value: 1.55e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677286257 246 GTVPVGRVETGVLKPGMVVTFAPAGV-----TTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFV 311
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
231-314 |
3.41e-14 |
|
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: 67.54 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 231 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGF 310
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 677286257 311 VASD 314
Cdd:cd16267 81 ILCD 84
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
14-309 |
8.35e-14 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 73.55 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 14 GHVDAGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--ALWKfETEKFYCTIID 91
Cdd:PRK10512 7 GHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWP-QPDGRVLGFID 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 92 APGHRDFIKNMITGTSQADLAILVIASGTGEFeagfakeGQTREH-ALLAFTlGVKQMIVAVNKMDDAgwAEARYNEIQT 170
Cdd:PRK10512 58 VPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRV--DEARIAEVRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 171 EVKRFLKTVGYnpDKVPFIPISGFRGDNMLERSDNLKwykgpilveainLCEPPKRPNDKPLRLPLQDVYKIGGIGTVPV 250
Cdd:PRK10512 128 QVKAVLREYGF--AEAKLFVTAATEGRGIDALREHLL------------QLPEREHAAQHRFRLAIDRAFTVKGAGLVVT 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 677286257 251 GRVETGVLKPGMvvTFAPAGVTTEVKSVEMH--HEQLPEANPGDNVGFNVK-NVSVKELKRG 309
Cdd:PRK10512 194 GTALSGEVKVGD--TLWLTGVNKPMRVRGLHaqNQPTEQAQAGQRIALNIAgDAEKEQINRG 253
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-265 |
2.05e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 72.05 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRTiEKFEKeaaemgkgsfkyawVLDKLKAERERGITIDIALWKFETEKFYCT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 89 IIDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEagfakegQTREHALLAFTLGVKQmIVAVNKMDDAGwaeARYNEI 168
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKP-IVVINKVDRPG---ARPDWV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 169 QTEVKRFLKTVGYNPDKV--PFIPISGFRGDNMLERSDnLKWYKGPILVEAINLCEPPKRPNDKPLRLPLQDVYKIGGIG 246
Cdd:PRK10218 141 VDQVFDLFVNLDATDEQLdfPIVYASALNGIAGLDHED-MAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVG 219
|
250
....*....|....*....
gi 677286257 247 TVPVGRVETGVLKPGMVVT 265
Cdd:PRK10218 220 VIGIGRIKRGKVKPNQQVT 238
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-156 |
2.83e-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: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIdkrtiekFEKEAaemgkGSFKYawvLDKLKAERERGITID---IALwKFETEK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 85 ------FYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTreHALL--AFTLGVKqMIVAVN 153
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVD----------AVEGvcvQT--ETVLrqALEERVK-PVLVIN 132
|
...
gi 677286257 154 KMD 156
Cdd:cd01885 133 KID 135
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-196 |
2.85e-13 |
|
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: 72.00 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITIDIAL----WKfeTEK 84
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAAttceWK--GHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 85 FycTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTrEHALlaftlgvKQM-------IVAVNKMDD 157
Cdd:COG0480 76 I--NIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQT-ETVW-------RQAdkygvprIVFVNKMDR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 677286257 158 AGwaeARYNEIQTEVKRFLKTvgyNPdkVPF-IPI---SGFRG 196
Cdd:COG0480 139 EG---ADFDRVLEQLKERLGA---NP--VPLqLPIgaeDDFKG 173
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-159 |
6.63e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 70.75 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKR-TIEKFEKEAaemgkgsfkyawvlDKLKAERERGITIDIAL----WKfete 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 677286257 84 KFYCTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTREHALLAFTLGVKQMIVaVNKMDDAG 159
Cdd:PRK13351 72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-------VQPQTETVWRQADRYGIPRLIF-INKMDRVG 139
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
231-311 |
3.39e-12 |
|
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: 61.73 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 231 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGF 310
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 677286257 311 V 311
Cdd:cd04089 79 V 79
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-177 |
3.76e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 68.23 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 13 IGHVDAGKSTTTGHLIYKCGGIDKR-TIEkfEKEAaemgkgsfkyawVLDKLKAERERGITIDIALWKFETEKFYCTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 92 APGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTRehALLAFT--LGVKQMIVaVNKMDDAGwaeARYNEIQ 169
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMDRAG---ADFFRVL 133
|
....*...
gi 677286257 170 TEVKRFLK 177
Cdd:PRK12740 134 AQLQEKLG 141
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-302 |
5.21e-12 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 67.74 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 7 HI-NLVVIGHVDAGKSTTTGHLIYKCGGIDKRtiekfekeaaEMGkgsfkyAWVLDKLKAERERGITID---IAL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 82 T-EKFYCTIIDAPGHRDFiknmitgT---SQAdL-----AILVIASGTGeFEAgfakegQTREHALLAFTLGVKqmIVAV 152
Cdd:COG0481 69 DgETYQLNLIDTPGHVDF-------SyevSRS-LaacegALLVVDASQG-VEA------QTLANVYLALENDLE--IIPV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 153 -NKMDDAGwaeARYNEIQTEVKrflKTVGYNPDKVpfIPISGFRG---DNMLERsdnlkwykgpiLVEAINlcePPKRPN 228
Cdd:COG0481 132 iNKIDLPS---ADPERVKQEIE---DIIGIDASDA--ILVSAKTGigiEEILEA-----------IVERIP---PPKGDP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 229 DKPLRlPL-----QDVYKiggiGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSV---EMHHEQLPEANPGDnVGF---N 297
Cdd:COG0481 190 DAPLQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvfTPKMTPVDELSAGE-VGYiiaG 263
|
....*
gi 677286257 298 VKNVS 302
Cdd:COG0481 264 IKDVR 268
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-173 |
1.11e-11 |
|
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: 64.92 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKR-TIEKfekeaaemgkGSFkyawVLDKLKAERERGITIDIALWKFETEKFYC 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 88 TIIDAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTREHALLAFTLGVKQMIVaVNKMDDAGwaeARYNE 167
Cdd:cd04170 67 NLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMDRAR---ADFDK 135
|
....*.
gi 677286257 168 IQTEVK 173
Cdd:cd04170 136 TLAALR 141
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-292 |
1.43e-10 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 63.12 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRtiekfeKEAAEMgkgsfkyawVLDKLKAERERGITIdiaLWKfetekfyCT 88
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK-------NT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 89 ----------IIDAPGHRDF------IKNMitgtsqADLAILVIAsgtgefeagfAKEG---QTR---EHALlafTLGVK 146
Cdd:COG1217 63 avrykgvkinIVDTPGHADFggeverVLSM------VDGVLLLVD----------AFEGpmpQTRfvlKKAL---ELGLK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 147 qMIVAVNKMDDAGwaeARYNEIQTEVKRFLKTVGYNPDKVPFiPI------SGFRGDNMLERSDNLKwykgPILvEAI-N 219
Cdd:COG1217 124 -PIVVINKIDRPD---ARPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDLT----PLF-DTIlE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 220 LCEPPKRPNDKPLRlpLQ------DVYkIGGIGtvpVGRVETGVLKPGM-VVTFAPAGVTTEVKSVEMH-HEQL-----P 286
Cdd:COG1217 194 HVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQqVALIKRDGKVEKGKITKLFgFEGLervevE 267
|
....*.
gi 677286257 287 EANPGD 292
Cdd:COG1217 268 EAEAGD 273
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
12-199 |
2.95e-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: 59.02 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 12 VIGHVDAGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDIALWKFETEKFY 86
Cdd:cd01887 5 VMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDVKI 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 87 --CTIIDAPGHRDFiKNMIT-GTSQADLAILVIAsgtgefeagfAKEG---QTRE---HALLAFTlgvkQMIVAVNKMDd 157
Cdd:cd01887 49 pgITFIDTPGHEAF-TNMRArGASVTDIAILVVA----------ADDGvmpQTIEainHAKAANV----PIIVAINKID- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 677286257 158 agwAEARYNEIQTEVKRFLKTVGYNPD----KVPFIPISGFRGDNM 199
Cdd:cd01887 113 ---KPYGTEADPERVKNELSELGLVGEewggDVSIVPISAKTGEGI 155
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
231-314 |
8.26e-10 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 55.20 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 231 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMH-HEQLPEANPGDNVGFNVKNVSVKELKRG 309
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 677286257 310 FVASD 314
Cdd:cd03698 80 DILSS 84
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
8.58e-10 |
|
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: 59.43 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITIDIALWKFETEKFYCT 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IGEVHGGGATM-----------DWMEQERERGITIQSAATTCFWKDHRIN 67
|
90
....*....|
gi 677286257 89 IIDAPGHRDF 98
Cdd:cd01886 68 IIDTPGHVDF 77
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-207 |
1.46e-09 |
|
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: 57.22 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGidkrtiekfEKEAAEMGKGsfkyawVLDKLKAERERGITIdiaLWKfETEKFY-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 87 --CTIIDAPGHRDF------IKNMitgtsqADLAILVIAsgtgefeagfAKEG---QTREHALLAFTLGVKqMIVAVNKM 155
Cdd:cd01891 65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVD----------ASEGpmpQTRFVLKKALEAGLK-PIVVINKI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 677286257 156 DDAGwaeARYNEIQTEVKRFLKTVGYNPDKVPFiPI------SGFRGDNMLERSDNLK 207
Cdd:cd01891 128 DRPD---ARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLD 181
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-156 |
2.74e-09 |
|
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: 57.61 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 12 VIGHVDAGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYAwVLDKLKAERERGITIDIALWKFETEKFYCTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 677286257 91 DAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTRehallaftlgvKQMIVA----------VNKMD 156
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-------VEPQTR-----------KLFEVCrlrgipiitfINKLD 134
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
232-296 |
3.40e-09 |
|
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: 53.34 E-value: 3.40e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 677286257 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGVTTEVKSVEMHHEQLPEANPGDNVGF 296
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
238-311 |
1.13e-08 |
|
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: 52.22 E-value: 1.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677286257 238 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAG----VTTEVKSVEMHHEQLPEANPGDNVGFNVKNVSVKELKRGFV 311
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-337 |
7.69e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 54.24 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 8 INLVVIGHVDAGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITIDIA-----LWKFET 82
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLGyanakIYKCPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 83 ---------------EKFYC-------------TIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG--- 131
Cdd:PTZ00327 87 cprptcyqsygsskpDNPPCpgcghkmtlkrhvSFVDCPGHDILMATMLNGAAVMDAALLLIA----------ANEScpq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 132 -QTREHALLAFTLGVKQMIVAVNKMDDAGWAEA--RYNEIqtevKRFLKtvGYNPDKVPFIPISGFRGDNMlersDNLKW 208
Cdd:PTZ00327 157 pQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAqdQYEEI----RNFVK--GTIADNAPIIPISAQLKYNI----DVVLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 209 YkgpiLVEAINLcepPKRPNDKPLRLPLQ---DVYKIGG-----IGTVPVGRVETGVLK--------PGMVVTFAPAGVT 272
Cdd:PTZ00327 227 Y----ICTQIPI---PKRDLTSPPRMIVIrsfDVNKPGEdienlKGGVAGGSILQGVLKvgdeieirPGIISKDSGGEFT 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 677286257 273 -----TEVKSVEMHHEQLPEANPGdnvgfnvknvsvkelkrGFVASDSKNDPAMGAADFL-AQviVLNHPG 337
Cdd:PTZ00327 300 crpirTRIVSLFAENNELQYAVPG-----------------GLIGVGTTIDPTLTRADRLvGQ--VLGYPG 351
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
12-199 |
9.70e-08 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 54.45 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 12 VIGHVDAGKSTTtghliykcggIDK-RTIEKFEKEAAemgkgsfkyawvldklkaererGITIDIA----LWKFETEKFY 86
Cdd:CHL00189 249 ILGHVDHGKTTL----------LDKiRKTQIAQKEAG----------------------GITQKIGayevEFEYKDENQK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 87 CTIIDAPGHRDFIKNMITGTSQADLAILVIASGTGefeagfaKEGQTREhALLAFTLGVKQMIVAVNKMDDAGwaeARYN 166
Cdd:CHL00189 297 IVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKAN---ANTE 365
|
170 180 190
....*....|....*....|....*....|....*....
gi 677286257 167 EIQTEVkrflktVGYN--PDK----VPFIPISGFRGDNM 199
Cdd:CHL00189 366 RIKQQL------AKYNliPEKwggdTPMIPISASQGTNI 398
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
9.80e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 54.28 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 1 MGKEKVHINLVVIGHVDAGKSTTTGHLIYKCGGIDkrtiekfEKEAAEmgkgsfkyAWVLDKLKAERERGITID---IAL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*....
gi 677286257 78 WkFE--------TEKFYCTIIDAPGHRDF 98
Cdd:PTZ00416 78 Y-YEhdledgddKQPFLINLIDSPGHVDF 105
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-156 |
5.82e-07 |
|
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: 49.96 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKcggidkrtIEKFEKEAAEMGKgSFKYawvLDKLKAERERGITI-----DIALWKFETE 83
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ--------THKRTPSVKLGWK-PLRY---TDTRKDEQERGISIksnpiSLVLEDSKGK 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 677286257 84 KFYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEGQTREHALL---AFTLGVKqMIVAVNKMD 156
Cdd:cd04167 70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVD----------VVEGLTSVTERLirhAIQEGLP-MVLVINKID 134
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-201 |
1.57e-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: 47.84 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 11 VVIGHVDAGKSTTTGHLIYKcggidkrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDIALWKFETEKFYC--T 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVYVKELDKGKVklV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 89 IIDAPGHRDFIKNMITGT-----SQADLAILVIASGTGEFEagfakEGQTREHALLAFTLGVKqMIVAVNKMDDAGWAEA 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESE-----EDAKLLILRRLRKEGIP-IILVGNKIDLLEEREV 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 677286257 164 RYNEIQTEVKRFLktvgynpdKVPFIPISGFRGDNMLE 201
Cdd:cd00882 125 EELLRLEELAKIL--------GVPVFEVSAKTGEGVDE 154
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-98 |
2.25e-06 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 49.86 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRTiekfekeAAEmgkgsfkyAWVLDKLKAERERGITIDIA----LWKFETEK 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
|
90
....*....|....
gi 677286257 85 FYCTIIDAPGHRDF 98
Cdd:PRK07560 87 YLINLIDTPGHVDF 100
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-201 |
5.76e-06 |
|
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: 46.21 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 8 INLVVIGHVDAGKSTTTGHLIYKCGGIDkrtiekfekeaaEMGKGSFKYAWVLdklkAERERGITIDIALWkfetekfyc 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT------------EYYPGTTRNYVTT----VIEEDGKTYKFNLL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 88 tiiDAPGHRDFIKNMITGTSQADLAILVIASGTGEFEAGFAKEGQTREHALLAfTLGVKqMIVAVNKMDdagwaeARYNE 167
Cdd:TIGR00231 57 ---DTAGQEDYDAIRRLYYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVP-IILVGNKID------LKDAD 125
|
170 180 190
....*....|....*....|....*....|....
gi 677286257 168 IQTEVKRFLKTVGYNpdkvPFIPISGFRGDNMLE 201
Cdd:TIGR00231 126 LKTHVASEFAKLNGE----PIIPLSAETGKNIDS 155
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-98 |
2.68e-05 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 46.64 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 9 NLVVIGHVDAGKSTTTGHLIYKCGGIdkrtiekfEKEAAemgkGSFKYAwvlDKLKAERERGITI------------DIA 76
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGII--------AQEVA----GDVRMT---DTRADEAERGITIkstgislyyemtDES 85
|
90 100
....*....|....*....|....*.
gi 677286257 77 LWKFETEK----FYCTIIDAPGHRDF 98
Cdd:PLN00116 86 LKDFKGERdgneYLINLIDSPGHVDF 111
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
70-156 |
2.34e-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: 43.46 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 70 GITIDIALWKFETEKFYCTIIDAPGHRDFIKNMITGTSQADLAILVIAsgtgefeagfAKEG---QTRE---HALLAftl 143
Cdd:COG0532 36 GITQHIGAYQVETNGGKITFLDTPGHEAFTAMRARGAQVTDIVILVVA----------ADDGvmpQTIEainHAKAA--- 102
|
90
....*....|...
gi 677286257 144 GVKqMIVAVNKMD 156
Cdd:COG0532 103 GVP-IIVAINKID 114
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
326-427 |
3.46e-04 |
|
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: 39.42 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 326 FLAQVIVLNHPGEIKNGYAPVLDCHTAHIACKFAEIrskmdrrtgkelekDPKTIKSGDAAMVLM----QPskpmvvesf 401
Cdd:cd03708 6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISI--------------DKEVLRTGDRALVRFrflyRP--------- 62
|
90 100
....*....|....*....|....*..
gi 677286257 402 qEYPPLG-RFAVRDMRsTVAVGVIKEV 427
Cdd:cd03708 63 -EYLREGqRLIFREGR-TKGIGTVTKV 87
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-201 |
7.98e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 40.35 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 8 INLVVIGHVDAGKSTttghLIYKcggidkrtiekfekeaaemgkgsFKYAWVlDKLKAERERGITIDIALWKFETEKFYC 87
Cdd:COG1100 4 KKIVVVGTGGVGKTS----LVNR-----------------------LVGDIF-SLEKYLSTNGVTIDKKELKLDGLDVDL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 88 TIIDAPGHRDFIK---NMITGTSQADLAILVIAsgtGEFEAGFAKEgqtREHALLAFTLGVK-QMIVAVNKMDdagwaea 163
Cdd:COG1100 56 VIWDTPGQDEFREtrqFYARQLTGASLYLFVVD---GTREETLQSL---YELLESLRRLGKKsPIILVLNKID------- 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 677286257 164 RYNEIQTEVKRFLKTVGYNPDKVPFIPISGFRGDNMLE 201
Cdd:COG1100 123 LYDEEEIEDEERLKEALSEDNIVEVVATSAKTGEGVEE 160
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
326-427 |
9.19e-04 |
|
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: 38.37 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677286257 326 FLAQVIVLN------HPGeIKNGYAPVLDCHTAHIACKFaeirskmDRRTGKELekdpktIKSGDAAMVLMQPSKPMVVE 399
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRI-------DLPEGKEM------VMPGEDTSVKLTLLKPMVLE 71
|
90 100
....*....|....*....|....*...
gi 677286257 400 SFQeypplgRFAVRDMRSTVAVGVIKEV 427
Cdd:cd03706 72 KGQ------RFTLREGGRTIGTGVVTKL 93
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
237-311 |
1.35e-03 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 37.27 E-value: 1.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 677286257 237 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfAPAGVTTeVKSVEMHHEQLPEANPGDNVGFNVKNVSvkELKRGFV 311
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKGVAL-IRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
|
|
| |
