|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
2-430 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 795.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 2 SAITTLAQTTSRLLLRPTNATAPGLYLTR----------------RTFAAAGDKFNRDKPHVNIGTIGHVDHGKTTLTQA 65
Cdd:PLN03127 1 MASVVLRNPNSKRLLPFSSQIYCACRGSApstsasisaaddrqspSPWWRSMATFTRTKPHVNVGTIGHVDHGKTTLTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 66 ITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG 145
Cdd:PLN03127 81 ITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 146 PMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDFYDFNGDETPIIRGSALAAAEGRDPELGANAV 225
Cdd:PLN03127 161 PMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTNDEIGKNAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 226 LELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNH--NAKTTCTGVEMFKKLLD 303
Cdd:PLN03127 241 LKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPggPLKTTVTGVEMFKKILD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 304 YGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSQDEGGRHTPFFSNYRPQFFFRTADVTGDLKLREG 383
Cdd:PLN03127 321 QGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 224008444 384 TEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGTGIVTKVHG 430
Cdd:PLN03127 401 VKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGVVSKVLS 447
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
36-428 |
0e+00 |
|
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: 780.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 36 AGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHID 115
Cdd:COG0050 2 AKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 116 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDFY 195
Cdd:COG0050 82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 196 DFNGDETPIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNV 275
Cdd:COG0050 162 GFPGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 276 GDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSQDEGGR 355
Cdd:COG0050 242 GDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224008444 356 HTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:COG0050 322 HTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
36-428 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 779.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 36 AGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHID 115
Cdd:PRK00049 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 116 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDFY 195
Cdd:PRK00049 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 196 DFNGDETPIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNV 275
Cdd:PRK00049 162 DFPGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 276 GDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSQDEGGR 355
Cdd:PRK00049 242 GEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224008444 356 HTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:PRK00049 322 HTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKI 394
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
36-428 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 758.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 36 AGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHID 115
Cdd:PRK12735 2 AKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 116 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDFY 195
Cdd:PRK12735 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 196 DFNGDETPIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNV 275
Cdd:PRK12735 162 DFPGDDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 276 GDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSQDEGGR 355
Cdd:PRK12735 242 GDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGR 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224008444 356 HTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:PRK12735 322 HTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKI 394
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
35-428 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 732.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 35 AAGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHI 114
Cdd:PRK12736 1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 115 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDF 194
Cdd:PRK12736 81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 195 YDFNGDETPIIRGSALAAAEGRDPELgaNAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVN 274
Cdd:PRK12736 161 YDFPGDDIPVIRGSALKALEGDPKWE--DAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 275 VGDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSQDEGG 354
Cdd:PRK12736 239 VGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224008444 355 RHTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:PRK12736 319 RHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEI 392
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
35-428 |
0e+00 |
|
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: 672.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 35 AAGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHI 114
Cdd:TIGR00485 1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 115 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDF 194
Cdd:TIGR00485 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 195 YDFNGDETPIIRGSALAAAEGrDPELGAnAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVN 274
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEG-DAEWEA-KILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 275 VGDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSQDEGG 354
Cdd:TIGR00485 239 VGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224008444 355 RHTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:TIGR00485 319 RHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKI 392
|
|
| tufA |
CHL00071 |
elongation factor Tu |
36-428 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 643.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 36 AGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHID 115
Cdd:CHL00071 2 AREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 116 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDFY 195
Cdd:CHL00071 82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 196 DFNGDETPIIRGSALAAAEG--RDPEL--GANA----VLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGR 267
Cdd:CHL00071 162 DFPGDDIPIVSGSALLALEAltENPKIkrGENKwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 268 IEQGKVNVGDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYC 347
Cdd:CHL00071 242 IERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 348 LSQDEGGRHTPFFSNYRPQFFFRTADVTGDLKLREG-----TEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRTVGT 422
Cdd:CHL00071 322 LTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESFTAddgskTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGA 401
|
....*.
gi 224008444 423 GIVTKV 428
Cdd:CHL00071 402 GVVSKI 407
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
12-428 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 544.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 12 SRLLLRPTNATAPGLYLTRRTFA--AAGDKFNRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPE 89
Cdd:PLN03126 45 SSFLSPFSTTTTSTSQRRRRSFTvrAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 90 EKARKITINTSHIEYETANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFL 169
Cdd:PLN03126 125 ERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 170 NKCDMVDDEELLELVEMEIRELLDFYDFNGDETPIIRGSALAAAEG--RDPEL--GANA----VLELMAAVDETIPEPTR 241
Cdd:PLN03126 205 NKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEAlmENPNIkrGDNKwvdkIYELMDAVDSYIPIPQR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 242 DLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKRE 321
Cdd:PLN03126 285 QTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 322 DVERGQVLCKPGSISTAKKFEAEIYCLSQDEGGRHTPFFSNYRPQFFFRTADVTGDL-----KLREGTEMVMPGDNTTLD 396
Cdd:PLN03126 365 DIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMV 444
|
410 420 430
....*....|....*....|....*....|..
gi 224008444 397 VELITPVPIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:PLN03126 445 VELIVPVACEQGMRFAIREGGKTVGAGVIQSI 476
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
45-239 |
7.75e-133 |
|
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: 380.01 E-value: 7.75e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 45 PHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVK 124
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 125 NMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIRELLDFYDFNGDETPI 204
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 224008444 205 IRGSALAAAEGRDPELGANAVLELMAAVDETIPEP 239
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
42-428 |
4.80e-78 |
|
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: 248.31 E-value: 4.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 42 RDKPHVNIGTIGHVDHGKTTL-------TQAIT-KVLSE-KGWSKAMSYED------IDRAPEEKARKITINTSHIEYET 106
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDeHIIEKyEEEAEKKGKESfkfawvMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 107 ANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVD-DEELLELVE 185
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 186 MEIRELLDFYDFNGDETPIIRGSALaaaegrdpeLGANAVLE-----------LMAAVDEtIPEPTRDLDKPFLMPIEDV 254
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAW---------KGDNVVKKsdnmpwyngptLLEALDN-LKEPEKPVDKPLRIPIQDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 255 FSIAGRGTVVTGRIEQGKVNVGDDlevVGFNHNAKTT-CTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPG 333
Cdd:COG5256 233 YSISGIGTVPVGRVETGVLKVGDK---VVFMPAGVVGeVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 334 SIST-AKKFEAEIYCLsqdeggRH-TPFFSNYRPQFFFRTADV-------TGDLKLREGTEM------VMPGDNTTLDVE 398
Cdd:COG5256 310 NPPTvAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVactfvelVSKLDPRTGQVKeenpqfLKTGDAAIVKIK 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 224008444 399 LITPVPIEA-------GlRFNMREGGRTVGTGIVTKV 428
Cdd:COG5256 384 PTKPLVIEKfkefpqlG-RFAIRDMGQTVAAGVVLDV 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
44-237 |
1.02e-75 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 233.96 E-value: 1.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 44 KPHVNIGTIGHVDHGKTTLTQAITKVL---SEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHA 120
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTgaiSKRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 121 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCDMVDDEELLELVEMEIRELLDFYDFNGD 200
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 224008444 201 ETPIIRGSALaAAEGrdpelganaVLELMAAVDETIP 237
Cdd:pfam00009 160 FVPVVPGSAL-KGEG---------VQTLLDALDEYLP 186
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
42-429 |
1.22e-73 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 236.75 E-value: 1.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 42 RDKPHVNIGTIGHVDHGKTTLT------------QAITKVLSEkgwSKAMSYED------IDRAPEEKARKITINTSHIE 103
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVgrllyetgaideHIIEELREE---AKEKGKESfkfawvMDRLKEERERGVTIDLAHKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 104 YETANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATD--GPMPQTREHILLAKQVGMPKLVVFLNKCDMVD-DEEL 180
Cdd:PRK12317 79 FETDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 181 LELVEMEIRELLDFYDFNGDETPIIRGSALAaaegrdpelGANAVLE-----------LMAAVDeTIPEPTRDLDKPFLM 249
Cdd:PRK12317 159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFE---------GDNVVKKsenmpwyngptLLEALD-NLKPPEKPTDKPLRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 250 PIEDVFSIAGRGTVVTGRIEQGKVNVGDDL-----EVVGfnhNAKTtctgVEMFKKLLDYGMAGDNVGALLRGLKREDVE 324
Cdd:PRK12317 229 PIQDVYSISGVGTVPVGRVETGVLKVGDKVvfmpaGVVG---EVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 325 RGQVLCKPGSIST-AKKFEAEIYCLsqdeggRH-TPFFSNYRPQFFFRTADV--------------TGDLKlREGTEMVM 388
Cdd:PRK12317 302 RGDVCGHPDNPPTvAEEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQVA-EENPQFIK 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 224008444 389 PGDNTTLDVELITPVPIEA-------GlRFNMREGGRTVGTGIVTKVH 429
Cdd:PRK12317 375 TGDAAIVKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDVK 421
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
47-425 |
4.06e-64 |
|
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: 217.09 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 47 VNIGTIGHVDHGKTTLTQAITKVlsekgwskamsyeDIDRAPEEKARKITINT--SHIEYEtANRHYGHIDCPGHADYVK 124
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGI-------------DTDRLKEEKKRGITIDLgfAYLPLP-DGRRLGFVDVPGHEKFIK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 125 NMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMvDDEELLELVEMEIRELLDFYDFNGdeTPI 204
Cdd:COG3276 67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFLED--API 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 205 IRGSALaAAEGRDpelganavlELMAAVDETIPE-PTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVG 283
Cdd:COG3276 144 VPVSAV-TGEGID---------ELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 284 FNHnaKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPGSISTAKKFEAEIYCLSqdegGRHTPFFSNY 363
Cdd:COG3276 214 SGK--PVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQ 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224008444 364 RPQFFFRTADVTGDLKLREGTEMVmPGDNTTLDVELITPVPIEAGLRFNMREGG--RTVGTGIV 425
Cdd:COG3276 288 RVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
338-425 |
5.29e-54 |
|
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their 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. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.
Pssm-ID: 294006 [Multi-domain] Cd Length: 90 Bit Score: 174.62 E-value: 5.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 338 AKKFEAEIYCLSQDEGGRHTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGG 417
Cdd:cd03707 3 HTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIREGG 82
|
....*...
gi 224008444 418 RTVGTGIV 425
Cdd:cd03707 83 RTVGAGVV 90
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
48-210 |
9.76e-54 |
|
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: 177.10 E-value: 9.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVKNMI 127
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 128 TGAAQMDGGILVVAATDGPMPQTREHILLAKQvGMPKLVVFLNKCDMvDDEELLELVEMEIRELL---DFYDFNGDETPI 204
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLkliGFTFLKGKDVPI 158
|
....*.
gi 224008444 205 IRGSAL 210
Cdd:cd00881 159 IPISAL 164
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
47-423 |
6.78e-53 |
|
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: 186.23 E-value: 6.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 47 VNIGTIGHVDHGKTTLTQAITKVlsekgwskamsyeDIDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVKNM 126
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 127 ITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDmVDDEELLELVEMEIRELLDFYDFNGDETPIIr 206
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIFLKNAKIFK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 207 gsaLAAAEGRDPELGANAVLELMAAVDetipepTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNH 286
Cdd:TIGR00475 146 ---TSAKTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 287 NAKTtcTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLCKPgsISTAKKFEAEIYClsqdeggrHTPFFSNYRPQ 366
Cdd:TIGR00475 217 EVRV--KAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP--EDPKLRVVVKFIA--------EVPLLELQPYH 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 224008444 367 FFFRTADVTGDLKLREGT--EMVMPgdnttldveliTPVPIEAGLRFNMREGGRTVGTG 423
Cdd:TIGR00475 285 IAHGMSVTTGKISLLDKGiaLLTLD-----------APLILAKGDKLVLRDSSGNFLAG 332
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
247-333 |
4.93e-50 |
|
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: 164.23 E-value: 4.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 247 FLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERG 326
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80
|
....*..
gi 224008444 327 QVLCKPG 333
Cdd:cd03697 81 MVLAKPG 87
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
42-428 |
1.12e-48 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 171.85 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 42 RDKPHVNIGTIGHVDHGKTTLTQ-------AITKVLSEKgwskamsYED---------------IDRAPEEKARKITINT 99
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGhliykcgGIDKRTIEK-------FEKeaaemgkgsfkyawvLDKLKAERERGITIDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 100 SHIEYETANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILLAKQVGMPKLVVFLNKC 172
Cdd:PTZ00141 76 ALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 173 DMVDDEELLE---LVEMEIRELLDFYDFNGDETPIIRGSALAAAE--GRDPELGANAVLELMAAVDeTIPEPTRDLDKPF 247
Cdd:PTZ00141 156 DDKTVNYSQErydEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNmiEKSDNMPWYKGPTLLEALD-TLEPPKRPVDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 248 LMPIEDVFSIAGRGTVVTGRIEQGKVNVGDdleVVGFNHNAKTT-CTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERG 326
Cdd:PTZ00141 235 RLPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSGVTTeVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 327 QVL--CKPGSISTAKKFEAEIYCLS---QDEGGrHTPF-----------FSNYRPQFFFRTADVtgdlkLREGTEMVMPG 390
Cdd:PTZ00141 312 YVAsdSKNDPAKECADFTAQVIVLNhpgQIKNG-YTPVldchtahiackFAEIESKIDRRSGKV-----LEENPKAIKSG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 224008444 391 DNTTLDVELITPVPIEA-------GlRFNMREGGRTVGTGIVTKV 428
Cdd:PTZ00141 386 DAAIVKMVPTKPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSV 429
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
41-430 |
2.16e-41 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 153.94 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 41 NRDKPHVNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYedIDRAPEEKARKITINTSHIEY---------------- 104
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYAVYgfdddgpvrmknplrk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 105 -------ETANRHYGHIDCPGHADYVKNMITG--AAQMDGGILVVAATDGPMPQTREH--ILLAkqVGMPKLVVfLNKCD 173
Cdd:COG5258 195 tdrarvvEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHlgILLA--MDLPVIVA-ITKID 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 174 MVDDEELLELVEmEIRELLDfydfNGDETPII---RGSALAAAEGRD----PELGANAV----LELMAAVDETIPEPTRD 242
Cdd:COG5258 272 KVDDERVEEVER-EIENLLR----IVGRTPLEvesRHDVDAAIEEINgrvvPILKTSAVtgegLDLLDELFERLPKRATD 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 243 LDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEV--VGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKR 320
Cdd:COG5258 347 EDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgpTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEE 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 321 EDVERGQVLCKPGSISTA-KKFEAEIYCLSqdeggrH-TPFFSNYRPQFFFRTADVTGDLKlREGTEMVMPGDNTTLDVE 398
Cdd:COG5258 427 EELERGMVLLPRDADPKAvREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVRLR 499
|
410 420 430
....*....|....*....|....*....|...
gi 224008444 399 -LITPVPIEAGLRFNMREgGRTVGTGIVTKVHG 430
Cdd:COG5258 500 fKYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
45-348 |
4.04e-41 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 150.59 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 45 PHVNIGTIGHVDHGKTTLTQAITKVlsekgWSkamsyediDRAPEEKARKITINTSHIE--------------YETAN-- 108
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGV-----WT--------DTHSEELKRGISIRLGYADaeiykcpecdgpecYTTEPvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 109 ----------RHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLAKQVGMPKLVVFLNKCDMVDD 177
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 178 EELLELVEmEIRELLDFYdfNGDETPIIRGSALAaaegrdpelGANaVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSI 257
Cdd:TIGR03680 150 EKALENYE-EIKEFVKGT--VAENAPIIPVSALH---------NAN-IDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 258 AGRGT--------VVTGRIEQGKVNVGDDLEVV-GFNH---------NAKTTCTGVEMFKKLLDYGMAGDNVG---ALLR 316
Cdd:TIGR03680 217 NKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVekggktkwePIYTEITSLRAGGYKVEEARPGGLVGvgtKLDP 296
|
330 340 350
....*....|....*....|....*....|...
gi 224008444 317 GLKREDVERGQVLCKPGSIS-TAKKFEAEIYCL 348
Cdd:TIGR03680 297 ALTKADALAGQVVGKPGTLPpVWESLELEVHLL 329
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
334-428 |
8.86e-41 |
|
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: 140.48 E-value: 8.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 334 SISTAKKFEAEIYCLSQDEGGRHTPFFSNYRPQFFFRTADVTGDL----------KLREGTEMVMPGDNTTLDVELITPV 403
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkldpgGVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 224008444 404 PIEAGLRFNMREGGRTVGTGIVTKV 428
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
45-281 |
1.56e-38 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 143.44 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 45 PHVNIGTIGHVDHGKTTLTQAITKVlsekgWSkamsyediDRAPEEKARKITINTSHIE--------------YETAN-- 108
Cdd:COG5257 4 PEVNIGVVGHVDHGKTTLVQALTGV-----WT--------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTEPkc 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 109 ----------RHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLAKQVGMPKLVVFLNKCDMVDD 177
Cdd:COG5257 71 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 178 EELLELVEmEIRELLDfyDFNGDETPIIRGSALAaaegrdpelGANaVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSI 257
Cdd:COG5257 151 ERALENYE-QIKEFVK--GTVAENAPIIPVSAQH---------KVN-IDALIEAIEEEIPTPERDLSKPPRMLVARSFDV 217
|
250 260 270
....*....|....*....|....*....|..
gi 224008444 258 AGRGT--------VVTGRIEQGKVNVGDDLEV 281
Cdd:COG5257 218 NKPGTppkdlkggVIGGSLIQGVLKVGDEIEI 249
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
45-281 |
2.21e-38 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 143.07 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 45 PHVNIGTIGHVDHGKTTLTQAITKVlsekgWSkamsyediDRAPEEKARKITI-------------NTSHIEYETAN--- 108
Cdd:PRK04000 8 PEVNIGMVGHVDHGKTTLVQALTGV-----WT--------DRHSEELKRGITIrlgyadatirkcpDCEEPEAYTTEpkc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 109 ----------RHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLAKQVGMPKLVVFLNKCDMvDD 177
Cdd:PRK04000 75 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL-VS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 178 EELLELVEMEIRELLDfydfnG---DETPIIRGSALAaaegrdpelGANAVLeLMAAVDETIPEPTRDLDKPFLM----- 249
Cdd:PRK04000 154 KERALENYEQIKEFVK-----GtvaENAPIIPVSALH---------KVNIDA-LIEAIEEEIPTPERDLDKPPRMyvars 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 224008444 250 --------PIEDVfsiagRGTVVTGRIEQGKVNVGDDLEV 281
Cdd:PRK04000 219 fdvnkpgtPPEKL-----KGGVIGGSLIQGVLKVGDEIEI 253
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
49-285 |
3.54e-38 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 145.96 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 49 IGTIGHVDHGKTTLTQAITKVlsekgwskamsyeDIDRAPEEKARKITINTSHIEYETAN-RHYGHIDCPGHADYVKNMI 127
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAITGV-------------NADRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 128 TGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEmEIRELLDFYDFngDETPIIrg 207
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRR-QVKAVLREYGF--AEAKLF-- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224008444 208 sALAAAEGRDPELGANAVLELmaavdetiPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFN 285
Cdd:PRK10512 145 -VTAATEGRGIDALREHLLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN 213
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
49-242 |
8.87e-38 |
|
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: 135.04 E-value: 8.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 49 IGTIGHVDHGKTTLTQAITKVlsekgwskamsyeDIDRAPEEKARKITINT--SHIEYETaNRHYGHIDCPGHADYVKNM 126
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLgfAYLDLPD-GKRLGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 127 ITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMvDDEELLELVEMEIRELLDFYDFNGdeTPIIR 206
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLAD--APIFP 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 224008444 207 GSALaAAEGRDpelganavlELMAAVDEtIPEPTRD 242
Cdd:cd04171 145 VSSV-TGEGIE---------ELKNYLDE-LAEPQSK 169
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
42-428 |
2.81e-37 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 141.00 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 42 RDKPHVNIGTIGHVDHGKTTLT------------QAITKVLSEKGWSKAMSYED---IDRAPEEKARKITINTSHIEYET 106
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTghliyklggidkRVIERFEKEAAEMNKRSFKYawvLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 107 ANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMP-------QTREHILLAKQVGMPKLVVFLNKCDMVDDEE 179
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 180 LLELVEMEIRELLDFYD---FNGDETPIIrgsALAAAEG-----RDPELGANAVLELMAAVDEtIPEPTRDLDKPFLMPI 251
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKkvgYNPDKIPFV---PISGFEGdnmieRSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 252 EDVFSIAGRGTVVTGRIEQGKVNVGddlEVVGFNHNAKTT-CTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVL- 329
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 330 -CKPGSISTAKKFEAEIYCLSQ--DEGGRHTPFFSNYRPQFFFRTADVTGDLKLREGTEM------VMPGDNTTLDVELI 400
Cdd:PLN00043 316 nSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFVKMIPT 395
|
410 420 430
....*....|....*....|....*....|....
gi 224008444 401 TPVPIEAGL------RFNMREGGRTVGTGIVTKV 428
Cdd:PLN00043 396 KPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
48-173 |
1.39e-36 |
|
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: 133.39 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLT------------QAITKVLSEkgwSKAMSYED------IDRAPEEKARKITINTSHIEYETANR 109
Cdd:cd01883 1 NLVVIGHVDAGKSTLTghllyklggvdkRTIEKYEKE---AKEMGKESfkyawvLDKLKEERERGVTIDVGLAKFETEKY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224008444 110 HYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG-------PMPQTREHILLAKQVGMPKLVVFLNKCD 173
Cdd:cd01883 78 RFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
340-428 |
3.37e-33 |
|
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: 120.03 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 340 KFEAEIYCLSQDEGGRHTPFFSNYRPQFFFRTADVTGDLKLREGTEMVMPGDNTTLDVELITPVPIEAGLRFNMREGGRT 419
Cdd:cd03706 5 HFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREGGRT 84
|
....*....
gi 224008444 420 VGTGIVTKV 428
Cdd:cd03706 85 IGTGVVTKL 93
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
42-345 |
5.84e-30 |
|
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: 120.19 E-value: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 42 RDKPHVNIGTIGHVDHGKTTLtqaI------TKVLSE------KGWSKAMSYEDIDRAP------EEKARKITINTSHIE 103
Cdd:COG2895 13 ENKDLLRFITCGSVDDGKSTL---IgrllydTKSIFEdqlaalERDSKKRGTQEIDLALltdglqAEREQGITIDVAYRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 104 YETANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKcdmvddeellel 183
Cdd:COG2895 90 FSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNK------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 184 veM---------------EIREL---LDFYD--------FNGD-------ETPIIRGSALaaaegrdpelganavLELMa 230
Cdd:COG2895 158 --MdlvdyseevfeeivaDYRAFaakLGLEDitfipisaLKGDnvverseNMPWYDGPTL---------------LEHL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 231 avdETIPEPTRDLDKPFLMPIEDV--FSIAGRGtvVTGRIEQGKVNVGDdlEVVGFNHNAKTTCTGVEMFKKLLDYGMAG 308
Cdd:COG2895 220 ---ETVEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGD--EVVVLPSGKTSTVKSIVTFDGDLEEAFAG 292
|
330 340 350
....*....|....*....|....*....|....*....
gi 224008444 309 DNVGalLRgLKRE-DVERGQVLCKPGS-ISTAKKFEAEI 345
Cdd:COG2895 293 QSVT--LT-LEDEiDISRGDVIVAADApPEVADQFEATL 328
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
48-332 |
3.21e-28 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 117.02 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKGW--SKAMSYEDIdrapeEKARKITI---NTShIEYEtaNRHYGHIDCPGH 119
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAvaERVMDSNDL-----ERERGITIlakNTA-IRYN--GTKINIVDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 120 ADY------VKNMItgaaqmDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVfLNKCDMVDDEELLElvemeIRELLD 193
Cdd:TIGR01394 75 ADFggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEV-----VDEVFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 194 -FYDFNGDET----PIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRI 268
Cdd:TIGR01394 143 lFAELGADDEqldfPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224008444 269 EQGKVNVGDDleVVGFNHNAKTT---CTGVEMFKKL----LDYGMAGDNVGalLRGLkrEDVERGQVLCKP 332
Cdd:TIGR01394 223 HRGTVKKGQQ--VALMKRDGTIEngrISKLLGFEGLerveIDEAGAGDIVA--VAGL--EDINIGETIADP 287
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
38-334 |
8.77e-28 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 114.72 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 38 DKFNRDKPHV-------NIGTIGHVDHGKTTLTQAITKVLSEkgwskamsyedidRAPEEKARKITIntsHIEYETAN-- 108
Cdd:PTZ00327 19 DKLTPLTPEVisrqatiNIGTIGHVAHGKSTVVKALSGVKTV-------------RFKREKVRNITI---KLGYANAKiy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 109 ----------------------------------RHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREH 153
Cdd:PTZ00327 83 kcpkcprptcyqsygsskpdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 154 ILLAKQVGMPKLVVFLNKCDMVDDEELLELVEmEIRELLDfyDFNGDETPIIRGSAlaaaegrdpELGAN--AVLELMAa 231
Cdd:PTZ00327 163 LAAVEIMKLKHIIILQNKIDLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPISA---------QLKYNidVVLEYIC- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 232 vdETIPEPTRDLDKPFLM----------PIEDVFSIagRGTVVTGRIEQGKVNVGDDLEV----VGFNHNAKTTCTG--- 294
Cdd:PTZ00327 230 --TQIPIPKRDLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIrpgiISKDSGGEFTCRPirt 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 224008444 295 --VEMF--KKLLDYGMAGD--NVGALLR-GLKREDVERGQVLCKPGS 334
Cdd:PTZ00327 306 riVSLFaeNNELQYAVPGGliGVGTTIDpTLTRADRLVGQVLGYPGK 352
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
47-174 |
1.63e-27 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 108.12 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 47 VNIGTIGHVDHGKTTLTQAITKVlsekgWSkamsyediDRAPEEKARKITI-----------------NTSHIEYETAN- 108
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGV-----WT--------VRHKEELKRNITIklgyanakiykcpncgcPRPYDTPECECp 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224008444 109 ---------RHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDG-PMPQTREHILLAKQVGMPKLVVFLNKCDM 174
Cdd:cd01888 68 gcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDL 143
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
47-217 |
2.86e-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 eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 102.06 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 47 VNIGTIGHVDHGKTTLTQAITKVLSEKGwskamsyedIDRAPEEKARKITIN-------TSHIEYETANRHYGH------ 113
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIASTAA---------FDKNPQSQERGITLDlgfssfeVDKPKHLEDNENPQIenyqit 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 114 -IDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAkQVGMPKLVVFLNKCDMvDDEELLELVEMEIRELL 192
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIG-ELLCKPLIVVLNKIDL-IPEEERKRKIEKMKKRL 149
|
170 180
....*....|....*....|....*..
gi 224008444 193 D--FYDFNGDETPIIrgsALAAAEGRD 217
Cdd:cd01889 150 QktLEKTRLKDSPII---PVSAKPGEG 173
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
48-335 |
1.55e-24 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 106.26 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKgwskamsyEDI-DRA----PEEKARKITI---NTShIEYEtanrhyGH--- 113
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALlkqSGTFREN--------QEVaERVmdsnDLERERGITIlakNTA-VRYK------GVkin 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 114 -IDCPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLAK--QVGMpKLVVFLNKCDmvddeellelv 184
Cdd:COG1217 73 iVDTPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGL-KPIVVINKID----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 185 emeiR----------ELLD-FYDFNGDET----PIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEPTRDLDKPFLM 249
Cdd:COG1217 133 ----RpdarpdevvdEVFDlFIELGATDEqldfPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 250 pieDVFSIA-----GRgtVVTGRIEQGKVNVGDDLEVV---GFNHNAKTTctgvemfkKLLDYgmagdnvgallRGLKRE 321
Cdd:COG1217 209 ---LVTNLDysdyvGR--IAIGRIFRGTIKKGQQVALIkrdGKVEKGKIT--------KLFGF-----------EGLERV 264
|
330
....*....|....
gi 224008444 322 DVERGQvlckPGSI 335
Cdd:COG1217 265 EVEEAE----AGDI 274
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
51-174 |
8.68e-22 |
|
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: 92.63 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 51 TIGHVDHGKTTL-------TQAIT--KVLS-EKGWSKAMSYEDIDRA------PEEKARKITINTSHIEYETANRHYGHI 114
Cdd:cd04166 4 TCGSVDDGKSTLigrllydSKSIFedQLAAlERSKSSGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 115 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDM 174
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
48-335 |
2.11e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 96.70 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLtqaITKVLSEKGW--SKAMSYEDI-DRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVK 124
Cdd:PRK10218 7 NIAIIAHVDHGKTTL---VDKLLQQSGTfdSRAETQERVmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 125 NMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMpKLVVFLNKCDMVDDEELLElvemeIRELLDFYdFNGDET-- 202
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGL-KPIVVINKVDRPGARPDWV-----VDQVFDLF-VNLDATde 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 203 ----PIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEPTRDLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDD 278
Cdd:PRK10218 157 qldfPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQ 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224008444 279 LEVV---GFNHNAKT----TCTGVEMFKKllDYGMAGDNVGalLRGLKREDVErgQVLCKPGSI 335
Cdd:PRK10218 237 VTIIdseGKTRNAKVgkvlGHLGLERIET--DLAEAGDIVA--ITGLGELNIS--DTVCDTQNV 294
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
48-239 |
8.58e-20 |
|
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: 86.88 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKGW--SKAMSYEDIdrapeEKARKITI---NTShIEYEtanrhyGH----ID 115
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALlkqSGTFRENEEvgERVMDSNDL-----ERERGITIlakNTA-ITYK------DTkiniID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 116 CPGHADY------VKNMItgaaqmDGGILVVAATDGPMPQTRehILLAK--QVGMPKLVVfLNKCDMVDDeellelvemE 187
Cdd:cd01891 72 TPGHADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLKPIVV-INKIDRPDA---------R 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224008444 188 IRELLD-----FYDFNGDET----PIIRGSALAAAEGRDPELGANAVLELMAAVDETIPEP 239
Cdd:cd01891 134 PEEVVDevfdlFLELNATDEqldfPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
53-210 |
4.04e-18 |
|
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: 81.36 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 53 GHVDHGKTTLTQAI--TKVlsekgwskamsyedidrAPEEkARKIT--INTSHIEYETANRHYGHIDCPGHADYvKNMIT 128
Cdd:cd01887 7 GHVDHGKTTLLDKIrkTNV-----------------AAGE-AGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 129 GAAQM-DGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCDMVDDEELLELVEMEirELLDFY----DFNGDeTP 203
Cdd:cd01887 68 RGASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEADPERVKN--ELSELGlvgeEWGGD-VS 143
|
....*..
gi 224008444 204 IIRGSAL 210
Cdd:cd01887 144 IVPISAK 150
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
48-173 |
6.87e-18 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 81.89 E-value: 6.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQ---AITKVLSEKGWSKAMsYEDIDraPEEKARKITINTSHI----EYETANRHYGH-----ID 115
Cdd:cd01885 2 NICIIAHVDHGKTTLSDsllASAGIISEKLAGKAR-YLDTR--EDEQERGITIKSSAIslyfEYEEEKMDGNDylinlID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 224008444 116 CPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILLAKQVGMPKLVVFLNKCD 173
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT-ETVLRQALEERVKPVLVINKID 135
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
247-331 |
9.05e-18 |
|
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: 77.57 E-value: 9.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 247 FLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTtcTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERG 326
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78
|
....*
gi 224008444 327 QVLCK 331
Cdd:cd03696 79 FVLSE 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
244-333 |
9.21e-18 |
|
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: 78.00 E-value: 9.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 244 DKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDdleVVGFN-HNAKTTCTGVEMFKKLLDYGMAGDNVGALLRGLKRED 322
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGM---VVTFApAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78
|
90
....*....|.
gi 224008444 323 VERGQVLCKPG 333
Cdd:cd03693 79 IKRGDVAGDSK 89
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
52-173 |
1.05e-17 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 85.56 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 52 IGHVDHGKTTLTQAI---TKVLSEKGwskamSYED----IDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVK 124
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIG-----EVEDgtttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 224008444 125 NMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLvVFLNKCD 173
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMD 123
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
48-173 |
1.37e-17 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 85.30 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQ---AITKVLSEK--GWSKAMSYEDidrapEEKARKITINTSHI----EYETANRHYGHIDCPG 118
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSDnllAGAGMISEElaGEQLALDFDE-----EEQARGITIKAANVsmvhEYEGKEYLINLIDTPG 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 224008444 119 HADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHIL---LAKQVgmpKLVVFLNKCD 173
Cdd:PRK07560 97 HVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVLrqaLRERV---KPVLFINKVD 150
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
37-284 |
1.42e-17 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 84.82 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 37 GDKFNRDKPHVNIgtIGHVDHGKTTLTQAITKVlsekgwskamsyedidRAPEEKARKIT--INTSHIEYETaNRHYGHI 114
Cdd:TIGR00487 80 GDLLVERPPVVTI--MGHVDHGKTSLLDSIRKT----------------KVAQGEAGGITqhIGAYHVENED-GKMITFL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 115 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCDMVDDEELlelvemEIRELLDF 194
Cdd:TIGR00487 141 DTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPD------RVKQELSE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 195 YDFN----GDETPIIRGSALAAAegrdpelGANAVLE---LMAAVDETIPEPTRDLDKPFLmpieDVFSIAGRGTVVTGR 267
Cdd:TIGR00487 214 YGLVpedwGGDTIFVPVSALTGD-------GIDELLDmilLQSEVEELKANPNGQASGVVI----EAQLDKGRGPVATVL 282
|
250
....*....|....*..
gi 224008444 268 IEQGKVNVGDDLeVVGF 284
Cdd:TIGR00487 283 VQSGTLRVGDIV-VVGA 298
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
48-173 |
4.57e-17 |
|
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: 83.56 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKGwskamSYED----IDRAPEEKARKITINTS--HIEYEtanrhyGH----I 114
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIG-----EVHDgntvMDWMPEEQERGITITSAatTCEWK------GHkiniI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 115 DCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTrEHIL-LAKQVGMPKLvVFLNKCD 173
Cdd:COG0480 80 DTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT-ETVWrQADKYGVPRI-VFVNKMD 137
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
48-173 |
1.00e-16 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 79.20 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKGW-SKAMSYEDIDRApeEKARKITINTSHIEYETANRHYGHIDCPGHADYV 123
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLlytSGAIRELGSvDKGTTRTDSMEL--ERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 224008444 124 KNMITGAAQMDGGILVVAATDGPMPQTRehIL--LAKQVGMPKlVVFLNKCD 173
Cdd:cd04168 79 AEVERSLSVLDGAILVISAVEGVQAQTR--ILfrLLRKLNIPT-IIFVNKID 127
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
261-330 |
3.66e-16 |
|
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: 72.68 E-value: 3.66e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224008444 261 GTVVTGRIEQGKVNVGDDLEVVGFNHNAK---TTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDVERGQVLC 330
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
48-173 |
2.10e-15 |
|
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: 75.71 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKGwskamSYED----IDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHA 120
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLG-----RVEDgntvSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 224008444 121 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLvVFLNKCD 173
Cdd:cd04170 76 DFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
48-343 |
2.52e-15 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 78.01 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQaitKVLSEKGW-SKAMSYED--IDRAPEEKARKITINTSHI----EYETANRHYGHIDCPGHA 120
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSD---NLLAGAGMiSEELAGQQlyLDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGHV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 121 DYVKNMITGAAQMDGGILVVAATDGPMPQTrEHILLAKQVGMPKLVVFLNKCDMVDDEELLELVEMEIR----------- 189
Cdd:TIGR00490 98 DFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVLRQALKENVKPVLFINKVDRLINELKLTPQELQERfikiitevnkl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 190 -------ELLDFYDFNGDETPIIRGSALA----------------------AAEGRDPELGANAVLE--LMAAVDETIPE 238
Cdd:TIGR00490 177 ikamapeEFRDKWKVRVEDGSVAFGSAYYnwaisvpsmkktgigfkdiykyCKEDKQKELAKKSPLHqvVLDMVIRHLPS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 239 PTR-------------------------DLDKPFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTTCT 293
Cdd:TIGR00490 257 PIEaqkyripviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQV 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 224008444 294 GVEMFKKLL--DYGMAGdNVGALLrGLKreDVERGQVLCKPGSISTAkkFEA 343
Cdd:TIGR00490 337 GVYMGPERVevDEIPAG-NIVAVI-GLK--DAVAGETICTTVENITP--FES 382
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
51-345 |
1.47e-14 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 75.74 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 51 TIGHVDHGKTTLtqaITKVLSEkgwSKaMSYED------------------IDRA------PEEKARKITINTSHIEYET 106
Cdd:PRK05506 29 TCGSVDDGKSTL---IGRLLYD---SK-MIFEDqlaalerdskkvgtqgdeIDLAllvdglAAEREQGITIDVAYRYFAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 107 ANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELvem 186
Cdd:PRK05506 102 PKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFD--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 187 EIREllDFYDFN-----GDETPI----IRGSALAAAEGRDPELGANAVLELMaavdETIPEPTRDLDKPFLMPIEDV--- 254
Cdd:PRK05506 179 EIVA--DYRAFAaklglHDVTFIpisaLKGDNVVTRSARMPWYEGPSLLEHL----ETVEIASDRNLKDFRFPVQYVnrp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 255 ---FsiagRGtvVTGRIEQGKVNVGDdlEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGALLRglKREDVERGQVLCK 331
Cdd:PRK05506 253 nldF----RG--FAGTVASGVVRPGD--EVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLAR 322
|
330
....*....|....*
gi 224008444 332 PGSI-STAKKFEAEI 345
Cdd:PRK05506 323 ADNRpEVADQFDATV 337
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
51-345 |
2.38e-14 |
|
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: 74.33 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 51 TIGHVDHGKTTLtqaITKVLsekgWSKAMSYED------------------IDRA------PEEKARKITINTSHIEYET 106
Cdd:TIGR02034 5 TCGSVDDGKSTL---IGRLL----HDTKQIYEDqlaalerdskkhgtqggeIDLAllvdglQAEREQGITIDVAYRYFST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 107 ANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELvem 186
Cdd:TIGR02034 78 DKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFE--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 187 EIREllDFYDFNG-----DETPI----IRGSALAAAEGRDPELGANAVLELMAAVdetipEPTRDL-DKPFLMPIEDV-- 254
Cdd:TIGR02034 155 NIKK--DYLAFAEqlgfrDVTFIplsaLKGDNVVSRSESMPWYSGPTLLEILETV-----EVERDAqDLPLRFPVQYVnr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 255 ----FsiagRGtvVTGRIEQGKVNVGDdlEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVgaLLRgLKRE-DVERGQVL 329
Cdd:TIGR02034 228 pnldF----RG--YAGTIASGSVHVGD--EVVVLPSGRSSRVARIVTFDGDLEQARAGQAV--TLT-LDDEiDISRGDLL 296
|
330
....*....|....*..
gi 224008444 330 CKPGSI-STAKKFEAEI 345
Cdd:TIGR02034 297 AAADSApEVADQFAATL 313
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
48-173 |
4.57e-14 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 74.22 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAItkvLSEKGWSKAM-SYED----IDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADY 122
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERI---LFYTGKIHKMgEVEDgttvTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDF 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 224008444 123 VKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLvVFLNKCD 173
Cdd:PRK13351 87 TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMD 136
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
51-345 |
8.61e-14 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 73.02 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 51 TIGHVDHGKTTLtqaITKVLsekgWSKAMSYED------------------IDRA------PEEKARKITINTSHIEYET 106
Cdd:PRK05124 32 TCGSVDDGKSTL---IGRLL----HDTKQIYEDqlaslhndskrhgtqgekLDLAllvdglQAEREQGITIDVAYRYFST 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 107 ANRHYGHIDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVFLNKCDMVDDEELLELvem 186
Cdd:PRK05124 105 EKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFE--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 187 EIREllDFYDFNGDETPI--IRGSALAAAEG--------RDPELGANAVLELMaavdETIPEPTRDLDKPFLMPIEDV-- 254
Cdd:PRK05124 182 RIRE--DYLTFAEQLPGNldIRFVPLSALEGdnvvsqseSMPWYSGPTLLEVL----ETVDIQRVVDAQPFRFPVQYVnr 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 255 -------FSiagrGTVVTGRieqgkVNVGDDLEVV--GFNHNAKTTCTgvemFKKLLDYGMAGDnvgALLRGLKRE-DVE 324
Cdd:PRK05124 256 pnldfrgYA----GTLASGV-----VKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGE---AITLVLEDEiDIS 319
|
330 340
....*....|....*....|..
gi 224008444 325 RGQVLCKPGS-ISTAKKFEAEI 345
Cdd:PRK05124 320 RGDLLVAADEaLQAVQHASADV 341
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
51-173 |
2.79e-13 |
|
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: 71.20 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 51 TI-GHVDHGKTTLTQAI--TKVLS-EKGwskamsyedidrapeekarKIT--INTSHIEYEtanrhyGH----IDCPGHA 120
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIrkTNVAAgEAG-------------------GITqhIGAYQVETN------GGkitfLDTPGHE 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 224008444 121 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCD 173
Cdd:COG0532 63 AFTAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
48-239 |
9.62e-13 |
|
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: 66.40 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI---TKVLSEKGWSKAMsyedIDRAPEEKARKITI--NTSHIEYETANRH---YGHIDCPGH 119
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKEQV----LDSMDLERERGITIkaQAVRLFYKAKDGEeylLNLIDTPGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 120 ADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMpKLVVFLNKCDMVDDEELLELVemEIRELLDFydfng 199
Cdd:cd01890 78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAADPDRVKQ--EIEDVLGL----- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 224008444 200 DETPIIRGSalaAAEGrdpeLGANAVLElmaAVDETIPEP 239
Cdd:cd01890 150 DASEAILVS---AKTG----LGVEDLLE---AIVERIPPP 179
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
247-330 |
2.25e-12 |
|
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: 62.28 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 247 FLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTtcTGVEMFKKLLDYGMAGDNVGalLRGLKREDVERG 326
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRV--TSIERFHEEVDEAKAGDIVG--IGILGVKDILTG 76
|
....
gi 224008444 327 QVLC 330
Cdd:cd01342 77 DTLT 80
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
45-210 |
1.29e-11 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 66.39 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 45 PHVNIgtIGHVDHGKTTLTQAITKvlsekgwskamsyediDRAPEEKARKITINTS----HIEYETANRHYGHIDCPGHA 120
Cdd:CHL00189 245 PIVTI--LGHVDHGKTTLLDKIRK----------------TQIAQKEAGGITQKIGayevEFEYKDENQKIVFLDTPGHE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 121 DYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCDMVDDEELlelvemEIRELLDFYDFN-- 198
Cdd:CHL00189 307 AFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTE------RIKQQLAKYNLIpe 379
|
170
....*....|....
gi 224008444 199 --GDETPIIRGSAL 210
Cdd:CHL00189 380 kwGGDTPMIPISAS 393
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
340-425 |
3.70e-11 |
|
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: 59.71 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 340 KFEAEIYCLsqdegGRHTPFFSNYRPQFFFRTADVTG---------DLKLREGT--EMVMPGDNTTLDVELITPVPIEAG 408
Cdd:cd01513 5 KFDAKVIVL-----EHPKPIRPGYKPVMDVGTAHVPGriakllskeDGKTKEKKppDSLQPGENGTVEVELQKPVVLERG 79
|
90 100
....*....|....*....|...
gi 224008444 409 ------LRFNMREGGRTVGTGIV 425
Cdd:cd01513 80 kefptlGRFALRDGGRTVGAGLI 102
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
246-330 |
4.99e-11 |
|
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: 58.68 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 246 PFLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLEVVgfnhNAKTTCT--GVEMFKKLLDYGMAGDNVGALLRGLKREDV 323
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVM----PSNETATvkSIEIDDEPVDWAVAGDNVTLTLTGIDPNHL 76
|
....*..
gi 224008444 324 ERGQVLC 330
Cdd:cd16267 77 RVGSILC 83
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
48-173 |
5.56e-11 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 61.90 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLT-----QAITKVLSEKGWSKAMSYEDIDRapEEKARKITINTSHIEYETAN-RHYGH----IDCP 117
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRYTDTRK--DEQERGISIKSNPISLVLEDsKGKSYliniIDTP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 224008444 118 GHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCD 173
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLP-MVLVINKID 134
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
43-173 |
1.14e-10 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 63.53 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 43 DKPHV--NIGTIGHVDHGKTTLTQA-ITK--VLSEKGWSKAmSYEDIDraPEEKARKITINTS----HIEYETANRHYGH 113
Cdd:PTZ00416 14 DNPDQirNMSVIAHVDHGKSTLTDSlVCKagIISSKNAGDA-RFTDTR--ADEQERGITIKSTgislYYEHDLEDGDDKQ 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 114 ------IDCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEHIL---LAKQVgmpKLVVFLNKCD 173
Cdd:PTZ00416 91 pflinlIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVLrqaLQERI---RPVLFINKVD 155
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
246-330 |
1.32e-10 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 57.49 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 246 PFLMPIEDVFSiaGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTT---CTGVEMfkkllDYGMAGDNVGALLRGLKRED 322
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTgiyIDEEEV-----DSAKPGENVKLKLKGVEEED 73
|
....*...
gi 224008444 323 VERGQVLC 330
Cdd:cd04089 74 ISPGFVLC 81
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
246-330 |
4.69e-10 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 55.97 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 246 PFLMPIEDVFSiAGRGTVVTGRIEQGKVNVGDDLEVVGFNHNAKTTCTGVEMFKKlLDYGMAGDNVGALLRGLKREDVER 325
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78
|
....*
gi 224008444 326 GQVLC 330
Cdd:cd03698 79 GDILS 83
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
48-173 |
3.14e-09 |
|
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: 57.50 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAI------TKVLSE-KGWSKAMsyediDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHA 120
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEvHGGGATM-----DWMEQERERGITIQSAATTCFWKDHRINIIDTPGHV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 224008444 121 DYVKNMITGAAQMDGGILVVAATDGPMPQT----REhillAKQVGMPKlVVFLNKCD 173
Cdd:cd01886 76 DFTIEVERSLRVLDGAVAVFDAVAGVQPQTetvwRQ----ADRYGVPR-IAFVNKMD 127
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
247-329 |
7.57e-09 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 52.61 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 247 FLMPIEDVFSIAGRGTVVTGRIEQGKVNVGDDLeVVGFNHNAK---TTCTGVEMFKKLLDYGMAGDNVGALLRGLKREDV 323
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADGKfrpVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*.
gi 224008444 324 ERGQVL 329
Cdd:cd03694 80 RKGMVL 85
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
30-174 |
4.46e-08 |
|
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: 54.14 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 30 RRTFAaagdkfnrdkphvnigTIGHVDHGKTTLTQ-------AIT---KVLSEKGWSKAMSyediDRAPEEKARKITINT 99
Cdd:cd04169 2 RRTFA----------------IISHPDAGKTTLTEklllfggAIQeagAVKARKSRKHATS----DWMEIEKQRGISVTS 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224008444 100 SHIEYETANRHYGHIDCPGHADYVKN---MITGAaqmDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCDM 174
Cdd:cd04169 62 SVMQFEYKGCVINLLDTPGHEDFSEDtyrTLTAV---DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
47-173 |
4.61e-08 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 52.37 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 47 VNIGTIGHVDHGKTTLTQAITKVlseKGwSKAMSYEDIDRapeekarkiTINTSHIEYETANRHYGHIDCPGHADYVK-- 124
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---KG-SITEYYPGTTR---------NYVTTVIEEDGKTYKFNLLDTAGQEDYDAir 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 224008444 125 ----NMITGAAQM-DGGILVVAATDGPMPQTREHILLAKQvGMPkLVVFLNKCD 173
Cdd:TIGR00231 69 rlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHHADS-GVP-IILVGNKID 120
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
52-210 |
4.31e-07 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 49.38 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 52 IGHVDHGKTTLTQAITkvlsekgwskamsYEDIDRAPEEKARKITINTSHIEYETANRHYGHIDCPGHADYVKNMITGAA 131
Cdd:cd00882 3 VGRGGVGKSSLLNALL-------------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 132 QM-----DGGILVVAATDGPMPQTREHILLAKQVGMPK-LVVFLNKCDMVDDEEllelvemEIRELLDFYDFNGDETPII 205
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDLLEERE-------VEELLRLEELAKILGVPVF 142
|
....*
gi 224008444 206 RGSAL 210
Cdd:cd00882 143 EVSAK 147
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
43-173 |
1.14e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 50.88 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 43 DKPH--VNIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYEDIDRAPEEKARKITINTSHIE--YETANRHYGH----- 113
Cdd:PLN00116 14 DKKHniRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITIKSTGISlyYEMTDESLKDfkger 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224008444 114 ---------IDCPGHADYvKNMITGAAQM-DGGILVVAATDGPMPQTrEHIL---LAKQVgmpKLVVFLNKCD 173
Cdd:PLN00116 94 dgneylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVLrqaLGERI---RPVLTVNKMD 161
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
251-329 |
6.63e-06 |
|
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: 43.82 E-value: 6.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224008444 251 IEDVFSIAGRgTVVTGRIEQGKVNVGDDLeVVGFNHnakTTCTGVEMFKKLLDYGMAGDNVGALLRGlkREDVERGQVL 329
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-KGDKGV---ALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
52-173 |
1.05e-05 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 47.89 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 52 IGHVDHGKTTLTQAI--TKVLSEK--GWSKAMSYEDIDRAPEEKARKITINTSHIEYETANRHYghIDCPGHADYVKNMI 127
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIrgTAVVKKEagGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTNLRK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 224008444 128 TGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCD 173
Cdd:TIGR00491 88 RGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKID 132
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
53-173 |
5.71e-05 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 45.17 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 53 GHVDHGKTTLTQAI--TKVLS-EKGwskamsyedidrapeekarKIT--INTSHIEYETANRHYGH-------------- 113
Cdd:PRK04004 13 GHVDHGKTTLLDKIrgTAVAAkEAG-------------------GITqhIGATEVPIDVIEKIAGPlkkplpiklkipgl 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224008444 114 --IDCPGHADYVKNMITGAAQMDGGILVVAATDGPMPQTREHILLAKQVGMPkLVVFLNKCD 173
Cdd:PRK04004 74 lfIDTPGHEAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTP-FVVAANKID 134
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
247-329 |
2.62e-04 |
|
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: 39.47 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 247 FLMPIEDV--FSIAGRGtvVTGRIEQGKVNVGDdlEVVGFNHNAKTTCTGVEMFKKLLDYGMAGDNVGalLRgLKRE-DV 323
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGD--EVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVT--LT-LEDEiDV 73
|
....*.
gi 224008444 324 ERGQVL 329
Cdd:cd03695 74 SRGDLI 79
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
48-174 |
3.20e-03 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 38.81 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224008444 48 NIGTIGHVDHGKTTLTQAITKVLSEKGWSKAMSYedIDRAPEEKArkiTINTSHIEYET---------ANRHYGH----- 113
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLN--LFRHKHEVE---SGRTSSVSNDIlgfdsdgevVNYPDNHlgeld 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224008444 114 -------------IDCPGHADYVKNMITG--AAQMDGGILVVAATDGPMPQTREHILLAKQVGMPKLVVfLNKCDM 174
Cdd:cd04165 76 veiceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDM 150
|
|
| |
