|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-460 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 911.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 161 PYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 321 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 460
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-457 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 714.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 161 PYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGwkvtrkdgnasgTTLLEALDCILPPTR 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 321 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 14422440 401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQK 457
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-444 |
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: 687.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagisKNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 161 pYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 321 RRGNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 14422440 401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 444
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-445 |
0e+00 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 682.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 161 pYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 321 RRGNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:COG5256 300 KRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 14422440 401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKA 445
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-444 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 674.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEppY 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 163 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPT 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRR 322
Cdd:PRK12317 223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 323 GNVAGdSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIV 402
Cdd:PRK12317 303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 14422440 403 DMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 444
Cdd:PRK12317 382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPA 423
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-238 |
1.48e-159 |
|
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: 449.63 E-value: 1.48e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYE 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 169 EIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWkvtrkdgnasgtTLLEALDCILPP 238
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-447 |
1.82e-93 |
|
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: 289.29 E-value: 1.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 4 EKTHINIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFE 81
Cdd:COG2895 14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 82 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTE 159
Cdd:COG2895 92 TPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDArkGVLE---------QTRRHSYIASLLGIRHVVVAVNKMDLVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 160 ppYSQKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPT 239
Cdd:COG2895 163 --YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 240 RPTDKPLRLPLQDVYKiggigtvP-------VGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGF-- 310
Cdd:COG2895 227 DRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 311 --NVknvsvkDVRRGNVAGDSkNDPPMEAAGFTAQVIILN-HPGQISAGYapVLDCHTAHIACKFAELKEKIDRRSGKKL 387
Cdd:COG2895 300 edEI------DISRGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHE 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14422440 388 EdgPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVIKAVDKKAAG 447
Cdd:COG2895 371 A--ADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGALRRAAN 430
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-238 |
2.71e-77 |
|
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: 238.96 E-value: 2.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGVKqLIVGVNKMDSTeppySQ 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14422440 165 KRYEEIVKEVS-TYIKKIGYNPDTVAFVPISGWNGDNMlepsanmpwfkgwkvtrkdgnasgTTLLEALDCILPP 238
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
335-438 |
5.41e-74 |
|
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: 227.46 E-value: 5.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 335 MEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVES 414
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 14422440 415 FSDYPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-235 |
3.30e-61 |
|
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: 198.56 E-value: 3.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAAEMGKgsFKYAWVLDKLKAERERGITIDISLWKFETSKY 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYS 163
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDArkGVLE---------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14422440 164 QKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCI 235
Cdd:cd04166 148 EEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
242-332 |
4.34e-61 |
|
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: 193.94 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 321
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 14422440 322 RGNVAGDSKND 332
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-438 |
5.29e-61 |
|
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: 204.14 E-value: 5.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGK--GSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 92 APGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYSQKRYEEIV 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 172 KEVSTYIKKIGynPDTVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPLRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 252 DVYKI-----GGIGTVPVGRVetgvlKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVRRGN-- 324
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSV-----HVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDll 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 325 VAGDSkndPPMEAAGFTAQVIIL-NHPgqISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEdgPKFLKSGDAAIVD 403
Cdd:TIGR02034 297 AAADS---APEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGA--AKSLELNEIGRVN 369
|
410 420 430
....*....|....*....|....*....|....*..
gi 14422440 404 MVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 370 LSLDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-462 |
5.31e-59 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 204.39 E-value: 5.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMG--KGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 92 APGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYSQKRYEE 169
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDArkGVLT---------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 170 IVKEVSTYIKKIGYNpdTVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPLRLP 249
Cdd:PRK05506 180 IVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 250 LQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVgfnvkNVSVKD---VR 321
Cdd:PRK05506 246 VQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidIS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 322 RGNVAGDSkNDPPMEAAGFTAQVIILN----HPGqisAGYapVLDCHTAHIACKFAELKEKIDRRSgkkLEDGP-KFLKS 396
Cdd:PRK05506 316 RGDMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAaKTLEL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14422440 397 GDAAIVDMVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVIKAVDKKAAG----AGKVTK---SAQKAQKAK 462
Cdd:PRK05506 387 NEIGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIDFALRRATNvhwqASDVSRearAARKGQKPA 461
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-325 |
9.31e-58 |
|
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: 195.37 E-value: 9.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 156 DSTEPPYSQKRYEEIVKE-VSTYikkiGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEALD 233
Cdd:COG0050 139 DMVDDEELLELVEMEVRElLSKY----GFPGDDTPIIRGSALKA---LEGDPDPEWEKKiLE------------LMDAVD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 234 CILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPvNVTTEVKSVEMHHEALSEALPGDNVG 309
Cdd:COG0050 200 SYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVG 278
|
330
....*....|....*.
gi 14422440 310 FNVKNVSVKDVRRGNV 325
Cdd:COG0050 279 LLLRGIKREDVERGQV 294
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-345 |
5.75e-57 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 195.52 E-value: 5.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 14 GHVDSGKSTTTGHLIYkcggiDKRTIekFEKEAAEMGKGSFK---------YAWVLDKLKAERERGITIDISLWKFETSK 84
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYSQ 164
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 165 KRYEEIVKEVSTYIKKIGYNPDtVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDK 244
Cdd:PRK05124 178 EVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 245 PLRLPLQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkD 319
Cdd:PRK05124 245 PFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--D 317
|
330 340
....*....|....*....|....*.
gi 14422440 320 VRRGNVAGDSKNDPPMeAAGFTAQVI 345
Cdd:PRK05124 318 ISRGDLLVAADEALQA-VQHASADVV 342
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-443 |
1.54e-56 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 192.08 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLiykcggidkrtiekfEKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 156 DSTEPPYSQKRYEEIVKE-VSTYikkiGYNPDTVAFVPISGW---NGDNMLEPSANmpwfkgwkvtrkdgnasgtTLLEA 231
Cdd:PRK12736 139 DLVDDEELLELVEMEVRElLSEY----DFPGDDIPVIRGSALkalEGDPKWEDAIM-------------------ELMDA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 232 LDCILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVnVTTEVKSVEMHHEALSEALPGDN 307
Cdd:PRK12736 196 VDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDN 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 308 VGFNVKNVSVKDVRRGNVAGDSKNDPPmeAAGFTAQVIILN------HPGqISAGYAPVLDCHTAhiackfaelkekiDR 381
Cdd:PRK12736 275 VGVLLRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYILTkeeggrHTP-FFNNYRPQFYFRTT-------------DV 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14422440 382 RSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAVDK 443
Cdd:PRK12736 339 TGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGL------KFAIREGGRTVGAGTVTEILD 394
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-325 |
8.35e-56 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 190.40 E-value: 8.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFK-YAWVlDKLKAERERGITID 74
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITIN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 75 ISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNK 154
Cdd:PRK00049 65 TAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 155 MDSTEPPysqkryE--EIVK-EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLE 230
Cdd:PRK00049 138 CDMVDDE------EllELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLE------------LMD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 231 ALDCILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHEALSEALPGD 306
Cdd:PRK00049 197 AVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGD 275
|
330
....*....|....*....
gi 14422440 307 NVGFNVKNVSVKDVRRGNV 325
Cdd:PRK00049 276 NVGALLRGIKREDVERGQV 294
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-325 |
1.51e-53 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 184.27 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 156 DSTEPPysqkryE--EIVK-EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEA 231
Cdd:PRK12735 139 DMVDDE------EllELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLE------------LMDA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 232 LDCILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHEALSEALPGDN 307
Cdd:PRK12735 198 VDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDN 276
|
330
....*....|....*...
gi 14422440 308 VGFNVKNVSVKDVRRGNV 325
Cdd:PRK12735 277 VGVLLRGTKREDVERGQV 294
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-203 |
2.26e-53 |
|
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: 177.10 E-value: 2.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaaemgkgsfkyaWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAyTLGVKQLIVGVNKMDSTeppySQKRYE 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRV----GEEDFD 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 14422440 169 EIVKEVSTYIKKIGY---NPDTVAFVPISGWNGDNMLE 203
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-441 |
3.62e-52 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 182.89 E-value: 3.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppy 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 163 SQKRYEEIVKEVSTYIKKIGYNPDTvafVPISGWNGDNMLEPSANMPwfkgwKVTRKDGNASGTT--LLEALDCILP-PT 239
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 240 RPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHEALSEALPGDNVGFNVKNVSV 317
Cdd:PLN03126 284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 318 KDVRRGNVAGDSKNDPPMEAagFTAQVIILNHP--GQIS---AGYAPVLDCHTAHIACKFAELKEKIDRRSgkkledgpK 392
Cdd:PLN03126 364 ADIQRGMVLAKPGSITPHTK--FEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------K 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 14422440 393 FLKSGDAA--IVDMVpgKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 441
Cdd:PLN03126 434 MVMPGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-438 |
4.13e-52 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 180.92 E-value: 4.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAWVlDKLKAERERGITIDISLWKFET 82
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPy 162
Cdd:CHL00071 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVDDE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 163 sqKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANM-----PWFKgwKVtrkdgnasgTTLLEALDCILP 237
Cdd:CHL00071 145 --ELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgenKWVD--KI---------YNLMDAVDSYIP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 238 -PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHEALSEALPGDNVGFNVKN 314
Cdd:CHL00071 212 tPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETktTTVTGLEMFQKTLDEGLAGDNVGILLRG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 315 VSVKDVRRGNVAGDSKNDPPMeaAGFTAQVIILN------HPGqISAGYAPVLDCHTAHIACKFaelkekidrrsgkkle 388
Cdd:CHL00071 292 IQKEDIERGMVLAKPGTITPH--TKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKI---------------- 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 14422440 389 dgpKFLKSGDAAIVDMV-PGK--PMCVESFSdypPLG-----RFAVRDMRQTVAVGVI 438
Cdd:CHL00071 353 ---ESFTADDGSKTEMVmPGDriKMTVELIY---PIAiekgmRFAIREGGRTVGAGVV 404
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-441 |
1.62e-51 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 180.41 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPY 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 163 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNmlepsanmpwfkgwkvtRKDGNASGTTLLEALDCILP-PTRP 241
Cdd:PLN03127 195 LLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTN-----------------DEIGKNAILKLMDAVDEYIPePVRV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAP-VNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSV 317
Cdd:PLN03127 258 LDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 318 KDVRRGNVAgdSKNDPPMEAAGFTAQVIILN------HPGQISaGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGP 391
Cdd:PLN03127 338 EDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFS-NYRPQFYLRTADVTGKV-------------ELPEGV 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 14422440 392 KFLKSGDAAIVDMVPGKPMCVEsfsdypPLGRFAVRDMRQTVAVGVIKAV 441
Cdd:PLN03127 402 KMVMPGDNVTAVFELISPVPLE------PGQRFALREGGRTVGAGVVSKV 445
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-441 |
2.44e-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: 173.04 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:TIGR00485 8 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPY 162
Cdd:TIGR00485 73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 163 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnASGTTLLEALDCILP-PTRP 241
Cdd:TIGR00485 146 LLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWE-------------------AKILELMDAVDEYIPtPERE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTE--VKSVEMHHEALSEALPGDNVGFNVKNVSVKD 319
Cdd:TIGR00485 207 IDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKttVTGVEMFRKELDEGRAGDNVGLLLRGIKREE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 320 VRRGNVAGDSKNDPPMEAagFTAQVIILN------HPGQISaGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGPKF 393
Cdd:TIGR00485 287 IERGMVLAKPGSIKPHTK--FEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDVTGTI-------------ELPEGVEM 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 14422440 394 LKSGD--AAIVDMVpgKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 441
Cdd:TIGR00485 351 VMPGDnvKMTVELI--SPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-325 |
3.30e-37 |
|
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: 143.90 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFE-TSKYY 86
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLGFAYLPlPDGRR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREH-ALLAyTLGVKQLIVGVNKMDSTEPPys 163
Cdd:COG3276 53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAdeGVMP---------QTREHlAILD-LLGIKRGIVVLTKADLVDEE-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 164 qkRYEEIVKEVSTYIKkiGYNPDTVAFVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnasgttLLEALDCIL--PPTRP 241
Cdd:COG3276 121 --WLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEGIDE------------------------LRAALDALAaaVPARD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 321
Cdd:COG3276 173 ADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIE 252
|
....
gi 14422440 322 RGNV 325
Cdd:COG3276 253 RGDV 256
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
333-441 |
1.45e-35 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 127.38 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 333 PPMEAAGFTAQVIILNH-----PGQISAGYAPVLDCHTAHIACKFAELKEKIDrrSGKKLEDgPKFLKSGDAAIVDMVPG 407
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 14422440 408 KPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 441
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-323 |
1.76e-33 |
|
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: 133.07 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFETSKYYV 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDSTEppysqkry 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDA-----DEGVMT--QTGEHLAVLDLLGIPHTIVVITKADRVN-------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 168 EEIVKEVSTYIKKIgynpdtvafvpisgwngdnmLEPSANMPWFKGWKVTRKDGNASG------TTLLEALDcilppTRP 241
Cdd:TIGR00475 118 EEEIKRTEMFMKQI--------------------LNSYIFLKNAKIFKTSAKTGQGIGelkkelKNLLESLD-----IKR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 321
Cdd:TIGR00475 173 IQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLK 252
|
..
gi 14422440 322 RG 323
Cdd:TIGR00475 253 RG 254
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-238 |
2.84e-33 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 124.23 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 6 THINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKY 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPysqk 165
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVDDE---- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14422440 166 ryE--EIVK-EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKgwKVtrkdgnasgTTLLEALDCILPP 238
Cdd:cd01884 135 --EllELVEmEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPNKWVD--KI---------LELLDALDSYIPT 194
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
337-438 |
7.29e-31 |
|
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: 114.80 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 337 AAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKleDGPKFLKSGDAAIVDMVPGKPMCVESFS 416
Cdd:cd01513 3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGK 80
|
90 100
....*....|....*....|..
gi 14422440 417 DYPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513 81 EFPTLGRFALRDGGRTVGAGLI 102
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
340-438 |
8.58e-26 |
|
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: 101.09 E-value: 8.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 340 FTAQVIILNHPGQI-SAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDY 418
Cdd:cd03704 6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
|
90 100
....*....|....*....|
gi 14422440 419 PPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03704 86 PQLGRFTLRDEGKTIAIGKV 105
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-199 |
6.98e-25 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 100.37 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETSKYyV 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFayLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDSTEPPysqkRY 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RL 121
|
170 180 190
....*....|....*....|....*....|..
gi 14422440 168 EEIVKEVSTYIKKIGYNPDTVafVPISGWNGD 199
Cdd:cd04171 122 ELVEEEILELLAGTFLADAPI--FPVSSVTGE 151
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
340-441 |
4.89e-19 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 82.21 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 340 FTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYP 419
Cdd:cd04093 8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKDNK 87
|
90 100
....*....|....*....|..
gi 14422440 420 PLGRFAVRDMRQTVAVGVIKAV 441
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 ... |
246-325 |
6.88e-19 |
|
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: 80.77 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNvsVKDVRRGNV 325
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-238 |
1.73e-17 |
|
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: 81.12 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAaemgkGSFKYawvLDKLKAERERGITID---ISLwKFETSK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 ------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTreHALL--AYTLGVKQLIVgVNK 154
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAveGVCV---------QT--ETVLrqALEERVKPVLV-INK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 155 MD------STEPPYSQKRYEEIVKEVSTYIKKIG---YNPDTVAFVPISGwngdNMLEPSAnmpwFKGWKVTRKDGNASG 225
Cdd:cd01885 134 IDrlilelKLSPEEAYQRLLRIVEDVNAIIETYApeeFKQEKWKFSPQKG----NVAFGSA----LDGWGFTIIKFADIY 205
|
250
....*....|...
gi 14422440 226 TTLLEALDCILPP 238
Cdd:cd01885 206 AVLEMVVKHLPSP 218
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-335 |
1.10e-16 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 81.82 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DISLWK--- 79
Cdd:PRK04000 10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKcpd 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 80 FETSKYYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN-----GQTREH 136
Cdd:PRK04000 62 CEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAA-----------NepcpqPQTKEH 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 137 ALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTyikkigynpdTVA----FVPISGWNGDNMlepsanmpwfk 212
Cdd:PRK04000 131 LMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKG----------TVAenapIIPVSALHKVNI----------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 213 gwkvtrkDgnasgtTLLEALDCILP-PTRPTDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKPG 275
Cdd:PRK04000 190 -------D------ALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPG 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14422440 276 MVVTFAP----VNVTTEVKSVEMHHEALSEALPGDNVGFNVK---NVSVKDVRRGNVAGDSKNDPPM 335
Cdd:PRK04000 257 IKVEEGGktkwEPITTKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPPV 323
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-323 |
2.18e-16 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 81.60 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMGkgsfkyAWVLDKLKAERERGITID---ISL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 82 TSKYYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAA--GVgefEAgiskngQTREHALLAYTLGVKQLIVg 151
Cdd:COG0481 69 DGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDAsqGV---EA------QTLANVYLALENDLEIIPV- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 152 VNKMD--STEPpysqkryEEIVKEVstyIKKIGYNPDTVafVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnasgttLL 229
Cdd:COG0481 132 INKIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSAKTGIGIEE------------------------IL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 230 EAL-DCILPPTRPTDKPLRlPL-----QDVYKiggiGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSV-----EMHH-E 297
Cdd:COG0481 176 EAIvERIPPPKGDPDAPLQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvftpKMTPvD 250
|
330 340
....*....|....*....|....*....
gi 14422440 298 ALSealPGDnVGF---NVKNvsVKDVRRG 323
Cdd:COG0481 251 ELS---AGE-VGYiiaGIKD--VRDARVG 273
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-156 |
3.37e-16 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 77.66 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaemgkGSfkyawV------LDKLKAERERGITIDISLWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14422440 83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTRE--HALLAYTLGVkqlIVGVNKMD 156
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAveGV---------QAQTRIlfRLLRKLNIPT---IIFVNKID 127
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
248-325 |
5.94e-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: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 248 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN--VTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKetLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-198 |
1.04e-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: 74.88 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMgkgsfkYAWVLDKLKAERERGITID---ISL-WKFETSK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EM------KEQVLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 YYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGVGeFEAgiskngQTREHALLAYTLGVKQLIVgVNKMD--STE 159
Cdd:cd01890 66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDlpAAD 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 14422440 160 PPYSQKRYEEIvkevstyikkIGYNPDTVafVPISGWNG 198
Cdd:cd01890 136 PDRVKQEIEDV----------LGLDASEA--ILVSAKTG 162
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
246-325 |
1.70e-15 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 71.40 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
260-325 |
1.30e-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: 68.45 E-value: 1.30e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14422440 260 GTVPVGRVETGVLKPGMVVTFAPVNV-----TTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-212 |
2.90e-14 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 71.09 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAAEMGKGsfkyawVLDKLKAERERGITIdisLWKfETSKYY-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEAGISkngQTR---EHALLAytlGVKqLIVGVNKM 155
Cdd:cd01891 65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDA----SEGPMP---QTRfvlKKALEA---GLK-PIVVINKI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14422440 156 DSteppySQKRYEEIVKEVSTYIKKIGYNPDTVAFvPI------SGWNGDNMLEPSANM-PWFK 212
Cdd:cd01891 128 DR-----PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLdPLFE 185
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-203 |
4.01e-14 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 70.76 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTTTGHLiykcGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DISLWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 83 SKYY----------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN-----GQTRE 135
Cdd:cd01888 53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSE 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14422440 136 HALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKevstYIKkiGYNPDTVAFVPIS---GWNGDNMLE 203
Cdd:cd01888 122 HLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVK--GTIAENAPIIPISaqlKYNIDVLCE 186
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-194 |
6.15e-14 |
|
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: 70.09 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTTTghliykcggidkRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDISLWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTSLA------------KALSEIASTAA------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 81 -------ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGvKQLIVGVN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14422440 154 KMDSTePPYSQKRYEEIVKEV--STYIKKIGYNpdtVAFVPIS 194
Cdd:cd01889 129 KIDLI-PEEERKRKIEKMKKRlqKTLEKTRLKD---SPIIPVS 167
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
245-328 |
9.96e-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: 66.38 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 245 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 324
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 14422440 325 VAGD 328
Cdd:cd16267 81 ILCD 84
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-324 |
2.34e-13 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 72.01 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--SLWKFETSKYyV 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTREH-ALLAYTlGVKQLIVGVNKMDSTEPPYSQ 164
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACddGV---------MAQTREHlAILQLT-GNPMLTVALTKADRVDEARIA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 165 KRYEEIVKEVSTYikkigynpdtvafvpisGWNGDNMLEPSANmpwfkgwkvtrkdgnaSGT---TLLEALDCILPPTRP 241
Cdd:PRK10512 124 EVRRQVKAVLREY-----------------GFAEAKLFVTAAT----------------EGRgidALREHLLQLPEREHA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVK-NVSVKDV 320
Cdd:PRK10512 171 AQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQI 250
|
....
gi 14422440 321 RRGN 324
Cdd:PRK10512 251 NRGD 254
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-279 |
5.57e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 70.89 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKeaaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVgVNKMDSteppySQKRYE 168
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDR-----PGARPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 169 EIVKEVSTYIKKIGYNPDTVAFvPI---SGWNGDNMLEpsanmpwfkgwkvtRKDGNASGTTLLEAL-DCILPPTRPTDK 244
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQLDF-PIvyaSALNGIAGLD--------------HEDMAEDMTPLYQAIvDHVPAPDVDLDG 203
|
250 260 270
....*....|....*....|....*....|....*
gi 14422440 245 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVT 279
Cdd:PRK10218 204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-120 |
1.03e-12 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 70.07 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110
....*....|....*....|....*....|....
gi 14422440 89 IIDAPGHRDFIKNMITGTSQADCAVLIV--AAGV 120
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFdaVAGV 111
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-211 |
2.32e-12 |
|
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: 66.14 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKcggidkrtIEKFEKEAAEMGKgSFKYawvLDKLKAERERGITID---ISLwKFETSK- 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ--------THKRTPSVKLGWK-PLRY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 --YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVgefeaGISKNG-QTREHALLaytLGVKQLIVgVNKMDS--TE 159
Cdd:cd04167 69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTeRLIRHAIQ---EGLPMVLV-INKIDRliLE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14422440 160 ---PP---YSQKRYeeIVKEVSTYIKKIGyNPDTVAFVPISGwngdNMLEPSANMPWF 211
Cdd:cd04167 140 lklPPtdaYYKLRH--TIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
2.60e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 68.82 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAaemgkgsfkyawvlDKLKAERERGITIDISL----WKfets 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14422440 84 KYYVTIIDAPGHRDFiknmitgTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVgVNKMD 156
Cdd:PRK13351 72 NHRINLIDTPGHIDF-------TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIF-INKMD 136
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-279 |
2.70e-12 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 68.89 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAAEMgkgsfkyawVLDKLKAERERGITIdisLWKfETSKYY-- 86
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK-NTAVRYkg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEagisknG---QTR---EHALlayTLGVKqLIVGV 152
Cdd:COG1217 69 vkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 153 NKMDsteppysqK---RYEEIVKEVSTYIKKIGYNPDTVAFvPI------SGWNGDNMLEPSANMpwfkgwkvtrkdgna 223
Cdd:COG1217 129 NKID--------RpdaRPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDL--------------- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14422440 224 sgTTLLEA-LDCILPPTRPTDKPLRlpLQ------DVYkIGGIGtvpVGRVETGVLKPGMVVT 279
Cdd:COG1217 185 --TPLFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVA 239
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
245-325 |
4.13e-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: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 245 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 324
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 14422440 325 V 325
Cdd:cd04089 79 V 79
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-156 |
4.80e-12 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 66.08 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaaemgkGSFkyawVLDKLKAERERGITIDISLWKFETSKYYV 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14422440 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISknGQTREHALLAYTLGVKQLIVgVNKMD 156
Cdd:cd04170 67 NLIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRIIF-INKMD 127
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-156 |
7.98e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 67.46 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14422440 92 APGHRDFIKNMITGTSQADCAVLIVAAgVGEFEAgiskngQTRehALLAYT--LGVKQLIVgVNKMD 156
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCA-VGGVEP------QTE--TVWRQAekYGVPRIIF-VNKMD 123
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
5.66e-11 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 62.89 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITID---ISL-WKfetsK 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IGEVHGGGATM-----------DWMEQERERGITIQsaaTTCfWK----D 63
|
90
....*....|....
gi 14422440 85 YYVTIIDAPGHRDF 98
Cdd:cd01886 64 HRINIIDTPGHVDF 77
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
1.04e-10 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 62.23 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYAwVLDKLKAERERGITIDISLWKFETSKYYVTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 14422440 91 DAPGHRDFIKNMITGTSQADCAVLIVAAGVG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
245-328 |
1.11e-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: 57.90 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 245 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMH-HEALSEALPGDNVGFNVKNVSVKDVRRG 323
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 14422440 324 NVAGD 328
Cdd:cd03698 80 DILSS 84
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
9-185 |
2.77e-10 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 60.00 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaaemGKGSFKYAwvLDKLKAERERGITIDISL----------- 77
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTSSVSNdilgfdsdgev 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 78 --WK-----------FETSKYYVTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGvgefeAGIskNGQTREHALLAYT 142
Cdd:cd04165 64 vnYPdnhlgeldveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGAN-----AGI--IGMTKEHLGLALA 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14422440 143 LGVKQLIVgVNKMDSTEppysqkryEEIVKEVSTYIKKIGYNP 185
Cdd:cd04165 137 LKVPVFVV-VTKIDMTP--------ANVLQETLKDLKRLLKSP 170
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-201 |
2.16e-09 |
|
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: 56.33 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDISLWKFETSK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 YY--VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLAYTlgvkQLIVGVNKMD 156
Cdd:cd01887 47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAAddGVMP---------QTIEainHAKAANV----PIIVAINKID 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14422440 157 stEPPYSQKRYEEIVKEVSTYikkiGYNPD----TVAFVPISGWNGDNM 201
Cdd:cd01887 113 --KPYGTEADPERVKNELSEL----GLVGEewggDVSIVPISAKTGEGI 155
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
252-325 |
2.74e-09 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 53.76 E-value: 2.74e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14422440 252 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN----VTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-190 |
5.26e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 58.34 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 3 KEKTHI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeAAEmgkgsfkyAWVLDKLKAERERGITID---ISLW 78
Cdd:PRK07560 15 KNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKaanVSMV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 79 -KFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQT--------REHallaytlgVKQ 147
Cdd:PRK07560 80 hEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAveGVMP---------QTetvlrqalRER--------VKP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14422440 148 LIVgVNKMD------STEPPYSQKRYEEIVKEVSTYIKkiGYNPD-------------TVAF 190
Cdd:PRK07560 143 VLF-INKVDrlikelKLTPQEMQQRLLKIIKDVNKLIK--GMAPEefkekwkvdvedgTVAF 201
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
1.20e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 57.37 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAAEmgkgsfkyAWVLDKLKAERERGITID---ISL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*...
gi 14422440 78 ---WKFETSK----YYVTIIDAPGHRDF 98
Cdd:PTZ00416 78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-203 |
2.47e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 56.17 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITIDI-----SLWKFE- 81
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLgyanaKIYKCPk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 82 ---------------------------TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN---- 130
Cdd:PTZ00327 87 cprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------Nescp 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14422440 131 -GQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKkigynpDTVAFVPIS---GWNGDNMLE 203
Cdd:PTZ00327 156 qPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIA------DNAPIIPISaqlKYNIDVVLE 226
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
246-325 |
8.82e-08 |
|
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: 49.49 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKN-VsvkDVRRGN 324
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77
|
.
gi 14422440 325 V 325
Cdd:cd03695 78 L 78
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-98 |
1.46e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 53.96 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfEKEAAemgkGSFKYAwvlDKLKAERERGITID---ISL 77
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGII--------AQEVA----GDVRMT---DTRADEAERGITIKstgISL 77
|
90 100 110
....*....|....*....|....*....|....
gi 14422440 78 W-------------KFETSKYYVTIIDAPGHRDF 98
Cdd:PLN00116 78 YyemtdeslkdfkgERDGNEYLINLIDSPGHVDF 111
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-203 |
5.50e-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: 46.30 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETSKYYVT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 89 IIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGVGEFEAGIskngqTREHALLAYTLGVKQLIVGvNKMDsteppys 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKID------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14422440 164 qKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLE 203
Cdd:cd00882 118 -LLEEREVEELLRLEELAKILG--VPVFEVSAKTGEGVDE 154
|
|
| FERM_C_CCM1 |
cd13197 |
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ... |
394-429 |
7.65e-06 |
|
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.
Pssm-ID: 270018 Cd Length: 100 Bit Score: 44.53 E-value: 7.65e-06
10 20 30
....*....|....*....|....*....|....*.
gi 14422440 394 LKSGDAAIVDMVpGKPMCVESFSDYPPLGRFAVRDM 429
Cdd:cd13197 37 METKALLLSLKY-GCFMWQLGDADTCFQIHSLENKM 71
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
340-404 |
1.62e-05 |
|
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: 43.28 E-value: 1.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14422440 340 FTAQVIILNHPGQISAGYAPVLDCHTAHIACKFaelkEKIDRrsgkkledgpKFLKSGDAAIVDM 404
Cdd:cd03708 6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDK----------EVLRTGDRALVRF 56
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-203 |
1.28e-04 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 44.44 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 10 IVVIGHVDSGKSTTtghliykcggIDK-RTIEKFEKEAAemgkgsfkyawvldklkaererGITIDIS----LWKFETSK 84
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDKiRKTQIAQKEAG----------------------GITQKIGayevEFEYKDEN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTRE---HALLAYTlgvkQLIVGVNKMDSTepp 161
Cdd:CHL00189 295 QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA-----DDGVKP--QTIEainYIQAANV----PIIVAINKIDKA--- 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14422440 162 ysQKRYEEIVKEVSTY---IKKIGynpDTVAFVPIS---GWNGDNMLE 203
Cdd:CHL00189 361 --NANTERIKQQLAKYnliPEKWG---GDTPMIPISasqGTNIDKLLE 403
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
251-325 |
2.58e-04 |
|
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: 39.59 E-value: 2.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14422440 251 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfAPVNVTTeVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVRRGNV 325
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKGVAL-IRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
12-98 |
5.46e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 42.43 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYA---WvldkLKAERERGITIDISLWKFETSKYYV 87
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81
|
90
....*....|.
gi 14422440 88 TIIDAPGHRDF 98
Cdd:PRK00741 82 NLLDTPGHEDF 92
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-203 |
1.02e-03 |
|
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: 39.66 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 8 INIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfekeaaEMGKGSFKYAWVLdklkAERERGITidislwkfetskYYV 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT------------EYYPGTTRNYVTT----VIEEDGKT------------YKF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 88 TIIDAPGHRDFIKNMITGTSQADcAVLIVAAG---VGEFEAGISKNGQTREHALlayTLGVKQLIVGvNKMDsteppysq 164
Cdd:TIGR00231 54 NLLDTAGQEDYDAIRRLYYPQVE-RSLRVFDIvilVLDVEEILEKQTKEIIHHA---DSGVPIILVG-NKID-------- 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 14422440 165 KRYEEIVKEVSTYIKKIGYNPdtvaFVPISGWNGDNMLE 203
Cdd:TIGR00231 121 LKDADLKTHVASEFAKLNGEP----IIPLSAETGKNIDS 155
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-233 |
1.27e-03 |
|
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: 41.15 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 10 IVVI-GHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDISLWKFETS 83
Cdd:COG0532 6 VVTVmGHVDHGKTS------------------------------------LLDAIRktnvAAGEaGGITQHIGAYQVETN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLAytlGVKqLIVGVNKMDst 158
Cdd:COG0532 50 GGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAAddGVMP---------QTIEainHAKAA---GVP-IIVAINKID-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 159 eppysqkryeeivkevstyikKIGYNPDTV------------------AFVPISGWNGDN-------------MLEPSAN 207
Cdd:COG0532 115 ---------------------KPGANPDRVkqelaehglvpeewggdtIFVPVSAKTGEGidellemillqaeVLELKAN 173
|
250 260
....*....|....*....|....*..
gi 14422440 208 mpwfkgwkvtrKDGNASGTTlLEA-LD 233
Cdd:COG0532 174 -----------PDRPARGTV-IEAkLD 188
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
340-438 |
5.55e-03 |
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Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 36.05 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14422440 340 FTAQVIILN------HPGqISAGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGPKFLKSGDAAIVDMVPGKPMCVE 413
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRI-------------DLPEGKEMVMPGEDTSVKLTLLKPMVLE 71
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90 100
....*....|....*....|....*
gi 14422440 414 sfsdypPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03706 72 ------KGQRFTLREGGRTIGTGVV 90
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