|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-427 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 770.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 81 ESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEAGIAEQGQTREHALLAYTLGIKQVIVAVNKMDDSTV 160
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 161 EYKKERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQD 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 241 VFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVGDVSRD 320
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 321 PPKQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVV 400
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCV 400
|
410 420
....*....|....*....|....*..
gi 385861629 401 EQFQQYPALGRFAVRDMKQTVAVGVIR 427
Cdd:PTZ00141 401 EVFNEYPPLGRFAVRDMKQTVAVGVIK 427
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-428 |
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: 620.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 81 ESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKQVIVAVNKMDDstV 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDG-------VMGQTREHAFLARTLGINQLIVAVNKMDA--V 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 161 EYKKERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQD 240
Cdd:COG5256 152 NYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 241 VFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVGDVSrD 320
Cdd:COG5256 232 VYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD-N 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 321 PPKQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVV 400
Cdd:COG5256 311 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVI 390
|
410 420
....*....|....*....|....*...
gi 385861629 401 EQFQQYPALGRFAVRDMKQTVAVGVIRN 428
Cdd:COG5256 391 EKFKEFPQLGRFAIRDMGQTVAAGVVLD 418
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-426 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 611.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 3 KEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKFES 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 83 AKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagIAEQGQTREHALLAYTLGIKQVIVAVNKMDdsTVEY 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDA-----GGVMPQTREHVFLARTLGINQLIVAINKMD--AVNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 163 KKERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQDVF 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 243 EISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVGDVSrDPP 322
Cdd:PRK12317 235 SISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD-NPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 323 KQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVVEQ 402
Cdd:PRK12317 314 TVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEK 393
|
410 420
....*....|....*....|....
gi 385861629 403 FQQYPALGRFAVRDMKQTVAVGVI 426
Cdd:PRK12317 394 VKEIPQLGRFAIRDMGQTIAAGMV 417
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-427 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 582.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 81 ESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEAGIAEQGQTREHALLAYTLGIKQVIVAVNKMDDSTV 160
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 161 EYKKERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQD 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 241 VFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVGDVSRD 320
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 321 PPKQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVV 400
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVV 400
|
410 420
....*....|....*....|....*..
gi 385861629 401 EQFQQYPALGRFAVRDMKQTVAVGVIR 427
Cdd:PLN00043 401 ETFSEYPPLGRFAVRDMRQTVAVGVIK 427
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-426 |
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: 580.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 81 ESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEAgiaeQGQTREHALLAYTLGIKQVIVAVNKMDdsTV 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFEV----QPQTREHAFLARTLGINQLIVAINKMD--SV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 161 EYKKERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQD 240
Cdd:TIGR00483 155 NYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 241 VFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVGDvSRD 320
Cdd:TIGR00483 235 VYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGH-PDN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 321 PPKQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVV 400
Cdd:TIGR00483 314 PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVI 393
|
410 420
....*....|....*....|....*.
gi 385861629 401 EQFQQYPALGRFAVRDMKQTVAVGVI 426
Cdd:TIGR00483 394 EAVKEIPPLGRFAIRDMGQTVAAGMI 419
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-227 |
1.40e-138 |
|
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: 395.71 E-value: 1.40e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKFESAKYMFT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 IIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEAGIAEQGQTREHALLAYTLGIKQVIVAVNKMDDSTVEYKKERYD 168
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 385861629 169 EISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPK 227
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPPE 219
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-427 |
3.16e-101 |
|
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: 308.17 E-value: 3.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 4 EKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKFESA 83
Cdd:COG2895 14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 84 KYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagIAEQgqTREHALLAYTLGIKQVIVAVNKMDdsTVEYK 163
Cdd:COG2895 94 KRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKG-----VLEQ--TRRHSYIASLLGIRHVVVAVNKMD--LVDYS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 164 KERYDEISTEMTRVLTSIGYkqEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQDV-- 241
Cdd:COG2895 165 EEVFEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVnr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 242 -------FeisgigtvpSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGF----NVkgipasDIKR 310
Cdd:COG2895 243 pnldfrgY---------AGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtledEI------DISR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 311 GFVVGDVSrDPPKQCVSFEAqMII--SNHPGKIHAGYqpVFDCHTAHIACKFAKLVQRIDRRHGKKvtEEPEWIQKDDAA 388
Cdd:COG2895 308 GDVIVAAD-APPEVADQFEA-TLVwmDEEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEH--EAADSLELNDIG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 385861629 389 VVIVEPGKPLVVEQFQQYPALGRFAV--RDMKQTVAVGVIR 427
Cdd:COG2895 382 RVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIR 422
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-226 |
1.73e-71 |
|
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: 223.56 E-value: 1.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 5 KEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRklaqiektaielGKGAFKYAFVMDNLKAERERGITIDISLWKFESAK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKR------------GEVKGEGEAGLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 85 YMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKqVIVAVNKMDDSTveykK 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRVD----G 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385861629 165 ERYDEISTEMTRVL-TSIGYKQEQFRFIPISGFVGDNMTdksanlswwtggTLLDTLDVLVPP 226
Cdd:pfam00009 137 AELEEVVEEVSRELlEKYGEDGEFVPVVPGSALKGEGVQ------------TLLDALDEYLPS 187
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-228 |
4.67e-70 |
|
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: 220.52 E-value: 4.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAI-ELGKGAFKYAFVMDNLKAERERGITIDISLWKFESAKYMF 87
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERSKSsGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 88 TIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDdsTVEYKKERY 167
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD--LVDYDEEVF 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385861629 168 DEISTEMTRVLTSIGYkqEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDvLVPPKR 228
Cdd:cd04166 152 EEIKADYLAFAASLGI--EDITFIPISALEGDNVVSRSENMPWYKGPTLLEHLE-TVEIAS 209
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-426 |
3.00e-67 |
|
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: 219.94 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 14 GHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGK--GAFKYAFVMDNLKAERERGITIDISLWKFESAKYMFTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDdsTVEYKKERYDEIS 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 172 TEMTRVLTSIGYKqeQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQDV----FEISGI 247
Cdd:TIGR02034 158 KDYLAFAEQLGFR--DVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVnrpnLDFRGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 248 gtvpSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGipASDIKRG-FVVGDVSRDPPKQcv 326
Cdd:TIGR02034 236 ----AGTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDD--EIDISRGdLLAAADSAPEVAD-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 327 SFEAQMI-ISNHPgkIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKvtEEPEWIQKDDAAVVIVEPGKPLVVEQFQQ 405
Cdd:TIGR02034 308 QFAATLVwMAEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEK--GAAKSLELNEIGRVNLSLDEPIAFDPYAE 383
|
410 420
....*....|....*....|...
gi 385861629 406 YPALGRFAV--RDMKQTVAVGVI 426
Cdd:TIGR02034 384 NRTTGAFILidRLSNRTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
5-330 |
3.79e-66 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 222.88 E-value: 3.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 5 KEHINLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELG--KGAFKYAFVMDNLKAERERGITIDISLWKFES 82
Cdd:PRK05506 22 KSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 83 AKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDdsTVEY 162
Cdd:PRK05506 102 PKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMD--LVDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 163 KKERYDEISTEMTRVLTSIGYkqEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQDV- 241
Cdd:PRK05506 173 DQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVn 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 242 --------FeisgigtvpSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVkgipASDIkrgfv 313
Cdd:PRK05506 251 rpnldfrgF---------AGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEI----- 312
|
330 340
....*....|....*....|....*
gi 385861629 314 vgDVSR--------DPPKQCVSFEA 330
Cdd:PRK05506 313 --DISRgdmlaradNRPEVADQFDA 335
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-428 |
1.13e-62 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 209.77 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 14 GHVDAGKSTTTGHLIYKCGGIDKRKLAQIEKTAIELGK--GAFKYAFVMDNLKAERERGITIDISLWKFESAKYMFTIID 91
Cdd:PRK05124 34 GSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTqgEKLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDdsTVEYKKERYDEIS 171
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMD--LVDYSEEVFERIR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 172 TEMTRVLTSIGYkQEQFRFIPISGFVGDNMTDKSANLSWWTGGTLLDTLDVLVPPKRPYDKPLRLPVQDV----FEISGI 247
Cdd:PRK05124 185 EDYLTFAEQLPG-NLDIRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVnrpnLDFRGY 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 248 gtvpSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGipASDIKRGFVVGDVSRDPPkQCVS 327
Cdd:PRK05124 264 ----AGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLED--EIDISRGDLLVAADEALQ-AVQH 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 328 FEAQMI-ISNHPgkIHAGYQpvFDchtahiaCKFA--KLVQRIDRRHGK--------KVTEEpewIQKDDAAVVIVEPGK 396
Cdd:PRK05124 337 ASADVVwMAEQP--LQPGQS--YD-------IKIAgkKTRARVDAIRYQvdintltqREAEN---LPLNGIGLVELTFDE 402
|
410 420 430
....*....|....*....|....*....|....
gi 385861629 397 PLVVEQFQQYPALGRFAV--RDMKQTVAVGVIRN 428
Cdd:PRK05124 403 PLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVRE 436
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-427 |
3.92e-60 |
|
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: 201.15 E-value: 3.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKE-----KEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLT---------------AAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 76 SLWKFESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 156 DDSTVEykkERYDEISTEMTRVLTSIGYKQEQFRFIPISGFV---GDNMTDksanlswWTGG--TLLDTLDVLVP-PKRP 229
Cdd:COG0050 139 DMVDDE---ELLELVEMEVRELLSKYGFPGDDTPIIRGSALKaleGDPDPE-------WEKKilELMDAVDSYIPePERD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 230 YDKPLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIapAGIV----TDVKSIEMHHTQLPEAVPGDVIGFNVKGIPA 305
Cdd:COG0050 209 TDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEI--VGIRdtqkTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 306 SDIKRGFVV---GDVsrdppKQCVSFEAQM-IISNHPGKIH----AGYQPVFDCHTAHI--ACKFAKLVqridrrhgkkv 375
Cdd:COG0050 287 EDVERGQVLakpGSI-----TPHTKFEAEVyVLSKEEGGRHtpffNGYRPQFYFRTTDVtgVITLPEGV----------- 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 385861629 376 teepEWIQKDDAAVVIVEPGKPLVVEQFQqypalgRFAVRDMKQTVAVGVIR 427
Cdd:COG0050 351 ----EMVMPGDNVTMTVELITPIAMEEGL------RFAIREGGRTVGAGVVT 392
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-426 |
2.19e-59 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 199.01 E-value: 2.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKE-----KEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLT---------------AAITKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 76 SLWKFESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 156 DDSTVEykkERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKsanlswWTGGT--LLDTLDVLVP-PKRPYDK 232
Cdd:PRK12736 139 DLVDDE---ELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPK------WEDAImeLMDAVDEYIPtPERDTDK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 233 PLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIapAGIVTDVKS----IEMHHTQLPEAVPGDVIGFNVKGIPASDI 308
Cdd:PRK12736 210 PFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEI--VGIKETQKTvvtgVEMFRKLLDEGQAGDNVGVLLRGVDRDEV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 309 KRGFVV---GDVSrdPPKQcvsFEAQM-IISNHPGKIH----AGYQPVFDCHTAhiackfaklvqriDRRHGKKVTEEPE 380
Cdd:PRK12736 288 ERGQVLakpGSIK--PHTK---FKAEVyILTKEEGGRHtpffNNYRPQFYFRTT-------------DVTGSIELPEGTE 349
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 385861629 381 WIQKDDAAVVIVEPGKPLVVEQfqqypalG-RFAVRDMKQTVAVGVI 426
Cdd:PRK12736 350 MVMPGDNVTITVELIHPIAMEQ-------GlKFAIREGGRTVGAGTV 389
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-426 |
4.15e-55 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 187.70 E-value: 4.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKE-----KEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDI 75
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLT---------------AAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 76 SLWKFESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNK- 154
Cdd:PRK00049 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKc 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 155 --MDDstveykKERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSAnlswWTGGT--LLDTLDVLVP-PKRP 229
Cdd:PRK00049 139 dmVDD------EELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDDDEE----WEKKIleLMDAVDSYIPtPERA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 230 YDKPLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIapAGI----VTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPA 305
Cdd:PRK00049 209 IDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI--VGIrdtqKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 306 SDIKRGFVV---GDVSrdPPKQcvsFEAQM-IISNHPGKIH----AGYQPVFDCHTAHI--ACKFaklvqridrrhgkkv 375
Cdd:PRK00049 287 EDVERGQVLakpGSIT--PHTK---FEAEVyVLSKEEGGRHtpffNGYRPQFYFRTTDVtgVIEL--------------- 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 385861629 376 TEEPEWIQKDDAAVVIVEPGKPLVVEQFQqypalgRFAVRDMKQTVAVGVI 426
Cdd:PRK00049 347 PEGVEMVMPGDNVEMTVELIAPIAMEEGL------RFAIREGGRTVGAGVV 391
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
323-426 |
6.56e-54 |
|
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: 175.07 E-value: 6.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 323 KQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVVEQ 402
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 385861629 403 FQQYPALGRFAVRDMKQTVAVGVI 426
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-428 |
9.88e-54 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 186.36 E-value: 9.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 3 KEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIdkrklaqiektaielGKGAFKYAFVMDNLKAERERGITIDISLWKFES 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASM---------------GGSAPKKYDEIDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 83 AKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDDSTVEy 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVDDE- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 163 kkERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVG-----DNMTDKSANLSWWTG-GTLLDTLDVLVP-PKRPYDKPLR 235
Cdd:PLN03126 214 --ELLELVELEVRELLSSYEFPGDDIPIISGSALLAlealmENPNIKRGDNKWVDKiYELMDAVDSYIPiPQRQTDLPFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 236 LPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIV--TDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFV 313
Cdd:PLN03126 292 LAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 314 VGDVSRDPPKQcvSFEAQM-IISNHPGKIH----AGYQPVFDCHTAHIACKFAKLVQRIDrrhgkkvtEEPEWIQKDDAA 388
Cdd:PLN03126 372 LAKPGSITPHT--KFEAIVyVLKKEEGGRHspffAGYRPQFYMRTTDVTGKVTSIMNDKD--------EESKMVMPGDRV 441
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 385861629 389 VVIVEPGKPLVVEQFQqypalgRFAVRDMKQTVAVGVIRN 428
Cdd:PLN03126 442 KMVVELIVPVACEQGM------RFAIREGGKTVGAGVIQS 475
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-428 |
2.20e-53 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 183.44 E-value: 2.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 3 KEKEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKFES 82
Cdd:TIGR00485 8 RTKPHVNVGTIGHVDHGKTTLT---------------AAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 83 AKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDDSTVEy 162
Cdd:TIGR00485 73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 163 kkERYDEISTEMTRVLTSIGYKQEQfrfIPIsgfVGDNMTDKSANLSWWTGGT--LLDTLDVLVP-PKRPYDKPLRLPVQ 239
Cdd:TIGR00485 145 --ELLELVEMEVRELLSQYDFPGDD---TPI---IRGSALKALEGDAEWEAKIleLMDAVDEYIPtPEREIDKPFLLPIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 240 DVFEISGIGTVPSGRVESGIMKPAQNIVIapAGI----VTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVG 315
Cdd:TIGR00485 217 DVFSITGRGTVVTGRVERGIIKVGEEVEI--VGLkdtrKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 316 DVSRDPPKQcvSFEAQM-IISNHPGKIH----AGYQPVFDCHTAHIACKFaklvqridrrhgkKVTEEPEWIQKDDAAVV 390
Cdd:TIGR00485 295 KPGSIKPHT--KFEAEVyVLSKEEGGRHtpffSGYRPQFYFRTTDVTGTI-------------ELPEGVEMVMPGDNVKM 359
|
410 420 430
....*....|....*....|....*....|....*...
gi 385861629 391 IVEPGKPLVVEQFQqypalgRFAVRDMKQTVAVGVIRN 428
Cdd:TIGR00485 360 TVELISPIALEQGM------RFAIREGGRTVGAGVVSK 391
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-353 |
1.68e-52 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 180.80 E-value: 1.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKE-----KEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEkfertKPHVNVGTIGHVDHGKTTLT---------------AAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 76 SLWKFESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNK- 154
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKc 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 155 --MDDstveykKERYDEISTEMTRVLTSIGYKQEQfrfIPI---SGFVGDNMTDKSAnlswWTGG--TLLDTLDVLVP-P 226
Cdd:PRK12735 139 dmVDD------EELLELVEMEVRELLSKYDFPGDD---TPIirgSALKALEGDDDEE----WEAKilELMDAVDSYIPeP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 227 KRPYDKPLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIapAGI----VTDVKSIEMHHTQLPEAVPGDVIGFNVKG 302
Cdd:PRK12735 206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEI--VGIketqKTTVTGVEMFRKLLDEGQAGDNVGVLLRG 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 385861629 303 IPASDIKRGFVV---GDVSrdPPKQcvsFEAQM-IISNHPGKIH----AGYQPVFDCHT 353
Cdd:PRK12735 284 TKREDVERGQVLakpGSIK--PHTK---FEAEVyVLSKEEGGRHtpffNGYRPQFYFRT 337
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-428 |
8.19e-52 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 179.38 E-value: 8.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 3 KEKEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKT-AIELGKGAFKYAFVmDNLKAERERGITIDISLWKFE 81
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLT---------------AAITMTlAAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 82 SAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDDSTVE 161
Cdd:CHL00071 72 TENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVDDE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 162 ykkERYDEISTEMTRVLTSIGYKQEQFRFIPISGFVGDNMTDKSANLS----WWTGG--TLLDTLDVLVP-PKRPYDKPL 234
Cdd:CHL00071 145 ---ELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIKrgenKWVDKiyNLMDAVDSYIPtPERDTDKPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 235 RLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAGI--VTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGF 312
Cdd:CHL00071 222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLREtkTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 313 VVGDV-SRDPPKQcvsFEAQM-IISNHPGKIH----AGYQPVFDCHTAHIACKFAKLVQRIDrrhgkkvtEEPEWIQKDD 386
Cdd:CHL00071 302 VLAKPgTITPHTK---FEAQVyILTKEEGGRHtpffPGYRPQFYVRTTDVTGKIESFTADDG--------SKTEMVMPGD 370
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 385861629 387 AAVVIVEPGKPLVVEQFQqypalgRFAVRDMKQTVAVGVIRN 428
Cdd:CHL00071 371 RIKMTVELIYPIAIEKGM------RFAIREGGRTVGAGVVSK 406
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-426 |
1.08e-50 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 177.32 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 3 KEKEHINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKgAFKYAF-VMDNLKAERERGITIDISLWKFE 81
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLT---------------AAITKVLAEEGK-AKAVAFdEIDKAPEEKARGITIATAHVEYE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 82 SAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVAVNKMDdsTVE 161
Cdd:PLN03127 121 TAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVD--VVD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 162 yKKERYDEISTEMTRVLTSIGYKQEQfrfIPI------SGFVGDNMT-DKSANLSwwtggtLLDTLDVLVP-PKRPYDKP 233
Cdd:PLN03127 192 -DEELLELVEMELRELLSFYKFPGDE---IPIirgsalSALQGTNDEiGKNAILK------LMDAVDEYIPePVRVLDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 234 LRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIA----PAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIK 309
Cdd:PLN03127 262 FLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVglrpGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 310 RGFVVGDV-SRDPPKQcvsFEAQM-IISNHPGKIH----AGYQPVFDCHTAHIACKFaklvqridrrhgkKVTEEPEWIQ 383
Cdd:PLN03127 342 RGQVICKPgSIKTYKK---FEAEIyVLTKDEGGRHtpffSNYRPQFYLRTADVTGKV-------------ELPEGVKMVM 405
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 385861629 384 KDDAAVVIVEPGKPLVVEQFQqypalgRFAVRDMKQTVAVGVI 426
Cdd:PLN03127 406 PGDNVTAVFELISPVPLEPGQ------RFALREGGRTVGAGVV 442
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-203 |
2.10e-50 |
|
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: 168.63 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQIektaielgkgafkyaFVMDNLKAERERGITIDISLWKFESAKYMFT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 IIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKqVIVAVNKMDdstvEYKKERYD 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEG-------VEPQTREHLNIALAGGLP-IIVAVNKID----RVGEEDFD 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 385861629 169 EISTEMTRVLTSIGY---KQEQFRFIPISGFVGDNMTD 203
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
231-320 |
2.84e-45 |
|
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: 151.96 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 231 DKPLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKR 310
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKR 81
|
90
....*....|
gi 385861629 311 GFVVGDVSRD 320
Cdd:cd03693 82 GDVAGDSKND 91
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
14-314 |
2.21e-41 |
|
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: 155.46 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 14 GHVDAGKSTttghLIYKCGGIDkrklaqiekTaielgkgafkyafvmDNLKAERERGITIDI--SLWKFESAKYMfTIID 91
Cdd:COG3276 7 GHIDHGKTT----LVKALTGID---------T---------------DRLKEEKKRGITIDLgfAYLPLPDGRRL-GFVD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDstrggfeagiAEQG---QTREH-ALLAyTLGIKQVIVAVNKMDdsTVEykKERY 167
Cdd:COG3276 58 VPGHEKFIKNMLAGAGGIDLVLLVVA----------ADEGvmpQTREHlAILD-LLGIKRGIVVLTKAD--LVD--EEWL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 168 DEISTEMTRVLTSIGYkqEQFRFIPISGFVGDNMTDksanlswwtggtLLDTLDVLV--PPKRPYDKPLRLPVQDVFEIS 245
Cdd:COG3276 123 ELVEEEIRELLAGTFL--EDAPIVPVSAVTGEGIDE------------LRAALDALAaaVPARDADGPFRLPIDRVFSIK 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385861629 246 GIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVV 314
Cdd:COG3276 189 GFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVL 257
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-390 |
5.03e-41 |
|
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: 153.88 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 8 INLVVIGHVDAGKSTttghLIYKCGGIDKrklaqiektaielgkgafkyafvmDNLKAERERGITIDISLWKFESAKYMF 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 88 TIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKQVIVAVNKMDDStveyKKERY 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-------VMTQTGEHLAVLDLLGIPHTIVVITKADRV----NEEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 168 DEISTEMTRVLTSIGYKQEQfRFIPISGFVGDNMTDKSANLSwwtggTLLDTLDVLvppkrPYDKPLRLPVQDVFEISGI 247
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFLKNA-KIFKTSAKTGQGIGELKKELK-----NLLESLDIK-----RIQKPLRMAIDRAFKVKGA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 248 GTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVgDVSRDPPKQcVS 327
Cdd:TIGR00475 191 GTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI-LTPEDPKLR-VV 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385861629 328 FEAQMIISNHPGKIHagyqpvfdcHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVV 390
Cdd:TIGR00475 269 VKFIAEVPLLELQPY---------HIAHGMSVTTGKISLLDKGIALLTLDAPLILAKGDKLVL 322
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
321-428 |
9.54e-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: 119.29 E-value: 9.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 321 PPKQCVSFEAQMIISNH-----PGKIHAGYQPVFDCHTAHIACKFAKLVQRIDrrhGKKVTEEPEWIQKDDAAVVIVEPG 395
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD---PGGVSENPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|...
gi 385861629 396 KPLVVEQFQqypalgRFAVRDMKQTVAVGVIRN 428
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTE 104
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
7-156 |
1.25e-32 |
|
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: 122.31 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 7 HINLVVIGHVDAGKSTTTghliykcggidkrklAQIEKTAIELGKGAFKYAFVMDNLKAERERGITIDISLWKFESAKYM 86
Cdd:cd01884 2 HVNVGTIGHVDHGKTTLT---------------AAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 87 FTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKQVIVAVNKMD 156
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDG-------PMPQTREHLLLARQVGVPYIVVFLNKAD 129
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
325-426 |
2.68e-24 |
|
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: 96.31 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 325 CVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKvtEEPEWIQKDDAAVVIVEPGKPLVVEQFQ 404
Cdd:cd01513 3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGK 80
|
90 100
....*....|....*....|..
gi 385861629 405 QYPALGRFAVRDMKQTVAVGVI 426
Cdd:cd01513 81 EFPTLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-184 |
3.05e-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: 95.75 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 14 GHVDAGKSTttghLIYKCGGIDKrklaqiektaielgkgafkyafvmDNLKAERERGITIDISL--WKFESAKYMfTIID 91
Cdd:cd04171 6 GHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFayLDLPDGKRL-GFID 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDstrggfeagiAEQG---QTREHALLAYTLGIKQVIVAVNKMDdsTVEykKERYD 168
Cdd:cd04171 57 VPGHEKFVKNMLAGAGGIDAVLLVVA----------ADEGimpQTREHLEILELLGIKKGLVVLTKAD--LVD--EDRLE 122
|
170
....*....|....*.
gi 385861629 169 EISTEMTRVLTSIGYK 184
Cdd:cd04171 123 LVEEEILELLAGTFLA 138
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
325-426 |
4.87e-19 |
|
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: 82.22 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 325 CVSFEAQ-MIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVVEQF 403
Cdd:cd03704 3 VTEFEAQiVILDLLKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETF 82
|
90 100
....*....|....*....|...
gi 385861629 404 QQYPALGRFAVRDMKQTVAVGVI 426
Cdd:cd03704 83 KDFPQLGRFTLRDEGKTIAIGKV 105
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
234-314 |
6.60e-19 |
|
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: 80.65 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 234 LRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFV 313
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
.
gi 385861629 314 V 314
Cdd:cd03696 81 L 81
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-322 |
7.93e-19 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 87.99 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 8 INLVVIGHVDAGKSTTTGHL--------------------------IYKCGGIDKRKLAQIEKTAIELGKgafkyafvmd 61
Cdd:PRK04000 10 VNIGMVGHVDHGKTTLVQALtgvwtdrhseelkrgitirlgyadatIRKCPDCEEPEAYTTEPKCPNCGS---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 62 nlKAERERGITIdislwkfesakymftiIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiAEQGQTREHALLAY 141
Cdd:PRK04000 80 --ETELLRRVSF----------------VDAPGHETLMATMLSGAALMDGAILVIAANEP------CPQPQTKEHLMALD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 142 TLGIKQVIVAVNKMDDSTVEYKKERYDEIsTEMTRvltsiGYKQEQFRFIPISGFVGDNMtdksanlswwtgGTLLDTLD 221
Cdd:PRK04000 136 IIGIKNIVIVQNKIDLVSKERALENYEQI-KEFVK-----GTVAENAPIIPVSALHKVNI------------DALIEAIE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 222 VLVP-PKRPYDKPLRLPVQDVFEISGIGTVPS--------GRVESGIMKPAQNIVIAPaG-------------IVTDVKS 279
Cdd:PRK04000 198 EEIPtPERDLDKPPRMYVARSFDVNKPGTPPEklkggvigGSLIQGVLKVGDEIEIRP-GikveeggktkwepITTKIVS 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 385861629 280 IEMHHTQLPEAVPGDVIGFNVKGIPA---SDIKRGFVVGDVSRDPP 322
Cdd:PRK04000 277 LRAGGEKVEEARPGGLVGVGTKLDPSltkADALAGSVAGKPGTLPP 322
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-194 |
2.04e-18 |
|
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: 82.80 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 8 INLVVIGHVDAGKSTTTghliykcggidkRKLAQIEKTAielgkgafkyAFvmDNLKAERERGITIDISLWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTSLA------------KALSEIASTA----------AF--DKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 81 -------ESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKQVIVaVN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLCKPLIVV-LN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 385861629 154 KMDDSTVEYKKERYDEISTEMTRVLTSIGYKQEQfrFIPIS 194
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKTRLKDSP--IIPVS 167
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-156 |
5.03e-18 |
|
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: 81.43 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRKL-AQiektaielgkgafkyafVMDNLKAERERGITID---ISL-WKFESA 83
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSEREMkEQ-----------------VLDSMDLERERGITIKaqaVRLfYKAKDG 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385861629 84 K-YMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRgGFEAgiaeqgQTREHALLAYTLGIKqVIVAVNKMD 156
Cdd:cd01890 65 EeYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQ-GVEA------QTLANFYLALENNLE-IIPVINKID 130
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
234-315 |
5.27e-18 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 78.08 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 234 LRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIpaSDIKRGFV 313
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTGDT 78
|
..
gi 385861629 314 VG 315
Cdd:cd01342 79 LT 80
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-197 |
8.76e-17 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 78.81 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIdKRKLAqiektaielGKgafkyAFVMDNLKAERERGITID---ISL------WK 79
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGII-SEKLA---------GK-----ARYLDTREDEQERGITIKssaISLyfeyeeEK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 80 FESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRggfeaGIAEQGQT--REhallAYTLGIKQVIVaVNKMDD 157
Cdd:cd01885 67 MDGNDYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAVE-----GVCVQTETvlRQ----ALEERVKPVLV-INKIDR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 385861629 158 STVEyKKERYDEISTEMTRV----------LTSIGYKQEQFRFIPISGFV 197
Cdd:cd01885 137 LILE-LKLSPEEAYQRLLRIvedvnaiietYAPEEFKQEKWKFSPQKGNV 185
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
321-426 |
1.01e-16 |
|
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: 75.66 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 321 PPKQCVSFEAQMIISNHPGKIHAGYQPVFDCHTAHIACKFAKLVQRIDRRHGKKVTEEPEWIQKDDAAVVIVEPGKPLVV 400
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*.
gi 385861629 401 EQFQQYPALGRFAVRDMKQTVAVGVI 426
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIV 106
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-308 |
1.31e-16 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 81.99 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRklAQIEktaiELgkgafkyafVMDNLKAERERGITIdisLWKFESAKYMFT 88
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN--QEVA----ER---------VMDSNDLERERGITI---LAKNTAVRYKGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 ---IIDAPGHRDF------IKNMitgtsqADAALLVIDStrggFEagiaeqG---QTR---EHALlayTLGIKqVIVAVN 153
Cdd:COG1217 70 kinIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVVIN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 154 KMD--DSTVEykkERYDEI--------STEmtrvltsigykqEQFRFiPI------SGFVGDNMTDKSANLSwwtggTLL 217
Cdd:COG1217 130 KIDrpDARPD---EVVDEVfdlfielgATD------------EQLDF-PVvyasarNGWASLDLDDPGEDLT-----PLF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 218 DT-LDVLVPPKRPYDKPLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNI-VIAPAGIVTDVKSIEMHHTQ------LPE 289
Cdd:COG1217 189 DTiLEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVaLIKRDGKVEKGKITKLFGFEglerveVEE 268
|
330
....*....|....*....
gi 385861629 290 AVPGDVIGFNvkGIPASDI 308
Cdd:COG1217 269 AEAGDIVAIA--GIEDINI 285
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-226 |
1.37e-16 |
|
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: 77.63 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIyKCGGIDKRKLAQIEKtaielgkgafkyafVMDNLKAERERGITIdisLWKFESAKY--- 85
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALL-KQSGTFRENEEVGER--------------VMDSNDLERERGITI---LAKNTAITYkdt 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 86 MFTIIDAPGHRDF------IKNMitgtsqADAALLVIDSTRGGFEagiaeqgQTR---EHALLAytlGIKqVIVAVNKMD 156
Cdd:cd01891 66 KINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKID 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385861629 157 DStveykKERYDEISTEMTRVLTSIGYKQEQFRFiPI------SGFVGDNMTDKSANLSwwtggTLLDTLDVLVPP 226
Cdd:cd01891 129 RP-----DARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLD-----PLFETIIEHVPA 193
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-175 |
3.16e-16 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 77.66 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIdkRKLAQIEKtaielgKGAFkyafvMDNLKAERERGITIDISLWKFESAKYMFT 88
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAI--RELGSVDK------GTTR-----TDSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 IIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTRE--HALLAYTLgikQVIVAVNKMDDSTVEYKKeR 166
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTRIlfRLLRKLNI---PTIIFVNKIDRAGADLEK-V 136
|
....*....
gi 385861629 167 YDEISTEMT 175
Cdd:cd04168 137 YQEIKEKLS 145
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
14-386 |
3.21e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 80.87 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 14 GHVDAGKSTttghLIYKCGGIDKrklaqiektaielgkgafkyafvmDNLKAERERGITIDI--SLWKFESAKyMFTIID 91
Cdd:PRK10512 7 GHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGR-VLGFID 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREH-ALLAYTlGIKQVIVAVNKMDdsTVEykKERYDEI 170
Cdd:PRK10512 58 VPGHEKFLSNMLAGVGGIDHALLVVACDDG-------VMAQTREHlAILQLT-GNPMLTVALTKAD--RVD--EARIAEV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 171 STEMTRVLTSIGYKQEQFrfipisgFVGDNMTDKSAnlswwtgGTLLDTLDVLVPPKRPYDKPLRLPVQDVFEISGIGTV 250
Cdd:PRK10512 126 RRQVKAVLREYGFAEAKL-------FVTAATEGRGI-------DALREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 251 PSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKG-IPASDIKRgfvvGD--VSRDPP----K 323
Cdd:PRK10512 192 VTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINR----GDwlLADAPPepftR 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385861629 324 QCVSFEAQMIISNhpgkihagYQPVFDCHTA-HIACKFAKLVQRIdrrhGKKVTEEPEWIQKDD 386
Cdd:PRK10512 268 VIVELQTHTPLTQ--------WQPLHIHHAAsHVTGRVSLLEDNL----AELVLDTPLWLADND 319
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-268 |
3.47e-16 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 80.91 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKRKLAQiEKtaielgkgafkyafVMDNLKAERERGITIDISLWKFESAKYMFT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQ-ER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 IIDAPGHRDFIKNMITGTSQADAALLVIDSTRGGFEagiaeqgQTREHALLAYTLGIKQVIVaVNKMDDSTVeykkeRYD 168
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDRPGA-----RPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 169 EISTEMTRVLTSIGYKQEQFRFiPI------SGFVGDNMTDKSANLSwwtggTLLDTLDVLVP-PKRPYDKPLRLPVQDV 241
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQLDF-PIvyasalNGIAGLDHEDMAEDMT-----PLYQAIVDHVPaPDVDLDGPFQMQISQL 212
|
250 260
....*....|....*....|....*..
gi 385861629 242 FEISGIGTVPSGRVESGIMKPAQNIVI 268
Cdd:PRK10218 213 DYNSYVGVIGIGRIKRGKVKPNQQVTI 239
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
236-315 |
3.69e-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: 73.32 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 236 LPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIA--PAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFV 313
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
..
gi 385861629 314 VG 315
Cdd:cd03697 83 LA 84
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
3.71e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 77.68 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIdkRKLAQIEK-TAielgkgafkyafVMDNLKAERERGITIDISL----WKfesa 83
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKI--HKMGEVEDgTT------------VTDWMPQEQERGITIESAAtscdWD---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385861629 84 KYMFTIIDAPGHRDFiknmitgTSQADAALLVIDSTRGGFEAGIAEQGQTREHALLAYTLGIKQVIVaVNKMD 156
Cdd:PRK13351 72 NHRINLIDTPGHIDF-------TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIF-INKMD 136
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
6-156 |
4.56e-15 |
|
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: 77.39 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 6 EHI-NLVVIGHVDAGKSTTTGHLIYKCGGIDKrklaqI----EKTAielgkgafkyafVMDNLKAERERGITIDISL--- 77
Cdd:COG0480 7 EKIrNIGIVAHIDAGKTTLTERILFYTGAIHR-----IgevhDGNT------------VMDWMPEEQERGITITSAAttc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 78 -WKfesaKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTrggfeAGIAEQGQTREHALLAYtlgikQV--IVAVNK 154
Cdd:COG0480 70 eWK----GHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAV-----AGVEPQTETVWRQADKY-----GVprIVFVNK 135
|
..
gi 385861629 155 MD 156
Cdd:COG0480 136 MD 137
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
248-315 |
1.16e-14 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 68.45 E-value: 1.16e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385861629 248 GTVPSGRVESGIMKPAQNIVIAPAG-----IVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFVVG 315
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgkkkIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-181 |
1.65e-14 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 75.86 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIDkrklaqiEKTAielGKGAFkyafvMDNLKAERERGITID---ISL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNA---GDARF-----TDTRADEQERGITIKstgISL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 78 WkFE--------SAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRggfeaGIAEQGQT--REhallAYTLGIKQ 147
Cdd:PTZ00416 78 Y-YEhdledgddKQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVE-----GVCVQTETvlRQ----ALQERIRP 147
|
170 180 190
....*....|....*....|....*....|....
gi 385861629 148 VIVaVNKMDDSTVEYKKErYDEISTEMTRVLTSI 181
Cdd:PTZ00416 148 VLF-INKVDRAILELQLD-PEEIYQNFVKTIENV 179
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-156 |
1.70e-14 |
|
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: 73.40 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 12 VIGHVDAGKSTTTGHLIYKCGGIdkrklaqieKTAIEL-GKGAFKYAfVMDNLKAERERGITIDISLWKFESAKYMFTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385861629 91 DAPGHRDFIKNMITGTSQADAALLVIDSTRgGFEAgiaeqgQTREHALLAYTLGIKqVIVAVNKMD 156
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAK-GVEP------QTRKLFEVCRLRGIP-IITFINKLD 134
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-201 |
1.19e-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: 69.22 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 8 INLVVIGHVDAGKSTTTGHLiykcggidkrklaqiektaielgKGAFKYAFvmdnlKAERERGITI-----DISLWKFES 82
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKAL-----------------------SGVWTVRH-----KEELKRNITIklgyaNAKIYKCPN 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 83 AKY----------------------MFTIIDAPGHRDFIKNMITGTSQADAALLVIDstrgGFEAgiAEQGQTREHALLA 140
Cdd:cd01888 53 CGCprpydtpececpgcggetklvrHVSFVDCPGHEILMATMLSGAAVMDGALLLIA----ANEP--CPQPQTSEHLAAL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385861629 141 YTLGIKQVIVAVNKMDDSTVEYKKERYDEIStemTRVLTSIGykqEQFRFIPISGFVGDNM 201
Cdd:cd01888 127 EIMGLKHIIILQNKIDLVKEEQALENYEQIK---EFVKGTIA---ENAPIIPISAQLKYNI 181
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-156 |
1.35e-13 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 72.85 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 13 IGHVDAGKSTTTGHLIYKCGGIDKrkLAQIE-KTAielgkgafkyafVMDNLKAERERGITIDISLWKFESAKYMFTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHR--IGEVEdGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTRehALLAYT--LGIKqVIVAVNKMD 156
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVP-RIIFVNKMD 123
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
6-156 |
2.42e-13 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 71.97 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 6 EHI-NLVVIGHVDAGKSTTTGHLIYKCGGIDKRKL-AQiektaielgkgafkyafVMDNLKAERERGITID---ISL-WK 79
Cdd:COG0481 4 KNIrNFSIIAHIDHGKSTLADRLLELTGTLSEREMkEQ-----------------VLDSMDLERERGITIKaqaVRLnYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 80 FESAK-YMFTIIDAPGHRDFiknmitgT---SQADAA----LLVIDSTRgGFEAgiaeqgQTREHALLAYTLGIKqVIVA 151
Cdd:COG0481 67 AKDGEtYQLNLIDTPGHVDF-------SyevSRSLAAcegaLLVVDASQ-GVEA------QTLANVYLALENDLE-IIPV 131
|
....*
gi 385861629 152 VNKMD 156
Cdd:COG0481 132 INKID 136
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-156 |
3.45e-13 |
|
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: 69.54 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKrklaqieKTAIELGKGafkyafVMDNLKAERERGITIDISLWKFESAKYMFT 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDR-------LGRVEDGNT------VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385861629 89 IIDAPGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREHALLAYTLGIKQVIVaVNKMD 156
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMD 127
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
233-316 |
5.35e-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: 61.38 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 233 PLRLPVQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGF 312
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 385861629 313 VVGD 316
Cdd:cd16267 81 ILCD 84
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-156 |
2.62e-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: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYKCGGIDKrklaqIEKTAielGKGAfkyafVMDNLKAERERGITID---ISL-WKfesaK 84
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHK-----IGEVH---GGGA-----TMDWMEQERERGITIQsaaTTCfWK----D 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385861629 85 YMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTrggfeAGIAEQGQT--REhallAYTLGIKQvIVAVNKMD 156
Cdd:cd01886 64 HRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAV-----AGVQPQTETvwRQ----ADRYGVPR-IAFVNKMD 127
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-117 |
3.22e-11 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 62.67 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLIYkcggiDKRKlaqiEKTAIELGKGAFKYafvMDNLKAERERGITID---ISLwKFESAK- 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIE-----QTHK----RTPSVKLGWKPLRY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
|
90 100 110
....*....|....*....|....*....|....*
gi 385861629 85 --YMFTIIDAPGHRDFIKNMITGTSQADAALLVID 117
Cdd:cd04167 69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVD 103
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-156 |
7.31e-11 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 64.36 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 1 MGKEKEHINLVVIGHVDAGKSTTTGHLIYKCGGIdkrklaqiektAIELGKGafkyAFVMDNLKAERERGITID---ISL 77
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGII-----------AQEVAGD----VRMTDTRADEAERGITIKstgISL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 78 W---KFESAK----------YMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRggfeaGIAEQGQTrehaLLAYTLG 144
Cdd:PLN00116 78 YyemTDESLKdfkgerdgneYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIE-----GVCVQTET----VLRQALG 148
|
170
....*....|....
gi 385861629 145 --IKQVIVaVNKMD 156
Cdd:PLN00116 149 erIRPVLT-VNKMD 161
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
87-322 |
1.54e-10 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 62.71 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 87 FTIIDAPGHRDFIKNMITGTSQADAALLVIdstrGGFEAgiAEQGQTREHALLAYTLGIKQVIVAVNKMDDSTVEYKKER 166
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLI----AANES--CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 167 YDEIStemTRVLTSIGykqEQFRFIPISGFVGDNMTdksanlswwtggTLLDTLDVLVP-PKRPYDKPLRLPVQDVFEIS 245
Cdd:PTZ00327 193 YEEIR---NFVKGTIA---DNAPIIPISAQLKYNID------------VVLEYICTQIPiPKRDLTSPPRMIVIRSFDVN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 246 G--------IGTVPSGRVESGIMKPAQNIVIAPaGIV--------------TDVKSIEMHHTQLPEAVPGDVIGFNVKGI 303
Cdd:PTZ00327 255 KpgedienlKGGVAGGSILQGVLKVGDEIEIRP-GIIskdsggeftcrpirTRIVSLFAENNELQYAVPGGLIGVGTTID 333
|
250 260
....*....|....*....|..
gi 385861629 304 PA---SDIKRGFVVGDVSRDPP 322
Cdd:PTZ00327 334 PTltrADRLVGQVLGYPGKLPE 355
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
233-313 |
2.23e-10 |
|
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: 56.72 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 233 PLRLPVQDVFeiSGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGF 312
Cdd:cd04089 1 PLRMPILDKY--KDMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 385861629 313 V 313
Cdd:cd04089 79 V 79
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
234-311 |
3.34e-10 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 56.03 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 234 LRLPVQDV----FEISGIgtvpSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMHHTQLPEAVPGDVIGFNVKgiPASDIK 309
Cdd:cd03695 1 FRFPVQYVnrpnLDFRGY----AGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLE--DEIDVS 74
|
..
gi 385861629 310 RG 311
Cdd:cd03695 75 RG 76
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-121 |
2.14e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 59.49 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 3 KEKEHI-NLVVIGHVDAGKSTTTGHLIYKCGGIDKrKLAqiektaielGKgafkyAFVMDNLKAERERGITID---ISLW 78
Cdd:PRK07560 15 KNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMISE-ELA---------GE-----QLALDFDEEEQARGITIKaanVSMV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 385861629 79 -KFESAKYMFTIIDAPGHRDFIKNMITGTSQADAALLVIDSTRG 121
Cdd:PRK07560 80 hEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEG 123
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
238-314 |
3.00e-09 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 53.76 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 238 VQDVFEISGIGTVPSGRVESGIMKPAQNIVIAPAG----IVTDVKSIEMHHTQLPEAVPGDVIGFNVKGIPASDIKRGFV 313
Cdd:cd03694 5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
.
gi 385861629 314 V 314
Cdd:cd03694 85 L 85
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
233-316 |
4.58e-09 |
|
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: 53.27 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 233 PLRLPVQDVFEiSGIGTVPSGRVESGIMKPAQNIVIAPAGIVTDVKSIEMH-HTQLPEAVPGDVIGFNVKGIPASDIKRG 311
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 385861629 312 FVVGD 316
Cdd:cd03698 80 DILSS 84
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
12-203 |
1.19e-08 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 54.02 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 12 VIGHVDAGKSTTtghliykcggIDKrklaqIEKTAIelgkgafkyafvmdnlkAERE-RGIT--IDISLWKFESAKYMFT 88
Cdd:cd01887 5 VMGHVDHGKTTL----------LDK-----IRKTNV-----------------AAGEaGGITqhIGAYQVPIDVKIPGIT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 IIDAPGHRDFiKNMIT-GTSQADAALLVIDSTRgGFEAgiaeqgQTRE---HALLAYTlgikQVIVAVNKMD-DSTVEYK 163
Cdd:cd01887 53 FIDTPGHEAF-TNMRArGASVTDIAILVVAADD-GVMP------QTIEainHAKAANV----PIIVAINKIDkPYGTEAD 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 385861629 164 KERYdeistemTRVLTSIGYKQEQFR----FIPISGFVGDNMTD 203
Cdd:cd01887 121 PERV-------KNELSELGLVGEEWGgdvsIVPISAKTGEGIDD 157
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-203 |
4.56e-08 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 52.37 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 8 INLVVIGHVDAGKSTTTGHLIYKCGGIDKRKlAQIEKTAIELgkgafkyafvmdnlkAERERGITidislwkfesakYMF 87
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYY-PGTTRNYVTT---------------VIEEDGKT------------YKF 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 88 TIIDAPGHRDFIKNMITGTSQADAALLVIDST--RGGFEAGIAEQGQTREHALlayTLGIKqVIVAVNKMDDSTVEYKKE 165
Cdd:TIGR00231 54 NLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVilVLDVEEILEKQTKEIIHHA---DSGVP-IILVGNKIDLKDADLKTH 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 385861629 166 RYDEIStemtrvltsigyKQEQFRFIPISGFVGDNMTD 203
Cdd:TIGR00231 130 VASEFA------------KLNGEPIIPLSAETGKNIDS 155
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
9-182 |
5.30e-08 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 53.45 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 9 NLVVIGHVDAGKSTTTGHLiyKCGGIDK-RKLAQIektaielgkGAFKYafvmdnlKAERERGITIDISL---------- 77
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVL--TQGELDNgRGKARL---------NLFRH-------KHEVESGRTSSVSNdilgfdsdge 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 78 ---WK-----------FESAKYMFTIIDAPGHRDFIKNMITGTS--QADAALLVIDSTRGGfeagiaeQGQTREHALLAY 141
Cdd:cd04165 63 vvnYPdnhlgeldveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 385861629 142 TLGIKqVIVAVNKMD---DSTVEykkerydEISTEMTRVLTSIG 182
Cdd:cd04165 136 ALKVP-VFVVVTKIDmtpANVLQ-------ETLKDLKRLLKSPG 171
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-203 |
4.14e-07 |
|
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: 49.38 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 11 VVIGHVDAGKSTTTGHLIYKcggidkrklaqiektaielgkgafKYAFVmdnlkaERERGITIDISL--WKFESAKYMFT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------EVGEV------SDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 89 IIDAPGHRDFIKNMITGT-----SQADAALLVIDSTRggfeaGIAEQGQTREHALLAYTLGIKqVIVAVNKMDdstveyK 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTD-----RESEEDAKLLILRRLRKEGIP-IILVGNKID------L 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 385861629 164 KERYDEISTEMTRVLtsigYKQEQFRFIPISGFVGDNMTD 203
Cdd:cd00882 119 LEEREVEELLRLEEL----AKILGVPVFEVSAKTGEGVDE 154
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
12-121 |
6.45e-07 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 51.67 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 12 VIGHVDAGKSTTTGHLIYKCGGIdkrKLAQIEKtaielGKGAFKYAfVMDNLKAERERGITIDISLWKFESAKYMFTIID 91
Cdd:PRK00741 15 IISHPDAGKTTLTEKLLLFGGAI---QEAGTVK-----GRKSGRHA-TSDWMEMEKQRGISVTSSVMQFPYRDCLINLLD 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 385861629 92 APGHRDFiknmitgtSQ--------ADAALLVIDSTRG 121
Cdd:PRK00741 86 TPGHEDF--------SEdtyrtltaVDSALMVIDAAKG 115
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
8-156 |
2.43e-05 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 44.59 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 8 INLVVIGHVDAGKSTttghLIYkcggidkrklaqiektaielgkgafkyAFVMDNLKAERE---RGITIDISLWKFESAK 84
Cdd:COG1100 4 KKIVVVGTGGVGKTS----LVN---------------------------RLVGDIFSLEKYlstNGVTIDKKELKLDGLD 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 85 YMFTIIDAPGHRDFIK---NMITGTSQADAALLVIDSTRggfeagiaeqGQTREHALLAYT----LGIK-QVIVAVNKMD 156
Cdd:COG1100 53 VDLVIWDTPGQDEFREtrqFYARQLTGASLYLFVVDGTR----------EETLQSLYELLEslrrLGKKsPIILVLNKID 122
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
238-313 |
7.77e-05 |
|
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: 41.13 E-value: 7.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385861629 238 VQDVFEISGiGTVPSGRVESGIMKPAQNiVIAPAGIVTdVKSIEMHHTQLPEAVPGDVIGFNVKGIPasDIKRGFV 313
Cdd:cd16265 5 VEKVFKILG-RQVLTGEVESGVIYVGYK-VKGDKGVAL-IRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
12-201 |
5.07e-04 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 42.51 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 12 VIGHVDAGKSTttghLIYKcggIDKRKLAQIEKTAIELGKGAFKyafvmdnlkaerergitidiSLWKFESAKYMFTIID 91
Cdd:CHL00189 249 ILGHVDHGKTT----LLDK---IRKTQIAQKEAGGITQKIGAYE--------------------VEFEYKDENQKIVFLD 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385861629 92 APGHRDFIKNMITGTSQADAALLVIDSTRGgfeagiaEQGQTREhallaytlGIKQV-------IVAVNKMD--DSTVEY 162
Cdd:CHL00189 302 TPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE--------AINYIqaanvpiIVAINKIDkaNANTER 366
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 385861629 163 KKE---RYDEISTEMTrvltsigykqEQFRFIPISGFVGDNM 201
Cdd:CHL00189 367 IKQqlaKYNLIPEKWG----------GDTPMIPISASQGTNI 398
|
|
| |
