|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-446 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 917.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 161 KYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 241 VYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 321 PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV 400
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 18390827 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKK 446
Cdd:PTZ00141 401 EVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKEGSGTKAAAKAKKK 446
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-447 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 898.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 161 KYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 241 VYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 321 PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV 400
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18390827 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKG 447
Cdd:PLN00043 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAKKK 447
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-433 |
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: 664.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQMICCCNKMDATtp 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDAV-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 161 KYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
Cdd:COG5256 152 NYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 241 VYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSkDD 320
Cdd:COG5256 232 VYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 321 PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV 400
Cdd:COG5256 311 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVI 390
|
410 420 430
....*....|....*....|....*....|...
gi 18390827 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKD 433
Cdd:COG5256 391 EKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-432 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 652.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 3 KEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKY 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDA-----GGVMPQTREHVFLARTLGINQLIVAINKMDAV--NY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 163 SKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVY 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 243 KIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSkDDPA 322
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHP-DNPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 323 KGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVET 402
Cdd:PRK12317 314 TVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEK 393
|
410 420 430
....*....|....*....|....*....|
gi 18390827 403 FSEYPPLGRFAVRDMRQTVAVGVIKSVDKK 432
Cdd:PRK12317 394 VKEIPQLGRFAIRDMGQTIAAGMVIDVKPA 423
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-433 |
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: 649.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagisKDGQTREHALLAFTLGVKQMICCCNKMDatTP 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMD--SV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 161 KYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
Cdd:TIGR00483 155 NYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 241 VYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSkDD 320
Cdd:TIGR00483 235 VYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHP-DN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 321 PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV 400
Cdd:TIGR00483 314 PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVI 393
|
410 420 430
....*....|....*....|....*....|...
gi 18390827 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKD 433
Cdd:TIGR00483 394 EAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-227 |
6.51e-156 |
|
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: 440.00 E-value: 6.51e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYD 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18390827 169 EIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPK 227
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
9-429 |
3.78e-94 |
|
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: 290.45 E-value: 3.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGI--DKrvIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIAlWKFETT--- 83
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVA-YRYFSTpkr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 84 KYycTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpKYS 163
Cdd:COG2895 96 KF--IIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLV--DYS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 164 KARYDEIIKEVSSYLKKVGYNPdkIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYK 243
Cdd:COG2895 165 EEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 244 iggigtvP-------VGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGF----NVknvavkDLKRGY 312
Cdd:COG2895 243 -------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtledEI------DISRGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 313 VASnSKDDPAKGAANFTSQVIIMN-HPGQIGNGYapVLDCHTSHIAVKFSEILTKIDRRSGKEIekEPKFLKNGDAGMVK 391
Cdd:COG2895 310 VIV-AADAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHE--AADSLELNDIGRVT 384
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18390827 392 MTPTKPMVVETFSEYPPLGRFAV--RDMRQTVAVGVIKSV 429
Cdd:COG2895 385 LRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGA 424
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-222 |
2.97e-76 |
|
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: 235.88 E-value: 2.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 5 KFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAaemnkrsfkyawVLDKLKAERERGITIDIALWKFETTK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKqMICCCNKMDATTpkysK 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRVD----G 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18390827 165 ARYDEIIKEVSS-YLKKVGYNPDKIPFVPISGFEGDNMierstnldwykgPTLLEALDQ 222
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV------------QTLLDALDE 183
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
323-426 |
4.27e-67 |
|
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).
Pssm-ID: 294004 [Multi-domain] Cd Length: 104 Bit Score: 209.36 E-value: 4.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 323 KGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVET 402
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 18390827 403 FSEYPPLGRFAVRDMRQTVAVGVI 426
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-223 |
5.30e-65 |
|
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: 207.81 E-value: 5.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGI--DK-RVIERFEKEAAEMNKrsFKYAWVLDKLKAERERGITIDIALWKFETTKY 85
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 86 YCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpKYSKA 165
Cdd:cd04166 79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLV--DYDEE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18390827 166 RYDEIIKEVSSYLKKVGYNPdkIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQI 223
Cdd:cd04166 150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETV 205
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-426 |
1.45e-64 |
|
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: 213.39 E-value: 1.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 14 GHVDSGKSTTTGHLIYklggiDKRVIerFEKEAAEMNKRSFK---------YAWVLDKLKAERERGITIDIALWKFETTK 84
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLAALERDSKKhgtqggeidLALLVDGLQAEREQGITIDVAYRYFSTDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpKYSK 164
Cdd:TIGR02034 80 RKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLV--DYDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 165 ARYDEIIKEVSSYLKKVGYNPdkIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKI 244
Cdd:TIGR02034 151 EVFENIKKDYLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 245 -----GGIGTVPVGRVEtgmikPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAvkDLKRGYVASNSkD 319
Cdd:TIGR02034 229 nldfrGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDLLAAA-D 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 320 DPAKGAANFTSQVIIM-NHPGQIGNGYapVLDCHTSHIAVKFSEILTKIDRRSGKeiEKEPKFLKNGDAGMVKMTPTKPM 398
Cdd:TIGR02034 301 SAPEVADQFAATLVWMaEEPLLPGRSY--DLKLGTRKVRASVAAIKHKVDVNTLE--KGAAKSLELNEIGRVNLSLDEPI 376
|
410 420 430
....*....|....*....|....*....|
gi 18390827 399 VVETFSEYPPLGRFAV--RDMRQTVAVGVI 426
Cdd:TIGR02034 377 AFDPYAENRTTGAFILidRLSNRTVGAGMI 406
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-442 |
2.42e-60 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 203.99 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 14 GHVDSGKSTTTGHLIYklggiDKRVIerFEKEAAEMNKRSFK---------YAWVLDKLKAERERGITIDIALWKFETTK 84
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpKYSK 164
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLV--DYSE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 165 ARYDEIIKEVSSYLKKVGYNPDkIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKI 244
Cdd:PRK05124 178 EVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 245 -----GGIGTvpvgrVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAvkDLKRGYVASNSKD 319
Cdd:PRK05124 257 nldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--DISRGDLLVAADE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 320 DPAKGaANFTSQVIIMN-HPGQIGNGYApvLDCHTSHIAVKFSEILTKIDRRSGKEIEKEpkFLKNGDAGMVKMTPTKPM 398
Cdd:PRK05124 330 ALQAV-QHASADVVWMAeQPLQPGQSYD--IKIAGKKTRARVDAIRYQVDINTLTQREAE--NLPLNGIGLVELTFDEPL 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 18390827 399 VVETFSEYPPLGRFAV--RDMRQTVAVGVIKSVDKKDPTGAKVTKA 442
Cdd:PRK05124 405 VLDPYQQNRVTGGFIFidRLTNVTVGAGMVREPLAQATAAPSEFSA 450
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-426 |
5.07e-59 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 204.01 E-value: 5.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 14 GHVDSGKSTTTGHLIYklggiDKRVIerFEKEAAEMNKRSFK---------YAWVLDKLKAERERGITIDIALWKFETTK 84
Cdd:PRK05506 31 GSVDDGKSTLIGRLLY-----DSKMI--FEDQLAALERDSKKvgtqgdeidLALLVDGLAAEREQGITIDVAYRYFATPK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATtpKYSK 164
Cdd:PRK05506 104 RKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLV--DYDQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 165 ARYDEIIKEVSSYLKKVGYNpdKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKI 244
Cdd:PRK05506 175 EVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVNRP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 245 -----GGIGTvpvgrVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAvkDLKRGYVASNSkD 319
Cdd:PRK05506 253 nldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADEI--DISRGDMLARA-D 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 320 DPAKGAANFTSQVIIMN-HPGQIGNGYapVLDCHTSHIAVKFSEILTKIDRRSgkeIEKEP-KFLKNGDAGMVKMTPTKP 397
Cdd:PRK05506 325 NRPEVADQFDATVVWMAeEPLLPGRPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAaKTLELNEIGRCNLSTDAP 399
|
410 420 430
....*....|....*....|....*....|.
gi 18390827 398 MVVETFSEYPPLGRFAV--RDMRQTVAVGVI 426
Cdd:PRK05506 400 IAFDPYARNRTTGSFILidRLTNATVGAGMI 430
|
|
| tufA |
CHL00071 |
elongation factor Tu |
1-426 |
1.61e-58 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 197.49 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKF-----HINIVVIGHVDSGKSTTTGHLIYKLggidkrvierfekeAAEMNKRSFKYAWVlDKLKAERERGITIDI 75
Cdd:CHL00071 1 MAREKFerkkpHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTREHALLAFTLGVKQMICCC 152
Cdd:CHL00071 66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAA----------DGpmpQTKEHILLAKQVGVPNIVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 153 NKMDATTPkyskaryDEII----KEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLD-----WY-KGPTLLEALDQ 222
Cdd:CHL00071 136 NKEDQVDD-------EELLelveLEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIKrgenkWVdKIYNLMDAVDS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 223 -INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVT---FAPTGLTTeVKSVEMHHESLLEALPGDNVGF 298
Cdd:CHL00071 209 yIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 299 NVKNVAVKDLKRGYVAsnSKDDPAKGAANFTSQVIIMN------HPGqIGNGYAPvldchtsHIAVKFSEILTKIDRRSG 372
Cdd:CHL00071 288 LLRGIQKEDIERGMVL--AKPGTITPHTKFEAQVYILTkeeggrHTP-FFPGYRP-------QFYVRTTDVTGKIESFTA 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 18390827 373 KEiEKEPKFLKNGDAgmVKMTPT--KPMVVETFSeypplgRFAVRDMRQTVAVGVI 426
Cdd:CHL00071 358 DD-GSKTEMVMPGDR--IKMTVEliYPIAIEKGM------RFAIREGGRTVGAGVV 404
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-313 |
3.26e-58 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 196.14 E-value: 3.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKF-----HINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAaemnkRSFKYawvLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEKFertkpHVNIGTIGHVDHGKTTLTA-------AITKVLAKKGGAKA-----KAYDQ---IDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTREHALLAFTLGVKQMICCC 152
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAT----------DGpmpQTREHILLARQVGVPYIVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 153 NKMDATTPKyskarydEIIK----EVSSYLKKVGYNPDKIPFVPISGF---EGDnmiersTNLDWYKGPT-LLEALDQ-I 223
Cdd:COG0050 136 NKCDMVDDE-------ELLElvemEVRELLSKYGFPGDDTPIIRGSALkalEGD------PDPEWEKKILeLMDAVDSyI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 224 NEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPG---MVVTFAPTgLTTEVKSVEMHHESLLEALPGDNVGFNV 300
Cdd:COG0050 203 PEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLL 281
|
330
....*....|...
gi 18390827 301 KNVAVKDLKRGYV 313
Cdd:COG0050 282 RGIKREDVERGQV 294
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
230-320 |
6.92e-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: 185.08 E-value: 6.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 230 SDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLK 309
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 18390827 310 RGYVASNSKDD 320
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-313 |
6.55e-56 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 190.01 E-value: 6.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKF-----HINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAaemnkrsFKYAWVlDKLKAERERGITIDI 75
Cdd:PRK00049 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGAEA-------KAYDQI-DKAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTREHALLAFTLGVKQMICCC 152
Cdd:PRK00049 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 153 NKMDATTPkyskaryDEIIK----EVSSYLKKVGYNPDKIPFVPISGFEGdnmIERSTNLDWYKG-PTLLEALDQ-INEP 226
Cdd:PRK00049 136 NKCDMVDD-------EELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLELMDAVDSyIPTP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 227 KRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPG---MVVTFAPTGLTTeVKSVEMHHESLLEALPGDNVGFNVKNV 303
Cdd:PRK00049 206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGALLRGI 284
|
330
....*....|
gi 18390827 304 AVKDLKRGYV 313
Cdd:PRK00049 285 KREDVERGQV 294
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-313 |
1.37e-54 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 186.69 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKF-----HINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAAemnkrsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEKFdrskpHVNIGTIGHVDHGKTTLTA-------AITKVLAERGLNQAK-------DYDSI-DAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTREHALLAFTLGVKQMICCC 152
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAAT----------DGpmpQTREHILLARQVGVPYLVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 153 NKMDATTPkyskaryDEIIK----EVSSYLKKVGYNPDKIPFVPISGF---EGDNmierstnlDWYKG-PTLLEALDQ-I 223
Cdd:PRK12736 136 NKVDLVDD-------EELLElvemEVRELLSEYDFPGDDIPVIRGSALkalEGDP--------KWEDAiMELMDAVDEyI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 224 NEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPG---MVVTFAPTgLTTEVKSVEMHHESLLEALPGDNVGFNV 300
Cdd:PRK12736 201 PTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLL 279
|
330
....*....|...
gi 18390827 301 KNVAVKDLKRGYV 313
Cdd:PRK12736 280 RGVDRDEVERGQV 292
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-313 |
4.13e-53 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 182.73 E-value: 4.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKF-----HINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAaemnkRSFKYawvLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGGEA-----KAYDQ---IDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTREHALLAFTLGVKQMICCC 152
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 153 NKMDATTPKyskarydEIIK----EVSSYLKKVGYNPDKIPFVPISGFEGdnmIERSTNLDWYKG-PTLLEALDQ-INEP 226
Cdd:PRK12735 136 NKCDMVDDE-------ELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLELMDAVDSyIPEP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 227 KRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPG---MVVTFAPTGLTTeVKSVEMHHESLLEALPGDNVGFNVKNV 303
Cdd:PRK12735 206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVGVLLRGT 284
|
330
....*....|
gi 18390827 304 AVKDLKRGYV 313
Cdd:PRK12735 285 KREDVERGQV 294
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-429 |
2.13e-52 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 183.28 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 3 KEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDattpKY 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQD----QV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 163 SKARYDEIIK-EVSSYLKKVGYNPDKIPFVPISGFEG------DNMIERSTNlDWY-KGPTLLEALDQ-INEPKRPSDKP 233
Cdd:PLN03126 211 DDEELLELVElEVRELLSSYEFPGDDIPIISGSALLAlealmeNPNIKRGDN-KWVdKIYELMDAVDSyIPIPQRQTDLP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 234 LRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLT--TEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRG 311
Cdd:PLN03126 290 FLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 312 YVAsnSKDDPAKGAANFTSQVIIMNHP-----GQIGNGYAPVLDCHTSHIAVKFSEILTKIDrrsgkeieKEPKFLKNGD 386
Cdd:PLN03126 370 MVL--AKPGSITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMRTTDVTGKVTSIMNDKD--------EESKMVMPGD 439
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 18390827 387 AGMVKMTPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
Cdd:PLN03126 440 RVKMVVELIVPVACEQGM------RFAIREGGKTVGAGVIQSI 476
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
1-429 |
6.34e-51 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 176.89 E-value: 6.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKF-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDI 75
Cdd:TIGR00485 1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQ---------------IDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
Cdd:TIGR00485 66 AHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 156 DATTpkySKARYDEIIKEVSSYLKKVGYNPDKIPFV---PISGFEGDNMIERstnldwyKGPTLLEALDQ-INEPKRPSD 231
Cdd:TIGR00485 139 DMVD---DEELLELVEMEVRELLSQYDFPGDDTPIIrgsALKALEGDAEWEA-------KILELMDAVDEyIPTPEREID 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 232 KPLRLPLQDVYKIGGIGTVPVGRVETGMIKPG---MVVTFAPTGLTTeVKSVEMHHESLLEALPGDNVGFNVKNVAVKDL 308
Cdd:TIGR00485 209 KPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDNVGLLLRGIKREEI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 309 KRGYVAsnSKDDPAKGAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIekepkfLKNGDAg 388
Cdd:TIGR00485 288 ERGMVL--AKPGSIKPHTKFEAEVYVLSK--EEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEM------VMPGDN- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 18390827 389 mVKMTPT--KPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
Cdd:TIGR00485 357 -VKMTVEliSPIALEQGM------RFAIREGGRTVGAGVVSKI 392
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-429 |
1.84e-50 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 177.32 E-value: 1.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 3 KEKFHINIVVIGHVDSGKSTTTGhliyklgGIDKRVIERFEKEAAEMNKrsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTA-------AITKVLAEEGKAKAVAFDE--------IDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 163 SKARYDEIIKEVSSYLKkvgYNPDKIPFV---PISGFEGDN-MIERSTNLDwykgptLLEALDQ-INEPKRPSDKPLRLP 237
Cdd:PLN03127 195 LLELVEMELRELLSFYK---FPGDEIPIIrgsALSALQGTNdEIGKNAILK------LMDAVDEyIPEPVRVLDKPFLMP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 238 LQDVYKIGGIGTVPVGRVETGMIKPG---MVVTFAPTG-LTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYV 313
Cdd:PLN03127 266 IEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 314 AsnSKDDPAKGAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIekepkfLKNGDAGMVKMT 393
Cdd:PLN03127 346 I--CKPGSIKTYKKFEAEIYVLTK--DEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKM------VMPGDNVTAVFE 415
|
410 420 430
....*....|....*....|....*....|....*.
gi 18390827 394 PTKPMVVEtfseypPLGRFAVRDMRQTVAVGVIKSV 429
Cdd:PLN03127 416 LISPVPLE------PGQRFALREGGRTVGAGVVSKV 445
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-226 |
1.42e-49 |
|
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: 166.70 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFekeaaemnkrsfkyaWVLDKLKAERERGITIDIALWKFETTKYYCT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQMIcCCNKMDattpKYSKARYD 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEG-------VEPQTREHLNIALAGGLPIIV-AVNKID----RVGEEDFD 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390827 169 EIIKEVSSYLKKVGY---NPDKIPFVPISGFEGDNMierstnldwykgPTLLEALDQINEP 226
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGI------------EELLDAIVEHLPP 182
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-313 |
2.47e-39 |
|
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: 149.68 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 8 INIVVIGHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDI--ALWKFETTKY 85
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGIDT------------------------DRLKEEKKRGITIDLgfAYLPLPDGRR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 86 yCTVIDAPGHRDFIKNMITGTSQADCAVLIIDsttggfeagiSKDG---QTREH-ALLAFtLGVKQMICCCNKMDATTPk 161
Cdd:COG3276 53 -LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADLVDE- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 162 yskARYDEIIKEVSSYLKkvGYNPDKIPFVPISGFEGDNMierstnldwykgPTLLEALDQINE--PKRPSDKPLRLPLQ 239
Cdd:COG3276 120 ---EWLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEGI------------DELRAALDALAAavPARDADGPFRLPID 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390827 240 DVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYV 313
Cdd:COG3276 183 RVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDV 256
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-221 |
1.16e-34 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 127.70 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 7 HINIVVIGHVDSGKSTTTGHLIYKLggidkrvierfekeaAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYY 86
Cdd:cd01884 2 HVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 87 CTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTREHALLAFTLGVKQMICCCNKMDATTpkys 163
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSAT----------DGpmpQTREHLLLARQVGVPYIVVFLNKADMVD---- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390827 164 karyDE-----IIKEVSSYLKKVGYNPDKIPFVPISGF---EGDNmiersTNLDWYKGPTLLEALD 221
Cdd:cd01884 133 ----DEellelVEMEVRELLSKYGFDGDDTPIVRGSALkalEGDD-----PNKWVDKILELLDALD 189
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-386 |
2.87e-34 |
|
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: 135.00 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 8 INIVVIGHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDIALWKFETTKYYC 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDsttggfeagiSKDG---QTREHALLAFTLGVKQMICCCNKMDattpKYSK 164
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKAD----RVNE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 165 ARYDEIIKEVSSYLKKVGYNPDKIPFVpISGFEGDNMIERSTNLdwykgPTLLEALDQINEpkrpsDKPLRLPLQDVYKI 244
Cdd:TIGR00475 119 EEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL-----KNLLESLDIKRI-----QKPLRMAIDRAFKV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 245 GGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKG 324
Cdd:TIGR00475 188 KGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRV 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390827 325 AANFTSQViimnhpgqigngyaPVLDCHTSHIAVKFSEI---LTKIDRRSGKEIEKEPKFLKNGD 386
Cdd:TIGR00475 268 VVKFIAEV--------------PLLELQPYHIAHGMSVTtgkISLLDKGIALLTLDAPLILAKGD 318
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
321-429 |
1.76e-33 |
|
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: 121.60 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 321 PAKGAANFTSQVIIMNH-----PGQIGNGYAPVLDCHTSHIAVKFSEILTKIDrrsGKEIEKEPKFLKNGDAGMVKMTPT 395
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD---PGGVSENPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 18390827 396 KPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
323-426 |
2.11e-27 |
|
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: 105.17 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 323 KGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEieKEPKFLKNGDAGMVKMTPTKPMVVET 402
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLER 78
|
90 100
....*....|....*....|....
gi 18390827 403 FSEYPPLGRFAVRDMRQTVAVGVI 426
Cdd:cd01513 79 GKEFPTLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-230 |
6.20e-23 |
|
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: 94.98 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 10 IVVIGHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDI--ALWKFETTKYyC 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGKR-L 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDattpKYSKARY 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKAD----LVDEDRL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390827 168 DEIIKEVSSYLKKVGYNPdkIPFVPISGFEGDNmIERstnldwykgptLLEALDQINEPKRPS 230
Cdd:cd04171 122 ELVEEEILELLAGTFLAD--APIFPVSSVTGEG-IEE-----------LKNYLDELAEPQSKD 170
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
328-426 |
4.49e-21 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 294003 [Multi-domain] Cd Length: 108 Bit Score: 87.61 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 328 FTSQVIIMNHPGQI-GNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVETFSEY 406
Cdd:cd03704 6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
|
90 100
....*....|....*....|
gi 18390827 407 PPLGRFAVRDMRQTVAVGVI 426
Cdd:cd03704 86 PQLGRFTLRDEGKTIAIGKV 105
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-297 |
3.09e-20 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 92.22 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 8 INIVVIGHVDSGKSTttghLIYKLGGIdkrvierfekeaaemnkrsfkyaWVlDKLKAERERGITI-----DIALWKFE- 81
Cdd:PRK04000 10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKCPd 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 82 -------TTKYYC-----------TV--IDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAgiskdgQTREHaLLAF 141
Cdd:PRK04000 62 ceepeayTTEPKCpncgsetellrRVsfVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 142 T-LGVKQMICCCNKMDATTPKYSKARYDEIIKEVSsylkkvGYNPDKIPFVPISGFEGdnmiersTNLDwykgpTLLEAL 220
Cdd:PRK04000 135 DiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVK------GTVAENAPIIPVSALHK-------VNID-----ALIEAI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 221 DQ-INEPKRPSDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---MIKPGMVVT------FAPtgLTTEV 277
Cdd:PRK04000 197 EEeIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEeggktkWEP--ITTKI 274
|
330 340
....*....|....*....|
gi 18390827 278 KSVEMHHESLLEALPGDNVG 297
Cdd:PRK04000 275 VSLRAGGEKVEEARPGGLVG 294
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
321-429 |
9.02e-19 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 81.44 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 321 PAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVV 400
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 18390827 401 ETFSEYPPLGRFAVRDMRQTVAVGVIKSV 429
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
234-313 |
1.92e-17 |
|
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: 76.53 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 234 LRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNvaVKDLKRGYV 313
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-267 |
3.18e-16 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 80.91 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaAEMNKRsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSR---------AETQER------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKARYD 168
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIV-VINKVDR-----PGARPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 169 EIIKEVSSYLKKVGYNPDKIPFV--------PISGFEGDNMIERSTnldwykgPTLLEALDQINEPKRPSDKPLRLPLQD 240
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQLDFPivyasalnGIAGLDHEDMAEDMT-------PLYQAIVDHVPAPDVDLDGPFQMQISQ 211
|
250 260
....*....|....*....|....*..
gi 18390827 241 VYKIGGIGTVPVGRVETGMIKPGMVVT 267
Cdd:PRK10218 212 LDYNSYVGVIGIGRIKRGKVKPNQQVT 238
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-198 |
5.50e-16 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 75.65 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaaEMNKRsfkyawVLDKLKAERERGITID---IAL-WKFETTK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EMKEQ------VLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYC-TVIDAPGHRDFikNMITGTSQADC--AVLIIDSTTgGFEAgiskdgQTREHALLAFTLGVKqMICCCNKMDATTpk 161
Cdd:cd01890 66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQ-GVEA------QTLANFYLALENNLE-IIPVINKIDLPA-- 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 18390827 162 yskARYDEIIKEVSSYLkkvGYNPDKIpfVPISGFEG 198
Cdd:cd01890 134 ---ADPDRVKQEIEDVL---GLDASEA--ILVSAKTG 162
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
234-316 |
6.32e-16 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 72.56 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 234 LRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYV 313
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
...
gi 18390827 314 ASN 316
Cdd:cd03696 81 LSE 83
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
236-315 |
6.54e-16 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 72.55 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 236 LPLQDVYKIGGIGTVPVGRVETGMIKPGM---VVTFAPTgLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGY 312
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKET-LKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81
|
...
gi 18390827 313 VAS 315
Cdd:cd03697 82 VLA 84
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
7-304 |
1.75e-15 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 78.52 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 7 HI-NIVVIGHVDSGKSTTTGHLIYKLGGIDKRvierfekeaaEMNkrsfkyAWVLDKLKAERERGITID---IAL-WKFE 81
Cdd:COG0481 5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 82 T-TKYYCTVIDAPGHRDFiknmitgT-----SQADC--AVLIIDSTTgGFEAgiskdgQTREHALLAFTLGVKqMICCCN 153
Cdd:COG0481 69 DgETYQLNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQ-GVEA------QTLANVYLALENDLE-IIPVIN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 154 KMDATTpkyskARYDEIIKEVSsylKKVGYNPDKIpfVPISGFEGDNMIErstnldwykgptLLEAL-DQINEPKRPSDK 232
Cdd:COG0481 134 KIDLPS-----ADPERVKQEIE---DIIGIDASDA--ILVSAKTGIGIEE------------ILEAIvERIPPPKGDPDA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 233 PLRlPL-----QDVYKiggiGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSV-----EMHHESLLEAlpGDnVGF---N 299
Cdd:COG0481 192 PLQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvftpKMTPVDELSA--GE-VGYiiaG 263
|
....*
gi 18390827 300 VKNVA 304
Cdd:COG0481 264 IKDVR 268
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-198 |
3.53e-15 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 73.55 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 8 INIVVIGHVDSGKSTTTghliyklggidkRVIERFEKEAAemnkrsfkyawvLDKLKAERERGITIDIALWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTSLA------------KALSEIASTAA------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 81 -------ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGvKQMICCCN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18390827 154 KMDATTPKYSKARYDEIIKEVSSYLKKVgyNPDKIPFVPISGFEG 198
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVSAKPG 171
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-195 |
1.25e-14 |
|
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: 72.65 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIdkrvierFEKEAAEmnkrsfkyAWVLDKLKAERERGITID---IALwKFETTK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLAGK--------ARYLDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 ------YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTtggfeagiskDG---QTreHALL--AFTLGVKqMICCCN 153
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAV----------EGvcvQT--ETVLrqALEERVK-PVLVIN 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18390827 154 KMD------ATTPKYSKARYDEIIKEVSSYLKKVG---YNPDKIPFVPISG 195
Cdd:cd01885 133 KIDrlilelKLSPEEAYQRLLRIVEDVNAIIETYApeeFKQEKWKFSPQKG 183
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-174 |
1.03e-13 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 70.34 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDK--RVierfekeaaeMNKRSFkyawvLDKLKAERERGITIDIALWKFETTKYY 86
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRElgSV----------DKGTTR-----TDSMELERQRGITIFSAVASFQWEDTK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 87 CTVIDAPGHRDFIKNMITGTSQADCAVLIIdSTTGGFEAgiskdgQTRehaLLAFTLgvKQM----ICCCNKMDAttpky 162
Cdd:cd04168 66 VNIIDTPGHMDFIAEVERSLSVLDGAILVI-SAVEGVQA------QTR---ILFRLL--RKLniptIIFVNKIDR----- 128
|
170
....*....|..
gi 18390827 163 SKARYDEIIKEV 174
Cdd:cd04168 129 AGADLEKVYQEI 140
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
248-313 |
1.43e-13 |
|
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: 65.36 E-value: 1.43e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390827 248 GTVPVGRVETGMIKPGMVVTFAP-----TGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYV 313
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-209 |
3.86e-13 |
|
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: 68.00 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIyKLGGIdkrvierfEKEAAEMNKRsfkyawVLDKLKAERERGITIdiaLWKFETTKYYCT 88
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALL-KQSGT--------FRENEEVGER------VMDSNDLERERGITI---LAKNTAITYKDT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 89 ---VIDAPGHRDF------IKNMitgtsqADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKqMICCCNKMDAtt 159
Cdd:cd01891 66 kinIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRFVLKKALEAGLK-PIVVINKIDR-- 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18390827 160 pkySKARYDEIIKEVSSYLKKVGYNPDKIPFvPI------SGFEGDNMIERSTNLD 209
Cdd:cd01891 130 ---PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLD 181
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-228 |
8.73e-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: 66.91 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 8 INIVVIGHVDSGKSTttghLIYKLGGIdkrvierfekeaaemnkrsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:cd01888 1 INIGTIGHVAHGKTT----LVKALSGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 83 TKYY-------CTV---------------IDAPGHRDFIKNMITGTSQADCAVLIIDsttgGFEAgiSKDGQTREHaLLA 140
Cdd:cd01888 53 CGCPrpydtpeCECpgcggetklvrhvsfVDCPGHEILMATMLSGAAVMDGALLLIA----ANEP--CPQPQTSEH-LAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 141 F-TLGVKQMICCCNKMDATTPKYSKARYDEIIKevssYLKkvGYNPDKIPFVPISGFEGDNMIerstnldwykgpTLLEA 219
Cdd:cd01888 126 LeIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVK--GTIAENAPIIPISAQLKYNID------------VLCEY 187
|
250
....*....|
gi 18390827 220 L-DQINEPKR 228
Cdd:cd01888 188 IvKKIPTPPR 197
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-198 |
1.39e-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: 69.69 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKrvIERFEKEAAEMnkrsfkyawvlDKLKAERERGITIDIAL----WKfettK 84
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAAttceWK----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTrEHALlaftlgvKQM-------ICCCNKMDA 157
Cdd:COG0480 74 HKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQT-ETVW-------RQAdkygvprIVFVNKMDR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18390827 158 TtpkysKARYDEIIKEVSSYLKKvgyNPdkIPF-VPI---SGFEG 198
Cdd:COG0480 139 E-----GADFDRVLEQLKERLGA---NP--VPLqLPIgaeDDFKG 173
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-267 |
1.78e-12 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 69.28 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIyKLGGI---DKRVIERfekeaaemnkrsfkyawVLDKLKAERERGITIdiaLWKfettky 85
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALL-KQSGTfreNQEVAER-----------------VMDSNDLERERGITI---LAK------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 86 yCT----------VIDAPGHRDF------IKNMitgtsqADCAVLIIDSttggFEagiskdG---QTR---EHALlafTL 143
Cdd:COG1217 61 -NTavrykgvkinIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---EL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 144 GVKqMICCCNKMDattpkysK--ARYDEIIKEVSSYLKKVGYNPDKIPFvPI------SGFEGDNMIERSTNLDwykgPt 215
Cdd:COG1217 121 GLK-PIVVINKID-------RpdARPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDLT----P- 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18390827 216 LLEA-LDQINEPKRPSDKPLRlpLQ------DVYkIGGIGtvpVGRVETGMIKPGMVVT 267
Cdd:COG1217 187 LFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVA 239
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-311 |
1.81e-12 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 69.31 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 10 IVVIGHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDI--ALWKFETTKYYc 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRVL- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIdsttggfeagISKDG---QTREH-ALLAFTlGVKQMICCCNKMDattpKYS 163
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVV----------ACDDGvmaQTREHlAILQLT-GNPMLTVALTKAD----RVD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 164 KARYDEIIKEVSSYLKKVGYnpDKIPFVPISGFEGDNMierstnldwykgPTLLEALDQINEPKRPSDKPLRLPLQDVYK 243
Cdd:PRK10512 119 EARIAEVRRQVKAVLREYGF--AEAKLFVTAATEGRGI------------DALREHLLQLPEREHAAQHRFRLAIDRAFT 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390827 244 IGGIGTVPVGRVETGMIKPGMvvTFAPTGLTTEVKSVEMH--HESLLEALPGDNVGFNVKNVAVK-DLKRG 311
Cdd:PRK10512 185 VKGAGLVVTGTALSGEVKVGD--TLWLTGVNKPMRVRGLHaqNQPTEQAQAGQRIALNIAGDAEKeQINRG 253
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
233-315 |
2.30e-12 |
|
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: 62.53 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 233 PLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGY 312
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
...
gi 18390827 313 VAS 315
Cdd:cd16267 81 ILC 83
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
233-313 |
1.44e-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: 60.19 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 233 PLRLPLQDVYKigGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGY 312
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 18390827 313 V 313
Cdd:cd04089 79 V 79
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-198 |
3.34e-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: 63.66 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYkLGGIDKRVIERFEKEAaemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILY-YTGRIHKIGEVHGGGA------------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDStTGGFEAgiskdgQtrehallafTLGV-KQM-------ICCCNKMDATtp 160
Cdd:cd01886 68 IIDTPGHVDFTIEVERSLRVLDGAVAVFDA-VAGVQP------Q---------TETVwRQAdrygvprIAFVNKMDRT-- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18390827 161 kysKARYDEIIKEVSSylkKVGYNPDKIpFVPI---SGFEG 198
Cdd:cd01886 130 ---GADFYRVVEQIRE---KLGANPVPL-QLPIgaeDDFEG 163
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
233-316 |
4.20e-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: 59.05 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 233 PLRLPLQDVYKiGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMH-HESLLEALPGDNVGFNVKNVAVKDLKRG 311
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 18390827 312 YVASN 316
Cdd:cd03698 80 DILSS 84
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-181 |
1.05e-10 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 63.82 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKrvIERFEKEAAEMnkrsfkyawvlDKLKAERERGITIDIAL----WKfettK 84
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHK--MGEVEDGTTVT-----------DWMPQEQERGITIESAAtscdWD----N 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTgGFEAgiskdgQTREHALLAFTLGVKQmICCCNKMDATtpkysK 164
Cdd:PRK13351 73 HRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVT-GVQP------QTETVWRQADRYGIPR-LIFINKMDRV-----G 139
|
170
....*....|....*..
gi 18390827 165 ARYDEIIKEVSSYLKKV 181
Cdd:PRK13351 140 ADLFKVLEDIEERFGKR 156
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-178 |
1.69e-10 |
|
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: 61.46 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRviERFEKEAAemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYYCT 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRL--GRVEDGNT-----------VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQMIcCCNKMDAttpkySKARYD 168
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRII-FINKMDR-----ARADFD 134
|
170
....*....|
gi 18390827 169 EIIKEVSSYL 178
Cdd:cd04170 135 KTLAALREAF 144
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-179 |
1.79e-10 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 60.36 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYklggidkrvierFEKEAAEMNKRSFKYAWVLDKLKAERERGITI-----DIALWKFETT 83
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIE------------QTHKRTPSVKLGWKPLRYTDTRKDEQERGISIksnpiSLVLEDSKGK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTggfeaGISKdgQTREHALLAFTLGVKqMICCCNKMD------- 156
Cdd:cd04167 70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTS--VTERLIRHAIQEGLP-MVLVINKIDrlilelk 141
|
170 180
....*....|....*....|....
gi 18390827 157 -ATTPKYSKARYdeIIKEVSSYLK 179
Cdd:cd04167 142 lPPTDAYYKLRH--TIDEINNYIA 163
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-179 |
6.41e-10 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 61.30 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 13 IGHVDSGKSTTTGHLIYKLGGIDKrvIERFEKEAAemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYYCTVIDA 92
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHR--IGEVEDGTT-----------TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 93 PGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTRehALLAFT--LGVKQMIcCCNKMDATtpkysKARYDEI 170
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRII-FVNKMDRA-----GADFFRV 132
|
....*....
gi 18390827 171 IKEVSSYLK 179
Cdd:PRK12740 133 LAQLQEKLG 141
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
234-298 |
2.46e-09 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 53.72 E-value: 2.46e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390827 234 LRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGF 298
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-121 |
8.29e-09 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 56.45 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 12 VIGHVDSGKSTTTGHLIYKLGGIdkrvierfeKEAAEMN-KRSFKYAwVLDKLKAERERGITIDIALWKFETTKYYCTVI 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVKaRKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110
....*....|....*....|....*....|.
gi 18390827 91 DAPGHRDFIKNMITGTSQADCAVLIIDSTTG 121
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-293 |
2.94e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 55.78 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 8 INIVVIGHVDSGKSTttghLIYKLGGIdKRVierfekeaaemnkrsfkyawvldKLKAERERGITIDIA-----LWKFE- 81
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV-KTV-----------------------RFKREKVRNITIKLGyanakIYKCPk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 82 ---------------------------TTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIdsttggfeAGISK--DGQ 132
Cdd:PTZ00327 87 cprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLI--------AANEScpQPQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 133 TREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIIKevssYLKkvGYNPDKIPFVPISGfegdnmiERSTNLDwyk 212
Cdd:PTZ00327 159 TSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRN----FVK--GTIADNAPIIPISA-------QLKYNID--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 213 gpTLLEAL-DQINEPKRPSDKPLRL----------PLQDVYKI-GGI--GTVPVGRVETG---MIKPGMVV-----TFAP 270
Cdd:PTZ00327 223 --VVLEYIcTQIPIPKRDLTSPPRMivirsfdvnkPGEDIENLkGGVagGSILQGVLKVGdeiEIRPGIISkdsggEFTC 300
|
330 340
....*....|....*....|...
gi 18390827 271 TGLTTEVKSVEMHHESLLEALPG 293
Cdd:PTZ00327 301 RPIRTRIVSLFAENNELQYAVPG 323
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-98 |
5.99e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 55.25 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVierfekeAAEmnkrsfkyAWVLDKLKAERERGITIDIA----LWKFETTK 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
|
90
....*....|....
gi 18390827 85 YYCTVIDAPGHRDF 98
Cdd:PRK07560 87 YLINLIDTPGHVDF 100
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-121 |
1.24e-07 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 54.28 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 1 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDkrvierfEKEAAEmnkrsfkyAWVLDKLKAERERGITID---IAL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18390827 78 WkFETT--------KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTG 121
Cdd:PTZ00416 78 Y-YEHDledgddkqPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEG 128
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
240-313 |
1.50e-07 |
|
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: 48.76 E-value: 1.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390827 240 DVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTG----LTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYV 313
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-225 |
1.87e-06 |
|
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: 47.85 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 10 IVVIGHVDSGKSTttghliyklggidkrvierfekeaaemnkrsfkyawVLDKLK----AERE-RGITIDIALWKFETTK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 85 YY--CTVIDAPGHRDFiKNMIT-GTSQADCAVLIIDSTTgGFEAgiskdgQTRE---HALLAFTlgvkQMICCCNKMDAT 158
Cdd:cd01887 47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADD-GVMP------QTIEainHAKAANV----PIIVAINKIDKP 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390827 159 TPKyskaryDEIIKEVSSYLKKVGYNPD----KIPFVPISGFEGDNMierstnldwykgPTLLEALDQINE 225
Cdd:cd01887 115 YGT------EADPERVKNELSELGLVGEewggDVSIVPISAKTGEGI------------DDLLEAILLLAE 167
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-203 |
4.07e-06 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 46.68 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 11 VVIGHVDSGKSTTTGHLIYKlggidkrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDIALWKFETTKYYCTV- 89
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVYVKELDKGKVKLv 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 90 -IDAPGHRDFIKNMITGT-----SQADCAVLIIDSTTggfeaGISKDGQTREHALLAFTLGVKqMICCCNKMDattpkys 163
Cdd:cd00882 51 lVDTPGLDEFGGLGREELarlllRGADLILLVVDSTD-----RESEEDAKLLILRRLRKEGIP-IILVGNKID------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18390827 164 kaRYDEIIKEVSSYLKKVGYNPDkIPFVPISGFEGDNMIE 203
Cdd:cd00882 118 --LLEEREVEELLRLEELAKILG-VPVFEVSAKTGEGVDE 154
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
9-121 |
5.83e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 48.95 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390827 9 NIVVIGHVDSGKSTTTGHLIYKLGGIDKRVierfekeAAEmnkrsfkyAWVLDKLKAERERGITID---IALWkFETT-- 83
Cdd:PLN00116 21 NMSVIAHVDHGKSTLTDSLVAAAGIIAQEV-------AGD--------VRMTDTRADEAERGITIKstgISLY-YEMTde 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18390827 84 ------------KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTG 121
Cdd:PLN00116 85 slkdfkgerdgnEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEG 134
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
239-297 |
1.51e-03 |
|
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 37.27 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18390827 239 QDVYKIGGiGTVPVGRVETGMIKPGMVVTFAPtgLTTEVKSVEMHHESLLEALPGDNVG 297
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVKGDK--GVALIRAIEREHRKVDFAVAGDEVA 61
|
|
| |
