|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-457 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 901.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 81 ETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 161 PYSENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTKMPWFKGwqierkegkadgKCLIEALDAILPPAR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 321 RRGYVAGDSKNNPPKGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1983980483 401 IVNLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKEASGGKVTKAAEK 457
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKEGSGTKAAAKAKK 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: 703.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 81 ETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 161 PYSENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTKMPWFKGwqierkegkadgKCLIEALDAILPPAR 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 321 RRGYVAGDSKNNPPKGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAA 400
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1983980483 401 IVNLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKEASGGKVTKAAEK 457
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-445 |
0e+00 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 680.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 81 ETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 161 pYSENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTKMPWFKgwqierkegkadGKCLIEALDAILPPAR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 321 RRGYVAGDSkNNPPKGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAA 400
Cdd:COG5256 300 KRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1983980483 401 IVNLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKE 445
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-445 |
0e+00 |
|
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]
Pssm-ID: 129574 [Multi-domain] Cd Length: 426 Bit Score: 675.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 81 ETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 161 pYSENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTKMPWFKgwqierkegkadGKCLIEALDAILPPAR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 321 RRGYVAGDSKnNPPKGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1983980483 401 IVNLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKE 445
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-445 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 672.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 3 KEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 GKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppY 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 163 SENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTKMPWFKgwqierkegkadGKCLIEALDAILPPARPT 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRR 322
Cdd:PRK12317 223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 323 GYVAGdSKNNPPKGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAAIV 402
Cdd:PRK12317 303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1983980483 403 NLVPSKPLCVESFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKE 445
Cdd:PRK12317 382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPAK 424
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-238 |
1.12e-158 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 447.71 E-value: 1.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETGKYYVT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSENRFE 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 169 EIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTKMPWFKGWqierkegkadgkCLIEALDAILPP 238
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-441 |
2.59e-97 |
|
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: 299.31 E-value: 2.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETGKYY 86
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENR 166
Cdd:COG2895 97 FIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 167 FEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEPSTKMPWFkgwqierkegkaDGKCLIEALDAILPPARPTDKPL 246
Cdd:COG2895 168 FEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 247 RLPLQDVYKiggigtvP-------VGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVK---NVS 316
Cdd:COG2895 234 RFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 317 vkelrRGYVAGDSkNNPPKGASDFTAQVIVLN-HPGQISNGYtpVLDCHTAHIACKFAEIKEKVDRRSGksTEDNPKSIK 395
Cdd:COG2895 307 -----RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTL--EHEAADSLE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1983980483 396 SGDAAIVNLVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVIKAV 441
Cdd:COG2895 377 LNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGA 424
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-238 |
4.43e-75 |
|
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: 233.57 E-value: 4.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 5 KIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETGK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySE 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983980483 165 NRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEpstkmpwfkgwqierkegkadgkcLIEALDAILPP 238
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
335-438 |
7.95e-71 |
|
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: 219.37 E-value: 7.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 335 KGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAAIVNLVPSKPLCVES 414
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 1983980483 415 FQEFPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-438 |
5.13e-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: 214.93 E-value: 5.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGK--GSFKYAWVLDKLKAERERGITIDIALWKFETGKYYVTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 92 APGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFEEIK 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 172 KEVSSYIKKIGynPAAVAFVPISGWHGDNMLEPSTKMPWFKgwqierkegkadGKCLIEALDAILPPARPTDKPLRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYS------------GPTLLEILETVEVERDAQDLPLRFPVQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 252 DVYKI-----GGIGTVPVGRVETGvlkpGTIVVfAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSvkELRRG--Y 324
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSVHVG----DEVVV-LPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGdlL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 325 VAGDsknNPPKGASDFTAQVIVL-NHPgqISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEdnPKSIKSGDAAIVN 403
Cdd:TIGR02034 297 AAAD---SAPEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGA--AKSLELNEIGRVN 369
|
410 420 430
....*....|....*....|....*....|....*..
gi 1983980483 404 LVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 370 LSLDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-240 |
3.06e-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: 201.26 E-value: 3.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAQEMGKgsFKYAWVLDKLKAERERGITIDIALWKFETGKY 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEN 165
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983980483 166 RFEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEPSTKMPWFKgwqierkegkadGKCLIEALDAIlPPAR 240
Cdd:cd04166 150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV-EIAS 209
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-463 |
5.65e-62 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 212.48 E-value: 5.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMG--KGSFKYAWVLDKLKAERERGITIDIALWKFETGKYYVTIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 92 APGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENRFEEIK 171
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 172 KEVSSYIKKIGYnpAAVAFVPISGWHGDNMLEPSTKMPWFkgwqierkegkaDGKCLIEALDAILPPARPTDKPLRLPLQ 251
Cdd:PRK05506 182 ADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 252 DVYKI-----GGIGTvpvgrVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKN---VSvkelrRG 323
Cdd:PRK05506 248 YVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS-----RG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 324 YVAGDSkNNPPKGASDFTAQVIVLN----HPGqisNGYtpVLDCHTAHIACKFAEIKEKVD-----RRSGKSTEDNpksi 394
Cdd:PRK05506 318 DMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDvntleRLAAKTLELN---- 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980483 395 ksgDAAIVNLVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVI-----KAVNFKEASgGKVTKAAEKATKGKK 463
Cdd:PRK05506 388 ---EIGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIdfalrRATNVHWQA-SDVSREARAARKGQK 459
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
242-332 |
2.18e-58 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 187.01 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELR 321
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 1983980483 322 RGYVAGDSKNN 332
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-203 |
8.24e-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: 183.65 E-value: 8.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaqemgkgsfkyaWVLDKLKAERERGITIDIALWKFETGKYYVT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVKQLIVGVNKMDSTeppySENRFE 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFD 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1983980483 169 EIKKEVSSYIKKIGY---NPAAVAFVPISGWHGDNMLE 203
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-438 |
9.06e-56 |
|
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: 190.36 E-value: 9.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKI-----HINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKfekeaqemGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEKFertkpHVNIGTIGHVDHGKTTLTA-------AITKVLAKK--------GGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 76 ALWKFETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 156 DSTEPPYSENRFE-EIKKEVSSYikkiGYNPAAVAFVPISGWhgdNMLEPSTKMPWFKgwQIERkegkadgkcLIEALDA 234
Cdd:COG0050 139 DMVDDEELLELVEmEVRELLSKY----GFPGDDTPIIRGSAL---KALEGDPDPEWEK--KILE---------LMDAVDS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 235 ILP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---IVVFAPAnLTTEVKSVEMHHEALQEAVPGDNVGF 310
Cdd:COG0050 201 YIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDeveIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 311 NVKNVSVKELRRGYVAgdSKNNPPKGASDFTAQVIVLN-------HPgqISNGYTPVLDCHTAHI--ACKFAEIKEKVdr 381
Cdd:COG0050 280 LLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVLSkeeggrhTP--FFNGYRPQFYFRTTDVtgVITLPEGVEMV-- 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1983980483 382 rsgkstedNPksiksGDAA--IVNLVpsKPLCVESFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:COG0050 354 --------MP-----GDNVtmTVELI--TPIAMEEGL------RFAIREGGRTVGAGVV 391
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-441 |
1.89e-54 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 189.06 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 3 KEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 GKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppy 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 163 SENRFEEIKKEVSSYIKKIGYNPAAvafVPISGWHGDNMLEPSTKMPwfkgwQIERKEGKADGKC--LIEALDAILP-PA 239
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 240 RPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIV--VFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSV 317
Cdd:PLN03126 284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdiVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 318 KELRRGYVAgdSKNNPPKGASDFTAQVIVLNHP--GQIS---NGYTPVLDCHTAHIACKFAEIKEKVDRRSgkstednpK 392
Cdd:PLN03126 364 ADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------K 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1983980483 393 SIKSGDAA--IVNLVpsKPLCVESFQefpplgRFAVRDMRQTVAVGVIKAV 441
Cdd:PLN03126 434 MVMPGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-347 |
2.17e-54 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 186.55 E-value: 2.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKI-----HINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK00049 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGAEAK-------AYDQI-DKAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 76 ALWKFETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK00049 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 156 DSTEppySENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEPSTKMPWFKgwQIERkegkadgkcLIEALDAI 235
Cdd:PRK00049 139 DMVD---DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEK--KILE---------LMDAVDSY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 236 LP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---IVVFAPANLTTeVKSVEMHHEALQEAVPGDNVGFN 311
Cdd:PRK00049 202 IPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEeveIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGAL 280
|
330 340 350
....*....|....*....|....*....|....*.
gi 1983980483 312 VKNVSVKELRRGYVAgdSKNNPPKGASDFTAQVIVL 347
Cdd:PRK00049 281 LRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-438 |
6.07e-54 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 187.43 E-value: 6.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 14 GHVDSGKSTTTGHLIYkcggiDKRTI-----EKFEKEAQEMGKGSFK--YAWVLDKLKAERERGITIDIALWKFETGKYY 86
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQIyedqlASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTEKRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSENR 166
Cdd:PRK05124 109 FIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 167 FEEIKKEVSSYIKKIGYNPaAVAFVPISGWHGDNMLEPSTKMPWFKgwqierkegkadGKCLIEALDAILPPARPTDKPL 246
Cdd:PRK05124 180 FERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYS------------GPTLLEVLETVDIQRVVDAQPF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 247 RLPLQDVYKI-----GGIGTvpvgrVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKN---VSvk 318
Cdd:PRK05124 247 RFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDeidIS-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 319 elrRGYVAGDSKNNPPKGASdFTAQVIVLNH----PGQ-----ISNGYTPVldchtahiacKFAEIKEKVDRRSGK--ST 387
Cdd:PRK05124 320 ---RGDLLVAADEALQAVQH-ASADVVWMAEqplqPGQsydikIAGKKTRA----------RVDAIRYQVDINTLTqrEA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1983980483 388 EdnpkSIKSGDAAIVNLVPSKPLCVESFQEFPPLGRFAV--RDMRQTVAVGVI 438
Cdd:PRK05124 386 E----NLPLNGIGLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMV 434
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-438 |
8.58e-54 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 185.55 E-value: 8.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDI 75
Cdd:CHL00071 1 MAREKFerkkpHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 76 ALWKFETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:CHL00071 66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 156 DSTEppySENRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEPSTKMPwfkgwQIERKEGKADGKC--LIEALD 233
Cdd:CHL00071 139 DQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKIynLMDAVD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 234 AILP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPANLTTeVKSVEMHHEALQEAVPGDNVG 309
Cdd:CHL00071 208 SYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRETKTTT-VTGLEMFQKTLDEGLAGDNVG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 310 FNVKNVSVKELRRGYVAgdSKNNPPKGASDFTAQVIVLN------HPGqISNGYTPVLDCHTAHIACKFAEIKEkvdrrs 383
Cdd:CHL00071 287 ILLRGIQKEDIERGMVL--AKPGTITPHTKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKIESFTA------ 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1983980483 384 gkSTEDNPKSIKSGDAAIVNLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:CHL00071 358 --DDGSKTEMVMPGDRIKMTVELIYPIAIEKGM------RFAIREGGRTVGAGVV 404
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-441 |
2.94e-53 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 183.61 E-value: 2.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKE-----KIHINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTA-------AITKVLAERGLNQAK-------DYDSI-DAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 76 ALWKFETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 156 DSTEPPYSENRFE-EIKKEVSSYikkigynpaavafvpisGWHGDNMlePSTKMPWFKGWQIERKEGKADGKcLIEALDA 234
Cdd:PRK12736 139 DLVDDEELLELVEmEVRELLSEY-----------------DFPGDDI--PVIRGSALKALEGDPKWEDAIME-LMDAVDE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 235 ILP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---IVVFAPAnLTTEVKSVEMHHEALQEAVPGDNVGF 310
Cdd:PRK12736 199 YIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDeveIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 311 NVKNVSVKELRRGYVAGDSKNNPPkgASDFTAQVIVLN------HPGQISNgYTPVLDCHTAHI--ACKFAEIKEKVdrR 382
Cdd:PRK12736 278 LLRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYILTkeeggrHTPFFNN-YRPQFYFRTTDVtgSIELPEGTEMV--M 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1983980483 383 SGksteDNPKsiksgdaAIVNLVpsKPLCVEsfqefpPLGRFAVRDMRQTVAVGVIKAV 441
Cdd:PRK12736 353 PG----DNVT-------ITVELI--HPIAME------QGLKFAIREGGRTVGAGTVTEI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-441 |
4.45e-53 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 184.64 E-value: 4.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 3 KEKIHINIVVIGHVDSGKSTTTGhliykcggidkrTIEKFEKEAQEMGKGSFKYawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTA------------AITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 GKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPY 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 163 SENRFEEIKKEVSSYIKkigynpaavafvpisgWHGDNmlepstkMPWFKGWQIERKEGKAD--GKC----LIEALDAIL 236
Cdd:PLN03127 195 LLELVEMELRELLSFYK----------------FPGDE-------IPIIRGSALSALQGTNDeiGKNailkLMDAVDEYI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 237 P-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAP-ANLTTEVKSVEMHHEALQEAVPGDNVGFN 311
Cdd:PLN03127 252 PePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 312 VKNVSVKELRRGYVAgdSKNNPPKGASDFTAQVIVLN------HPGQISNgYTPVLDCHTAHIACKFaEIKEKVdrrsgk 385
Cdd:PLN03127 332 LRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADVTGKV-ELPEGV------ 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980483 386 stednpKSIKSGDAAIVNLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVIKAV 441
Cdd:PLN03127 402 ------KMVMPGDNVTAVFELISPVPLEPGQ------RFALREGGRTVGAGVVSKV 445
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-347 |
2.03e-52 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 181.19 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 76 ALWKFETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 156 DSTEPPyseNRFEEIKKEVSSYIKKIGYNpaavafvpisgwhGDNmlepstkMPWFKGWQIERKEGKADGKC------LI 229
Cdd:PRK12735 139 DMVDDE---ELLELVEMEVRELLSKYDFP-------------GDD-------TPIIRGSALKALEGDDDEEWeakileLM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 230 EALDAILP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPaNLTTEVKSVEMHHEALQEAVPG 305
Cdd:PRK12735 196 DAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKE-TQKTTVTGVEMFRKLLDEGQAG 274
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1983980483 306 DNVGFNVKNVSVKELRRGYVAgdSKNNPPKGASDFTAQVIVL 347
Cdd:PRK12735 275 DNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-441 |
1.35e-50 |
|
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: 176.51 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:TIGR00485 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 76 ALWKFETGKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:TIGR00485 66 AHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 156 DSTEppySENRFEEIKKEVSSYIKKIGYnpaavafvpisgwhgdnmlePSTKMPWFKGWQIERKEGKADGKC----LIEA 231
Cdd:TIGR00485 139 DMVD---DEELLELVEMEVRELLSQYDF--------------------PGDDTPIIRGSALKALEGDAEWEAkileLMDA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 232 LDAILP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPANLTTeVKSVEMHHEALQEAVPGDN 307
Cdd:TIGR00485 196 VDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDN 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 308 VGFNVKNVSVKELRRGYVAgdSKNNPPKGASDFTAQVIVLN------HPGQISnGYTPVLDCHTAHIackfaeikekvdr 381
Cdd:TIGR00485 275 VGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDV------------- 338
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983980483 382 rSGKSTE-DNPKSIKSGDAAIVNLVPSKPLCVESFQefpplgRFAVRDMRQTVAVGVIKAV 441
Cdd:TIGR00485 339 -TGTIELpEGVEMVMPGDNVKMTVELISPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-438 |
1.65e-44 |
|
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: 164.70 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETGKY 85
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLgfAYLPLPDGRR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 86 yVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtLGVKQLIVGVNKMDSTEPPyse 164
Cdd:COG3276 53 -LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-LGIKRGIVVLTKADLVDEE--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 165 nRFEEIKKEVSSYIKKIGYNPAAVafVPISGWHGdnmlepstkmpwfkgwqierkEGKADgkcLIEALDAIL--PPARPT 242
Cdd:COG3276 121 -WLELVEEEIRELLAGTFLEDAPI--VPVSAVTG---------------------EGIDE---LRAALDALAaaVPARDA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRR 322
Cdd:COG3276 174 DGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIER 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 323 GYVAgdSKNNPPKGASDFTAQVIVLNHPGQ-ISNGyTPVLdCH--TAHIACKFAEIkekvdrrsgkstedNPKSIKSGDA 399
Cdd:COG3276 254 GDVL--AAPGALRPTDRIDVRLRLLPSAPRpLKHW-QRVH-LHhgTAEVLARVVLL--------------DREELAPGEE 315
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1983980483 400 AIVNLVPSKPLCVESFQefpplgRFAVRDM--RQTVAVGVI 438
Cdd:COG3276 316 ALAQLRLEEPLVAARGD------RFILRDYspRRTIGGGRV 350
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
333-441 |
1.76e-35 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 127.00 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 333 PPKGASDFTAQVIVLNH-----PGQISNGYTPVLDCHTAHIACKFAEIKEKVDrrSGKSTEdNPKSIKSGDAAIVNLVPS 407
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 1983980483 408 KPLCVESFQefpplgRFAVRDMRQTVAVGVIKAV 441
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-326 |
3.43e-33 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 131.92 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETGKYYV 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppysENRF 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 168 EEIKKEVSSYIKKIGYNPAAVAFVpISGWHGDNMlepstkmpwfkgwqierKEGKADGKCLIEALDailppARPTDKPLR 247
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGI-----------------GELKKELKNLLESLD-----IKRIQKPLR 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1983980483 248 LPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYVA 326
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI 257
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-238 |
7.77e-33 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 123.08 E-value: 7.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 6 IHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETGKY 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySEN 165
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD---DEE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983980483 166 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWhgdNMLEPSTKMPWFKgwQIERkegkadgkcLIEALDAILPP 238
Cdd:cd01884 136 LLELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVD--KILE---------LLDALDSYIPT 194
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
340-438 |
6.71e-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: 112.10 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 340 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKstEDNPKSIKSGDAAIVNLVPSKPLCVESFQEFP 419
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 1983980483 420 PLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-191 |
1.14e-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: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETGKYyV 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLGVKQLIVGVNKMDSTEPPysenRF 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RL 121
|
170 180
....*....|....*....|....
gi 1983980483 168 EEIKKEVSSYIKKIGYNPAAVAFV 191
Cdd:cd04171 122 ELVEEEILELLAGTFLADAPIFPV 145
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
340-438 |
1.47e-22 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 294003 [Multi-domain] Cd Length: 108 Bit Score: 91.85 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 340 FTAQVIVLNHPGQI-SNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAAIVNLVPSKPLCVESFQEF 418
Cdd:cd03704 6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
|
90 100
....*....|....*....|
gi 1983980483 419 PPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03704 86 PQLGRFTLRDEGKTIAIGKV 105
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
333-441 |
4.49e-19 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 82.21 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 333 PPKGASDFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEDNPKSIKSGDAAIVNLVPSKPLCV 412
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 1983980483 413 ESFQEFPPLGRFAVRDMRQTVAVGVIKAV 441
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-178 |
6.82e-19 |
|
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: 84.12 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFETGK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 85 YYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD--STE 159
Cdd:cd01890 66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDlpAAD 135
|
170
....*....|....*....
gi 1983980483 160 PpysenrfEEIKKEVSSYI 178
Cdd:cd01890 136 P-------DRVKQEIEDVL 147
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
246-325 |
1.83e-18 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 79.62 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNvsVKELRRGYV 325
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-316 |
4.37e-17 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 83.92 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 82 TGKYYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVN 153
Cdd:COG0481 69 DGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA------QTLANVYLALENDLEIIPV-IN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 154 KMD--STEPpysenrfEEIKKEVssyIKKIGYNPAAVafVPISGWHGDNMLEpstkmpwfkgwqierkegkadgkcLIEA 231
Cdd:COG0481 134 KIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSAKTGIGIEE------------------------ILEA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 232 LDAILPParPTDKPLRlPLQ--------DVYKiggiGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSV---EMHHEALQ 300
Cdd:COG0481 178 IVERIPP--PKGDPDA-PLQalifdswyDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvfTPKMTPVD 250
|
330
....*....|....*....
gi 1983980483 301 EAVPGDnVGF---NVKNVS 316
Cdd:COG0481 251 ELSAGE-VGYiiaGIKDVR 268
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
246-325 |
7.49e-17 |
|
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: 75.26 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-323 |
2.37e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 81.64 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETGKYyV 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTlGVKQLIVGVNKMDSTEPPysenR 166
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----R 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 167 FEEIKKEVSSYIKKIgynpaavafvpisGWHGDNMLEPSTkmpwfkgwqierKEGKAdgkclIEALDAIL----PPARPT 242
Cdd:PRK10512 122 IAEVRRQVKAVLREY-------------GFAEAKLFVTAA------------TEGRG-----IDALREHLlqlpEREHAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 243 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVK-NVSVKELR 321
Cdd:PRK10512 172 QHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQIN 251
|
..
gi 1983980483 322 RG 323
Cdd:PRK10512 252 RG 253
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-178 |
2.52e-16 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 78.05 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaqemgkGSfkyawV------LDKLKAERERGITIDIALWKFET 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 GKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgvKQL----IVGVNKMDsT 158
Cdd:cd04168 62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKID-R 128
|
170 180
....*....|....*....|
gi 1983980483 159 EPPYSENRFEEIKKEVSSYI 178
Cdd:cd04168 129 AGADLEKVYQEIKEKLSPDI 148
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
248-325 |
1.17e-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: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 248 LPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPaNLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGdevEIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81
|
.
gi 1983980483 325 V 325
Cdd:cd03697 82 V 82
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-309 |
1.40e-15 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 78.36 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:PRK04000 10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKCPD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 GK---YYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAgiskngQTREHaLLAF 141
Cdd:PRK04000 62 CEepeAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 142 T-LGVKQLIVGVNKMDSTEPPYSENRFEEIKKEVSSYIkkigynpAAVA-FVPISGWHGDNMlepstkmpwfkgwqierk 219
Cdd:PRK04000 135 DiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-------AENApIIPVSALHKVNI------------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 220 egkadgKCLIEALDAILP-PARPTDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKPGTIVVFAP 282
Cdd:PRK04000 190 ------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEEGG 263
|
330 340 350
....*....|....*....|....*....|.
gi 1983980483 283 AN----LTTEVKSVEMHHEALQEAVPGDNVG 309
Cdd:PRK04000 264 KTkwepITTKIVSLRAGGEKVEEARPGGLVG 294
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
260-325 |
1.38e-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: 1.38e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983980483 260 GTVPVGRVETGVLKPGTIVVFAPA-----NLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
245-328 |
5.34e-14 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 67.15 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 245 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 1983980483 325 VAGD 328
Cdd:cd16267 81 ILCD 84
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-194 |
9.32e-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: 69.70 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTttghliykcggIDKRTIEKFEKEAqemgkgsfkyawvLDKLKAERERGITIDIALWKFETGK--- 84
Cdd:cd01889 1 VNVGLLGHVDSGKTS-----------LAKALSEIASTAA-------------FDKNPQSQERGITLDLGFSSFEVDKpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 85 -----------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGvKQLIVGVN 153
Cdd:cd01889 57 lednenpqienYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1983980483 154 KMDSTEPPYSENRFEEIKKEVSSYIKKIgyNPAAVAFVPIS 194
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVS 167
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-181 |
1.34e-13 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 69.57 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAqemgkGSFKYawvLDKLKAERERGITID---IALwKFETGK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 85 ------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgeFEaGISKngQTreHALL--AFTLGVKQLIVgVNKMD 156
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----VE-GVCV--QT--ETVLrqALEERVKPVLV-INKID 135
|
170 180 190
....*....|....*....|....*....|...
gi 1983980483 157 --------STEPPYseNRFEEIKKEVSSYIKKI 181
Cdd:cd01885 136 rlilelklSPEEAY--QRLLRIVEDVNAIIETY 166
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-274 |
1.45e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 72.82 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekEAQEMgkgsfkyawVLDKLKAERERGITIDIALWKFETGKYYVT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA------ETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVgVNKMD--STEPPYSENR 166
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDrpGARPDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 167 FEEIKKEVSSYIKKIGYnPA--AVAFVPISGWHGDNMLEPSTkmPWFKGwqierkegkadgkclieALDAILPPARPTDK 244
Cdd:PRK10218 144 VFDLFVNLDATDEQLDF-PIvyASALNGIAGLDHEDMAEDMT--PLYQA-----------------IVDHVPAPDVDLDG 203
|
250 260 270
....*....|....*....|....*....|
gi 1983980483 245 PLRLPLQDVYKIGGIGTVPVGRVETGVLKP 274
Cdd:PRK10218 204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKP 233
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-201 |
6.24e-13 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 67.29 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTTTGHLiykcGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 GKYY----------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTRE 135
Cdd:cd01888 53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980483 136 HALLAFTLGVKQLIVGVNKMDSTEPPYSENRFEEIKKevssYIKKIGYNPAAVafVPISGWHGDNM 201
Cdd:cd01888 122 HLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVKGTIAENAPI--IPISAQLKYNI 181
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-121 |
1.09e-12 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 70.07 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtiekfekeaqeMGK---GSFkyawVLDKLKAERERGITIDIALWKFETGKY 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR------------IGEvhdGNT----VMDWMPEEQERGITITSAATTCEWKGH 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 1983980483 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTG 121
Cdd:COG0480 75 KINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG 110
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
3.65e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 68.44 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAqemgkgsfkyawvlDKLKAERERGITIDIAL----WKfetg 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983980483 84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD 156
Cdd:PRK13351 72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWRQADRYGIPRLIF-INKMD 136
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-156 |
3.67e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 68.61 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETGKYYVTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1983980483 92 APGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAFT--LGVKQLIVgVNKMD 156
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMD 123
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-156 |
5.78e-12 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 64.54 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAQEMGKGsfkyawVLDKLKAERERGITIdiaLWKfETGKYY-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR---EHALLAftlGVKqLIVGVNKM 155
Cdd:cd01891 65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKI 127
|
.
gi 1983980483 156 D 156
Cdd:cd01891 128 D 128
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-156 |
1.01e-11 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 65.31 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaqemgkGSFkyawVLDKLKAERERGITIDIALWKFETGKYYV 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1983980483 88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKQLIVgVNKMD 156
Cdd:cd04170 67 NLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMD 127
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
1.01e-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: 65.21 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETGKYYVT 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIG-EVHGGGA------------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90
....*....|
gi 1983980483 89 IIDAPGHRDF 98
Cdd:cd01886 68 IIDTPGHVDF 77
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
245-325 |
4.31e-11 |
|
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: 58.65 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 245 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 1983980483 325 V 325
Cdd:cd04089 79 V 79
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
245-328 |
8.28e-11 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 58.28 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 245 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMH-HEALQEAVPGDNVGFNVKNVSVKELRRG 323
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 1983980483 324 YVAGD 328
Cdd:cd03698 80 DILSS 84
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-306 |
2.66e-10 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 62.34 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKIhINIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAQEMgkgsfkyawVLDKLKAERERGITIdiaLWK- 79
Cdd:COG1217 1 MMREDI-RNIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAKn 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 80 --FETGKYYVTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG---QTR---EHALlafTLGV 145
Cdd:COG1217 62 taVRYKGVKINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 146 KqLIVGVNKMDSteppySENRFEEIKKEVSSYIKKIGYNPAAVAFvPI------SGWHGDNMLEPSTKMpwfkgwqierk 219
Cdd:COG1217 123 K-PIVVINKIDR-----PDARPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDL----------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 220 egkadgKCLIEA-LDAILPPARPTDKPLRlpLQ------DVYkIGGIGtvpVGRVETGVLKPG-TIVVFAPANLTTEVKS 291
Cdd:COG1217 185 ------TPLFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGqQVALIKRDGKVEKGKI 252
|
330 340
....*....|....*....|.
gi 1983980483 292 VEMH-HEALQ-----EAVPGD 306
Cdd:COG1217 253 TKLFgFEGLErveveEAEAGD 273
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
2.94e-10 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 60.69 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAQEM-GKGSFKYAwVLDKLKAERERGITIDIALWKFETGKYYVTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 1983980483 91 DAPGHRDFIKNMITGTSQADCAVLIVAAGTG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
9-182 |
3.29e-10 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 60.00 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaqemGKGSFKYAwvLDKLKAERERGIT---------------- 72
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTssvsndilgfdsdgev 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 73 ----IDIALWK----FETGKYYVTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFT 142
Cdd:cd04165 64 vnypDNHLGELdveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALA 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1983980483 143 LGVKQLIVgVNKMDSTeppySENRFEEIKKEVSSYIKKIG 182
Cdd:cd04165 137 LKVPVFVV-VTKIDMT----PANVLQETLKDLKRLLKSPG 171
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
252-325 |
4.52e-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: 56.07 E-value: 4.52e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983980483 252 DVYKIGGIGTVPVGRVETGVLKPGTIVVFAPAN----LTTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-211 |
5.07e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 59.20 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKcggIDKRTIEKFEKEAQEmgkgsfKYawvLDKLKAERERGITI-----DIALWKFETG 83
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIEQ---THKRTPSVKLGWKPL------RY---TDTRKDEQERGISIksnpiSLVLEDSKGK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--REhallAFTLGVKQLIVgVNKMDS--TE 159
Cdd:cd04167 70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH----AIQEGLPMVLV-INKIDRliLE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1983980483 160 ---PPYSENR-FEEIKKEVSSYIKKIGyNPAAVAFVPISGwhgdNMLEPSTKMPWF 211
Cdd:cd04167 140 lklPPTDAYYkLRHTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-201 |
2.06e-09 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 56.33 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaqemgkgsfkyawVLDKLK----AERE-RGITIDIalwkfetGK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHI-------GA 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 85 YYV---------TIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVG 151
Cdd:cd01887 40 YQVpidvkipgiTFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVA 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1983980483 152 VNKMDstEPPYSENRFEEIKKEVSSY---IKKIGYNpaaVAFVPISGWHGDNM 201
Cdd:cd01887 108 INKID--KPYGTEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
246-310 |
8.06e-09 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 52.18 E-value: 8.06e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983980483 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANLTTEVKSVEMHHEALQEAVPGDNVGF 310
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
4.52e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 55.44 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAqemGKGSFkyawvLDKLKAERERGITID---IAL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNA---GDARF-----TDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*...
gi 1983980483 78 ---WKFETGK----YYVTIIDAPGHRDF 98
Cdd:PTZ00416 78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-98 |
5.11e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 55.25 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeaqeMGKgsfkyAWVLDKLKAERERGITIDIA----LWKFETGK 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGE-----QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
|
90
....*....|....
gi 1983980483 85 YYVTIIDAPGHRDF 98
Cdd:PRK07560 87 YLINLIDTPGHVDF 100
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-305 |
2.72e-07 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 52.70 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaqemgkgsfkyawvldKLKAERERGITIDIA-----LWKFET 82
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLGyanakIYKCPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 83 ----GKY------------------------YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagiSKNGQTR 134
Cdd:PTZ00327 87 cprpTCYqsygsskpdnppcpgcghkmtlkrHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 135 EHALLAFTLGVKQLIVGVNKMDSTEPPYSENRFEEIKKEVSSYIKKigynpaAVAFVPISGWHGDNMlepstkmpwfkgw 214
Cdd:PTZ00327 161 EHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPISAQLKYNI------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 215 qierkegkadgKCLIEALDAILP-PARPTDKPLRLPLQ---DVYKIGG-----IGTVPVGRVETGVLK--------PGTI 277
Cdd:PTZ00327 222 -----------DVVLEYICTQIPiPKRDLTSPPRMIVIrsfDVNKPGEdienlKGGVAGGSILQGVLKvgdeieirPGII 290
|
330 340 350
....*....|....*....|....*....|...
gi 1983980483 278 VVFAPANLT-----TEVKSVEMHHEALQEAVPG 305
Cdd:PTZ00327 291 SKDSGGEFTcrpirTRIVSLFAENNELQYAVPG 323
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-98 |
5.65e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 52.03 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfekeAQEMGKGsfkyAWVLDKLKAERERGITID---IALW------- 78
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGII-----------AQEVAGD----VRMTDTRADEAERGITIKstgISLYyemtdes 85
|
90 100
....*....|....*....|....*.
gi 1983980483 79 ------KFETGKYYVTIIDAPGHRDF 98
Cdd:PLN00116 86 lkdfkgERDGNEYLINLIDSPGHVDF 111
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-208 |
2.17e-05 |
|
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: 44.75 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIAL--WKFETGKYYVT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 89 IIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHALLAFTLGVKQLIVGvNKMDSTEPPys 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKIDLLEER-- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1983980483 164 enrfEEIKKEVSSYIKKIGYNPaavaFVPISGWHGDNMLEPSTKM 208
Cdd:cd00882 123 ----EVEELLRLEELAKILGVP----VFEVSAKTGEGVDELFEKL 159
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-203 |
2.45e-05 |
|
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: 44.67 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 8 INIVVIGHVDSGKSTTTGHLIYKcggidkrtiEKFEKEAQEmgkGSFKYAWVLdklkAERERGITIDIALWkfetgkyyv 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---------KGSITEYYP---GTTRNYVTT----VIEEDGKTYKFNLL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 88 tiiDAPGHRDFIKNMITGTSQADcAVLIVAAGTG---EFEAGISKNGQTREHALlafTLGVKQLIVGvNKMDsteppyse 164
Cdd:TIGR00231 57 ---DTAGQEDYDAIRRLYYPQVE-RSLRVFDIVIlvlDVEEILEKQTKEIIHHA---DSGVPIILVG-NKID-------- 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 1983980483 165 NRFEEIKKEVSSYIKKIGYNPaavaFVPISGWHGDNMLE 203
Cdd:TIGR00231 121 LKDADLKTHVASEFAKLNGEP----IIPLSAETGKNIDS 155
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-201 |
1.06e-04 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 44.82 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 10 IVVIGHVDSGKSTTtghliykcggIDKrtIEKFEKEAQEMGkgsfkyawvldklkaererGITIDIA----LWKFETGKY 85
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDK--IRKTQIAQKEAG-------------------GITQKIGayevEFEYKDENQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREhALLAFTLGVKQLIVGVNKMDSTeppysEN 165
Cdd:CHL00189 296 KIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKA-----NA 362
|
170 180 190
....*....|....*....|....*....|....*....
gi 1983980483 166 RFEEIKKEVSSY---IKKIGynpAAVAFVPISGWHGDNM 201
Cdd:CHL00189 363 NTERIKQQLAKYnliPEKWG---GDTPMIPISASQGTNI 398
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
251-309 |
2.64e-04 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 39.59 E-value: 2.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1983980483 251 QDVYKIGGiGTVPVGRVETGVLKPGTIVVfaPANLTTEVKSVEMHHEALQEAVPGDNVG 309
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
340-381 |
8.81e-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: 38.27 E-value: 8.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1983980483 340 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDR 381
Cdd:cd03708 6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLR 47
|
|
| CysN_NoDQ_III |
cd04095 |
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ... |
337-438 |
1.25e-03 |
|
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N- and C-termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 294010 [Multi-domain] Cd Length: 103 Bit Score: 38.19 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 337 ASDFTAQVIVLNH-PGQISNGYtpVLDCHTAHIACKFAEIKEKVDRRSGKSTEDnpKSIKSGDAAIVNLVPSKPLCVESF 415
Cdd:cd04095 3 SDQFEATLVWMDEkPLQPGRRY--LLKHGTRTVRARVTEIDYRIDVNTLEREPA--DTLALNDIGRVTLRLAEPLAFDPY 78
|
90 100
....*....|....*....|....*.
gi 1983980483 416 QEFPPLGRFAVRDmRQ---TVAVGVI 438
Cdd:cd04095 79 AENRATGSFILID-RLtnaTVAAGMI 103
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
340-438 |
2.38e-03 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 37.21 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 340 FTAQVIVLN------HPGqISNGYTPVLDCHTAHIACKFAEIKEKvdrrsgkstednpKSIKSGDAAIVNLVPSKPLCVE 413
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRIDLPEGK-------------EMVMPGEDTSVKLTLLKPMVLE 71
|
90 100
....*....|....*....|....*
gi 1983980483 414 SFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:cd03706 72 KGQ------RFTLREGGRTIGTGVV 90
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
12-98 |
6.96e-03 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 38.96 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983980483 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAQEM-GKGSFKYA---WvldkLKAERERGITIDIALWKFETGKYYV 87
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81
|
90
....*....|.
gi 1983980483 88 TIIDAPGHRDF 98
Cdd:PRK00741 82 NLLDTPGHEDF 92
|
|
| |
