|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-460 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 909.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 81 ETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 161 AYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKgwkverkegnasGVSLLEALDTILPPTR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDI 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 321 RRGNVCGDSKADPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 401 IVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKsggAGKVTKSAQKAQK 460
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-457 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 708.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 81 ETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 161 AYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGwkverkegnasgVSLLEALDTILPPTR 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDI 320
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 321 RRGNVCGDSKADPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAA 400
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50054162 401 IVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQK 457
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-444 |
0e+00 |
|
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]
Pssm-ID: 129574 [Multi-domain] Cd Length: 426 Bit Score: 681.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 81 ETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagisKNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 161 aYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKgwkverkegnasGVSLLEALDTILPPTR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDI 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 321 RRGNVCGDSKaDPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 50054162 401 IVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKK 444
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-444 |
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: 677.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 81 ETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 161 aYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKgwkverkegnasGVSLLEALDTILPPTR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDI 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 321 RRGNVCGDSkADPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAA 400
Cdd:COG5256 300 KRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 50054162 401 IVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKK 444
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPK 422
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-444 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 675.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEpaY 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 163 SEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKgwkverkegnasGVSLLEALDTILPPTRPT 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRR 322
Cdd:PRK12317 223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 323 GNVCGdSKADPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIV 402
Cdd:PRK12317 303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 50054162 403 EMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKK 444
Cdd:PRK12317 382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPA 423
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-238 |
1.31e-160 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 452.72 E-value: 1.31e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYIT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYD 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 169 EIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWkverkegnasgvSLLEALDTILPP 238
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-438 |
1.11e-96 |
|
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: 297.38 E-value: 1.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 4 EKTHINIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFE 81
Cdd:COG2895 14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 82 TTKY-YItIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDST 158
Cdd:COG2895 92 TPKRkFI-IADTPGHEQYTRNMVTGASTADLAILLIDArkGVLE---------QTRRHSYIASLLGIRHVVVAVNKMDLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 159 EpaYSEKRYDEIVKEVSAYIKKIGYNPATvpFVPISGWHGDNMLEPSPNMPWFKgwkverkegnasGVSLLEALDTILPP 238
Cdd:COG2895 162 D--YSEEVFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 239 TRPTDKPLRLPLQDVYKiggigtvP-------VGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGF- 310
Cdd:COG2895 226 EDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLt 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 311 ---NVknvsvkDIRRGNVCgdSKAD-PPQEAAQFTSQVIILN-HPGQISAGYspVIDCHTAHIACKFAELKEKIDRRSGK 385
Cdd:COG2895 299 ledEI------DISRGDVI--VAADaPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLE 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 50054162 386 KLEdnPKSLKSGDAAIVEMVPGKPMCVESFSQYPPLGRFAV--RDMRQTVAVGVI 438
Cdd:COG2895 369 HEA--ADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMI 421
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-238 |
1.06e-78 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 242.82 E-value: 1.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETTK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 85 YYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGVKqLIVGVNKMDSTepaySE 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50054162 165 KRYDEIVKEVS-AYIKKIGYNPATVPFVPISGWHGDNMLEpspnmpwfkgwkverkegnasgvsLLEALDTILPP 238
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
336-438 |
6.97e-72 |
|
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: 222.07 E-value: 6.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 336 EAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESF 415
Cdd:cd03705 2 EAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETF 81
|
90 100
....*....|....*....|...
gi 50054162 416 SQYPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705 82 SEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-438 |
7.67e-65 |
|
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: 214.54 E-value: 7.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGK--GSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 92 APGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpaYSEKRYDEIV 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 172 KEVSAYIKKIGynPATVPFVPISGWHGDNMLEPSPNMPWFkgwkverkegnaSGVSLLEALDTILPPTRPTDKPLRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 252 DVYKI-----GGIGTVPVGRVEtgilrPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkDIRRGNVC 326
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 327 GdSKADPPQEAAQFTSQVIIL-NHPgqISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEdnPKSLKSGDAAIVEMV 405
Cdd:TIGR02034 297 A-AADSAPEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGA--AKSLELNEIGRVNLS 371
|
410 420 430
....*....|....*....|....*....|....*
gi 50054162 406 PGKPMCVESFSQYPPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 372 LDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-461 |
2.13e-63 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 216.33 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMG--KGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 92 APGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpaYSEKRYDE 169
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDArkGVLT---------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 170 IVKEVSAYIKKIGYnpATVPFVPISGWHGDNMLEPSPNMPWFkgwkverkegnaSGVSLLEALDTILPPTRPTDKPLRLP 249
Cdd:PRK05506 180 IVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 250 LQDVYKI-----GGIGTvpvgrVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVgfnvkNVSVKD---IR 321
Cdd:PRK05506 246 VQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidIS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 322 RGNVCGDSkADPPQEAAQFTSQVIILN----HPGqisAGYspVIDCHTAHIACKFAELKEKID-----RRSGKKLEDNpk 392
Cdd:PRK05506 316 RGDMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDvntleRLAAKTLELN-- 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50054162 393 slksgDAAIVEMVPGKPMCVESFSQYPPLGRFAV--RDMRQTVAVGVIK-------NVEKKSGGAGKVTKSAQKAQKA 461
Cdd:PRK05506 388 -----EIGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIDfalrratNVHWQASDVSREARAARKGQKP 460
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-235 |
3.87e-62 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 200.87 E-value: 3.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAAEMGKgsFKYAWVLDKLKAERERGITIDISLWKFETTKY 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 86 YITIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpaYS 163
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDArkGVLE---------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50054162 164 EKRYDEIVKEVSAYIKKIGYNPATvpFVPISGWHGDNMLEPSPNMPWFKgwkverkegnasGVSLLEALDTI 235
Cdd:cd04166 148 EEVFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
242-332 |
4.84e-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: 4.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIR 321
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 50054162 322 RGNVCGDSKAD 332
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-325 |
1.15e-57 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 195.37 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 76 SLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 156 DSTEpaysekryD----EIVK-EVSAYIKKIGYNPATVPFVPISGWhgdNMLEPSPNMPWFKgwKVERkegnasgvsLLE 230
Cdd:COG0050 139 DMVD--------DeellELVEmEVRELLSKYGFPGDDTPIIRGSAL---KALEGDPDPEWEK--KILE---------LMD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 231 ALDTILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGmvvtfAPVNI-------TTEVKSVEMHHEALSEA 302
Cdd:COG0050 197 AVDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVG-----DEVEIvgirdtqKTVVTGVEMFRKLLDEG 271
|
330 340
....*....|....*....|...
gi 50054162 303 LPGDNVGFNVKNVSVKDIRRGNV 325
Cdd:COG0050 272 EAGDNVGLLLRGIKREDVERGQV 294
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-443 |
9.81e-57 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 192.85 E-value: 9.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLiykcggidkrtiekfEKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 76 SLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 156 DSTEpaySEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGdnmLEPSPnmPWFKgwKVERkegnasgvsLLEALDTI 235
Cdd:PRK12736 139 DLVD---DEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKA---LEGDP--KWED--AIME---------LMDAVDEY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 236 LP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPG---MVVTFAPVNITTeVKSVEMHHEALSEALPGDNVGFN 311
Cdd:PRK12736 200 IPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKETQKTV-VTGVEMFRKLLDEGQAGDNVGVL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 312 VKNVSVKDIRRGNVCGDSKADPPQEaaQFTSQVIILN------HPGqISAGYSPVIDCHTAhiackfaelkekiDRRSGK 385
Cdd:PRK12736 279 LRGVDRDEVERGQVLAKPGSIKPHT--KFKAEVYILTkeeggrHTP-FFNNYRPQFYFRTT-------------DVTGSI 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 50054162 386 KLEDNPKSLKSGDAAIVEMVPGKPMCVESFSqypplgRFAVRDMRQTVAVGVIKNVEK 443
Cdd:PRK12736 343 ELPEGTEMVMPGDNVTITVELIHPIAMEQGL------KFAIREGGRTVGAGTVTEILD 394
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-238 |
2.20e-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: 184.81 E-value: 2.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaaemgkgsfkyaWVLDKLKAERERGITIDISLWKFETTKYYIT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAyTLGVKQLIVGVNKMDSTEPAysekRYD 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRVGEE----DFD 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50054162 169 EIVKEVSAYIKKIGY---NPATVPFVPISGWHGDNMLEpspnmpwfkgwkverkegnasgvsLLEALDTILPP 238
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------------------------LLDAIVEHLPP 182
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-441 |
3.12e-56 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 191.71 E-value: 3.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAWVlDKLKAERERGITIDISLWKFET 82
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpay 162
Cdd:CHL00071 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 163 sEKRYDEIVK-EVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMpwfkgwkverKEGNASGV----SLLEALDTILP 237
Cdd:CHL00071 143 -DEELLELVElEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKI----------KRGENKWVdkiyNLMDAVDSYIP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 238 -PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNIT--TEVKSVEMHHEALSEALPGDNVGFNVKN 314
Cdd:CHL00071 212 tPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETktTTVTGLEMFQKTLDEGLAGDNVGILLRG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 315 VSVKDIRRGNVCGDSKADPPQeaAQFTSQVIILN------HPGqISAGYSPVIDCHTAHIACKFaelkekidrrsgkkle 388
Cdd:CHL00071 292 IQKEDIERGMVLAKPGTITPH--TKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKI---------------- 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50054162 389 dnpKSLKSGDAAIVEMV-PGK--PMCVESFSqypPLG-----RFAVRDMRQTVAVGVIKNV 441
Cdd:CHL00071 353 ---ESFTADDGSKTEMVmPGDriKMTVELIY---PIAiekgmRFAIREGGRTVGAGVVSKI 407
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-347 |
7.78e-56 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 190.40 E-value: 7.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFK-YAWVlDKLKAERERGITID 74
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITIN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 75 ISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNK 154
Cdd:PRK00049 65 TAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 155 MDSTEpaysekryD----EIVK-EVSAYIKKIGYNPATVPFVPISGWHGdnmLEPSPNMPWFKgwKVERkegnasgvsLL 229
Cdd:PRK00049 138 CDMVD--------DeellELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEK--KILE---------LM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 230 EALDTILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPG---MVVTFAPVNITTeVKSVEMHHEALSEALPG 305
Cdd:PRK00049 196 DAVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAG 274
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 50054162 306 DNVGFNVKNVSVKDIRRGNVCGDSKADPPQeaAQFTSQVIIL 347
Cdd:PRK00049 275 DNVGALLRGIKREDVERGQVLAKPGSITPH--TKFEAEVYVL 314
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-438 |
1.87e-54 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 188.97 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 14 GHVDSGKSTTTGHLIYkcggiDKRTIekFEKEAAEMGKGSFK---------YAWVLDKLKAERERGITIDISLWKFETTK 84
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 85 YYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpaYSE 164
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 165 KRYDEIVKEVSAYIKKIGYNPaTVPFVPISGWHGDNMLEPSPNMPWFkgwkverkegnaSGVSLLEALDTILPPTRPTDK 244
Cdd:PRK05124 178 EVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 245 PLRLPLQDVYKI-----GGIGTvpvgrVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkD 319
Cdd:PRK05124 245 PFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--D 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 320 IRRGNVCGDSkADPPQEAAQFTSQVIILNhPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEdnPKSLKSGDA 399
Cdd:PRK05124 318 ISRGDLLVAA-DEALQAVQHASADVVWMA-EQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLTQRE--AENLPLNGI 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 50054162 400 AIVEMVPGKPMCVESFSQYPPLGRFAV--RDMRQTVAVGVI 438
Cdd:PRK05124 394 GLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMV 434
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-441 |
1.99e-54 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 189.06 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpay 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 163 SEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMpwfkgwkverKEGNASGV----SLLEALDTILP- 237
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALMENPNI----------KRGDNKWVdkiyELMDAVDSYIPi 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 238 PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNIT--TEVKSVEMHHEALSEALPGDNVGFNVKNV 315
Cdd:PLN03126 282 PQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 316 SVKDIRRGNVCgdSKADPPQEAAQFTSQVIILNHP--GQIS---AGYSPVIDCHTAHIACKFAELKEKIDRRSgkkledn 390
Cdd:PLN03126 362 QKADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES------- 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50054162 391 pKSLKSGDAA--IVEMVpgKPMCVESFSqypplgRFAVRDMRQTVAVGVIKNV 441
Cdd:PLN03126 433 -KMVMPGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-347 |
1.18e-53 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 184.66 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 76 SLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 156 DSTEpaysEKRYDEIVK-EVSAYIKKIGYNPATVPFVPISGWHGdnmLEPSPNMPWFKgwKVERkegnasgvsLLEALDT 234
Cdd:PRK12735 139 DMVD----DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEA--KILE---------LMDAVDS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 235 ILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPG---MVVTFAPVNITTeVKSVEMHHEALSEALPGDNVGF 310
Cdd:PRK12735 201 YIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVGV 279
|
330 340 350
....*....|....*....|....*....|....*..
gi 50054162 311 NVKNVSVKDIRRGNVCGDSKADPPQeaAQFTSQVIIL 347
Cdd:PRK12735 280 LLRGTKREDVERGQVLAKPGSIKPH--TKFEAEVYVL 314
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-441 |
1.64e-51 |
|
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: 178.82 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:TIGR00485 8 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpay 162
Cdd:TIGR00485 73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 163 SEKRYDEIVKEVSAYIKKIGYnpatvpfvpisgwhgdnmlePSPNMPWFKGWKVERKEGNASGVS----LLEALDTILP- 237
Cdd:TIGR00485 143 DEELLELVEMEVRELLSQYDF--------------------PGDDTPIIRGSALKALEGDAEWEAkileLMDAVDEYIPt 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 238 PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTE--VKSVEMHHEALSEALPGDNVGFNVKNV 315
Cdd:TIGR00485 203 PEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKttVTGVEMFRKELDEGRAGDNVGLLLRGI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 316 SVKDIRRGNVCGDSKADPPQeaAQFTSQVIILN------HPGQISaGYSPVIDCHTAHIACKFaelkekidrrsgkKLED 389
Cdd:TIGR00485 283 KREEIERGMVLAKPGSIKPH--TKFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDVTGTI-------------ELPE 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 50054162 390 NPKSLKSGD--AAIVEMVpgKPMCVESFSqypplgRFAVRDMRQTVAVGVIKNV 441
Cdd:TIGR00485 347 GVEMVMPGDnvKMTVELI--SPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-441 |
3.54e-51 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 179.64 E-value: 3.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpay 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVD--- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 163 sEKRYDEIVK-EVSAYIKKIGYNPATVPFVPISGWHGdnmlepspnmpwFKGwkVERKEGNASGVSLLEALDTILP-PTR 240
Cdd:PLN03127 192 -DEELLELVEmELRELLSFYKFPGDEIPIIRGSALSA------------LQG--TNDEIGKNAILKLMDAVDEYIPePVR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPG---MVVTFAP-VNITTEVKSVEMHHEALSEALPGDNVGFNVKNVS 316
Cdd:PLN03127 257 VLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 317 VKDIRRGNVCgdSKADPPQEAAQFTSQVIILN------HPGQISaGYSPVIDCHTAHIACKFaelkekidrrsgkKLEDN 390
Cdd:PLN03127 337 REDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFS-NYRPQFYLRTADVTGKV-------------ELPEG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50054162 391 PKSLKSGD--AAIVEMVpgKPMCVEsfsqypPLGRFAVRDMRQTVAVGVIKNV 441
Cdd:PLN03127 401 VKMVMPGDnvTAVFELI--SPVPLE------PGQRFALREGGRTVGAGVVSKV 445
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-325 |
3.20e-40 |
|
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: 152.76 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISlwkfettkyY- 86
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLG---------Fa 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 87 ---------ITIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREH-ALLAyTLGVKQLIVGVNK 154
Cdd:COG3276 44 ylplpdgrrLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAdeGVMP---------QTREHlAILD-LLGIKRGIVVLTK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 155 MDSTEPAysekRYDEIVKEVSAYIKkiGYNPATVPFVPISGWHGDNMLEpspnmpwfkgwkverkegnasgvsLLEALDT 234
Cdd:COG3276 114 ADLVDEE----WLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEGIDE------------------------LRAALDA 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 235 IL--PPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNV 312
Cdd:COG3276 164 LAaaVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNL 243
|
330
....*....|...
gi 50054162 313 KNVSVKDIRRGNV 325
Cdd:COG3276 244 AGVEKEEIERGDV 256
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
333-441 |
3.98e-35 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 126.23 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 333 PPQEAAQFTSQVIILNH-----PGQISAGYSPVIDCHTAHIACKFAELKEKIDrrSGKKLEdNPKSLKSGDAAIVEMVPG 407
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 50054162 408 KPMCVESFSqypplgRFAVRDMRQTVAVGVIKNV 441
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-238 |
1.13e-34 |
|
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: 128.09 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 6 THINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKY 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 86 YITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEpaysEK 165
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD----DE 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50054162 166 RYDEIVK-EVSAYIKKIGYNPATVPFVPISGWhgdNMLEPSPNMPWFKgwKVERkegnasgvsLLEALDTILPP 238
Cdd:cd01884 135 ELLELVEmEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVD--KILE---------LLDALDSYIPT 194
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-333 |
1.52e-32 |
|
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: 130.38 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFETTKYYI 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDSTEpaysekry 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDA-----DEGVMT--QTGEHLAVLDLLGIPHTIVVITKADRVN-------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 168 DEIVKEVSAYIKKIgynpatvpfvpisgwhgdnmLEPSPNMPWFKGWKVERKEGNASG------VSLLEALDtilppTRP 241
Cdd:TIGR00475 118 EEEIKRTEMFMKQI--------------------LNSYIFLKNAKIFKTSAKTGQGIGelkkelKNLLESLD-----IKR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIR 321
Cdd:TIGR00475 173 IQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLK 252
|
330
....*....|..
gi 50054162 322 RGnVCGDSKADP 333
Cdd:TIGR00475 253 RG-LLILTPEDP 263
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
340-438 |
2.62e-30 |
|
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: 113.26 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 340 FTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKleDNPKSLKSGDAAIVEMVPGKPMCVESFSQYP 419
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 50054162 420 PLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-194 |
1.05e-25 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 102.68 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETTKYyI 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFayLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDSTEPAysekRY 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RL 121
|
170 180
....*....|....*....|....*..
gi 50054162 168 DEIVKEVSAYIKKIGYNPAtvPFVPIS 194
Cdd:cd04171 122 ELVEEEILELLAGTFLADA--PIFPVS 146
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
340-441 |
8.00e-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: 95.70 E-value: 8.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 340 FTSQVIILNHPGQI-SAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQY 418
Cdd:cd03704 6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
|
90 100
....*....|....*....|...
gi 50054162 419 PPLGRFAVRDMRQTVAVGVIKNV 441
Cdd:cd03704 86 PQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
246-327 |
1.74e-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: 82.70 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 246 LRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNvsVKDIRRGNV 325
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
..
gi 50054162 326 CG 327
Cdd:cd01342 79 LT 80
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-309 |
2.82e-18 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 86.44 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DISLWK--- 79
Cdd:PRK04000 10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKcpd 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 80 FETTKYYIT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN-----GQTREH 136
Cdd:PRK04000 62 CEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAA-----------NepcpqPQTKEH 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 137 ALLAYTLGVKQLIVGVNKMD--STEPAysEKRYDEIVKEVSAYIkkigynPATVPFVPISGWHGDNMlepspnmpwfkgw 214
Cdd:PRK04000 131 LMALDIIGIKNIVIVQNKIDlvSKERA--LENYEQIKEFVKGTV------AENAPIIPVSALHKVNI------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 215 kverkegnasgVSLLEALDTILP-PTRPTDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG--I-LRPGMV 277
Cdd:PRK04000 190 -----------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeIeIRPGIK 258
|
330 340 350
....*....|....*....|....*....|....*.
gi 50054162 278 VTFAP----VNITTEVKSVEMHHEALSEALPGDNVG 309
Cdd:PRK04000 259 VEEGGktkwEPITTKIVSLRAGGEKVEEARPGGLVG 294
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
340-441 |
3.40e-18 |
|
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: 79.90 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 340 FTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYP 419
Cdd:cd04093 8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKDNK 87
|
90 100
....*....|....*....|..
gi 50054162 420 PLGRFAVRDMRQTVAVGVIKNV 441
Cdd:cd04093 88 ELGRFVLRRGGETIAAGIVTEI 109
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-181 |
1.07e-17 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 81.51 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAaemgkGSFKYawvLDKLKAERERGITID---ISLwKFETTK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 85 ------YYITIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTreHALL--AYTLGVKQLIVgVNK 154
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAveGVCV---------QT--ETVLrqALEERVKPVLV-INK 133
|
170 180 190
....*....|....*....|....*....|....*
gi 50054162 155 MD--------STEPAYseKRYDEIVKEVSAYIKKI 181
Cdd:cd01885 134 IDrlilelklSPEEAY--QRLLRIVEDVNAIIETY 166
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-178 |
2.50e-17 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 81.13 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaemgkGSfkyawV------LDKLKAERERGITIDISLWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTRE--HALLAYTLGVkqlIVGVNKMDsT 158
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAveGV---------QAQTRIlfRLLRKLNIPT---IIFVNKID-R 128
|
170 180
....*....|....*....|
gi 50054162 159 EPAYSEKRYDEIVKEVSAYI 178
Cdd:cd04168 129 AGADLEKVYQEIKEKLSPDI 148
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
246-326 |
2.14e-16 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 73.71 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 246 LRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNV 325
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
.
gi 50054162 326 C 326
Cdd:cd03696 81 L 81
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-323 |
1.09e-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: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMGkgsfkyAWVLDKLKAERERGITID---ISL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 82 T-TKYYITIIDAPGHRDFiknmitgT-----SQADC--AVLIVAA--GVgefEAgiskngQTREHALLAYTLGVKQLIVg 151
Cdd:COG0481 69 DgETYQLNLIDTPGHVDF-------SyevsrSLAACegALLVVDAsqGV---EA------QTLANVYLALENDLEIIPV- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 152 VNKMD--STEPaysekryDEIVKEVsayIKKIGYNPATVpfVPISGwhgdnmlepspnmpwfkgwkverKEGnaSGV-SL 228
Cdd:COG0481 132 INKIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSA-----------------------KTG--IGIeEI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 229 LEALDTILPPtrPTDKPLRlPLQ--------DVYKiggiGTVPVGRVETGILRPGMVVTFAPVNITTEVKSV-----EMH 295
Cdd:COG0481 175 LEAIVERIPP--PKGDPDA-PLQalifdswyDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvftpKMT 247
|
330 340 350
....*....|....*....|....*....|..
gi 50054162 296 H-EALSealPGDnVGF---NVKNvsVKDIRRG 323
Cdd:COG0481 248 PvDELS---AGE-VGYiiaGIKD--VRDARVG 273
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
248-325 |
1.52e-15 |
|
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: 71.78 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 248 LPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVN--ITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNV 325
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKetLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-156 |
2.82e-15 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 73.72 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMgkgsfkYAWVLDKLKAERERGITID---ISL-WKFET-T 83
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EM------KEQVLDSMDLERERGITIKaqaVRLfYKAKDgE 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50054162 84 KYYITIIDAPGHRDFikNMITGTSQADC--AVLIVAAGVGeFEAgiskngQTREHALLAYTLGVKQLIVgVNKMD 156
Cdd:cd01890 66 EYLLNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKID 130
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
260-325 |
1.26e-14 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 68.45 E-value: 1.26e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50054162 260 GTVPVGRVETGILRPGMVVTFAPV-----NITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNV 325
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-339 |
1.30e-14 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 76.24 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--SLWKFETTKYyI 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTREH-ALLAYTlGVKQLIVGVNKMDSTEPAyse 164
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACddGV---------MAQTREHlAILQLT-GNPMLTVALTKADRVDEA--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 165 kRYDEIVKEVSAYIKKIgynpatvpfvpisGWHGDNMLEPSPNmpwfkgwkverkEGnaSGVSLLEA-LDTILPPTRPTD 243
Cdd:PRK10512 121 -RIAEVRRQVKAVLREY-------------GFAEAKLFVTAAT------------EG--RGIDALREhLLQLPEREHAAQ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 244 KPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVK-NVSVKDIRR 322
Cdd:PRK10512 173 HRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINR 252
|
330
....*....|....*..
gi 50054162 323 GNVCgdsKADPPQEAAQ 339
Cdd:PRK10512 253 GDWL---LADAPPEPFT 266
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-194 |
1.42e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 72.01 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTTTghliykcggidkRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDISLWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTSLA------------KALSEIASTAA------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 81 -------ETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGvKQLIVGVN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50054162 154 KMDSTEPAYSEKRYDEIVKEVSAYIKKIgyNPATVPFVPIS 194
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVS 167
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-212 |
9.00e-14 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 69.54 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAAEMGKGsfkyawVLDKLKAERERGITIdisLWKFETTKY--- 85
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAKNTAITYkdt 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 86 YITIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEAGISkngQTR---EHALLAytlGVKqLIVGVNKMD 156
Cdd:cd01891 66 KINIIDTPGHADFggeverVLSM------VDGVLLLVDA----SEGPMP---QTRfvlKKALEA---GLK-PIVVINKID 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50054162 157 StepaySEKRYDEIVKEVSAYIKKIGYNPATVPFvPI------SGWHGDNMLEPSPNM-PWFK 212
Cdd:cd01891 129 R-----PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLdPLFE 185
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
245-325 |
2.29e-13 |
|
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: 65.23 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 245 PLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGN 324
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
.
gi 50054162 325 V 325
Cdd:cd16267 81 I 81
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-120 |
2.49e-13 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 72.00 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITIDISL----WKfettK 84
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAAttceWK----G 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 50054162 85 YYITIIDAPGHRDFIKNMITGTSQADCAVLIV--AAGV 120
Cdd:COG0480 74 HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFdaVAGV 111
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
4.67e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 71.14 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaAEMGKGSFkyawVLDKLKAERERGITIDISL----WKfettK 84
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKM---------GEVEDGTT----VTDWMPQEQERGITIESAAtscdWD----N 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50054162 85 YYITIIDAPGHRDFiknmitgTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVgVNKMD 156
Cdd:PRK13351 73 HRINLIDTPGHIDF-------TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIF-INKMD 136
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-279 |
1.02e-12 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 70.05 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAAEMgkgsfkyawVLDKLKAERERGITIdisLWK-----FETT 83
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAKntavrYKGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 84 KyyITIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEagisknG---QTR---EHALlayTLGVKqLIVG 151
Cdd:COG1217 70 K--INIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 152 VNKMDStepaySEKRYDEIVKEVSAYIKKIGynpAT-----VPFV---PISGWHGDNMLEPSPNMpwfkgwkverkegna 223
Cdd:COG1217 128 INKIDR-----PDARPDEVVDEVFDLFIELG---ATdeqldFPVVyasARNGWASLDLDDPGEDL--------------- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50054162 224 sgVSLLEA-LDTILPPTRPTDKPLRlpLQ------DVYkIGGIGtvpVGRVETGILRPGMVVT 279
Cdd:COG1217 185 --TPLFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVA 239
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-177 |
2.07e-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: 67.23 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaaemgkGSFkyawVLDKLKAERERGITIDISLWKFETTKYYI 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISknGQTREHALLAYTLGVKQLIVgVNKMDsTEPAysekRY 167
Cdd:cd04170 67 NLIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRIIF-INKMD-RARA----DF 133
|
170
....*....|
gi 50054162 168 DEIVKEVSAY 177
Cdd:cd04170 134 DKTLAALREA 143
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-156 |
3.90e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 68.23 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETTKYYITIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50054162 92 APGHRDFIKNMITGTSQADCAVLIVAAgVGEFEAgiskngQTRehALLAYT--LGVKQLIVgVNKMD 156
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCA-VGGVEP------QTE--TVWRQAekYGVPRIIF-VNKMD 123
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
245-325 |
5.94e-12 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 61.35 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 245 PLRLPLQDVYKigGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGN 324
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 50054162 325 V 325
Cdd:cd04089 79 V 79
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-279 |
8.72e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 67.04 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKeaaemgkgsfkyawVLDKLKAERERGITIDISLWKFETTKYYIT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVgVNKMD--STEPAYSEKR 166
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDrpGARPDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 167 YDEIVKEVSAYIKKIGYnpatvPFVPISGWHGDNMLEpspnmpwfkgwkverKEGNASGVS-LLEAL-DTILPPTRPTDK 244
Cdd:PRK10218 144 VFDLFVNLDATDEQLDF-----PIVYASALNGIAGLD---------------HEDMAEDMTpLYQAIvDHVPAPDVDLDG 203
|
250 260 270
....*....|....*....|....*....|....*
gi 50054162 245 PLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVT 279
Cdd:PRK10218 204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
1.33e-11 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 64.82 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITID---ISL-WKfettK 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IGEVHGGGATM-----------DWMEQERERGITIQsaaTTCfWK----D 63
|
90
....*....|....
gi 50054162 85 YYITIIDAPGHRDF 98
Cdd:cd01886 64 HRINIIDTPGHVDF 77
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-211 |
4.29e-11 |
|
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: 62.29 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLIYKcggidkrtIEKFEKEAAEMGKgSFKYawvLDKLKAERERGITID---ISLwKFETTK- 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ--------THKRTPSVKLGWK-PLRY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 85 --YYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVgefeaGISKNG-QTREHALLaytLGVKQLIVgVNKMDS---- 157
Cdd:cd04167 69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTeRLIRHAIQ---EGLPMVLV-INKIDRlile 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 50054162 158 -----TEpAYSEKRYdeIVKEVSAYIKKIGyNPATVPFVPISGwhgdNMLEPSPNMPWF 211
Cdd:cd04167 140 lklppTD-AYYKLRH--TIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
9.09e-11 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 62.23 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYAwVLDKLKAERERGITIDISLWKFETTKYYITII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 50054162 91 DAPGHRDFIKNMITGTSQADCAVLIVAAGVG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
252-325 |
5.60e-10 |
|
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: 55.69 E-value: 5.60e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50054162 252 DVYKIGGIGTVPVGRVETGILRPGMVVTFAPVN----ITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNV 325
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
245-325 |
9.60e-10 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 55.20 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 245 PLRLPLQDVYKiGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMH-HEALSEALPGDNVGFNVKNVSVKDIRRG 323
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
..
gi 50054162 324 NV 325
Cdd:cd03698 80 DI 81
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
1.04e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 60.83 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAAEmgkgsfkyAWVLDKLKAERERGITID---ISL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*....
gi 50054162 78 WkFETT--------KYYITIIDAPGHRDF 98
Cdd:PTZ00416 78 Y-YEHDledgddkqPFLINLIDSPGHVDF 105
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-98 |
1.22e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 60.65 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 3 KEKTHI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeAAEmgkgsfkyAWVLDKLKAERERGITID---ISLW 78
Cdd:PRK07560 15 KNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKaanVSMV 79
|
90 100
....*....|....*....|.
gi 50054162 79 -KFETTKYYITIIDAPGHRDF 98
Cdd:PRK07560 80 hEYEGKEYLINLIDTPGHVDF 100
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
9-185 |
4.36e-09 |
|
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: 56.53 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaaemGKGSFKYAwvLDKLKAERERGITIDISL----------- 77
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTSSVSNdilgfdsdgev 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 78 ----------WKFETTKY---YITIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGvgefeAGIskNGQTREHALLAYT 142
Cdd:cd04165 64 vnypdnhlgeLDVEICEKsskVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGAN-----AGI--IGMTKEHLGLALA 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50054162 143 LGVKQLIVgVNKMDSTEpaysekryDEIVKEVSAYIKKIGYNP 185
Cdd:cd04165 137 LKVPVFVV-VTKIDMTP--------ANVLQETLKDLKRLLKSP 170
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-201 |
1.16e-08 |
|
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: 54.40 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGIT--IDISLWKFET 82
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITqhIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 83 TKYYITIIDAPGHRDFiKNMIT-GTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLAYTlgvkQLIVGVNKMD 156
Cdd:cd01887 47 KIPGITFIDTPGHEAF-TNMRArGASVTDIAILVVAAddGVMP---------QTIEainHAKAANV----PIIVAINKID 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50054162 157 stEPAYSEKRYDEIVKEVSAY---IKKIGynpATVPFVPISGWHGDNM 201
Cdd:cd01887 113 --KPYGTEADPERVKNELSELglvGEEWG---GDVSIVPISAKTGEGI 155
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-305 |
2.43e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 56.17 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITIDI-----SLWKFE- 81
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLgyanaKIYKCPk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 82 ---------------------------TTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN---- 130
Cdd:PTZ00327 87 cprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------Nescp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 131 -GQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKevsaYIKkiGYNPATVPFVPISGWHGDNMlepspnmp 209
Cdd:PTZ00327 156 qPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRN----FVK--GTIADNAPIIPISAQLKYNI-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 210 wfkgwkverkegnasgVSLLEALDTILP-PTRPTDKPLRLPLQ---DVYKIGG-----IGTVPVGRVETGIL-------- 272
Cdd:PTZ00327 222 ----------------DVVLEYICTQIPiPKRDLTSPPRMIVIrsfDVNKPGEdienlKGGVAGGSILQGVLkvgdeiei 285
|
330 340 350
....*....|....*....|....*....|....*...
gi 50054162 273 RPGMVV-----TFAPVNITTEVKSVEMHHEALSEALPG 305
Cdd:PTZ00327 286 RPGIISkdsggEFTCRPIRTRIVSLFAENNELQYAVPG 323
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
246-325 |
2.63e-08 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 51.03 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 246 LRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKN-VsvkDIRRGN 324
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77
|
.
gi 50054162 325 V 325
Cdd:cd03695 78 L 78
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-98 |
5.49e-08 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.50 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfEKEAAemgkGSFKYAwvlDKLKAERERGITID---ISL 77
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGII--------AQEVA----GDVRMT---DTRADEAERGITIKstgISL 77
|
90 100 110
....*....|....*....|....*....|....*
gi 50054162 78 WkFETT--------------KYYITIIDAPGHRDF 98
Cdd:PLN00116 78 Y-YEMTdeslkdfkgerdgnEYLINLIDSPGHVDF 111
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-203 |
1.16e-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: 48.22 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETTKYYIT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 89 IIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGVGEFEAGIskngqTREHALLAYTLGVKQLIVGvNKMDstepays 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKID------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50054162 164 eKRYDEIVKEVSAYIKKIGYNPatVPFVPISGWHGDNMLE 203
Cdd:cd00882 118 -LLEEREVEELLRLEELAKILG--VPVFEVSAKTGEGVDE 154
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-201 |
1.18e-04 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 44.44 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 10 IVVIGHVDSGKSTTtghliykcggIDK-RTIEKFEKEAAemgkgsfkyawvldklkaererGITIDIS----LWKFETTK 84
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDKiRKTQIAQKEAG----------------------GITQKIGayevEFEYKDEN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 85 YYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREhALLAYTLGVKQLIVGVNKMDSTepaysE 164
Cdd:CHL00189 295 QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA-----DDGVKP--QTIE-AINYIQAANVPIIVAINKIDKA-----N 361
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50054162 165 KRYDEIVKEVSAY---IKKIGynpATVPFVPISGWHGDNM 201
Cdd:CHL00189 362 ANTERIKQQLAKYnliPEKWG---GDTPMIPISASQGTNI 398
|
|
| FERM_C_CCM1 |
cd13197 |
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ... |
393-429 |
2.84e-04 |
|
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.
Pssm-ID: 270018 Cd Length: 100 Bit Score: 39.91 E-value: 2.84e-04
10 20 30
....*....|....*....|....*....|....*..
gi 50054162 393 SLKSGDAAIVEMVpGKPMCVESFSQYPPLGRFAVRDM 429
Cdd:cd13197 36 NMETKALLLSLKY-GCFMWQLGDADTCFQIHSLENKM 71
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
339-441 |
2.97e-04 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 294007 [Multi-domain] Cd Length: 87 Bit Score: 39.42 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 339 QFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFaelkEKIDRrsgkklednpKSLKSGDAAIVEMvpgkpmcveSFSQY 418
Cdd:cd03708 5 EFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDK----------EVLRTGDRALVRF---------RFLYR 61
|
90 100
....*....|....*....|....*..
gi 50054162 419 P----PLGRFAVRDMRqTVAVGVIKNV 441
Cdd:cd03708 62 PeylrEGQRLIFREGR-TKGIGTVTKV 87
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-203 |
2.98e-04 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 41.20 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfekeaaEMGKGSFKYAWVLdklkAERERGITidislwkfettkYYI 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT------------EYYPGTTRNYVTT----VIEEDGKT------------YKF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 88 TIIDAPGHRDFIKNMITGTSQADcAVLIVAAG---VGEFEAGISKNGQTREHALlayTLGVKQLIVGvNKMDstepayse 164
Cdd:TIGR00231 54 NLLDTAGQEDYDAIRRLYYPQVE-RSLRVFDIvilVLDVEEILEKQTKEIIHHA---DSGVPIILVG-NKID-------- 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 50054162 165 KRyDEIVKEVSAYIKKIGYNPatvPFVPISGWHGDNMLE 203
Cdd:TIGR00231 121 LK-DADLKTHVASEFAKLNGE---PIIPLSAETGKNIDS 155
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
12-98 |
4.41e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 42.43 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYA---WvldkLKAERERGITIDISLWKFETTKYYI 87
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81
|
90
....*....|.
gi 50054162 88 TIIDAPGHRDF 98
Cdd:PRK00741 82 NLLDTPGHEDF 92
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-203 |
8.71e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 40.35 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 8 INIVVIGHVDSGKSTttghLIYKcggidkrtiekfekeaaemgkgsFKYAWVlDKLKAERERGITIDISLWKFETTKYYI 87
Cdd:COG1100 4 KKIVVVGTGGVGKTS----LVNR-----------------------LVGDIF-SLEKYLSTNGVTIDKKELKLDGLDVDL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 88 TIIDAPGHRDFIK---NMITGTSQADCAVLIVAagvGEFEagiskngQTREHALLAYT------LGVKQLIVGvNKMDst 158
Cdd:COG1100 56 VIWDTPGQDEFREtrqFYARQLTGASLYLFVVD---GTRE-------ETLQSLYELLEslrrlgKKSPIILVL-NKID-- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 50054162 159 epaysekRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLE 203
Cdd:COG1100 123 -------LYDEEEIEDEERLKEALSEDNIVEVVATSAKTGEGVEE 160
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
251-309 |
9.82e-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: 38.04 E-value: 9.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 50054162 251 QDVYKIGGiGTVPVGRVETGILRPGMVVTFApvNITTEVKSVEMHHEALSEALPGDNVG 309
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVKGD--KGVALIRAIEREHRKVDFAVAGDEVA 61
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-156 |
1.24e-03 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 41.15 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50054162 10 IVVI-GHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDISLWKFETT 83
Cdd:COG0532 6 VVTVmGHVDHGKTS------------------------------------LLDAIRktnvAAGEaGGITQHIGAYQVETN 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50054162 84 KYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLAytlGVKqLIVGVNKMD 156
Cdd:COG0532 50 GGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAAddGVMP---------QTIEainHAKAA---GVP-IIVAINKID 114
|
|
| |
