|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
1-424 |
0e+00 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 892.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141 1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 81 ETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEAGISKEGQTREHALLAFTLGVRQLIVGVNKMDLA-- 158
Cdd:PTZ00141 81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKtv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 159 EYKQKRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQD 238
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 239 VYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAGDSKKD 318
Cdd:PTZ00141 241 VYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKND 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 319 PPAGASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCV 398
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCV 400
|
410 420
....*....|....*....|....*.
gi 508737324 399 EAFTEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:PTZ00141 401 EVFNEYPPLGRFAVRDMKQTVAVGVI 426
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-424 |
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: 688.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256 1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 81 ETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEfeagiskEGQTREHALLAFTLGVRQLIVGVNKMDLAEY 160
Cdd:COG5256 81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 161 KQKRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVY 240
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 241 KIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAGDSKKdPP 320
Cdd:COG5256 234 SISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 321 AGASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCVEA 400
Cdd:COG5256 313 TVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEK 392
|
410 420
....*....|....*....|....
gi 508737324 401 FTEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:COG5256 393 FKEFPQLGRFAIRDMGQTVAAGVV 416
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
3-424 |
0e+00 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 683.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 3 KEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 83 SKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEfeagiSKEGQTREHALLAFTLGVRQLIVGVNKMDLAEYKQ 162
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG-----GVMPQTREHVFLARTLGINQLIVAINKMDAVNYDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 163 KRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVYKI 242
Cdd:PRK12317 157 KRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYSI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 243 GGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAGdSKKDPPAG 322
Cdd:PRK12317 237 SGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 323 ASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCVEAFT 402
Cdd:PRK12317 316 AEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVK 395
|
410 420
....*....|....*....|..
gi 508737324 403 EYPPLGRFAVRDMRQTVAVGVI 424
Cdd:PRK12317 396 EIPQLGRFAIRDMGQTIAAGMV 417
|
|
| EF-1_alpha |
TIGR00483 |
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ... |
1-424 |
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: 678.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483 1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 81 ETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagisKEGQTREHALLAFTLGVRQLIVGVNKMDLAEY 160
Cdd:TIGR00483 81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 161 KQKRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVY 240
Cdd:TIGR00483 157 DEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQDVY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 241 KIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAGDSkKDPP 320
Cdd:TIGR00483 237 SITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHP-DNPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 321 AGASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCVEA 400
Cdd:TIGR00483 316 KVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEA 395
|
410 420
....*....|....*....|....
gi 508737324 401 FTEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:TIGR00483 396 VKEIPPLGRFAIRDMGQTVAAGMI 419
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
1-424 |
0e+00 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 669.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043 1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 81 ETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEAGISKEGQTREHALLAFTLGVRQLIVGVNKMDLA-- 158
Cdd:PLN00043 81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 159 EYKQKRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQD 238
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 239 VYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAGDSKKD 318
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 319 PPAGASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCV 398
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVV 400
|
410 420
....*....|....*....|....*.
gi 508737324 399 EAFTEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:PLN00043 401 ETFSEYPPLGRFAVRDMRQTVAVGVI 426
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
9-224 |
4.50e-155 |
|
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: 437.69 E-value: 4.50e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKFETSKYSFT 88
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 89 IIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEAGISKEGQTREHALLAFTLGVRQLIVGVNKMDL--AEYKQKRYK 166
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDvtVNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 508737324 167 EIKKEISKTIKKIGYNPDKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPP 224
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPP 218
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-424 |
2.41e-106 |
|
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: 321.27 E-value: 2.41e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 4 EKTHVNIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEANDIGKGSFKYAWVLDKLKAERERGITIDIALWKFE 81
Cdd:COG2895 14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 82 TSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEYK 161
Cdd:COG2895 92 TPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 162 QKRYKEIKKEISKTIKKIGYNPdkVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVYK 241
Cdd:COG2895 165 EEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 242 iggigtvP-------VGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGF----NIknvsvkDIRRGN 310
Cdd:COG2895 243 -------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtledEI------DISRGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 311 VAGDSkKDPPAGASSFFAQVIVLN-HPGTISNGYtpVLDCHTAHIACKFTEIVTKIDRRSgkvLEELP-KSVKTGDAAMV 388
Cdd:COG2895 310 VIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNT---LEHEAaDSLELNDIGRV 383
|
410 420 430
....*....|....*....|....*....|....*...
gi 508737324 389 TLTPSKPMCVEAFTEYPPLGRFAV--RDMRQTVAVGVI 424
Cdd:COG2895 384 TLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMI 421
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
5-224 |
6.68e-79 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 242.43 E-value: 6.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 5 KTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAndigkgsfkyawVLDKLKAERERGITIDIALWKFETSK 84
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTREHALLAFTLGVRqLIVGVNKMDLAEykQKR 164
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRVD--GAE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508737324 165 YKEIKKEIS-KTIKKIGYNPDKVPFVPISGFHGDNMieagdnmswykgPTLLGALDSMEPP 224
Cdd:pfam00009 139 LEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------QTLLDALDEYLPS 187
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
9-224 |
3.72e-72 |
|
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: 225.91 E-value: 3.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEK-EANDIGKGSFKYAWVLDKLKAERERGITIDIALWKFETSKYSF 87
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERsKSSGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 88 TIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEYKQKRYKE 167
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 508737324 168 IKKEISKTIKKIGYNPdkVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPP 224
Cdd:cd04166 154 IKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIA 208
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
14-424 |
2.72e-71 |
|
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: 230.34 E-value: 2.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIGK--GSFKYAWVLDKLKAERERGITIDIALWKFETSKYSFTIID 91
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 92 APGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEYKQKRYKEIKKE 171
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 172 ISKTIKKIGYNPdkVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVYKI-----GGIG 246
Cdd:TIGR02034 160 YLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 247 TVPVGRVetgvlKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSvkDIRRGN--VAGDSkkdPPAGAS 324
Cdd:TIGR02034 238 TIASGSV-----HVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDllAAADS---APEVAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 325 SFFAQVIVLNHPgTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEElpKSVKTGDAAMVTLTPSKPMCVEAFTEY 404
Cdd:TIGR02034 308 QFAATLVWMAEE-PLLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA--KSLELNEIGRVNLSLDEPIAFDPYAEN 384
|
410 420
....*....|....*....|..
gi 508737324 405 PPLGRFAV--RDMRQTVAVGVI 424
Cdd:TIGR02034 385 RTTGAFILidRLSNRTVGAGMI 406
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
14-424 |
2.35e-68 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 228.66 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEANDIG--KGSFKYAWVLDKLKAERERGITIDIALWKFETSKYSFTIID 91
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 92 APGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEYKQKRYKEIKKE 171
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 172 ISKTIKKIGYNpdKVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVYKI-----GGIG 246
Cdd:PRK05506 184 YRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 247 TvpvgrVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSvkDIRRGN--VAGDskkDPPAGAS 324
Cdd:PRK05506 262 T-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADEI--DISRGDmlARAD---NRPEVAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 325 SFFAQVIVLN----HPGtisNGYtpVLDCHTAHIACKFTEIVTKIDRRSgkvLEELP-KSVKTGDAAMVTLTPSKPMCVE 399
Cdd:PRK05506 332 QFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAaKTLELNEIGRCNLSTDAPIAFD 403
|
410 420
....*....|....*....|....*..
gi 508737324 400 AFTEYPPLGRFAV--RDMRQTVAVGVI 424
Cdd:PRK05506 404 PYARNRTTGSFILidRLTNATVGAGMI 430
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
321-424 |
3.30e-66 |
|
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: 206.66 E-value: 3.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 321 AGASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCVEA 400
Cdd:cd03705 1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
|
90 100
....*....|....*....|....
gi 508737324 401 FTEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:cd03705 81 FSEYPPLGRFAVRDMRQTVAVGVI 104
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
14-424 |
2.76e-62 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 208.61 E-value: 2.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 14 GHVDSGKSTTTGHLIYkcggiDKRTIekFEKEANDIGKGSFK---------YAWVLDKLKAERERGITIDIALWKFETSK 84
Cdd:PRK05124 34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEYKQKR 164
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 165 YKEIKKEISKTIKKIGYNPDkVPFVPISGFHGDNMIEAGDNMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVYKI-- 242
Cdd:PRK05124 180 FERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 243 ---GGIGTvpvgrVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSvkDIRRGNVAGDSKKDP 319
Cdd:PRK05124 259 dfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--DISRGDLLVAADEAL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 320 PAGaSSFFAQVIVLN-HPGTISNGYtpvldchTAHIACKFT-----EIVTKIDRRSGK--VLEELPksvkTGDAAMVTLT 391
Cdd:PRK05124 332 QAV-QHASADVVWMAeQPLQPGQSY-------DIKIAGKKTrarvdAIRYQVDINTLTqrEAENLP----LNGIGLVELT 399
|
410 420 430
....*....|....*....|....*....|....*
gi 508737324 392 PSKPMCVEAFTEYPPLGRFAV--RDMRQTVAVGVI 424
Cdd:PRK05124 400 FDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMV 434
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
1-424 |
1.55e-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: 201.92 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKE-----KTHVNIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKfekeandiGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050 1 MAKEkfertKPHVNIGTIGHVDHGKTTLTA-------AITKVLAKK--------GGAKAKAYDQIDKAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 76 ALWKFETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKM 155
Cdd:COG0050 66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 156 DLAEykqkrYKE----IKKEISKTIKKIGYNPDKVPFVPISGFhgdNMIEAGDNMSWYKGPT-LLGALDSMEP-PTRPVD 229
Cdd:COG0050 139 DMVD-----DEEllelVEMEVRELLSKYGFPGDDTPIIRGSAL---KALEGDPDPEWEKKILeLMDAVDSYIPePERDTD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 230 KPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPPMISTeVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDI 306
Cdd:COG0050 211 KPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDTQKTV-VTGVEMFRKLLDEGEAGDNVGLLLRGIKREDV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 307 RRGNVAGDSKKDPPagASSFFAQVIVLN-------HPgtISNGYTPVLDCHTAHiackfteiVTkidrrsGKVleELPKS 379
Cdd:COG0050 290 ERGQVLAKPGSITP--HTKFEAEVYVLSkeeggrhTP--FFNGYRPQFYFRTTD--------VT------GVI--TLPEG 349
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 508737324 380 VKT---GDAAMVTLTPSKPMCVEAFTeypplgRFAVRDMRQTVAVGVI 424
Cdd:COG0050 350 VEMvmpGDNVTMTVELITPIAMEEGL------RFAIREGGRTVGAGVV 391
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
228-318 |
4.08e-59 |
|
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: 188.17 E-value: 4.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 228 VDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIR 307
Cdd:cd03693 1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|.
gi 508737324 308 RGNVAGDSKKD 318
Cdd:cd03693 81 RGDVAGDSKND 91
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
1-424 |
2.45e-58 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 196.32 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKE-----KTHVNIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEANDigkgsfkYAWVlDKLKAERERGITIDI 75
Cdd:PRK12736 1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTA-------AITKVLAERGLNQAKD-------YDSI-DAAPEEKERGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 76 ALWKFETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKM 155
Cdd:PRK12736 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 156 DLAEyKQKRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGDNmieaGDNmSWYKG-PTLLGALDSMEP-PTRPVDKPLR 233
Cdd:PRK12736 139 DLVD-DEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALE----GDP-KWEDAiMELMDAVDEYIPtPERDTDKPFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 234 LPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPPMISTeVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGN 310
Cdd:PRK12736 213 MPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKETQKTV-VTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 311 VAGDSKKDPPagASSFFAQVIVLN------HPGTISNgYTPVLDCHTahiackfTEIVTKIDrrsgkvLEELPKSVKTGD 384
Cdd:PRK12736 292 VLAKPGSIKP--HTKFKAEVYILTkeeggrHTPFFNN-YRPQFYFRT-------TDVTGSIE------LPEGTEMVMPGD 355
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 508737324 385 AAMVTLTPSKPMCVEAFTeypplgRFAVRDMRQTVAVGVI 424
Cdd:PRK12736 356 NVTITVELIHPIAMEQGL------KFAIREGGRTVGAGTV 389
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
1-311 |
2.27e-57 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 193.87 E-value: 2.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKE-----KTHVNIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAndigkgsFKYAWVlDKLKAERERGITIDI 75
Cdd:PRK00049 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGAEA-------KAYDQI-DKAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 76 ALWKFETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKM 155
Cdd:PRK00049 66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 156 DLAEykqkrYKEI----KKEISKTIKKIGYNPDKVPFVPISGFHGdnmIEAGDNMSWYKG-PTLLGALDSMEP-PTRPVD 229
Cdd:PRK00049 139 DMVD-----DEELlelvEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLELMDAVDSYIPtPERAID 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 230 KPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPPMiSTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDI 306
Cdd:PRK00049 211 KPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQ-KTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDV 289
|
....*
gi 508737324 307 RRGNV 311
Cdd:PRK00049 290 ERGQV 294
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-424 |
8.98e-57 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 194.45 E-value: 8.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 3 KEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeandigkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126 77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 83 SKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEyKQ 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 163 KRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHG------DNMIEAGDNMSWYKGPTLLGALDSMEP-PTRPVDKPLRLP 235
Cdd:PLN03126 214 ELLELVELEVRELLSSYEFPGDDIPIISGSALLAlealmeNPNIKRGDNKWVDKIYELMDAVDSYIPiPQRQTDLPFLLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 236 LQDVYKIGGIGTVPVGRVETGVLKPGMVVTFA--PPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAg 313
Cdd:PLN03126 294 VEDVFSITGRGTVATGRVERGTVKVGETVDIVglRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 314 dSKKDPPAGASSFFAQVIVLNHP--GTIS---NGYTPVLDCHTAHIACKFTEIVTKIDRRSgkvleelpKSVKTGDAAMV 388
Cdd:PLN03126 373 -AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------KMVMPGDRVKM 443
|
410 420 430
....*....|....*....|....*....|....*.
gi 508737324 389 TLTPSKPMCVEAFTeypplgRFAVRDMRQTVAVGVI 424
Cdd:PLN03126 444 VVELIVPVACEQGM------RFAIREGGKTVGAGVI 473
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
9-224 |
2.73e-56 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 184.04 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeandigkgsfkyaWVLDKLKAERERGITIDIALWKFETSKYSFT 88
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 89 IIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEfeagiskEGQTREHALLAFtLGVRQLIVGVNKMDLAeyKQKRYKEI 168
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV--GEEDFDEV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 508737324 169 KKEISKTIKKIGY---NPDKVPFVPISGFHGDNMieagdnmswykgPTLLGALDSMEPP 224
Cdd:cd00881 136 LREIKELLKLIGFtflKGKDVPIIPISALTGEGI------------EELLDAIVEHLPP 182
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-424 |
3.63e-56 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 190.94 E-value: 3.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 3 KEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEkeanDIgkgsfkyawvlDKLKAERERGITIDIALWKFET 82
Cdd:CHL00071 8 RKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYD----EI-----------DSAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 83 SKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEyKQ 162
Cdd:CHL00071 73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD-DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 163 KRYKEIKKEISKTIKKIGYNPDKVPFVPISG------FHGDNMIEAGDNMSWYKGPTLLGALDSMEP-PTRPVDKPLRLP 235
Cdd:CHL00071 145 ELLELVELEVRELLSKYDFPGDDIPIVSGSAllaleaLTENPKIKRGENKWVDKIYNLMDAVDSYIPtPERDTDKPFLMA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 236 LQDVYKIGGIGTVPVGRVETGVLKPGMVVTFA--PPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAG 313
Cdd:CHL00071 225 IEDVFSITGRGTVATGRIERGTVKVGDTVEIVglRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 314 DSKKDPPagASSFFAQVIVLN------HPGTISnGYTPVLDCHTAHIACKFTEIVTkiDRRSGKvleelpKSVKTGDAAM 387
Cdd:CHL00071 305 KPGTITP--HTKFEAQVYILTkeeggrHTPFFP-GYRPQFYVRTTDVTGKIESFTA--DDGSKT------EMVMPGDRIK 373
|
410 420 430
....*....|....*....|....*....|....*..
gi 508737324 388 VTLTPSKPMCVEAFTeypplgRFAVRDMRQTVAVGVI 424
Cdd:CHL00071 374 MTVELIYPIAIEKGM------RFAIREGGRTVGAGVV 404
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
1-311 |
7.06e-55 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 187.35 E-value: 7.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKE-----KTHVNIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEANDIGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735 1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 76 ALWKFETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKM 155
Cdd:PRK12735 66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 156 DLAEyKQKRYKEIKKEISKTIKKIGYNPDKVPFVPISGFHGdnmIEAGDNMSWYKG-PTLLGALDSMEP-PTRPVDKPLR 233
Cdd:PRK12735 139 DMVD-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLELMDAVDSYIPePERAIDKPFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 234 LPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPPMISTeVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGN 310
Cdd:PRK12735 215 MPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQ 293
|
.
gi 508737324 311 V 311
Cdd:PRK12735 294 V 294
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-424 |
4.39e-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: 182.28 E-value: 4.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 3 KEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeandigkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:TIGR00485 8 RTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQ---------------IDNAPEEKARGITINTAHVEYET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 83 SKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEyKQ 162
Cdd:TIGR00485 73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD-DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 163 KRYKEIKKEISKTIKKIGYNPDKVPFV---PISGFHGDNMIEAgdnmswyKGPTLLGALDSMEP-PTRPVDKPLRLPLQD 238
Cdd:TIGR00485 145 ELLELVEMEVRELLSQYDFPGDDTPIIrgsALKALEGDAEWEA-------KILELMDAVDEYIPtPEREIDKPFLLPIED 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 239 VYKIGGIGTVPVGRVETGVLKPGMVVTFA--PPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAGDSK 316
Cdd:TIGR00485 218 VFSITGRGTVVTGRVERGIIKVGEEVEIVglKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 317 KDPPagASSFFAQVIVLN------HPGTISnGYTPVLDCHTAHIackfteivtkidrrSGKVleELPKSVKT---GDAAM 387
Cdd:TIGR00485 298 SIKP--HTKFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDV--------------TGTI--ELPEGVEMvmpGDNVK 358
|
410 420 430
....*....|....*....|....*....|....*..
gi 508737324 388 VTLTPSKPMCVEAFTeypplgRFAVRDMRQTVAVGVI 424
Cdd:TIGR00485 359 MTVELISPIALEQGM------RFAIREGGRTVGAGVV 389
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-424 |
4.49e-53 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 183.87 E-value: 4.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 3 KEKTHVNIVVIGHVDSGKSTTTGhliykcggidkrTIEKFEKEANDIGKGSFKYawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127 57 RTKPHVNVGTIGHVDHGKTTLTA------------AITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYET 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 83 SKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEYKQ 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 163 kRYKEIKKEISKTIKKIGYNPDKVPFVPISGFH---GDNMiEAGDNmswyKGPTLLGALDSMEP-PTRPVDKPLRLPLQD 238
Cdd:PLN03127 195 -LLELVEMELRELLSFYKFPGDEIPIIRGSALSalqGTND-EIGKN----AILKLMDAVDEYIPePVRVLDKPFLMPIED 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 239 VYKIGGIGTVPVGRVETGVLKPG---MVVTFAP-PMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAgd 314
Cdd:PLN03127 269 VFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVI-- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 315 SKKDPPAGASSFFAQVIVLN------HPGTISNgYTPVLDCHTAHIackfteivtkidrrSGKVleELPKSVKT---GDA 385
Cdd:PLN03127 347 CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADV--------------TGKV--ELPEGVKMvmpGDN 409
|
410 420 430
....*....|....*....|....*....|....*....
gi 508737324 386 AMVTLTPSKPMCVEafteypPLGRFAVRDMRQTVAVGVI 424
Cdd:PLN03127 410 VTAVFELISPVPLE------PGQRFALREGGRTVGAGVV 442
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-424 |
5.93e-48 |
|
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: 173.56 E-value: 5.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 8 VNIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeandigkgsfkyawvlDKLKAERERGITIDI--ALWKFEtSKY 85
Cdd:COG3276 1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLgfAYLPLP-DGR 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 86 SFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAgqgefeagisKEG---QTREH-ALLAFtLGVRQLIVGVNKMDLAEyk 161
Cdd:COG3276 52 RLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA----------DEGvmpQTREHlAILDL-LGIKRGIVVLTKADLVD-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 162 QKRYKEIKKEISKTIKkiGYNPDKVPFVPISGFHGDNmIEAgdnmswykgptLLGALDSM--EPPTRPVDKPLRLPLQDV 239
Cdd:COG3276 119 EEWLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEG-IDE-----------LRAALDALaaAVPARDADGPFRLPIDRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 240 YKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNVAgdSKKDP 319
Cdd:COG3276 185 FSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVL--AAPGA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 320 PAGASSFFAQVIVLNH-PGTISNGyTPVLdCH--TAHIACKfteiVTKIDRrsgkvlEELPKsvktGDAAMVTLTPSKPM 396
Cdd:COG3276 263 LRPTDRIDVRLRLLPSaPRPLKHW-QRVH-LHhgTAEVLAR----VVLLDR------EELAP----GEEALAQLRLEEPL 326
|
410 420 430
....*....|....*....|....*....|.
gi 508737324 397 CVEAfteypplG-RFAVRDM--RQTVAVGVI 424
Cdd:COG3276 327 VAAR-------GdRFILRDYspRRTIGGGRV 350
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-224 |
8.53e-37 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 133.48 E-value: 8.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 6 THVNIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEkeanDIgkgsfkyawvlDKLKAERERGITIDIALWKFETSKY 85
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYD----EI-----------DKAPEEKARGITINTAHVEYETANR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 86 SFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEyKQKRY 165
Cdd:cd01884 66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 166 KEIKKEISKTIKKIGYNPDKVPFVPISGFhgdNMIEAGDNMSWYKG-PTLLGALDSMEPP 224
Cdd:cd01884 138 ELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVDKiLELLDALDSYIPT 194
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-309 |
6.76e-33 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 130.76 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 8 VNIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeandigkgsfkyawvlDKLKAERERGITIDIALWKFETSKYSF 87
Cdd:TIGR00475 1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 88 TIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTREHALLAFTLGVRQLIVGVNKMDLAEykQKRYKE 167
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEG-------VMTQTGEHLAVLDLLGIPHTIVVITKADRVN--EEEIKR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 168 IKKEISKTIKKIGYNPDKVPFVpISGFHGDNMIEAGDNmswykgptLLGALDSMEppTRPVDKPLRLPLQDVYKIGGIGT 247
Cdd:TIGR00475 124 TEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKE--------LKNLLESLD--IKRIQKPLRMAIDRAFKVKGAGT 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 508737324 248 VPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRG 309
Cdd:TIGR00475 193 VVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRG 254
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
319-424 |
1.26e-31 |
|
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: 116.60 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 319 PPAGASSFFAQVIVLNH-----PGTISNGYTPVLDCHTAHIACKFTEIVTKIDrrSGKVLEElPKSVKTGDAAMVTLTPS 393
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|.
gi 508737324 394 KPMCVEAFTeypplgRFAVRDMRQTVAVGVI 424
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVV 102
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
325-424 |
6.46e-27 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 103.63 E-value: 6.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 325 SFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKvlEELPKSVKTGDAAMVTLTPSKPMCVEAFTEY 404
Cdd:cd01513 5 KFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGKEF 82
|
90 100
....*....|....*....|
gi 508737324 405 PPLGRFAVRDMRQTVAVGVI 424
Cdd:cd01513 83 PTLGRFALRDGGRTVGAGLI 102
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-227 |
3.50e-25 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 101.14 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeandigkgsfkyawvlDKLKAERERGITIDI--ALWKFETSKySF 87
Cdd:cd04171 2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGK-RL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 88 TIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVGVNKMDLAEykQKRYKE 167
Cdd:cd04171 53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKADLVD--EDRLEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 168 IKKEISKTIKKIGYNPdkVPFVPISGFHGDNmIEAgdnmswykgptLLGALDSMEPPTRP 227
Cdd:cd04171 124 VEEEILELLAGTFLAD--APIFPVSSVTGEG-IEE-----------LKNYLDELAEPQSK 169
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-320 |
2.60e-22 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 98.39 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 8 VNIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeandigkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:PRK04000 10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKCPD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 83 S-----------------------KYSFtiIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagiSKEGQTREHaLL 139
Cdd:PRK04000 62 CeepeayttepkcpncgsetellrRVSF--VDAPGHETLMATMLSGAALMDGAILVIAANEP------CPQPQTKEH-LM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 140 AFT-LGVRQLIVGVNKMDLAEYKQ--KRYKEIKKEISKTIkkigynPDKVPFVPISGFHGDNmIEAgdnmswykgptLLG 216
Cdd:PRK04000 133 ALDiIGIKNIVIVQNKIDLVSKERalENYEQIKEFVKGTV------AENAPIIPVSALHKVN-IDA-----------LIE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 217 ALDS-MEPPTRPVDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKPGMVVT------FAPpmIST 273
Cdd:PRK04000 195 AIEEeIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEeggktkWEP--ITT 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 508737324 274 EVKSVEMHHQALEEAIPGDNVGFNIK---NVSVKDIRRGNVAGDSKKDPP 320
Cdd:PRK04000 273 KIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPP 322
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
323-424 |
6.23e-22 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 294003 [Multi-domain] Cd Length: 108 Bit Score: 89.92 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 323 ASSFFAQVIVLNHPGTI-SNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCVEAF 401
Cdd:cd03704 3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETF 82
|
90 100
....*....|....*....|...
gi 508737324 402 TEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:cd03704 83 KDFPQLGRFTLRDEGKTIAIGKV 105
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
232-311 |
3.35e-19 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 81.54 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNvsVKDIRRGNV 311
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-192 |
9.26e-19 |
|
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: 83.95 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 8 VNIVVIGHVDSGKSTttghliykcggIDKRTIEKFEKEAndigkgsfkyawvLDKLKAERERGITIDIALWKF------- 80
Cdd:cd01889 1 VNVGLLGHVDSGKTS-----------LAKALSEIASTAA-------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 81 -------ETSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTREHALLAFTLGVRqLIVGVN 153
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLCKP-LIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 508737324 154 KMDLAEYKQKRYKE--IKKEISKTIKKIgyNPDKVPFVPIS 192
Cdd:cd01889 129 KIDLIPEEERKRKIekMKKRLQKTLEKT--RLKDSPIIPVS 167
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
319-424 |
1.05e-18 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 81.05 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 319 PPAGASSFFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRRSGKVLEELPKSVKTGDAAMVTLTPSKPMCV 398
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*.
gi 508737324 399 EAFTEYPPLGRFAVRDMRQTVAVGVI 424
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIV 106
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-189 |
2.18e-17 |
|
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: 79.50 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeandigkgsfKYAWVLDKLKAERERGITID---IAL-WKFETSK 84
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSERE----------------MKEQVLDSMDLERERGITIKaqaVRLfYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 -YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTREHALLAFTLGVRQLIVgVNKMDLaeyKQK 163
Cdd:cd01890 66 eYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDATQG-------VEAQTLANFYLALENNLEIIPV-INKIDL---PAA 134
|
170 180
....*....|....*....|....*.
gi 508737324 164 RYKEIKKEISKTikkIGYNPDKVPFV 189
Cdd:cd01890 135 DPDRVKQEIEDV---LGLDASEAILV 157
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-310 |
4.82e-17 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 83.56 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeandigkgsfkyawvlDKLKAERERGITIDI--ALWKFETSKySF 87
Cdd:PRK10512 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGR-VL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 88 TIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFeagiskeGQTREH-ALLAFTlGVRQLIVGVNKMDLAEykQKRYK 166
Cdd:PRK10512 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVD--EARIA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 167 EIKKEISKTIKKIGYnpDKVPFVPISGFHGDNmIEAgdnmswykgptLLGALDSMEPPTRPVDKPLRLPLQDVYKIGGIG 246
Cdd:PRK10512 124 EVRRQVKAVLREYGF--AEAKLFVTAATEGRG-IDA-----------LREHLLQLPEREHAAQHRFRLAIDRAFTVKGAG 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508737324 247 TVPVGRVETGVLKPG--MVVTFA-PPMistEVKSVEMHHQALEEAIPGDNVGFNIK-NVSVKDIRRGN 310
Cdd:PRK10512 190 LVVTGTALSGEVKVGdtLWLTGVnKPM---RVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINRGD 254
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
9-202 |
7.25e-17 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 79.59 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaNDIGKGSFKyawvLDKLKAERERGITIDIALWKFETSKYSFT 88
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIREL---------GSVDKGTTR----TDSMELERQRGITIFSAVASFQWEDTKVN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 89 IIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTRehaLLAFTLgvRQL----IVGVNKMDLAEY-KQK 163
Cdd:cd04168 68 IIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKIDRAGAdLEK 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 508737324 164 RYKEIKKEISKTIkKIGYNPDKVPFVPISGFHGDNMIEA 202
Cdd:cd04168 136 VYQEIKEKLSPDI-VPMQKVGLYPNICDTNNIDDEQIET 173
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
234-311 |
8.00e-17 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 75.25 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 234 LPLQDVYKIGGIGTVPVGRVETGVLKPGM---VVTFAPPMISTeVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGN 310
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKETLKTT-VTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81
|
.
gi 508737324 311 V 311
Cdd:cd03697 82 V 82
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
9-309 |
9.29e-16 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 79.29 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEkfekeandigkgsfkyAWVLDKLKAERERGITID---IAL-WKFETSK 84
Cdd:COG0481 8 NFSIIAHIDHGKSTLADRLLELTGTLSEREMK----------------EQVLDSMDLERERGITIKaqaVRLnYKAKDGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 -YSFTIIDAPGHRDFiknmiT-----------GtsqadiAVLIVAAGQGeFEAgiskegQTREHALLAFTLGVRQLIVgV 152
Cdd:COG0481 72 tYQLNLIDTPGHVDF-----SyevsrslaaceG------ALLVVDASQG-VEA------QTLANVYLALENDLEIIPV-I 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 153 NKMDLAeykQKRYKEIKKEISKTikkIGYNPDKVpfVPISGFHGDNMIEagdnmswykgptLLGAL-DSMEPPTRPVDKP 231
Cdd:COG0481 133 NKIDLP---SADPERVKQEIEDI---IGIDASDA--ILVSAKTGIGIEE------------ILEAIvERIPPPKGDPDAP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 232 LRlPL-----QDVYKiggiGTVPVGRVETGVLKPGMVVTfappMIST----EVKSV---EMHHQALEEAIPGDnVGF--- 296
Cdd:COG0481 193 LQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIK----MMSTgkeyEVDEVgvfTPKMTPVDELSAGE-VGYiia 262
|
330
....*....|...
gi 508737324 297 NIKNvsVKDIRRG 309
Cdd:COG0481 263 GIKD--VRDARVG 273
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
232-311 |
8.94e-15 |
|
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: 69.09 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNV 311
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
246-311 |
1.06e-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: 68.83 E-value: 1.06e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508737324 246 GTVPVGRVETGVLKPGMVVTFAPP-----MISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNV 311
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
9-277 |
5.05e-14 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 73.97 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKeandigkgsfkyawVLDKLKAERERGITIDIALWKFETSKYSFT 88
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 89 IIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGEFEagiskegQTREHALLAFTLGVRQLIVgVNKMD----LAEYKQKR 164
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDrpgaRPDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 165 YKEIKKEISKTIKKIGYnpdkvPFVPISGFHGDNMIEAGDnMSWYKGPTLLGALDSMEPPTRPVDKPLRLPLQDVYKIGG 244
Cdd:PRK10218 144 VFDLFVNLDATDEQLDF-----PIVYASALNGIAGLDHED-MAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSY 217
|
250 260 270
....*....|....*....|....*....|...
gi 508737324 245 IGTVPVGRVETGVLKPGMVVTfappMISTEVKS 277
Cdd:PRK10218 218 VGVIGIGRIKRGKVKPNQQVT----IIDSEGKT 246
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
9-156 |
8.18e-14 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 73.54 E-value: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtiekfekeandIGK---GSFkyawVLDKLKAERERGITIDIALWKFETSKY 85
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHR------------IGEvhdGNT----VMDWMPEEQERGITITSAATTCEWKGH 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508737324 86 SFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTrEHALlaftlgvRQL-------IVGVNKMD 156
Cdd:COG0480 75 KINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQT-ETVW-------RQAdkygvprIVFVNKMD 137
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-193 |
2.05e-13 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 69.18 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIekfekeandigkGSFKYawvLDKLKAERERGITID---IALwKFETSK- 84
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSLLASAGIISEKLA------------GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 ------YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAgqgefeagisKEG---QTreHALL--AFTLGVRQLIVgVN 153
Cdd:cd01885 66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----------VEGvcvQT--ETVLrqALEERVKPVLV-IN 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 508737324 154 KMD--LAEYK------QKRYKEIKKEISKTIKKIG---YNPDKVPFVPISG 193
Cdd:cd01885 133 KIDrlILELKlspeeaYQRLLRIVEDVNAIIETYApeeFKQEKWKFSPQKG 183
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
9-156 |
6.24e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 70.75 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaNDIGKGSFkyawVLDKLKAERERGITIDIAL----WKfetsK 84
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKM---------GEVEDGTT----VTDWMPQEQERGITIESAAtscdWD----N 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 508737324 85 YSFTIIDAPGHRDFIKNMITGTSQADIAVLIvaagqgeFEAGISKEGQTREHALLAFTLGVRQLIVgVNKMD 156
Cdd:PRK13351 73 HRINLIDTPGHIDFTGEVERSLRVLDGAVVV-------FDAVTGVQPQTETVWRQADRYGIPRLIF-INKMD 136
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
231-314 |
2.77e-12 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 62.15 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 231 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGN 310
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 508737324 311 VAGD 314
Cdd:cd16267 81 ILCD 84
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
13-156 |
2.92e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 68.61 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAndigkgsfkyawVLDKLKAERERGITIDIALWKFETSKYSFTIID 91
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 508737324 92 APGHRDFIKNMITGTSQADIAVLIVAAgqgefEAGIskEGQTRehALLAFT--LGVRQLIVgVNKMD 156
Cdd:PRK12740 67 TPGHVDFTGEVERALRVLDGAVVVVCA-----VGGV--EPQTE--TVWRQAekYGVPRIIF-VNKMD 123
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
9-158 |
3.14e-12 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 66.46 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaNDIGKGSFkyawVLDKLKAERERGITIDIALWKFETSKYSFT 88
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRL---------GRVEDGNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 89 IIDAPGHRDFIKNMITGTSQADIAVLIVAAgqgefEAGIskEGQTREHALLAFTLGVRQLIVgVNKMDLA 158
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGV--EVGTEKVWEFLDDAKLPRIIF-INKMDRA 129
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
9-98 |
8.73e-12 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 65.21 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKEAndigkgsfkyawVLDKLKAERERGITIDIALWKFETSKYSFT 88
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIG-EVHGGGA------------TMDWMEQERERGITIQSAATTCFWKDHRIN 67
|
90
....*....|
gi 508737324 89 IIDAPGHRDF 98
Cdd:cd01886 68 IIDTPGHVDF 77
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
10-199 |
4.01e-11 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 61.33 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeandigkgsfkyawVLDKLK----AERE-RGITIDIALWKFETSK 84
Cdd:cd01887 3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 Y--SFTIIDAPGHRDFiKNMIT-GTSQADIAVLIVAAGQGeFEAgiskegQTRE---HALLAFTlgvrQLIVGVNKMDLA 158
Cdd:cd01887 47 KipGITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKIDKP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 508737324 159 EYKQKRYKEIKKEISktikKIGYNPD----KVPFVPISGFHGDNM 199
Cdd:cd01887 115 YGTEADPERVKNELS----ELGLVGEewggDVSIVPISAKTGEGI 155
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
231-311 |
6.00e-11 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 58.27 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 231 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGN 310
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78
|
.
gi 508737324 311 V 311
Cdd:cd04089 79 V 79
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
8-320 |
9.31e-11 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 63.48 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 8 VNIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeandigkgsfkyawvldKLKAERERGITIDIA-----LWKFE- 81
Cdd:PTZ00327 35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLGyanakIYKCPk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 82 ---------------------------TSKYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagiSKEGQTR 134
Cdd:PTZ00327 87 cprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQPQTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 135 EHALLAFTLGVRQLIVGVNKMDLA--EYKQKRYKEIKKEISKTIKkigynpDKVPFVPISGFHGDNMieagDNMSWYkgp 212
Cdd:PTZ00327 161 EHLAAVEIMKLKHIIILQNKIDLVkeAQAQDQYEEIRNFVKGTIA------DNAPIIPISAQLKYNI----DVVLEY--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 213 tllgALDSMEPPTRPVDKPLRLPLQ---DVYKIGG-----IGTVPVGRVETGVLKPGMVVTFAPPMIS------------ 272
Cdd:PTZ00327 228 ----ICTQIPIPKRDLTSPPRMIVIrsfDVNKPGEdienlKGGVAGGSILQGVLKVGDEIEIRPGIISkdsggeftcrpi 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 508737324 273 -TEVKSVEMHHQALEEAIPGDNVGFNIK---NVSVKDIRRGNVAGDSKKDPP 320
Cdd:PTZ00327 304 rTRIVSLFAENNELQYAVPGGLIGVGTTidpTLTRADRLVGQVLGYPGKLPE 355
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
9-207 |
3.28e-10 |
|
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: 59.14 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIyKCGGIDKRTIEKFEKeandigkgsfkyawVLDKLKAERERGITIdiaLWKFETSKYS-- 86
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALL-KQSGTFRENEEVGER--------------VMDSNDLERERGITI---LAKNTAITYKdt 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 87 -FTIIDAPGHRDF------IKNMitgtsqADIAVLIVAAgqgefeagisKEG---QTREHALLAFTLGVRqLIVGVNKMD 156
Cdd:cd01891 66 kINIIDTPGHADFggeverVLSM------VDGVLLLVDA----------SEGpmpQTRFVLKKALEAGLK-PIVVINKID 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 508737324 157 laeYKQKRYKEIKKEISKTIKKIGYNPDKVPFvPI------SGFHGDNMIEAGDNMS 207
Cdd:cd01891 129 ---RPDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLD 181
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
238-311 |
6.10e-10 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 55.69 E-value: 6.10e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508737324 238 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAP----PMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSVKDIRRGNV 311
Cdd:cd03694 7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdadgKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
12-156 |
2.46e-09 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 57.99 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEANDI-GKGSFKYAwVLDKLKAERERGITIDIALWKFETSKYSFTII 90
Cdd:cd04169 7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508737324 91 DAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQT-------REHALLAFTLgvrqlivgVNKMD 156
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-------VEPQTrklfevcRLRGIPIITF--------INKLD 134
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
231-314 |
3.99e-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: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 231 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMH-HQALEEAIPGDNVGFNIKNVSVKDIRRG 309
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79
|
....*
gi 508737324 310 NVAGD 314
Cdd:cd03698 80 DILSS 84
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-121 |
7.86e-09 |
|
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: 55.74 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYkcggidkrtiekFEKEANDIGKGSFKYAWVLDKLKAERERGITID---IALwKFETSK- 84
Cdd:cd04167 2 NVCIAGHLHHGKTSLLDMLIE------------QTHKRTPSVKLGWKPLRYTDTRKDEQERGISIKsnpISL-VLEDSKg 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 508737324 85 --YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQG 121
Cdd:cd04167 69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEG 107
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
1-98 |
2.96e-08 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 56.21 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEANDigkgsfkyAWVLDKLKAERERGITID---IAL 77
Cdd:PTZ00416 13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
|
90 100
....*....|....*....|....*....
gi 508737324 78 WkFE------TSKYSFTI--IDAPGHRDF 98
Cdd:PTZ00416 78 Y-YEhdledgDDKQPFLInlIDSPGHVDF 105
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
11-201 |
6.29e-08 |
|
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: 52.07 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeandigkgsfkyawvlDKLKAERERGITIDIAL--WKFETSKYSFT 88
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 89 IIDAPGHRDFIKNMITGT-----SQADIAVLIVAAGQGEfeagiSKEGQTREHALLAFTLGVRQLIVGvNKMDLAEYKQK 163
Cdd:cd00882 51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRE-----SEEDAKLLILRRLRKEGIPIILVG-NKIDLLEEREV 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 508737324 164 RYKEIKKEISKtikkigynPDKVPFVPISGFHGDNMIE 201
Cdd:cd00882 125 EELLRLEELAK--------ILGVPVFEVSAKTGEGVDE 154
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
9-265 |
9.60e-08 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 54.26 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiEKFEKEA---NDIgkgsfkyawvldklkaERERGITIdialwkfeTSK- 84
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQSGTFREN--QEVAERVmdsNDL----------------ERERGITI--------LAKn 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 -------YSFTIIDAPGHRDF------IKNMitgtsqADIAVLIVAAgqgefeagisKEG---QTR---EHALlafTLGV 145
Cdd:COG1217 62 tavrykgVKINIVDTPGHADFggeverVLSM------VDGVLLLVDA----------FEGpmpQTRfvlKKAL---ELGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 146 RqLIVGVNKMDlaeykqkrykeikkeisktikKIGYNPDKV--------------------PFV---PISGFHGDNMIEA 202
Cdd:COG1217 123 K-PIVVINKID---------------------RPDARPDEVvdevfdlfielgatdeqldfPVVyasARNGWASLDLDDP 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 203 GDNMSwykgPtLLGA-LDSMEPPTRPVDKPLRlpLQ------DVYkIGGIGtvpVGRVETGVLKPGMVVT 265
Cdd:COG1217 181 GEDLT----P-LFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVA 239
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
9-185 |
1.93e-07 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 53.33 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIekfekeandiGKgsfkyAWVLDKLKAERERGITIDIA----LWKFETSK 84
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDNLLAGAGMISEELA----------GE-----QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAgqgefeagisKEG---QTREHALLAFTLGVRQLIVgVNKMD--LAE 159
Cdd:PRK07560 87 YLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDA----------VEGvmpQTETVLRQALRERVKPVLF-INKVDrlIKE 155
|
170 180 190
....*....|....*....|....*....|..
gi 508737324 160 YK------QKRYKEIKKEISKTIKkiGYNPDK 185
Cdd:PRK07560 156 LKltpqemQQRLLKIIKDVNKLIK--GMAPEE 185
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
232-311 |
2.09e-07 |
|
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: 48.33 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 232 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKN-VsvkDIRRGN 310
Cdd:cd03695 1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77
|
.
gi 508737324 311 V 311
Cdd:cd03695 78 L 78
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
10-199 |
2.37e-07 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 53.30 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 10 IVVIGHVDSGKSTTtghliykcggIDK-RTIEKFEKEANdigkgsfkyawvldklkaererGITIDIA----LWKFETSK 84
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDKiRKTQIAQKEAG----------------------GITQKIGayevEFEYKDEN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 85 YSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAGQGefeagisKEGQTREhALLAFTLGVRQLIVGVNKMDLAEYKQKR 164
Cdd:CHL00189 295 QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKANANTER 366
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 508737324 165 ykeIKKEISKtikkigYN--PDK----VPFVPISGFHGDNM 199
Cdd:CHL00189 367 ---IKQQLAK------YNliPEKwggdTPMIPISASQGTNI 398
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
1-98 |
2.01e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 50.11 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 1 MGKEKTHVNIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEANDigkgsfkyAWVLDKLKAERERGITID---IAL 77
Cdd:PLN00116 13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIA-------QEVAGD--------VRMTDTRADEAERGITIKstgISL 77
|
90 100 110
....*....|....*....|....*....|....
gi 508737324 78 W-------------KFETSKYSFTIIDAPGHRDF 98
Cdd:PLN00116 78 YyemtdeslkdfkgERDGNEYLINLIDSPGHVDF 111
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
63-196 |
6.87e-06 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 46.27 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 63 LKAER-----ERGITIDIALWKFETSKYSFTIIDAPGHR---------DF--IKNMITGTSQADIAVLIVAAGQGEFE-- 124
Cdd:cd01895 23 LGEERvivsdIAGTTRDSIDVPFEYDGQKYTLIDTAGIRkkgkvtegiEKysVLRTLKAIERADVVLLVLDASEGITEqd 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508737324 125 ---AG-ISKEGqtrehallaftlgvRQLIVGVNKMDLAEYKQKRYKEIKKEISKTIKKIGYnpdkVPFVPISGFHG 196
Cdd:cd01895 103 lriAGlILEEG--------------KALIIVVNKWDLVEKDEKTMKEFEKELRRKLPFLDY----APIVFISALTG 160
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
237-311 |
1.42e-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: 43.05 E-value: 1.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508737324 237 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfaPPMISTEVKSVEMHHQALEEAIPGDNVGFNIKNVSvkDIRRGNV 311
Cdd:cd16265 6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
8-206 |
3.12e-05 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 43.90 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 8 VNIVVIGHVDSGKSTTTGHLIYKCGGIDKR--TIEKfekeanDIGKGSFkyawvldklkaeRERGITidialwkfetskY 85
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYypGTTR------NYVTTVI------------EEDGKT------------Y 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 86 SFTIIDAPGHRDFIKNMITGTSQA-------DIAVLIVAAGQGefeagisKEGQTREHALLAfTLGVRQLIVGvNKMDLA 158
Cdd:TIGR00231 52 KFNLLDTAGQEDYDAIRRLYYPQVerslrvfDIVILVLDVEEI-------LEKQTKEIIHHA-DSGVPIILVG-NKIDLK 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 508737324 159 EYKQKryKEIKKEISKTIKKigynpdkvPFVPISGFHGDNMIEAGDNM 206
Cdd:TIGR00231 123 DADLK--THVASEFAKLNGE--------PIIPLSAETGKNIDSAFKIV 160
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
10-192 |
4.67e-05 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 45.39 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 10 IVVI-GHVDSGKSTttghliykcggidkrtiekfekeandigkgsfkyawVLDKLK----AERE-RGITIDIALWKFETS 83
Cdd:COG0532 6 VVTVmGHVDHGKTS------------------------------------LLDAIRktnvAAGEaGGITQHIGAYQVETN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 84 KYSFTIIDAPGHRDFIKNMITGTSQADIAVLIVAAgqgefeagisKEG---QTRE---HALLAftlGVrQLIVGVNKMDL 157
Cdd:COG0532 50 GGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAA----------DDGvmpQTIEainHAKAA---GV-PIIVAINKIDK 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 508737324 158 AEYKQKRykeIKKEISktikKIGYNPD----KVPFVPIS 192
Cdd:COG0532 116 PGANPDR---VKQELA----EHGLVPEewggDTIFVPVS 147
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
10-202 |
9.31e-05 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 43.05 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 10 IVVIGHVDSGKSTttghLIYKcggidkrtiekfekeandigkgsFKYAWVlDKLKAERERGITIDIALWKFETSKYSFTI 89
Cdd:COG1100 6 IVVVGTGGVGKTS----LVNR-----------------------LVGDIF-SLEKYLSTNGVTIDKKELKLDGLDVDLVI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 90 IDAPGHRDFIK---NMITGTSQADIAVLIVAAgqgefeagiSKEGQTR---EHALLAFTLG--VRQLIVGvNKMDLA-EY 160
Cdd:COG1100 58 WDTPGQDEFREtrqFYARQLTGASLYLFVVDG---------TREETLQslyELLESLRRLGkkSPIILVL-NKIDLYdEE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 508737324 161 KQKRYKEIKKEISktikkigyNPDKVPFVPISGFHGDNMIEA 202
Cdd:COG1100 128 EIEDEERLKEALS--------EDNIVEVVATSAKTGEGVEEL 161
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
326-390 |
1.82e-04 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 294007 [Multi-domain] Cd Length: 87 Bit Score: 40.19 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 508737324 326 FFAQVIVLNHPGTISNGYTPVLDCHTAHIACKFTEIVTKIDRrsgkvleelpksvkTGDAAMVTL 390
Cdd:cd03708 6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLR--------------TGDRALVRF 56
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
326-424 |
8.94e-04 |
|
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.
Pssm-ID: 294005 [Multi-domain] Cd Length: 93 Bit Score: 38.37 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508737324 326 FFAQVIVLN------HPGtISNGYTPVLDCHTAHIACKFTeivtkidrrsgkvLEELPKSVKTGDAAMVTLTPSKPMCVE 399
Cdd:cd03706 6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRID-------------LPEGKEMVMPGEDTSVKLTLLKPMVLE 71
|
90 100
....*....|....*....|....*
gi 508737324 400 afteypPLGRFAVRDMRQTVAVGVI 424
Cdd:cd03706 72 ------KGQRFTLREGGRTIGTGVV 90
|
|
| FERM_C_CCM1 |
cd13197 |
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ... |
385-415 |
7.77e-03 |
|
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.
Pssm-ID: 270018 Cd Length: 100 Bit Score: 36.05 E-value: 7.77e-03
10 20 30
....*....|....*....|....*....|.
gi 508737324 385 AAMVTLTPSKPMCVEAFTEYPPLGRFAVRDM 415
Cdd:cd13197 41 ALLLSLKYGCFMWQLGDADTCFQIHSLENKM 71
|
|
| |
