|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-461 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 894.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 81 ETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEAGISKNGQTREHALLAQTLGVKQLIVACNKMDSTEP 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 161 PFSEARFTEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKGwaverkegnasgKTLLEALDSIIPPQR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 241 PTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDI 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 321 RRGSVCSDSKQDPAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAG 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569207 401 IVELIPTKPLCVESFTDYAPLGRFAVRDMRQTVAVGVIKSVEKSDGSSgkvTKSAQKAAPK 461
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKEGSG---TKAAAKAKKK 446
|
|
| 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: 715.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 81 ETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEAGISKNGQTREHALLAQTLGVKQLIVACNKMDSTEP 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 161 PFSEARFTEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKGwaverkegnasgKTLLEALDSIIPPQR 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 241 PTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDI 320
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 321 RRGSVCSDSKQDPAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAG 400
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 17569207 401 IVELIPTKPLCVESFTDYAPLGRFAVRDMRQTVAVGVIKSVEKSDGSSGKVTKSAQK 457
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-445 |
0e+00 |
|
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]
Pssm-ID: 129574 [Multi-domain] Cd Length: 426 Bit Score: 669.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 81 ETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagisKNGQTREHALLAQTLGVKQLIVACNKMDSTEp 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 161 pFSEARFTEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKgwaverkegnasGKTLLEALDSIIPPQR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 241 PTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDI 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 321 RRGSVCSDSKqDPAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAG 400
Cdd:TIGR00483 303 RRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 17569207 401 IVELIPTKPLCVESFTDYAPLGRFAVRDMRQTVAVGVIKSVEKSD 445
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-443 |
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: 667.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 81 ETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEfeagiskNGQTREHALLAQTLGVKQLIVACNKMDSTEp 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 161 pFSEARFTEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKgwaverkegnasGKTLLEALDSIIPPQR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 241 PTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDI 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 321 RRGSVCSDSkQDPAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAG 400
Cdd:COG5256 300 KRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 17569207 401 IVELIPTKPLCVESFTDYAPLGRFAVRDMRQTVAVGVIKSVEK 443
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKP 421
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-443 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 659.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 83 AKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACgtgefEAGISKNGQTREHALLAQTLGVKQLIVACNKMDSTEppF 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 163 SEARFTEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKgwaverkegnasGKTLLEALDSIIPPQRPT 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 243 DRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRR 322
Cdd:PRK12317 223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 323 GSVCSdSKQDPAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAGIV 402
Cdd:PRK12317 303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 17569207 403 ELIPTKPLCVESFTDYAPLGRFAVRDMRQTVAVGVIKSVEK 443
Cdd:PRK12317 382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKP 422
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-239 |
2.31e-158 |
|
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: 446.94 E-value: 2.31e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYIT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 89 IIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEAGISKNGQTREHALLAQTLGVKQLIVACNKMDSTEPPFSEARFT 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569207 169 EITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKGWaverkegnasgkTLLEALDSIIPPQ 239
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-441 |
6.11e-98 |
|
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: 300.85 E-value: 6.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKY- 85
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 86 YItIIDAPGHRDFIKNMITGTSQADCAVLVV-AcgtgefeagisKNG---QTREHALLAQTLGVKQLIVACNKMDSTEpp 161
Cdd:COG2895 97 FI-IADTPGHEQYTRNMVTGASTADLAILLIdA-----------RKGvleQTRRHSYIASLLGIRHVVVAVNKMDLVD-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 162 FSEARFTEITNEVSGFIKKIGYNPkaVPFVPISGFNGDNMLEVSSNMPWFKgwaverkegnasGKTLLEALDSIIPPQRP 241
Cdd:COG2895 163 YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAEDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 242 TDRPLRLPLQDVYKiggigtvP-------VGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGF---- 310
Cdd:COG2895 229 NDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtled 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 311 NVknvsvkDIRRGSVCSDSkQDPAKEARTFHAQVIIMN-HPGQISNGYtpVLDCHTAHIACKFNELKEKVDRRTGKKVEd 389
Cdd:COG2895 302 EI------DISRGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHEA- 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 17569207 390 fPKFLKSGDAGIVELIPTKPLCVESFTDYAPLGRFAV--RDMRQTVAVGVIKSV 441
Cdd:COG2895 372 -ADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGA 424
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-238 |
9.94e-79 |
|
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: 242.82 E-value: 9.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 5 KVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETAK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 85 YYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGefeagisKNGQTREHALLAQTLGVKqLIVACNKMDSTeppfSE 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17569207 165 ARFTEITNEVSG-FIKKIGYNPKAVPFVPISGFNGDNMlevssnmpwfkgwaverkegnasgKTLLEALDSIIPP 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 |
5.65e-68 |
|
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: 212.05 E-value: 5.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 335 KEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAGIVELIPTKPLCVES 414
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 17569207 415 FTDYAPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-438 |
8.54e-62 |
|
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: 206.45 E-value: 8.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGK--GSFKYAWVLDKLKAERERGITIDIALWKFETAKYYITIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 92 APGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEppFSEARFTEIT 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 172 NEVSGFIKKIGynPKAVPFVPISGFNGDNMLEVSSNMPWFkgwaverkegnaSGKTLLEALDSIIPPQRPTDRPLRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 252 DVYKI-----GGIGTVPVGRVEtgiikPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSvkDIRRGSVC 326
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 327 SdSKQDPAKEARTFHAQVIIM-NHPgqISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEdfPKFLKSGDAGIVELI 405
Cdd:TIGR02034 297 A-AADSAPEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGA--AKSLELNEIGRVNLS 371
|
410 420 430
....*....|....*....|....*....|....*
gi 17569207 406 PTKPLCVESFTDYAPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 372 LDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-443 |
1.41e-61 |
|
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: 205.38 E-value: 1.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKE-----KVHINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKfekeaqemGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLTA-------AITKVLAKK--------GGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 76 ALWKFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 156 DSTEPPfsearftEITN----EVSGFIKKIGYNPKAVPFVPISGFNGdnmLEVSSNMPWfkgwaverkegNASGKTLLEA 231
Cdd:COG0050 139 DMVDDE-------ELLElvemEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEW-----------EKKILELMDA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 232 LDSIIP-PQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG---MVVTFAPqNVTTEVKSVEMHHESLPEAVPGDN 307
Cdd:COG0050 198 VDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 308 VGFNVKNVSVKDIRRGSVCsdSKQDPAKEARTFHAQVIIMN-------HPgqISNGYTPVLDCHTAHI--ACKFNELKEK 378
Cdd:COG0050 277 VGLLLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVLSkeeggrhTP--FFNGYRPQFYFRTTDVtgVITLPEGVEM 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17569207 379 VdrRTGKKVEdfpkflksgdaGIVELIptKPLCVESFTdyaplgRFAVRDMRQTVAVGVIKSVEK 443
Cdd:COG0050 353 V--MPGDNVT-----------MTVELI--TPIAMEEGL------RFAIREGGRTVGAGVVTKIIE 396
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-235 |
6.64e-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: 197.79 E-value: 6.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAQEMGKgsFKYAWVLDKLKAERERGITIDIALWKFETAKY 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 86 YITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEppFSEA 165
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 166 RFTEITNEVSGFIKKIGYNPKAvpFVPISGFNGDNMLEVSSNMPWFKgwaverkegnasGKTLLEALDSI 235
Cdd:cd04166 150 VFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-438 |
1.09e-60 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 209.02 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMG--KGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYITIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 92 APGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEppFSEARFTEIT 171
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 172 NEVSGFIKKIGYNpkAVPFVPISGFNGDNMLEVSSNMPWFkgwaverkegnaSGKTLLEALDSIIPPQRPTDRPLRLPLQ 251
Cdd:PRK05506 182 ADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 252 DVYKI-----GGIGTvpvgrVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVgfnvkNVSVKD---IRRG 323
Cdd:PRK05506 248 YVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 324 S--VCSDskqDPAKEARTFHAQVIIMN----HPGqisNGYtpVLDCHTAHIACKFNELKEKVD-----RRTGKKvedfpk 392
Cdd:PRK05506 318 DmlARAD---NRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDvntleRLAAKT------ 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 17569207 393 fLKSGDAGIVELIPTKPLCVESFTDYAPLGRFAV--RDMRQTVAVGVI 438
Cdd:PRK05506 384 -LELNEIGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMI 430
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-443 |
4.16e-60 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 201.71 E-value: 4.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKE-----KVHINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTA-------AITKVLAERGLNQAK-------DYDSI-DAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 76 ALWKFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 156 DSTEPPfsearftEITN----EVSGFIKKIGYNPKAVPFVPISGF---NGDNmlevssnmPWFKgwAVERkegnasgktL 228
Cdd:PRK12736 139 DLVDDE-------ELLElvemEVRELLSEYDFPGDDIPVIRGSALkalEGDP--------KWED--AIME---------L 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 229 LEALDSIIP-PQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG---MVVTFAPqNVTTEVKSVEMHHESLPEAVP 304
Cdd:PRK12736 193 MDAVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKE-TQKTVVTGVEMFRKLLDEGQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 305 GDNVGFNVKNVSVKDIRRGSVCsdSKQDPAKEARTFHAQVIIMN------HPGQISNgYTPVLDCHTAHI--ACKFNELK 376
Cdd:PRK12736 272 GDNVGVLLRGVDRDEVERGQVL--AKPGSIKPHTKFKAEVYILTkeeggrHTPFFNN-YRPQFYFRTTDVtgSIELPEGT 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17569207 377 EKVdrRTGKKVEdfpkflksgdaGIVELIptKPLCVESFTdyaplgRFAVRDMRQTVAVGVIKSVEK 443
Cdd:PRK12736 349 EMV--MPGDNVT-----------ITVELI--HPIAMEQGL------KFAIREGGRTVGAGTVTEILD 394
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
242-332 |
4.25e-60 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 191.25 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 242 TDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIR 321
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 17569207 322 RGSVCSDSKQD 332
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-440 |
1.65e-58 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 199.75 E-value: 1.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 14 GHVDSGKSTTTGHLIYkcggiDKRTI-----EKFEKEAQEMGKGSFK--YAWVLDKLKAERERGITIDIALWKFETAKYY 86
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQIyedqlASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTEKRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 87 ITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEppFSEAR 166
Cdd:PRK05124 109 FIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 167 FTEITNEVSGFIKKIGYNPKaVPFVPISGFNGDNMLEVSSNMPWFkgwaverkegnaSGKTLLEALDSIIPPQRPTDRPL 246
Cdd:PRK05124 180 FERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 247 RLPLQDVYKI-----GGIGTvpvgrVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSvkDIR 321
Cdd:PRK05124 247 RFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--DIS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 322 RGSVCSDSKQDPAkEARTFHAQVIIMNH----PGQ-----ISNGYTPVldchtahiacKFNELKEKVDRRTGKK--VEDf 390
Cdd:PRK05124 320 RGDLLVAADEALQ-AVQHASADVVWMAEqplqPGQsydikIAGKKTRA----------RVDAIRYQVDINTLTQreAEN- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 17569207 391 pkfLKSGDAGIVELIPTKPLCVESFTDYAPLGRFAV--RDMRQTVAVGVIKS 440
Cdd:PRK05124 388 ---LPLNGIGLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-443 |
7.61e-58 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 195.79 E-value: 7.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKE-----KVHINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGAEAK-------AYDQI-DKAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 76 ALWKFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKM 155
Cdd:PRK00049 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 156 DSTEPPfsearftEITN----EVSGFIKKIGYNPKAVPFVPISGFNGdnmLEVSSNMPWFKgwAVERkegnasgktLLEA 231
Cdd:PRK00049 139 DMVDDE-------ELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEK--KILE---------LMDA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 232 LDSIIP-PQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG---MVVTFAPQNVTTeVKSVEMHHESLPEAVPGDN 307
Cdd:PRK00049 198 VDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 308 VGFNVKNVSVKDIRRGSVCsdSKQDPAKEARTFHAQVIIMN------HPGqISNGYTPVLDCHTAHI--ACKFNELKEKV 379
Cdd:PRK00049 277 VGALLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVLSkeeggrHTP-FFNGYRPQFYFRTTDVtgVIELPEGVEMV 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569207 380 drrtgkkvedFPkflksGD--AGIVELIptKPLCVESFTdyaplgRFAVRDMRQTVAVGVIKSVEK 443
Cdd:PRK00049 354 ----------MP-----GDnvEMTVELI--APIAMEEGL------RFAIREGGRTVGAGVVTKIIE 396
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-441 |
8.83e-57 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 194.27 E-value: 8.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 3 KEKVHINIVVIGHVDSGKSTTTGhliykcggidkrTIEKFEKEAQEMGKGSFKYawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTA------------AITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 83 AKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTE-PP 161
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDdEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 162 FSEARFTEItNEVSGFIKkigynpkavpfvpisgFNGDnmlevssNMPWFKGWAVERKEGNAS--GKT----LLEALDSI 235
Cdd:PLN03127 195 LLELVEMEL-RELLSFYK----------------FPGD-------EIPIIRGSALSALQGTNDeiGKNailkLMDAVDEY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 236 IP-PQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG---MVVTFAPQ-NVTTEVKSVEMHHESLPEAVPGDNVGF 310
Cdd:PLN03127 251 IPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGgPLKTTVTGVEMFKKILDQGQAGDNVGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 311 NVKNVSVKDIRRGSVCsdSKQDPAKEARTFHAQVIIMN------HPGQISNgYTPVLDCHTAHIACKFnELKEKVdrrtg 384
Cdd:PLN03127 331 LLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADVTGKV-ELPEGV----- 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17569207 385 kkvedfpKFLKSGD--AGIVELIPTKPLcvesftdyAPLGRFAVRDMRQTVAVGVIKSV 441
Cdd:PLN03127 402 -------KMVMPGDnvTAVFELISPVPL--------EPGQRFALREGGRTVGAGVVSKV 445
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-441 |
2.29e-56 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 194.06 E-value: 2.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 83 AKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEppf 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 163 SEARFTEITNEVSGFIKKIGYNPKAVPFVpisgfNGDNMLEVSSNMpwfKGWAVERKEGNASGKT--LLEALDSIIP-PQ 239
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEFPGDDIPII-----SGSALLALEALM---ENPNIKRGDNKWVDKIyeLMDAVDSYIPiPQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 240 RPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVT--TEVKSVEMHHESLPEAVPGDNVGFNVKNVSV 317
Cdd:PLN03126 284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 318 KDIRRGSVCsdSKQDPAKEARTFHAQVIIMNHP--GQIS---NGYTPVLDCHTAHIACKFNELKEKVDRRTgkkvedfpK 392
Cdd:PLN03126 364 ADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------K 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17569207 393 FLKSGD--AGIVELIptKPLCVESFTdyaplgRFAVRDMRQTVAVGVIKSV 441
Cdd:PLN03126 434 MVMPGDrvKMVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-238 |
5.61e-56 |
|
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: 184.04 E-value: 5.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaqemgkgsfkyaWVLDKLKAERERGITIDIALWKFETAKYYIT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 89 IIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEfeagiskNGQTREHALLAQtLGVKQLIVACNKMDSteppFSEARFT 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDR----VGEEDFD 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569207 169 EITNEVSGFIKKIGY---NPKAVPFVPISGFNGDNMLEvssnmpwfkgwaverkegnasgktLLEALDSIIPP 238
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------------------------LLDAIVEHLPP 182
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-325 |
1.30e-55 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 189.66 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 76 ALWKFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 156 DSTEPP----FSEARFTEITNEvsgfikkigYnpkavpfvpisGFNGDnmlevssNMPWFKGWAVERKEGNASGK----- 226
Cdd:PRK12735 139 DMVDDEelleLVEMEVRELLSK---------Y-----------DFPGD-------DTPIIRGSALKALEGDDDEEweaki 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 227 -TLLEALDSIIP-PQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG---MVVTFAPqNVTTEVKSVEMHHESLPE 301
Cdd:PRK12735 192 lELMDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKE-TQKTTVTGVEMFRKLLDE 270
|
330 340
....*....|....*....|....
gi 17569207 302 AVPGDNVGFNVKNVSVKDIRRGSV 325
Cdd:PRK12735 271 GQAGDNVGVLLRGTKREDVERGQV 294
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-438 |
2.69e-54 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 186.70 E-value: 2.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 83 AKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDS-TEPP 161
Cdd:CHL00071 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQvDDEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 162 FSEarFTEItnEVSGFIKKIGYNPKAVPFVPISGFNGdnmLEVSSNMPwfkgwAVERKEGNASGK--TLLEALDSIIP-P 238
Cdd:CHL00071 146 LLE--LVEL--EVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKiyNLMDAVDSYIPtP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 239 QRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVT---FAPQNVTTeVKSVEMHHESLPEAVPGDNVGFNVKNV 315
Cdd:CHL00071 214 ERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVGILLRGI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 316 SVKDIRRGSVCsdSKQDPAKEARTFHAQVIIMN------HPGqISNGYTPVLDCHTAHIACKFNELKEKvdrrTGKKVEd 389
Cdd:CHL00071 293 QKEDIERGMVL--AKPGTITPHTKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKIESFTAD----DGSKTE- 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 17569207 390 fpkFLKSGD--AGIVELIptKPLCVESFTdyaplgRFAVRDMRQTVAVGVI 438
Cdd:CHL00071 365 ---MVMPGDriKMTVELI--YPIAIEKGM------RFAIREGGRTVGAGVV 404
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-441 |
2.35e-53 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 183.82 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:TIGR00485 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 76 ALWKFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKM 155
Cdd:TIGR00485 66 AHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 156 D-STEPPFSEARFTEITNEVSGFikkigynpkavpfvpisGFNGDnmlevssNMPWFKGWAVERKEGNASGKT----LLE 230
Cdd:TIGR00485 139 DmVDDEELLELVEMEVRELLSQY-----------------DFPGD-------DTPIIRGSALKALEGDAEWEAkileLMD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 231 ALDSIIP-PQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG---MVVTFAPQNVTTeVKSVEMHHESLPEAVPGD 306
Cdd:TIGR00485 195 AVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 307 NVGFNVKNVSVKDIRRGSVCsdSKQDPAKEARTFHAQVIIMN------HPGQISnGYTPVLDCHTAHIACKFnELKEKVd 380
Cdd:TIGR00485 274 NVGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDVTGTI-ELPEGV- 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569207 381 rrtgkkvedfpKFLKSGD--AGIVELIptKPLCVESFTdyaplgRFAVRDMRQTVAVGVIKSV 441
Cdd:TIGR00485 349 -----------EMVMPGDnvKMTVELI--SPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-438 |
4.82e-45 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 166.24 E-value: 4.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFEtAKY 85
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLgfAYLPLP-DGR 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 86 YITIIDAPGHRDFIKNMITGTSQADCAVLVVACgtgefEAGISKngQTREHALLAQTLGVKQLIVACNKMDSTEPpfseA 165
Cdd:COG3276 52 RLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHLAILDLLGIKRGIVVLTKADLVDE----E 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 166 RFTEITNEVSGFIKkiGYNPKAVPFVPISGFNGDNMLEvssnmpwfkgwaverkegnasgktLLEALDSII--PPQRPTD 243
Cdd:COG3276 121 WLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEGIDE------------------------LRAALDALAaaVPARDAD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 244 RPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRG 323
Cdd:COG3276 175 GPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 324 SVCSDskQDPAKEARTFHAQVIIMNHPGQ-ISNGyTPVLdCH--TAHIACKFNELKEKVdrrtgkkvedfpkfLKSGDAG 400
Cdd:COG3276 255 DVLAA--PGALRPTDRIDVRLRLLPSAPRpLKHW-QRVH-LHhgTAEVLARVVLLDREE--------------LAPGEEA 316
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 17569207 401 IVELIPTKPLCVesftdyAPLGRFAVRDM--RQTVAVGVI 438
Cdd:COG3276 317 LAQLRLEEPLVA------ARGDRFILRDYspRRTIGGGRV 350
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-238 |
3.10e-37 |
|
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: 135.02 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 7 HINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETAKYY 86
Cdd:cd01884 2 HVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 87 ITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEPPfsE-A 165
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVDDE--ElL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569207 166 RFTEItnEVSGFIKKIGYNPKAVPFVPISGFNGdnmLEvssnmpwfkgwAVERKEGNASGKTLLEALDSIIPP 238
Cdd:cd01884 138 ELVEM--EVRELLSKYGFDGDDTPIVRGSALKA---LE-----------GDDPNKWVDKILELLDALDSYIPT 194
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-335 |
3.42e-37 |
|
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: 143.48 E-value: 3.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETAKYYI 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 88 TIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVACNKMDSTEppfsEARF 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 168 TEITNEVSGFIKKIGYNPKAVPFVpISGFNGDNMLEVSSNMpwfkgwaverkegnasgKTLLEALDSiippqRPTDRPLR 247
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL-----------------KNLLESLDI-----KRIQKPLR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 248 LPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGsVCS 327
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRG-LLI 257
|
....*...
gi 17569207 328 DSKQDPAK 335
Cdd:TIGR00475 258 LTPEDPKL 265
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
333-441 |
2.55e-35 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 126.61 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 333 PAKEARTFHAQVIIMNH-----PGQISNGYTPVLDCHTAHIACKFNELKEKVDrrTGKKVEDfPKFLKSGDAGIVELIPT 407
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 17569207 408 KPLCVESFTdyaplgRFAVRDMRQTVAVGVIKSV 441
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
340-438 |
2.81e-28 |
|
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: 107.48 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 340 FHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKveDFPKFLKSGDAGIVELIPTKPLCVESFTDYA 419
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 17569207 420 PLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-199 |
2.57e-27 |
|
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: 107.31 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETAKYyI 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 88 TIIDAPGHRDFIKNMITGTSQADCAVLVVACgtgefEAGISKngQTREHALLAQTLGVKQLIVACNKMDSTEPPFSEARF 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDEDRLELVE 125
|
170 180 190
....*....|....*....|....*....|..
gi 17569207 168 TEITNEVSgfikkiGYNPKAVPFVPISGFNGD 199
Cdd:cd04171 126 EEILELLA------GTFLADAPIFPVSSVTGE 151
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
335-438 |
4.01e-24 |
|
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: 96.47 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 335 KEARTFHAQVIIMNHPGQI-SNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAGIVELIPTKPLCVE 413
Cdd:cd03704 1 PVVTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLE 80
|
90 100
....*....|....*....|....*
gi 17569207 414 SFTDYAPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03704 81 TFKDFPQLGRFTLRDEGKTIAIGKV 105
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
333-441 |
3.17e-20 |
|
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: 85.67 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 333 PAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAGIVELIPTKPLCV 412
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 17569207 413 ESFTDYAPLGRFAVRDMRQTVAVGVIKSV 441
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
246-327 |
3.14e-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: 81.93 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 246 LRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNvsVKDIRRGSV 325
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
..
gi 17569207 326 CS 327
Cdd:cd01342 79 LT 80
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-309 |
3.89e-19 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 89.14 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKVH--INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI----- 73
Cdd:PRK04000 1 MMWEKVQpeVNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgya 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 74 DIALWKFETAK---YYIT------------------IIDAPGHRDFIKNMITGTSQADCAVLVVA----Cgtgefeagis 128
Cdd:PRK04000 53 DATIRKCPDCEepeAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAanepC---------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 129 KNGQTREHALLAQTLGVKQLIVACNKMDSTeppfSEARFTEITNEVSGFIKkiGYNPKAVPFVPISGFNGDNMlevssnm 208
Cdd:PRK04000 123 PQPQTKEHLMALDIIGIKNIVIVQNKIDLV----SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNI------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 209 pwfkgwaverkegnasgKTLLEALDSIIP-PQRPTDRPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG--I- 271
Cdd:PRK04000 190 -----------------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeIe 252
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17569207 272 IKPGMVVTFAP----QNVTTEVKSVEMHHESLPEAVPGDNVG 309
Cdd:PRK04000 253 IRPGIKVEEGGktkwEPITTKIVSLRAGGEKVEEARPGGLVG 294
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
246-328 |
9.83e-18 |
|
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: 77.57 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 246 LRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGSV 325
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
...
gi 17569207 326 CSD 328
Cdd:cd03696 81 LSE 83
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
248-325 |
1.24e-17 |
|
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: 77.56 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 248 LPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFA--PQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGSV 325
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-323 |
1.78e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 82.02 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETAKYyI 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 88 TIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFeagisknGQTREHALLAQTLGVKQLIVACNKMDSTEppfsEARF 167
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKADRVD----EARI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 168 TEITNEVSGFIKKIGYNpkAVPFVPISGFNGDNMlevssnmpwfkgwaverkegnasgKTLLEALDSIIPPQRPTDRPLR 247
Cdd:PRK10512 123 AEVRRQVKAVLREYGFA--EAKLFVTAATEGRGI------------------------DALREHLLQLPEREHAAQHRFR 176
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17569207 248 LPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVK-NVSVKDIRRG 323
Cdd:PRK10512 177 LAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINRG 253
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
245-328 |
2.57e-16 |
|
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: 73.70 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 245 PLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGS 324
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 17569207 325 VCSD 328
Cdd:cd16267 81 ILCD 84
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-156 |
7.03e-16 |
|
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: 75.26 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFETAK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17569207 85 YYI-TIIDAPGHRDFikNMITGTSQADC--AVLVVACGTGeFEAgiskngQTREHALLAQTLGVKqLIVACNKMD 156
Cdd:cd01890 66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLE-IIPVINKID 130
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-337 |
1.17e-15 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 79.29 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IALwkFET 82
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRL--NYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 83 AK----YYITIIDAPGHRDFiknmitgT-----SQADC--AVLVVACGTGeFEAgiskngQTREHALLAQTLGVKqLIVA 151
Cdd:COG0481 67 AKdgetYQLNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA------QTLANVYLALENDLE-IIPV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 152 CNKMD--STEPPfsearftEITNEVsgfIKKIGYNPKAVpfVPISGFNGDNMLEVssnmpwfkgwaverkegnasgktlL 229
Cdd:COG0481 132 INKIDlpSADPE-------RVKQEI---EDIIGIDASDA--ILVSAKTGIGIEEI------------------------L 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 230 EALDSIIPPqrPTDRPLRlPLQ--------DVYKiggiGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSV---EMHHES 298
Cdd:COG0481 176 EAIVERIPP--PKGDPDA-PLQalifdswyDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvfTPKMTP 248
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17569207 299 LPEAVPGDnVGF---NVKNvsVKDIRRGSVCSDSKqDPAKEA 337
Cdd:COG0481 249 VDELSAGE-VGYiiaGIKD--VRDARVGDTITLAK-NPAAEP 286
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-156 |
1.31e-15 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 75.73 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIekfekeaqemgkGSFKYawvLDKLKAERERGITID---IALwKFETAK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIISEKLA------------GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 85 ------YYITIIDAPGHRDFIKNMITGTSQADCAVLVVACgtgeFEaGISKngQTreHALLAQTL--GVKQLIVaCNKMD 156
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----VE-GVCV--QT--ETVLRQALeeRVKPVLV-INKID 135
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
260-325 |
2.13e-15 |
|
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: 70.76 E-value: 2.13e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569207 260 GTVPVGRVETGIIKPGMVVTFAPQNV-----TTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGSV 325
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-194 |
9.52e-15 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 72.40 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTttghliykcggIDKRTIEKFEKEAqemgkgsfkyawvLDKLKAERERGITIDIALWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTS-----------LAKALSEIASTAA-------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 81 -------ETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGefeagisKNGQTREHALLAQTLGvKQLIVACN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17569207 154 KMDSTEPPFSEARFTEITNEVSGFIKKIgyNPKAVPFVPIS 194
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVS 167
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-203 |
1.31e-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: 72.30 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTTTGHLiykcGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 83 AKYY----------------------ITIIDAPGHRDFIKNMITGTSQADCAVLVVA----CgtgefeagisKNGQTREH 136
Cdd:cd01888 53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAanepC----------PQPQTSEH 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 137 ALLAQTLGVKQLIVACNKMDSTEPPFSEARFTEITNevsgFIKkiGYNPKAVPFVPIS---GFNGDNMLE 203
Cdd:cd01888 123 LAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVK--GTIAENAPIIPISaqlKYNIDVLCE 186
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-198 |
2.14e-14 |
|
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: 75.47 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtiekfekeaqeMGK---GSFkyawVLDKLKAERERGITIDIALWKFETAKY 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR------------IGEvhdGNT----VMDWMPEEQERGITITSAATTCEWKGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 86 YITIIDAPGHRDFIKNMITGTSQADCAVLVVaCGTGEFEAgiskngQTREHALLAQTLGVKQlIVACNKMDSTeppfsEA 165
Cdd:COG0480 75 KINIIDTPGHVDFTGEVERSLRVLDGAVVVF-DAVAGVEP------QTETVWRQADKYGVPR-IVFVNKMDRE-----GA 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 17569207 166 RFTEITNEvsgfIKKIgYNPKAVPF-VPI---SGFNG 198
Cdd:COG0480 142 DFDRVLEQ----LKER-LGANPVPLqLPIgaeDDFKG 173
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
245-327 |
2.96e-14 |
|
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: 67.90 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 245 PLRLPLQDVYKigGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGS 324
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
....
gi 17569207 325 V-CS 327
Cdd:cd04089 79 VlCS 82
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-156 |
1.72e-13 |
|
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: 69.96 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaqemgkGSfkyawV------LDKLKAERERGITIDIALWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569207 83 AKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGefeagisKNGQTRehaLLAQTLgvKQL----IVACNKMD 156
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKID 127
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
8.64e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 70.37 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAqemgkgsfkyawvlDKLKAERERGITIDIAL----WKfeta 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17569207 84 KYYITIIDAPGHRDFIKNMITGTSQADCAVLVvacgtgeFEAGISKNGQTREHALLAQTLGVKQLIVAcNKMD 156
Cdd:PRK13351 72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVV-------FDAVTGVQPQTETVWRQADRYGIPRLIFI-NKMD 136
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-174 |
1.55e-12 |
|
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: 66.08 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAQEMGKGsfkyawVLDKLKAERERGITIdiaLWKfETAKYY-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 87 --ITIIDAPGHRDF------IKNMitgtsqADCAVLVVACGTGEFEagiskngQTR---EHALLAqtlGVKqLIVACNKM 155
Cdd:cd01891 65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKI 127
|
170
....*....|....*....
gi 17569207 156 DSteppfSEARFTEITNEV 174
Cdd:cd01891 128 DR-----PDARPEEVVDEV 141
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-165 |
2.09e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 69.38 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETAKYYITIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569207 92 APGHRDFIKNMITGTSQADCAVLVVaCGTGEFEAgiskngQTREHALLAQTLGVKQLIVAcNKMDSTEPPFSEA 165
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVV-CAVGGVEP------QTETVWRQAEKYGVPRIIFV-NKMDRAGADFFRV 132
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-198 |
3.97e-12 |
|
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: 66.36 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIA----LWKfetaK 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIG-EVHGGGA------------TMDWMEQERERGITIQSAattcFWK----D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 85 YYITIIDAPGHRDFIKNMITGTSQADCAVLVVaCGTGEFEagiskngqtrehallAQTLGV-KQL-------IVACNKMD 156
Cdd:cd01886 64 HRINIIDTPGHVDFTIEVERSLRVLDGAVAVF-DAVAGVQ---------------PQTETVwRQAdrygvprIAFVNKMD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17569207 157 STeppfsEARFTEITNEVsgfIKKIGYNPKAVpFVPI---SGFNG 198
Cdd:cd01886 128 RT-----GADFYRVVEQI---REKLGANPVPL-QLPIgaeDDFEG 163
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-156 |
4.73e-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: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaqemgkGSFkyawVLDKLKAERERGITIDIALWKFETAKYYI 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17569207 88 TIIDAPGHRDFIKNMITGTSQADCAVLVVacgtgEFEAGISknGQTREHALLAQTLGVKQLIVAcNKMD 156
Cdd:cd04170 67 NLIDTPGYADFVGETLSALRAVDAALIVV-----EAQSGVE--VGTEKVWEFLDDAKLPRIIFI-NKMD 127
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-279 |
4.76e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 68.20 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekEAQEMgkgsfkyawVLDKLKAERERGITIDIALWKFETAKYYIT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA------ETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 89 IIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEagiskngQTREHALLAQTLGVKQLIVaCNKMDSteppfSEARFT 168
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDR-----PGARPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 169 EITNEVSGFIKKIGYNPKAV--PFVPISGFNGDNMLEvssnmpwfkgwaverKEGNASGKT-LLEAL-DSIIPPQRPTDR 244
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQLdfPIVYASALNGIAGLD---------------HEDMAEDMTpLYQAIvDHVPAPDVDLDG 203
|
250 260 270
....*....|....*....|....*....|....*
gi 17569207 245 PLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVT 279
Cdd:PRK10218 204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
245-328 |
1.43e-11 |
|
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: 60.21 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 245 PLRLPLQDVYKiGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMH-HESLPEAVPGDNVGFNVKNVSVKDIRRG 323
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 17569207 324 SVCSD 328
Cdd:cd03698 80 DILSS 84
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-306 |
4.22e-11 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 65.04 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAQEMgkgsfkyawVLDKLKAERERGITIdialwkfeTAK---- 84
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI--------LAKntav 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 85 ----YYITIIDAPGHRDF------IKNMitgtsqADCAVLVV-AcgtgeFEagisknG---QTR---EHALlaqTLGVKq 147
Cdd:COG1217 65 rykgVKINIVDTPGHADFggeverVLSM------VDGVLLLVdA-----FE------GpmpQTRfvlKKAL---ELGLK- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 148 LIVACNKMDSteppfSEARFTEITNEVSG-FIkKIGYNPKAVPFvPI---SGFNgdnmlevssnmpwfkGWAVERKEGNA 223
Cdd:COG1217 124 PIVVINKIDR-----PDARPDEVVDEVFDlFI-ELGATDEQLDF-PVvyaSARN---------------GWASLDLDDPG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 224 SGKT-LLEA-LDSIIPPQRPTDRPLRlpLQ------DVYkIGGIGtvpVGRVETGIIKPGMVVTFAPQNVTTE---VKSV 292
Cdd:COG1217 182 EDLTpLFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVALIKRDGKVEkgkITKL 255
|
330
....*....|....*...
gi 17569207 293 EMHH----ESLPEAVPGD 306
Cdd:COG1217 256 FGFEglerVEVEEAEAGD 273
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-201 |
6.91e-11 |
|
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: 60.56 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaqemgkgsfkyawVLDKLK----AERE-RGITIDIALWKFETAK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 85 YY--ITIIDAPGHRDFiKNMIT-GTSQADCAVLVVACGTGeFEAgiskngQTRE---HALLAQTlgvkQLIVACNKMDst 158
Cdd:cd01887 47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID-- 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17569207 159 EPPFSEARFTEITNEVSgfikKIGYNP----KAVPFVPISGFNGDNM 201
Cdd:cd01887 113 KPYGTEADPERVKNELS----ELGLVGeewgGDVSIVPISAKTGEGI 155
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
1.67e-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: 61.46 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAQEM-GKGSFKYAwVLDKLKAERERGITIDIALWKFETAKYYITII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 17569207 91 DAPGHRDFIKNMITGTSQADCAVLVVACGTG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-211 |
1.89e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 60.36 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKcggIDKRTIEKFEKEAQEmgkgsfKYawvLDKLKAERERGITI-----DIALWKFETA 83
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ---THKRTPSVKLGWKPL------RY---TDTRKDEQERGISIksnpiSLVLEDSKGK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 84 KYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTgefeaGISKNGQTREHALLAQTLgvkQLIVACNKMDS--TE-- 159
Cdd:cd04167 70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERLIRHAIQEGL---PMVLVINKIDRliLElk 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17569207 160 -PPfSEARFT--EITNEVSGFIKKIGYNPKAVpFVPISGfngdNMLEVSSNMPWF 211
Cdd:cd04167 142 lPP-TDAYYKlrHTIDEINNYIASFSTTEGFL-VSPELG----NVLFASSKFGFC 190
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
246-325 |
2.56e-10 |
|
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: 56.42 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 246 LRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKN-VsvkDIRRGS 324
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77
|
.
gi 17569207 325 V 325
Cdd:cd03695 78 L 78
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
252-325 |
1.61e-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: 54.53 E-value: 1.61e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569207 252 DVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQN----VTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGSV 325
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-121 |
4.04e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 58.91 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAqemGKGSFkyawvLDKLKAERERGITID---IAL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNA---GDARF-----TDTRADEQERGITIKstgISL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17569207 78 ---WKFETAK----YYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTG 121
Cdd:PTZ00416 78 yyeHDLEDGDdkqpFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEG 128
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-98 |
7.81e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 57.95 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeaqeMGKgsfkyAWVLDKLKAERERGITIDIA----LWKFETAK 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGE-----QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
|
90
....*....|....
gi 17569207 85 YYITIIDAPGHRDF 98
Cdd:PRK07560 87 YLINLIDTPGHVDF 100
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-118 |
1.78e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 57.04 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfekeAQEMGKGsfkyAWVLDKLKAERERGITID---IALW------- 78
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGII-----------AQEVAGD----VRMTDTRADEAERGITIKstgISLYyemtdes 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17569207 79 ------KFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVAC 118
Cdd:PLN00116 86 lkdfkgERDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDC 131
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-305 |
3.95e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 55.40 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaqemgkgsfkyawvldKLKAERERGITIDIAlwkFETAKYY- 86
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLG---YANAKIYk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 87 -----------------------------------ITIIDAPGHRDFIKNMITGTSQADCAVLVVAcGTGEFeagisKNG 131
Cdd:PTZ00327 84 cpkcprptcyqsygsskpdnppcpgcghkmtlkrhVSFVDCPGHDILMATMLNGAAVMDAALLLIA-ANESC-----PQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 132 QTREHALLAQTLGVKQLIVACNKMDSTEPPFSEARFTEITNEVSGFIKkigynpKAVPFVPIS---GFNGDnmlevssnm 208
Cdd:PTZ00327 158 QTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIA------DNAPIIPISaqlKYNID--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 209 pwfkgwaverkegnasgkTLLEALDSIIP-PQRPTDRPLRL----------PLQDVYKI-GGI--GTVPVGRVETGI--- 271
Cdd:PTZ00327 223 ------------------VVLEYICTQIPiPKRDLTSPPRMivirsfdvnkPGEDIENLkGGVagGSILQGVLKVGDeie 284
|
330 340 350
....*....|....*....|....*....|....*....
gi 17569207 272 IKPGMVVTFAPQNVT-----TEVKSVEMHHESLPEAVPG 305
Cdd:PTZ00327 285 IRPGIISKDSGGEFTcrpirTRIVSLFAENNELQYAVPG 323
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
9-182 |
4.34e-07 |
|
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: 50.75 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaqemGKGSFKYAwvLDKLKAERERGIT---------------- 72
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTssvsndilgfdsdgev 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 73 ----IDIALWK----FETAKYYITIIDAPGHRDFIKNMITGTS--QADCAVLVVACGTGEfeagiskNGQTREHALLAQT 142
Cdd:cd04165 64 vnypDNHLGELdveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALA 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17569207 143 LGVKQLIVAcNKMDSTeppfSEARFTEITNEVSGFIKKIG 182
Cdd:cd04165 137 LKVPVFVVV-TKIDMT----PANVLQETLKDLKRLLKSPG 171
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-204 |
3.12e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 47.07 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIAL--WKFETAKYYIT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 89 IIDAPGHRDFIKNMITGT-----SQADCAVLVVACGTGEFEAGIskngqTREHALLAQTLGVKqLIVACNKMDSTEPpfs 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIP-IILVGNKIDLLEE--- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17569207 164 earfTEITNEVSGFIKKIGYNpkaVPFVPISGFNGDNMLEV 204
Cdd:cd00882 122 ----REVEELLRLEELAKILG---VPVFEVSAKTGEGVDEL 155
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
251-325 |
1.22e-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: 40.36 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17569207 251 QDVYKIGGiGTVPVGRVETGIIKPGMVVTfAPQNVTTeVKSVEMHHESLPEAVPGDNVGFNVKNVSvkDIRRGSV 325
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKGVAL-IRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-203 |
1.59e-04 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 44.05 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 10 IVVIGHVDSGKSTTtghliykcggIDKrtIEKFEKEAQEMGkgsfkyawvldklkaererGITIDIA----LWKFETAKY 85
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDK--IRKTQIAQKEAG-------------------GITQKIGayevEFEYKDENQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 86 YITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGefeagisKNGQTREHALLAQTLGVKqLIVACNKMD----STEPP 161
Cdd:CHL00189 296 KIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAINYIQAANVP-IIVAINKIDkanaNTERI 367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17569207 162 FSE-ARFTEITNEVSGfikkigynpkAVPFVPIS---GFNGDNMLE 203
Cdd:CHL00189 368 KQQlAKYNLIPEKWGG----------DTPMIPISasqGTNIDKLLE 403
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-203 |
9.74e-04 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 41.54 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 10 IVVI-GHVDSGKSTttghliykcggidkrtiekfekeaqemgkgsfkyawVLDKLK----AERE-RGITIDIALWKFETA 83
Cdd:COG0532 6 VVTVmGHVDHGKTS------------------------------------LLDAIRktnvAAGEaGGITQHIGAYQVETN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 84 KYYITIIDAPGHRDFIKNMITGTSQADCAVLVVAcgtgefeA--GISKngQTRE---HALLAqtlGVKqLIVACNKMDSt 158
Cdd:COG0532 50 GGKITFLDTPGHEAFTAMRARGAQVTDIVILVVA-------AddGVMP--QTIEainHAKAA---GVP-IIVAINKIDK- 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17569207 159 eppfSEARFTEITNEVSgfikKIGYNPKA----VPFVPISGFNG---DNMLE 203
Cdd:COG0532 116 ----PGANPDRVKQELA----EHGLVPEEwggdTIFVPVSAKTGegiDELLE 159
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-204 |
9.93e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 39.96 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTttghLIYKcggidkrtiekfekeaqemgkgsFKYAWVlDKLKAERERGITIDIALWKFETAKYYI 87
Cdd:COG1100 4 KKIVVVGTGGVGKTS----LVNR-----------------------LVGDIF-SLEKYLSTNGVTIDKKELKLDGLDVDL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 88 TIIDAPGHRDFIK---NMITGTSQADCAVLVVACgtgefeagiskngqTRE---------HALLAQTLGVKQLIVACNKM 155
Cdd:COG1100 56 VIWDTPGQDEFREtrqFYARQLTGASLYLFVVDG--------------TREetlqslyelLESLRRLGKKSPIILVLNKI 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17569207 156 DSTEPPfsearftEITNEvsGFIKKIGYNPKAVPFVPISGFNGDNMLEV 204
Cdd:COG1100 122 DLYDEE-------EIEDE--ERLKEALSEDNIVEVVATSAKTGEGVEEL 161
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
338-398 |
1.60e-03 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 294007 [Multi-domain] Cd Length: 87 Bit Score: 37.50 E-value: 1.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 338 RTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFnelkEKVDR---RTGKKVE-DF-----PKFLKSGD 398
Cdd:cd03708 4 WEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDKevlRTGDRALvRFrflyrPEYLREGQ 69
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
12-121 |
2.00e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 40.50 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAQEM-GKGSFKYA---WvldkLKAERERGITIDIALWKFETAKYYI 87
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17569207 88 TIIDAPGHRDFiknmitgtSQ--------ADCAVLVVACGTG 121
Cdd:PRK00741 82 NLLDTPGHEDF--------SEdtyrtltaVDSALMVIDAAKG 115
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
337-438 |
3.36e-03 |
|
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N- and C-termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 294010 [Multi-domain] Cd Length: 103 Bit Score: 37.03 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 337 ARTFHAQVIIMNH-PGQISNGYtpVLDCHTAHIACKFNELKEKVDRRTGKKVEDfpKFLKSGDAGIVELIPTKPLCVESF 415
Cdd:cd04095 3 SDQFEATLVWMDEkPLQPGRRY--LLKHGTRTVRARVTEIDYRIDVNTLEREPA--DTLALNDIGRVTLRLAEPLAFDPY 78
|
90 100
....*....|....*....|....*.
gi 17569207 416 TDYAPLGRFAVRDmRQ---TVAVGVI 438
Cdd:cd04095 79 AENRATGSFILID-RLtnaTVAAGMI 103
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-204 |
3.84e-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: 38.12 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 8 INIVVIGHVDSGKSTTTGHLIYKcggidkrtiEKFEKEAQEmgkGSFKYAWVLdklkAERERGITIDIALWkfetakyyi 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---------KGSITEYYP---GTTRNYVTT----VIEEDGKTYKFNLL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 88 tiiDAPGHRDFIKNMITGTSQADcAVLVVACGTG---EFEAGISKNGQTREHALlaqTLGVKqLIVACNKMDsteppfse 164
Cdd:TIGR00231 57 ---DTAGQEDYDAIRRLYYPQVE-RSLRVFDIVIlvlDVEEILEKQTKEIIHHA---DSGVP-IILVGNKID-------- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17569207 165 arftEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEV 204
Cdd:TIGR00231 121 ----LKDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSA 156
|
|
| GTP_EFTU_D4 |
pfam14578 |
Elongation factor Tu domain 4; Elongation factor Tu consists of several structural domains, ... |
264-314 |
7.12e-03 |
|
Elongation factor Tu domain 4; Elongation factor Tu consists of several structural domains, and this is usually the fourth.
Pssm-ID: 405293 [Multi-domain] Cd Length: 86 Bit Score: 35.69 E-value: 7.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17569207 264 VG-RVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKN 314
Cdd:pfam14578 20 VGvEVLGGIIKPGYPLIREDGREVGEIMQIQDNGKSLDEAKAGQEVAISIEG 71
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
340-438 |
1.00e-02 |
|
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: 35.28 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569207 340 FHAQVIIMN------HPGqISNGYTPVLDCHTAHIACKFNELKEKvdrrtgkkvedfpKFLKSGDAGIVELIPTKPLCVE 413
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRIDLPEGK-------------EMVMPGEDTSVKLTLLKPMVLE 71
|
90 100
....*....|....*....|....*
gi 17569207 414 sftdyaPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03706 72 ------KGQRFTLREGGRTIGTGVV 90
|
|
|