|
Name |
Accession |
Description |
Interval |
E-value |
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
40-437 |
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: 767.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 40 AAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCP 119
Cdd:COG0050 4 EKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 120 GHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGF 199
Cdd:COG0050 84 GHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 200 DGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGE 279
Cdd:COG0050 164 PGDDTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 280 ELEIVGHNSTpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRH 359
Cdd:COG0050 244 EVEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRH 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324761 360 SGFGENYRPQMFIRTADVTVVMRFPKEVEdhsMqVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE 437
Cdd:COG0050 323 TPFFNGYRPQFYFRTTDVTGVITLPEGVE---M-VMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
40-437 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 766.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 40 AAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCP 119
Cdd:PRK00049 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 120 GHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGF 199
Cdd:PRK00049 84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 200 DGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGE 279
Cdd:PRK00049 164 PGDDTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 280 ELEIVGHNSTpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRH 359
Cdd:PRK00049 244 EVEIVGIRDT-QKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRH 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324761 360 SGFGENYRPQMFIRTADVTVVMRFPKEVEdhsMqVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE 437
Cdd:PRK00049 323 TPFFNGYRPQFYFRTTDVTGVIELPEGVE---M-VMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVTKIIE 396
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
42-437 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 742.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 42 FDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGH 121
Cdd:PRK12735 6 FERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 122 ADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDG 201
Cdd:PRK12735 86 ADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 202 DNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEEL 281
Cdd:PRK12735 166 DDTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 282 EIVGHNSTpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRHSG 361
Cdd:PRK12735 246 EIVGIKET-QKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTP 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324761 362 FGENYRPQMFIRTADVTVVMRFPKEVEdhsMqVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE 437
Cdd:PRK12735 325 FFNGYRPQFYFRTTDVTGTIELPEGVE---M-VMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE 396
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
40-437 |
0e+00 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 718.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 40 AAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCP 119
Cdd:PRK12736 4 EKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 120 GHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGF 199
Cdd:PRK12736 84 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 200 DGDNAPIIMGSALCALEGRQPEigEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGE 279
Cdd:PRK12736 164 PGDDIPVIRGSALKALEGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 280 ELEIVGHNSTpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRH 359
Cdd:PRK12736 242 EVEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324761 360 SGFGENYRPQMFIRTADVTVVMRFPKEVEdhsmQVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE 437
Cdd:PRK12736 321 TPFFNNYRPQFYFRTTDVTGSIELPEGTE----MVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVTEILD 394
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
22-437 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 664.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 22 RLSSVISRTFSQTTTSYAAAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITIST 101
Cdd:PLN03127 35 SISAADDRQSPSPWWRSMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 102 AHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPE 181
Cdd:PLN03127 115 AHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 182 MLELVEMEMRELLNEYGFDGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISG 261
Cdd:PLN03127 195 LLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 262 RGTVVTGRVERGNLKKGEELEIVGHN-STPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKA 340
Cdd:PLN03127 275 RGTVATGRVEQGTIKVGEEVEIVGLRpGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 341 HTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVTVVMRFPKEVEdhsmQVMPGDNVEMECDLIHPTPLEVGQRFNI 420
Cdd:PLN03127 355 YKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVK----MVMPGDNVTAVFELISPVPLEPGQRFAL 430
|
410
....*....|....*..
gi 6324761 421 REGGRTVGTGLITRIIE 437
Cdd:PLN03127 431 REGGRTVGAGVVSKVLS 447
|
|
| tufA |
CHL00071 |
elongation factor Tu |
42-437 |
0e+00 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 662.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 42 FDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGH 121
Cdd:CHL00071 6 FERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 122 ADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDG 201
Cdd:CHL00071 86 ADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 202 DNAPIIMGSALCALEG--RQPEI--GEQA----IMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERG 273
Cdd:CHL00071 166 DDIPIVSGSALLALEAltENPKIkrGENKwvdkIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 274 NLKKGEELEIVGHNSTPLkTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSK 353
Cdd:CHL00071 246 TVKVGDTVEIVGLRETKT-TTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 354 EEGGRHSGFGENYRPQMFIRTADVTVVMRFPKEVEDHSMQ-VMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLI 432
Cdd:CHL00071 325 EEGGRHTPFFPGYRPQFYVRTTDVTGKIESFTADDGSKTEmVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVGAGVV 404
|
....*
gi 6324761 433 TRIIE 437
Cdd:CHL00071 405 SKILK 409
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
40-437 |
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: 645.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 40 AAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCP 119
Cdd:TIGR00485 4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 120 GHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGF 199
Cdd:TIGR00485 84 GHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 200 DGDNAPIIMGSALCALEGRqpEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGE 279
Cdd:TIGR00485 164 PGDDTPIIRGSALKALEGD--AEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 280 ELEIVGHNSTPlKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRH 359
Cdd:TIGR00485 242 EVEIVGLKDTR-KTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324761 360 SGFGENYRPQMFIRTADVTVVMRFPKEVEdhsmQVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE 437
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEGVE----MVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVSKILE 394
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
2-437 |
0e+00 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 552.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 2 SALLPRLLTRTAFKASGKLLRLSSVISRTFSQTTTSYAAAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFL 81
Cdd:PLN03126 35 SGKLKSLTLSSSFLSPFSTTTTSTSQRRRRSFTVRAARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 82 DYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQ 161
Cdd:PLN03126 115 KYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 162 VGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDGDNAPIIMGSALCALEG--RQPEI--GEQA----IMKLLDA 233
Cdd:PLN03126 195 VGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEAlmENPNIkrGDNKwvdkIYELMDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 234 VDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTPlKTTVTGIEMFRKELDSAMAGDN 313
Cdd:PLN03126 275 VDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETR-STTVTGVEMFQKILDEALAGDN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 314 AGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVT-VVMRFPKEVEDHSM 392
Cdd:PLN03126 354 VGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTgKVTSIMNDKDEESK 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 6324761 393 QVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE 437
Cdd:PLN03126 434 MVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVGAGVIQSIIE 478
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
47-241 |
2.33e-152 |
|
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: 429.70 E-value: 2.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 47 PHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIK 126
Cdd:cd01884 1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 127 NMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDGDNAPI 206
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 6324761 207 IMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTP 241
Cdd:cd01884 161 VRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
44-435 |
5.10e-88 |
|
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: 274.12 E-value: 5.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 44 RSKPHVNIGTIGHVDHGKTTL-------TAAIT-------KTLAAKGGANFLDYA-AIDKAPEERARGITISTAHVEYET 108
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDehiiekyEEEAEKKGKESFKFAwVMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 109 AKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLELVE 187
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 188 MEMRELLNEYGFDGDNAPIIMGSALCalegrqpeiGEQAIMK-----------LLDAVDEyIPTPERDLNKPFLMPVEDI 256
Cdd:COG5256 163 EEVSKLLKMVGYKVDKIPFIPVSAWK---------GDNVVKKsdnmpwyngptLLEALDN-LKEPEKPVDKPLRIPIQDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 257 FSISGRGTVVTGRVERGNLKKGEELEIVGHNstpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMV---LA 333
Cdd:COG5256 233 YSISGIGTVPVGRVETGVLKVGDKVVFMPAG---VVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVaghPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 334 KPGTVKahTKILASLYILskeeggRH-SGFGENYRPQMFIRTADVTVVM---------RFPKEVEDHSMQVMPGDNVEME 403
Cdd:COG5256 310 NPPTVA--EEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVACTFvelvskldpRTGQVKEENPQFLKTGDAAIVK 381
|
410 420 430
....*....|....*....|....*....|....*....
gi 6324761 404 CDLIHPTPLE-------VGqRFNIREGGRTVGTGLITRI 435
Cdd:COG5256 382 IKPTKPLVIEkfkefpqLG-RFAIRDMGQTVAAGVVLDV 419
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
46-240 |
2.48e-87 |
|
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: 264.00 E-value: 2.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 46 KPHVNIGTIGHVDHGKTTLTAAITKTLAA---KGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHA 122
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAiskRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 123 DYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVqHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDGD 202
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGV-PIIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324761 203 NAPIIMGSALCALegrqpeigeqAIMKLLDAVDEYIPT 240
Cdd:pfam00009 160 FVPVVPGSALKGE----------GVQTLLDALDEYLPS 187
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
44-435 |
1.10e-81 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 257.93 E-value: 1.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 44 RSKPHVNIGTIGHVDHGKTTL-------TAAI--------TKTLAAKGGANFlDYAAI-DKAPEERARGITISTAHVEYE 107
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIdehiieelREEAKEKGKESF-KFAWVmDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 108 TAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATD--GQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLE 184
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 185 LVEMEMRELLNEYGFDGDNAPIIMGSALCalegrqpeiGEQAIMK-----------LLDAVDEyIPTPERDLNKPFLMPV 253
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPDDIPFIPVSAFE---------GDNVVKKsenmpwyngptLLEALDN-LKPPEKPTDKPLRIPI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 254 EDIFSISGRGTVVTGRVERGNLKKGEELEIVghnstPLKTT--VTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMV 331
Cdd:PRK12317 231 QDVYSISGVGTVPVGRVETGVLKVGDKVVFM-----PAGVVgeVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 332 ---LAKPGTVkAHTkILASLYILskeeggRH-SGFGENYRPQMFIRTADVTV-VMRFPKEVEDHSMQVM--------PGD 398
Cdd:PRK12317 306 cghPDNPPTV-AEE-FTAQIVVL------QHpSAITVGYTPVFHAHTAQVACtFEELVKKLDPRTGQVAeenpqfikTGD 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 6324761 399 NVEMEcdlIHPT-PL------EVGQ--RFNIREGGRTVGTGLITRI 435
Cdd:PRK12317 378 AAIVK---IKPTkPLviekvkEIPQlgRFAIRDMGQTIAAGMVIDV 420
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
49-432 |
1.78e-72 |
|
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: 239.43 E-value: 1.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 49 VNIGTIGHVDHGKTTLTAAITktlaakgGANfldyaaIDKAPEERARGITI--STAHVEYEtAKRHYSHVDCPGHADYIK 126
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALT-------GID------TDRLKEEKKRGITIdlGFAYLPLP-DGRRLGFVDVPGHEKFIK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 127 NMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIdDPEMLELVEMEMRELLNEYGFdgDNAPI 206
Cdd:COG3276 67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLV-DEEWLELVEEEIRELLAGTFL--EDAPI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 207 ImgsALCALEGrqpeigeQAIMKLLDAVDEYI-PTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVG 285
Cdd:COG3276 144 V---PVSAVTG-------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 286 HNstpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILskeeggrhSGFGEN 365
Cdd:COG3276 214 SG---KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL--------PSAPRP 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324761 366 YRPQMFIR----TADVTVVMRF--PKEVEdhsmqvmPGDN--VEMECDliHPTPLEVGQRFNIREGG--RTVGTGLI 432
Cdd:COG3276 283 LKHWQRVHlhhgTAEVLARVVLldREELA-------PGEEalAQLRLE--EPLVAARGDRFILRDYSprRTIGGGRV 350
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
50-241 |
5.89e-62 |
|
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: 198.67 E-value: 5.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMI 129
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 130 TGAAQMDGAIIVVAATDGQMPQTREHLLLARQvGVQHIVVFVNKVDTIdDPEMLELVEMEMRELLNEYGF---DGDNAPI 206
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 6324761 207 IMGSALcalegrqpeIGEqAIMKLLDAVDEYIPTP 241
Cdd:cd00881 159 IPISAL---------TGE-GIEELLDAIVEHLPPP 183
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
44-432 |
5.87e-60 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 201.90 E-value: 5.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 44 RSKPHVNIGTIGHVDHGKTTLTAAITKTL--------------AAKGGANFLDYA-AIDKAPEERARGITISTAHVEYET 108
Cdd:PTZ00141 3 KEKTHINLVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAwVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 109 AKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMP-------QTREHLLLARQVGVQHIVVFVNKVD--TID- 178
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDdkTVNy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 179 DPEMLELVEMEMRELLNEYGFDGDNAPIIMGSALcalegrqpeIGEQAIMK-----------LLDAVDEYIPtPERDLNK 247
Cdd:PTZ00141 163 SQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGW---------QGDNMIEKsdnmpwykgptLLEALDTLEP-PKRPVDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 248 PFLMPVEDIFSISGRGTVVTGRVERGNLKKGeelEIVGHNSTPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLK 327
Cdd:PTZ00141 233 PLRLPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 328 RGMVL--AKPGTVKAHTKILASLYILSkeeggrHSG-FGENYRPQMFIRTADVT---------VVMRFPKEVEDHSMQVM 395
Cdd:PTZ00141 310 RGYVAsdSKNDPAKECADFTAQVIVLN------HPGqIKNGYTPVLDCHTAHIAckfaeieskIDRRSGKVLEENPKAIK 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 6324761 396 PGDN--VEMEcdlihPT-PLEVGQ--------RFNIREGGRTVGTGLI 432
Cdd:PTZ00141 384 SGDAaiVKMV-----PTkPMCVEVfneypplgRFAVRDMKQTVAVGVI 426
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
49-347 |
7.69e-55 |
|
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: 191.63 E-value: 7.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 49 VNIGTIGHVDHGKTTLTAAITKTlaakgganfldyaAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNM 128
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGI-------------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 129 ITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDpEMLELVEMEMRELLNEYGFDgDNAPIIM 208
Cdd:TIGR00475 68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIFL-KNAKIFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 209 GSalcALEGRQPEIGEQAIMKLLDAVDeyiptpERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNS 288
Cdd:TIGR00475 146 TS---AKTGQGIGELKKELKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINH 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324761 289 tplKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGT--------VKAHTKILAS 347
Cdd:TIGR00475 217 ---EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDpklrvvvkFIAEVPLLEL 280
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
47-338 |
4.17e-51 |
|
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: 177.55 E-value: 4.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 47 PHVNIGTIGHVDHGKTTLTAAITKTLaakgganfldyaaIDKAPEERARGITISTAHVEYETAK---------------- 110
Cdd:TIGR03680 3 PEVNIGMVGHVDHGKTTLTKALTGVW-------------TDTHSEELKRGISIRLGYADAEIYKcpecdgpecyttepvc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 111 ----------RHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDG-QMPQTREHLLLARQVGVQHIVVFVNKVDTIDD 179
Cdd:TIGR03680 70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDLVSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 180 PEMLELVEmEMRELLNeyGFDGDNAPIIMGSALCALEgrqpeigeqaIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSI 259
Cdd:TIGR03680 150 EKALENYE-EIKEFVK--GTVAENAPIIPVSALHNAN----------IDALLEAIEKFIPTPERDLDKPPLMYVARSFDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 260 SGRGT--------VVTGRVERGNLKKGEELEIV------GHNST---PLKTTVTGIEMFRKELDSAMAGDNAGV------ 316
Cdd:TIGR03680 217 NKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpgikveKGGKTkwePIYTEITSLRAGGYKVEEARPGGLVGVgtkldp 296
|
330 340
....*....|....*....|...
gi 6324761 317 -LLRGirrDQLKrGMVLAKPGTV 338
Cdd:TIGR03680 297 aLTKA---DALA-GQVVGKPGTL 315
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
43-338 |
2.77e-49 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 172.73 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 43 DRSKPHVNIGTIGHVDHGKTTLTAAITKTLAakgganfldyaaiDKAPEERARGITISTAHVE--------------YET 108
Cdd:PRK04000 4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatirkcpdceepeaYTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 109 AK------------RHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDG-QMPQTREHLLLARQVGVQHIVVFVNKVD 175
Cdd:PRK04000 71 EPkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 176 TIDDPEMLELVEmEMRELLNeyGFDGDNAPIIMGSALcalegrqpeiGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVED 255
Cdd:PRK04000 151 LVSKERALENYE-QIKEFVK--GTVAENAPIIPVSAL----------HKVNIDALIEAIEEEIPTPERDLDKPPRMYVAR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 256 IFSISGRGT--------VVTGRVERGNLKKGEELEI------VGHNST---PLKTTVTGIEMFRKELDSAMAGDNAGV-- 316
Cdd:PRK04000 218 SFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIrpgikvEEGGKTkwePITTKIVSLRAGGEKVEEARPGGLVGVgt 297
|
330 340
....*....|....*....|....*..
gi 6324761 317 -----LLRGirrDQLkRGMVLAKPGTV 338
Cdd:PRK04000 298 kldpsLTKA---DAL-AGSVAGKPGTL 320
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
249-336 |
8.59e-49 |
|
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: 161.15 E-value: 8.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 249 FLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKR 328
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKET-LKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79
|
....*...
gi 6324761 329 GMVLAKPG 336
Cdd:cd03697 80 GMVLAKPG 87
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
44-337 |
1.08e-48 |
|
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: 171.17 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 44 RSKPHVNIGTIGHVDHGKTTLTAAITKTLAakgganfldyaaiDKAPEERARGITISTAHVE--------------YETA 109
Cdd:COG5257 1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWT-------------DRHSEELKRGITIRLGYADatfykcpnceppeaYTTE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 110 K------------RHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDG--QmPQTREHLLLARQVGVQHIVVFVNKVD 175
Cdd:COG5257 68 PkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcpQ-PQTKEHLMALDIIGIKNIVIVQNKID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 176 TIDDPEMLELVEmEMRELLNeyGFDGDNAPIIMGSAlcalegrQPEIGeqaIMKLLDAVDEYIPTPERDLNKPFLMPVED 255
Cdd:COG5257 147 LVSKERALENYE-QIKEFVK--GTVAENAPIIPVSA-------QHKVN---IDALIEAIEEEIPTPERDLSKPPRMLVAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 256 IFSISGRGT--------VVTGRVERGNLKKGEELEIV------GHNST---PLKTTVTGIEMFRKELDSAMAGdnaGVLL 318
Cdd:COG5257 214 SFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpgikveKGGKTkyePITTTVVSLRAGGEEVEEAKPG---GLVA 290
|
330 340
....*....|....*....|....*.
gi 6324761 319 RG-------IRRDQLkRGMVLAKPGT 337
Cdd:COG5257 291 VGtkldpslTKSDSL-VGSVAGKPGT 315
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
50-212 |
6.57e-48 |
|
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: 163.43 E-value: 6.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTA-------AITK-TL-------AAKGGANFlDYA-AIDKAPEERARGITISTAHVEYETAKRHY 113
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGhllyklgGVDKrTIekyekeaKEMGKESF-KYAwVLDKLKEERERGVTIDVGLAKFETEKYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 114 SHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQ-------MPQTREHLLLARQVGVQHIVVFVNKVDTIDDP---EML 183
Cdd:cd01883 80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEfeagfekGGQTREHALLARTLGVKQLIVAVNKMDDVTVNwsqERY 159
|
170 180
....*....|....*....|....*....
gi 6324761 184 ELVEMEMRELLNEYGFDGDNAPIIMGSAL 212
Cdd:cd01883 160 DEIKKKVSPFLKKVGYNPKDVPFIPISGF 188
|
|
| EFTU_III |
cd03707 |
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ... |
339-432 |
1.39e-47 |
|
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: 158.06 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 339 KAHTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVTVVMRFPKEVEdhsmQVMPGDNVEMECDLIHPTPLEVGQRF 418
Cdd:cd03707 1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVE----MVMPGDNVKMTVELIHPIALEEGLRF 76
|
90
....*....|....
gi 6324761 419 NIREGGRTVGTGLI 432
Cdd:cd03707 77 AIREGGRTVGAGVV 90
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
44-435 |
8.04e-46 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 164.49 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 44 RSKPHVNIGTIGHVDHGKTTLTAAITKTL--------------AAKGGANFLDYA-AIDKAPEERARGITISTAHVEYET 108
Cdd:PLN00043 3 KEKVHINIVVIGHVDSGKSTTTGHLIYKLggidkrvierfekeAAEMNKRSFKYAwVLDKLKAERERGITIDIALWKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 109 AKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMP-------QTREHLLLARQVGVQHIVVFVNKVDTID--- 178
Cdd:PLN00043 83 TKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 179 DPEMLELVEMEMRELLNEYGFDGDNAPIImgsALCALEG-----RQPEIGEQAIMKLLDAVDEyIPTPERDLNKPFLMPV 253
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGdnmieRSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 254 EDIFSISGRGTVVTGRVERGNLKKGeelEIVGHNSTPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVL- 332
Cdd:PLN00043 239 QDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 333 -AKPGTVKAHTKILASLYILSkeeggrHSG-FGENYRPQMFIRTADVTVVM---------RFPKEVEDHSMQVMPGDNVE 401
Cdd:PLN00043 316 nSKDDPAKEAANFTSQVIIMN------HPGqIGNGYAPVLDCHTSHIAVKFaeiltkidrRSGKELEKEPKFLKNGDAGF 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 6324761 402 MECDLIHPTPLEVGQ------RFNIREGGRTVGTGLITRI 435
Cdd:PLN00043 390 VKMIPTKPMVVETFSeypplgRFAVRDMRQTVAVGVIKSV 429
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
53-336 |
1.89e-44 |
|
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: 160.25 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 53 TIGHVDHGKTTLT---------------AAITKTlAAKGGANFLDYA-AIDKAPEERARGITISTAHVEYETAKRHYSHV 116
Cdd:COG2895 22 TCGSVDDGKSTLIgrllydtksifedqlAALERD-SKKRGTQEIDLAlLTDGLQAEREQGITIDVAYRYFSTPKRKFIIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 117 DCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLELVEMEMRELLN 195
Cdd:COG2895 101 DTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADYRAFAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 196 EYGFDGDNA-PIimgSalcALEG-----RQPEI----GEqAIMKLLDAVdeyiPTPERDLNKPFLMPVEDI--FSISGRG 263
Cdd:COG2895 181 KLGLEDITFiPI---S---ALKGdnvveRSENMpwydGP-TLLEHLETV----EVAEDRNDAPFRFPVQYVnrPNLDFRG 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 264 tvVTGRVERGNLKKGEELEIVGHNSTplkTTVTGIEMFRKELDSAMAGDNAGVLLrgirRDQL--KRGMVLAKPG 336
Cdd:COG2895 250 --YAGTIASGTVRVGDEVVVLPSGKT---STVKSIVTFDGDLEEAFAGQSVTLTL----EDEIdiSRGDVIVAAD 315
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
43-437 |
1.29e-43 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 160.10 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 43 DRSKPHVNIGTIGHVDHGKTTLTAA-ITKTLAAKGGANfldYAAIDKAPEERARGIT--ISTA----------HVE---- 105
Cdd:COG5258 117 EKDPEHIVVGVAGHVDHGKSTLVGTlVTGKLDDGNGGT---RSFLDVQPHEVERGLSadLSYAvygfdddgpvRMKnplr 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 106 -------YETAKRHYSHVDCPGHADYIKNMITG--AAQMDGAIIVVAATDGQMPQTREHL--LLARQVGVqhiVVFVNKV 174
Cdd:COG5258 194 ktdrarvVEESDKLVSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLgiLLAMDLPV---IVAITKI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 175 DTIDDpEMLELVEMEMRELLNEYG---------FDGDNA---------PIIMGSALcALEGrqpeigeqaiMKLLDAVDE 236
Cdd:COG5258 271 DKVDD-ERVEEVEREIENLLRIVGrtplevesrHDVDAAieeingrvvPILKTSAV-TGEG----------LDLLDELFE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 237 YIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELeIVGHNSTP--LKTTVTGIEMFRKELDSAMAGDNA 314
Cdd:COG5258 339 RLPKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDEL-LIGPTKDGsfREVEVKSIEMHYHRVDKAEAGRIV 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 315 GVLLRGIRRDQLKRGMVLAKPGT-VKAHTKILASLYILSkeeggrH-SGFGENYRPQMFIRTADVTVvmRFPKEVEDhsm 392
Cdd:COG5258 418 GIALKGVEEEELERGMVLLPRDAdPKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAV--RFEPIDKG--- 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 6324761 393 QVMPGDN--VEMECdLIHPTPLEVGQRFNIREgGRTVGTGLITRIIE 437
Cdd:COG5258 487 YLLPGDSgrVRLRF-KYRPYYVEEGQRFVFRE-GRSKGVGTVTDILD 531
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
337-435 |
1.37e-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: 142.79 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 337 TVKAHTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVTV-VMRF-----PKEVEDHSMQVMPGDNVEMECDLIHPT 410
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkFVELlhkldPGGVSENPEFVMPGDNVIVTVELIKPI 80
|
90 100
....*....|....*....|....*
gi 6324761 411 PLEVGQRFNIREGGRTVGTGLITRI 435
Cdd:pfam03143 81 ALEKGQRFAIREGGRTVAAGVVTEI 105
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
51-212 |
4.35e-40 |
|
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: 141.20 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 51 IGTIGHVDHGKTTLTAAITktlaakgGANfldyaaIDKAPEERARGITI--STAHVEYETAKRhYSHVDCPGHADYIKNM 128
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALT-------GIE------TDRLPEEKKRGITIdlGFAYLDLPDGKR-LGFIDVPGHEKFVKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 129 ITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIdDPEMLELVEMEMRELLNEYGFdgDNAPIIM 208
Cdd:cd04171 68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLV-DEDRLELVEEEILELLAGTFL--ADAPIFP 144
|
....
gi 6324761 209 GSAL 212
Cdd:cd04171 145 VSSV 148
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
51-348 |
3.29e-37 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 143.27 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 51 IGTIGHVDHGKTTLTAAITktlaakgGANfldyaaIDKAPEERARGITISTAHVEY-ETAKRHYSHVDCPGHADYIKNMI 129
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAIT-------GVN------ADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 130 TGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLElVEMEMRELLNEYGFDGdnAPIIMG 209
Cdd:PRK10512 70 AGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAE--AKLFVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 210 SALCalegrqpeigEQAIMKLLDAVDEyIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNsT 289
Cdd:PRK10512 147 AATE----------GRGIDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN-K 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 290 PLKttVTGIEMFRKELDSAMAGDNAGVLLRG-IRRDQLKRGMVLAKPGTVKAHTKILASL 348
Cdd:PRK10512 215 PMR--VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGDWLLADAPPEPFTRVIVEL 272
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
26-353 |
7.64e-36 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 137.44 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 26 VISRtfsQTTtsyaaafdrskphVNIGTIGHVDHGKTTLTAAIT--KTLAAKgganfldyaaidkapEERARGITIstaH 103
Cdd:PTZ00327 28 VISR---QAT-------------INIGTIGHVAHGKSTVVKALSgvKTVRFK---------------REKVRNITI---K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 104 VEYETAK------------------------------------RHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDG 147
Cdd:PTZ00327 74 LGYANAKiykcpkcprptcyqsygsskpdnppcpgcghkmtlkRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 148 -QMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEmEMRELLNeyGFDGDNAPIIMGSalcalegrqpeigeqA 226
Cdd:PTZ00327 154 cPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYE-EIRNFVK--GTIADNAPIIPIS---------------A 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 227 IMKL-LDAVDEY----IPTPERDLNKPFLM----------PVEDIFSIsgRGTVVTGRVERGNLKKGEELEIV-GHNS-- 288
Cdd:PTZ00327 216 QLKYnIDVVLEYictqIPIPKRDLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISkd 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 289 -------TPLKTTVTGIEMFRKELDSAMAGDNAGVllrGI-------RRDQLkRGMVLAKPGTV-KAHTKILASLYILSK 353
Cdd:PTZ00327 294 sggeftcRPIRTRIVSLFAENNELQYAVPGGLIGV---GTtidptltRADRL-VGQVLGYPGKLpEVYAEIEIQYYLLRR 369
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
50-312 |
8.44e-35 |
|
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: 136.28 E-value: 8.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAI---TKTLAAKGGanfLDYAAIDKAPEERARGITIS---TAhVEYETAKRHYshVDCPGHAD 123
Cdd:TIGR01394 3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEA---VAERVMDSNDLERERGITILaknTA-IRYNGTKINI--VDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 124 Y------IKNMItgaaqmDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTID-DPEMlelVEMEMRELLNE 196
Cdd:TIGR01394 77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSaRPDE---VVDEVFDLFAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 197 YGFDGD--NAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGN 274
Cdd:TIGR01394 147 LGADDEqlDFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGT 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6324761 275 LKKGEELEIVGHNSTPLKTTVTGIEMF----RKELDSAMAGD 312
Cdd:TIGR01394 227 VKKGQQVALMKRDGTIENGRISKLLGFegleRVEIDEAGAGD 268
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
53-203 |
9.26e-34 |
|
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: 125.76 E-value: 9.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 53 TIGHVDHGKTTLT---------------AAITKTLAAKGGANFLDYA-AIDKAPEERARGITISTAHVEYETAKRHYSHV 116
Cdd:cd04166 4 TCGSVDDGKSTLIgrllydsksifedqlAALERSKSSGTQGEKLDLAlLVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 117 DCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLELVEMEMRELLN 195
Cdd:cd04166 84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAA 163
|
170
....*....|....*....
gi 6324761 196 EYGF-----------DGDN 203
Cdd:cd04166 164 SLGIeditfipisalEGDN 182
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
49-243 |
2.91e-33 |
|
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: 123.92 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 49 VNIGTIGHVDHGKTTLTAAITKTLAakgganfldyaaiDKAPEERARGITI-------------------STAHVEYE-- 107
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWT-------------VRHKEELKRNITIklgyanakiykcpncgcprPYDTPECEcp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 108 ------TAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDG--QmPQTREHLLLARQVGVQHIVVFVNKVDTIDD 179
Cdd:cd01888 68 gcggetKLVRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcpQ-PQTSEHLAALEIMGLKHIIILQNKIDLVKE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324761 180 PEMLELVEmEMRELLNeyGFDGDNAPIIMGSALCalegrqpeigEQAIMKLLDAVDEYIPTPER 243
Cdd:cd01888 147 EQALENYE-QIKEFVK--GTIAENAPIIPISAQL----------KYNIDVLCEYIVKKIPTPPR 197
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
50-312 |
7.15e-31 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 125.13 E-value: 7.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAITKTlaakGGAnFLDYAAI-----DKAPEERARGITIS---TAhVEYETAKRHYshVDCPGH 121
Cdd:COG1217 8 NIAIIAHVDHGKTTLVDALLKQ----SGT-FRENQEVaervmDSNDLERERGITILaknTA-VRYKGVKINI--VDTPGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 122 ADY------IKNMItgaaqmDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTID-DPEmlELVEmEMRELL 194
Cdd:COG1217 80 ADFggeverVLSMV------DGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVV-INKIDRPDaRPD--EVVD-EVFDLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 195 NEYGFDGD--NAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVER 272
Cdd:COG1217 150 IELGATDEqlDFPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6324761 273 GNLKKGEELEIVGHNSTPLKTTVTGIEMF----RKELDSAMAGD 312
Cdd:COG1217 230 GTIKKGQQVALIKRDGKVEKGKITKLFGFegleRVEVEEAEAGD 273
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
49-224 |
4.82e-29 |
|
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: 112.46 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 49 VNIGTIGHVDHGKTTLTAAITKTLAAkgganfldyAAIDKAPEERARGITI----STAHVEYETAKRHYSH--------- 115
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLdlgfSSFEVDKPKHLEDNENpqienyqit 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 116 -VDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTIDDPEMlELVEMEMRELL 194
Cdd:cd01889 72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEER-KRKIEKMKKRL 149
|
170 180 190
....*....|....*....|....*....|...
gi 6324761 195 NE--YGFDGDNAPIImgsALCALEGR-QPEIGE 224
Cdd:cd01889 150 QKtlEKTRLKDSPII---PVSAKPGEgEAELGG 179
|
|
| mtEFTU_III |
cd03706 |
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ... |
339-435 |
5.02e-28 |
|
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: 106.16 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 339 KAHTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVTVVMRFPKEVEdhsMqVMPGDNVEMECDLIHPTPLEVGQRF 418
Cdd:cd03706 1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKE---M-VMPGEDTSVKLTLLKPMVLEKGQRF 76
|
90
....*....|....*..
gi 6324761 419 NIREGGRTVGTGLITRI 435
Cdd:cd03706 77 TLREGGRTIGTGVVTKL 93
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
53-336 |
6.90e-28 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 116.18 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 53 TIGHVDHGKTTLT---------------AAITKTLAAKG-GANFLDYA-AIDKAPEERARGITISTAHVEYETAKRHYSH 115
Cdd:PRK05506 29 TCGSVDDGKSTLIgrllydskmifedqlAALERDSKKVGtQGDEIDLAlLVDGLAAEREQGITIDVAYRYFATPKRKFIV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 116 VDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLELVEMEMRELL 194
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAFA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 195 NEYGFdGDNAPIIMGsalcALEG--------RQPEIGEQAIMKLLDAVdeYIPTPERDlnKPFLMPVE-------DIFSI 259
Cdd:PRK05506 189 AKLGL-HDVTFIPIS----ALKGdnvvtrsaRMPWYEGPSLLEHLETV--EIASDRNL--KDFRFPVQyvnrpnlDFRGF 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324761 260 SgrGTVVTGRVergnlKKGEELEIVGHNSTplkTTVTGIEMFRKELDSAMAGDNAGVLLrgirRDQL--KRGMVLAKPG 336
Cdd:PRK05506 260 A--GTVASGVV-----RPGDEVVVLPSGKT---SRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIdiSRGDMLARAD 324
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
53-335 |
5.64e-27 |
|
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: 111.70 E-value: 5.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 53 TIGHVDHGKTTLT---------------AAITKTLAAKGG-ANFLDYA-AIDKAPEERARGITISTAHVEYETAKRHYSH 115
Cdd:TIGR02034 5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKHGTqGGEIDLAlLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 116 VDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLELVEMEMRELL 194
Cdd:TIGR02034 85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDyDEEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 195 NEYGFDgDNAPIIMGsalcALEG--------RQPEIGEQAIMKLLDAVDeyiptPERDLN-KPFLMPVEDI----FSISG 261
Cdd:TIGR02034 165 EQLGFR-DVTFIPLS----ALKGdnvvsrseSMPWYSGPTLLEILETVE-----VERDAQdLPLRFPVQYVnrpnLDFRG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 262 -RGTVVTGRVergnlKKGEELEIVGHNSTplkTTVTGIEMFRKELDSAMAGDNAGVLLRgiRRDQLKRGMVLAKP 335
Cdd:TIGR02034 235 yAGTIASGSV-----HVGDEVVVLPSGRS---SRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAA 299
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
50-317 |
2.49e-25 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 108.80 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLT-----AA--ITKTLAakGGANFLDYaaidkAPEERARGITISTAHV----EYETAKRHYSHVDC 118
Cdd:PRK07560 22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA--GEQLALDF-----DEEEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 119 PGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHiVVFVNKVD------TIDDPEMLE-LVEM--E 189
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKP-VLFINKVDrlikelKLTPQEMQQrLLKIikD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 190 MRELLNEYG---------FDGDNAPIIMGSAL-----------------------CaLEGRQPEIGEQAIMK--LLDAVD 235
Cdd:PRK07560 174 VNKLIKGMApeefkekwkVDVEDGTVAFGSALynwaisvpmmqktgikfkdiidyY-EKGKQKELAEKAPLHevVLDMVV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 236 EYIPTP-------------------------ERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTP 290
Cdd:PRK07560 253 KHLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKN 332
|
330 340
....*....|....*....|....*....
gi 6324761 291 lKTTVTGIEM--FRKELDSAMAGDNAGVL 317
Cdd:PRK07560 333 -RVQQVGIYMgpEREEVEEIPAGNIAAVT 360
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
50-312 |
7.14e-24 |
|
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: 104.59 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLT-------AAITKTLAakGGANFLDYAAidkapEERARGITISTAHV----EYETAKRHYSHVDC 118
Cdd:TIGR00490 21 NIGIVAHIDHGKTTLSdnllagaGMISEELA--GQQLYLDFDE-----QEQERGITINAANVsmvhEYEGNEYLINLIDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 119 PGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHiVVFVNKVDTIDDPEMLELVEMEMR------- 191
Cdd:TIGR00490 94 PGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKP-VLFINKVDRLINELKLTPQELQERfikiite 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 192 -----------ELLNEYGFDGDNAPIIMGSAL-----------------------CAlEGRQPEIGEQAIMK--LLDAVD 235
Cdd:TIGR00490 173 vnklikamapeEFRDKWKVRVEDGSVAFGSAYynwaisvpsmkktgigfkdiykyCK-EDKQKELAKKSPLHqvVLDMVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 236 EYIPTP-----ER--------------------DLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNStp 290
Cdd:TIGR00490 252 RHLPSPieaqkYRipviwkgdlnsevgkamlncDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKA-- 329
|
330 340
....*....|....*....|....*.
gi 6324761 291 lKTTVTGIEMF----RKELDSAMAGD 312
Cdd:TIGR00490 330 -KARIQQVGVYmgpeRVEVDEIPAGN 354
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
53-312 |
7.90e-23 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 100.37 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 53 TIGHVDHGKTTL-------TAAI-----------TKTLAAKGGAnfLDYAA-IDKAPEERARGITISTAHVEYETAKRHY 113
Cdd:PRK05124 32 TCGSVDDGKSTLigrllhdTKQIyedqlaslhndSKRHGTQGEK--LDLALlVDGLQAEREQGITIDVAYRYFSTEKRKF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 114 SHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTID-DPEMLELVEMEMRE 192
Cdd:PRK05124 110 IIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 193 LLNEYGFDGDnapiIMGSALCALEG--------RQPEIGEQAIMKLLdavdEYIPTPERDLNKPFLMPVEDI-------- 256
Cdd:PRK05124 190 FAEQLPGNLD----IRFVPLSALEGdnvvsqseSMPWYSGPTLLEVL----ETVDIQRVVDAQPFRFPVQYVnrpnldfr 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324761 257 -FSisgrGTVVTGRVergnlKKGEELEIV--GHNStplktTVTGIEMFRKELDSAMAGD 312
Cdd:PRK05124 262 gYA----GTLASGVV-----KVGDRVKVLpsGKES-----NVARIVTFDGDLEEAFAGE 306
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
50-241 |
7.42e-22 |
|
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: 92.66 E-value: 7.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITI---STAhVEYETAKrhYSHVDCPGHADY-- 124
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITIlakNTA-ITYKDTK--INIIDTPGHADFgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 125 ----IKNMItgaaqmDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTID-DPEMlelVEMEMRELLNEYGF 199
Cdd:cd01891 81 everVLSMV------DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDaRPEE---VVDEVFDLFLELNA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6324761 200 DGD--NAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTP 241
Cdd:cd01891 151 TDEqlDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
50-312 |
1.98e-21 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 96.70 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMI 129
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 130 TGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTID-DPEMLelVEMEMRELLNEYGFDGD-NAPII 207
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGaRPDWV--VDQVFDLFVNLDATDEQlDFPIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 208 MGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHN 287
Cdd:PRK10218 164 YASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260
....*....|....*....|....*....
gi 6324761 288 ST----PLKTTVTGIEMFRKELDSAMAGD 312
Cdd:PRK10218 244 GKtrnaKVGKVLGHLGLERIETDLAEAGD 272
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
55-212 |
2.60e-21 |
|
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: 90.22 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 55 GHVDHGKTTLTAAITKTLAAKGganfldyaaidkapeeRARGIT--ISTAHVEYETAKRHYSHVDCPGHADYiKNMITGA 132
Cdd:cd01887 7 GHVDHGKTTLLDKIRKTNVAAG----------------EAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 133 AQM-DGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVDTIDDPEmlELVEMEMREL--LNEYGFD-GDNAPIIM 208
Cdd:cd01887 70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTE--ADPERVKNELseLGLVGEEwGGDVSIVP 146
|
....
gi 6324761 209 GSAL 212
Cdd:cd01887 147 ISAK 150
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
47-279 |
3.50e-21 |
|
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: 95.99 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 47 PHVNIgtIGHVDHGKTTLTAAITKTLAAKGganfldyaaidkapeeRARGIT--ISTAHVEYETAKRhYSHVDCPGHADY 124
Cdd:TIGR00487 88 PVVTI--MGHVDHGKTSLLDSIRKTKVAQG----------------EAGGITqhIGAYHVENEDGKM-ITFLDTPGHEAF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 125 IKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKvdtIDDPEM-LELVEMEmrelLNEYGFD--- 200
Cdd:TIGR00487 149 TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINK---IDKPEAnPDRVKQE----LSEYGLVped 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 201 -GDNAPIIMGSALCAlegrqpeigeQAIMKLLDA------VDEYIPTPERDLNKpflmPVEDIFSISGRGTVVTGRVERG 273
Cdd:TIGR00487 221 wGGDTIFVPVSALTG----------DGIDELLDMillqseVEELKANPNGQASG----VVIEAQLDKGRGPVATVLVQSG 286
|
....*.
gi 6324761 274 NLKKGE 279
Cdd:TIGR00487 287 TLRVGD 292
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
50-236 |
1.89e-20 |
|
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: 89.60 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLT-------AAITKTLAAKGGANFLDYAAIdkapeERARGITISTAHVEYETAKRHYSHVDCPGHA 122
Cdd:cd04168 1 NIGILAHVDAGKTTLTesllytsGAIRELGSVDKGTTRTDSMEL-----ERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 123 DYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIvVFVNKVDT--IDdpemLELVEMEMRELLneygfd 200
Cdd:cd04168 76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTI-IFVNKIDRagAD----LEKVYQEIKEKL------ 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324761 201 gDNAPIIM--GSALCALEGRqPEIGEQAIMKLLDAVDE 236
Cdd:cd04168 145 -SPDIVPMqkVGLYPNICDT-NNIDDEQIETVAEGNDE 180
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
50-241 |
3.17e-20 |
|
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: 88.83 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAA-------ITKTLAakGGANFLDYAaidkaPEERARGITI-STA---HVEYETAKRHYSH--- 115
Cdd:cd01885 2 NICIIAHVDHGKTTLSDSllasagiISEKLA--GKARYLDTR-----EDEQERGITIkSSAislYFEYEEEKMDGNDyli 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 116 --VDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVDTI-----DDPE-----ML 183
Cdd:cd01885 75 nlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVK-PVLVINKIDRLilelkLSPEeayqrLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324761 184 ELVE--------MEMRELLNE-YGFDGDNAPIIMGSalcALEGRQPEIGEQA-IMKLLDAVDEYIPTP 241
Cdd:cd01885 154 RIVEdvnaiietYAPEEFKQEkWKFSPQKGNVAFGS---ALDGWGFTIIKFAdIYAVLEMVVKHLPSP 218
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
263-333 |
1.58e-19 |
|
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: 82.31 E-value: 1.58e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324761 263 GTVVTGRVERGNLKKGEELEIVGHNS--TPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLA 333
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
249-334 |
3.94e-19 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 81.42 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 249 FLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNstpLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKR 328
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG---KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77
|
....*.
gi 6324761 329 GMVLAK 334
Cdd:cd03696 78 GFVLSE 83
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
54-312 |
8.60e-19 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 89.03 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 54 IGHVDHGKTTLTAAI---TKTLAAKG----GANFLDYAaidkaPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIK 126
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGAIHRIGevedGTTTMDFM-----PEERERGISITSAATTCEWKGHKINLIDTPGHVDFTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 127 NMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIvVFVNKVD--------TIDD------------------- 179
Cdd:PRK12740 76 EVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRI-IFVNKMDragadffrVLAQlqeklgapvvplqlpigeg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 180 -----------------------------PEMLELVEmEMRE------------LLNEYgFDGDN--------------- 203
Cdd:PRK12740 155 ddftgvvdllsmkayrydeggpseeieipAELLDRAE-EAREellealaefddeLMEKY-LEGEElseeeikaglrkatl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 204 ----APIIMGSALcalegrqPEIGeqaIMKLLDAVDEYIPTP-----------------ERDLNKPFLMPVEDIFSISGR 262
Cdd:PRK12740 233 ageiVPVFCGSAL-------KNKG---VQRLLDAVVDYLPSPlevppvdgedgeegaelAPDPDGPLVALVFKTMDDPFV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 263 GTVVTGRVERGNLKKGEELeivgHNSTPLKTT-VTGI-EMF---RKELDSAMAGD 312
Cdd:PRK12740 303 GKLSLVRVYSGTLKKGDTL----YNSGTGKKErVGRLyRMHgkqREEVDEAVAGD 353
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
246-331 |
2.82e-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: 79.15 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 246 NKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIV-GHNSTPLKTtvtgIEMFRKELDSAMAGDNAGVLLRGIRRD 324
Cdd:cd03693 2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFApAGVTGEVKS----VEMHHEPLEEAIPGDNVGFNVKGVSVK 77
|
....*..
gi 6324761 325 QLKRGMV 331
Cdd:cd03693 78 DIKRGDV 84
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
50-175 |
1.22e-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: 85.48 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAI---TKTLAAKG----GANFLDYaaidkAPEERARGITISTA--HVEYEtaKRHYSHVDCPG 120
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERIlfyTGAIHRIGevhdGNTVMDW-----MPEEQERGITITSAatTCEWK--GHKINIIDTPG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 121 HADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIvVFVNKVD 175
Cdd:COG0480 84 HVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRI-VFVNKMD 137
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
50-175 |
4.88e-17 |
|
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: 80.72 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAI---TKTLAAKG----GANFLDYAaidkaPEERARGITIST--AHVEYETAKRHYshVDCPG 120
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGrvedGNTVSDYD-----PEEKKRKMSIETsvAPLEWNGHKINL--IDTPG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 121 HADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIvVFVNKVD 175
Cdd:cd04170 74 YADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRI-IFINKMD 127
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
50-175 |
8.84e-17 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 82.69 E-value: 8.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAI---TKTLAAKG----GANFLDYaaidkAPEERARGITISTAHVEYETAKRHYSHVDCPGHA 122
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERIlfyTGKIHKMGevedGTTVTDW-----MPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6324761 123 DYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIvVFVNKVD 175
Cdd:PRK13351 85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRL-IFINKMD 136
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
53-278 |
1.95e-16 |
|
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: 81.21 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 53 TI-GHVDHGKTTLTAAITKTLAAKGganfldyaaidkapeErARGIT--ISTAHVEYEtaKRHYSHVDCPGHADYIKNMI 129
Cdd:COG0532 8 TVmGHVDHGKTSLLDAIRKTNVAAG---------------E-AGGITqhIGAYQVETN--GGKITFLDTPGHEAFTAMRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 130 TGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVDTID-DPEML--ELVEMEMreLLNEYGfdGDNaPI 206
Cdd:COG0532 70 RGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGaNPDRVkqELAEHGL--VPEEWG--GDT-IF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 207 IMGSalcALEGrqpeigeQAIMKLLDA------VDEYIPTPERD---------LNKpflmpvedifsisGRGTVVTGRVE 271
Cdd:COG0532 144 VPVS---AKTG-------EGIDELLEMillqaeVLELKANPDRPargtvieakLDK-------------GRGPVATVLVQ 200
|
....*..
gi 6324761 272 RGNLKKG 278
Cdd:COG0532 201 NGTLKVG 207
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
249-333 |
2.19e-16 |
|
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: 73.84 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 249 FLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGhnsTPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRrdQLKR 328
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP---KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75
|
....*
gi 6324761 329 GMVLA 333
Cdd:cd01342 76 GDTLT 80
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
249-333 |
9.12e-15 |
|
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: 69.17 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 249 FLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIvGHNSTP--LKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQL 326
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLL-GPDADGkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79
|
....*..
gi 6324761 327 KRGMVLA 333
Cdd:cd03694 80 RKGMVLV 86
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
50-241 |
1.64e-14 |
|
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: 71.41 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAI---TKTLAAKGGAN-FLDYAAIdkapeERARGITI--STAHVEY--ETAKRHYSH-VDCPG 120
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLlelTGTVSEREMKEqVLDSMDL-----ERERGITIkaQAVRLFYkaKDGEEYLLNlIDTPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 121 HADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVqHIVVFVNKVDTID-DPEMlelVEMEMRELLneyGF 199
Cdd:cd01890 77 HVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNL-EIIPVINKIDLPAaDPDR---VKQEIEDVL---GL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324761 200 DGDNAPIImgsalCALEGrqpeigeQAIMKLLDAVDEYIPTP 241
Cdd:cd01890 150 DASEAILV-----SAKTG-------LGVEDLLEAIVERIPPP 179
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
50-175 |
3.63e-14 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 74.70 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLT------AAITKTLAAkGGANFLdyaaiDKAPEERARGITI-STA---HVEY---ETAKRHYS-- 114
Cdd:PTZ00416 21 NMSVIAHVDHGKSTLTdslvckAGIISSKNA-GDARFT-----DTRADEQERGITIkSTGislYYEHdleDGDDKQPFli 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 115 -HVDCPGHADYiKNMITGAAQM-DGAIIVVAATDGQMPQTrEHLLlaRQVGVQHI--VVFVNKVD 175
Cdd:PTZ00416 95 nLIDSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
47-234 |
1.93e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 72.56 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 47 PHVNIgtIGHVDHGKTTLTAAITKTLAAkgganfldyaaidkapEERARGITISTA----HVEYETAKRHYSHVDCPGHA 122
Cdd:CHL00189 245 PIVTI--LGHVDHGKTTLLDKIRKTQIA----------------QKEAGGITQKIGayevEFEYKDENQKIVFLDTPGHE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 123 DYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVDTIDDPemLELVEMEMRE--LLNEYGfd 200
Cdd:CHL00189 307 AFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQLAKynLIPEKW-- 381
|
170 180 190
....*....|....*....|....*....|....
gi 6324761 201 GDNAPIIMGSALcalegrqpeiGEQAIMKLLDAV 234
Cdd:CHL00189 382 GGDTPMIPISAS----------QGTNIDKLLETI 405
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
339-432 |
5.54e-13 |
|
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: 64.72 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 339 KAHTKILASLYILSKEEGGRHsgfgeNYRPQMFIRTADVTV-VMRFPKEV------EDHSMQVMPGDNVEMECDLIHPTP 411
Cdd:cd01513 1 QAVWKFDAKVIVLEHPKPIRP-----GYKPVMDVGTAHVPGrIAKLLSKEdgktkeKKPPDSLQPGENGTVEVELQKPVV 75
|
90 100
....*....|....*....|....*..
gi 6324761 412 LEVG------QRFNIREGGRTVGTGLI 432
Cdd:cd01513 76 LERGkefptlGRFALRDGGRTVGAGLI 102
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
50-185 |
1.16e-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: 63.83 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLT-----AAITKTLAAKGGANFLDYaaIDKAPEERARGITI-STAHVEYETAKRHYSHV----DCP 119
Cdd:cd04167 2 NVCIAGHLHHGKTSLLdmlieQTHKRTPSVKLGWKPLRY--TDTRKDEQERGISIkSNPISLVLEDSKGKSYLiniiDTP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324761 120 GHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVqHIVVFVNKVDTIddpeMLEL 185
Cdd:cd04167 80 GHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGL-PMVLVINKIDRL----ILEL 140
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
248-332 |
2.26e-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: 59.45 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 248 PFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTplkTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLK 327
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET---ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77
|
....*
gi 6324761 328 RGMVL 332
Cdd:cd16267 78 VGSIL 82
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
248-333 |
3.66e-11 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 59.05 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 248 PFLMPVEDIFSiSGRGTVVTGRVERGNLKKGEELEIVGHNSTplkTTVTGIEM-FRKELDSAMAGDNAGVLLRGIRRDQL 326
Cdd:cd03698 1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQD---AEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76
|
....*..
gi 6324761 327 KRGMVLA 333
Cdd:cd03698 77 QPGDILS 83
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
248-332 |
9.02e-11 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 57.88 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 248 PFLMPVEDIFSisGRGTVVTGRVERGNLKKGEELeIVGHNSTPLKttVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLK 327
Cdd:cd04089 1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKL-VLMPNKTKVE--VTGIYIDEEEVDSAKPGENVKLKLKGVEEEDIS 75
|
....*
gi 6324761 328 RGMVL 332
Cdd:cd04089 76 PGFVL 80
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
50-175 |
1.78e-10 |
|
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: 61.35 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLT-------AAITKTLAAKGGAnfldyAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHA 122
Cdd:cd01886 1 NIGIIAHIDAGKTTTTerilyytGRIHKIGEVHGGG-----ATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6324761 123 DYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIvVFVNKVD 175
Cdd:cd01886 76 DFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRI-AFVNKMD 127
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
50-175 |
2.42e-10 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 62.82 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLtaaiTKTLAAKGGANFLDYAA----IDKAPEERARGITISTAHVE--YETAKRHYSH-------- 115
Cdd:PLN00116 21 NMSVIAHVDHGKSTL----TDSLVAAAGIIAQEVAGdvrmTDTRADEAERGITIKSTGISlyYEMTDESLKDfkgerdgn 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324761 116 ------VDCPGHADYiKNMITGAAQM-DGAIIVVAATDGQMPQTrEHLLlaRQVGVQHI--VVFVNKVD 175
Cdd:PLN00116 97 eylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQALGERIrpVLTVNKMD 161
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
54-189 |
2.96e-10 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 60.69 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 54 IGHVDHGKTTLT-------AAITK--TLAAKGGANFL--DYAAIdkapeERARGITISTAHVEYETAKRHYSHVDCPGHA 122
Cdd:cd04169 8 ISHPDAGKTTLTeklllfgGAIQEagAVKARKSRKHAtsDWMEI-----EKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324761 123 DYIKN---MITGAaqmDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVD-TIDDP-EMLELVEME 189
Cdd:cd04169 83 DFSEDtyrTLTAV---DSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDrEGRDPlELLDEIENE 150
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
49-212 |
8.58e-09 |
|
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: 54.30 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 49 VNIGTIGHVDHGKTTLTAAITKTlaakgganfldyaaiDKAPEERARGIT--ISTAHVEYETAKRHYSHVDCPGHADYIK 126
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGN---------------KGSITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 127 ------NMITGAAQM-DGAIIVVAATDGQMPQTREhLLLARQVGVQhIVVFVNKVDTIDdpemlELVEMEMRELLNEYGF 199
Cdd:TIGR00231 67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKE-IIHHADSGVP-IILVGNKIDLKD-----ADLKTHVASEFAKLNG 139
|
170
....*....|...
gi 6324761 200 dgdnAPIIMGSAL 212
Cdd:TIGR00231 140 ----EPIIPLSAE 148
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
54-212 |
6.15e-08 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 52.07 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 54 IGHVDHGKTTLTaaitktlaakggaNFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMITGAA 133
Cdd:cd00882 3 VGRGGVGKSSLL-------------NALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 134 QM-----DGAIIVVAATDGQMPQTREHLLLARQVGVQ-HIVVFVNKVDTIDDPEMLELVEMEMRELLNeygfdgdNAPII 207
Cdd:cd00882 70 RLllrgaDLILLVVDSTDRESEEDAKLLILRRLRKEGiPIILVGNKIDLLEEREVEELLRLEELAKIL-------GVPVF 142
|
....*
gi 6324761 208 MGSAL 212
Cdd:cd00882 143 EVSAK 147
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
253-333 |
1.04e-07 |
|
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: 49.22 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 253 VEDIFSISGRgTVVTGRVERGNLKKGEELeIVGHNSTplktTVTGIEMFRKELDSAMAGDNAGVLLRGIRRdqLKRGMVL 332
Cdd:cd16265 5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-KGDKGVA----LIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76
|
.
gi 6324761 333 A 333
Cdd:cd16265 77 E 77
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
54-202 |
1.54e-07 |
|
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: 53.67 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 54 IGHVDHGKTTLTAAITKTLAAKG---------GANFLDYAAIDKAPEERARGITIstahveyETAKRHYSHVDCPGHADY 124
Cdd:TIGR00491 10 LGHVDHGKTTLLDKIRGTAVVKKeaggitqhiGASEVPTDVIEKICGDLLKSFKI-------KLKIPGLLFIDTPGHEAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 125 IKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVDTI------DDPEMLELVEM---------- 188
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTP-FVVAANKIDRIpgwkshEGYPFLESINKqeqrvrqnld 161
|
170
....*....|....*...
gi 6324761 189 ----EMRELLNEYGFDGD 202
Cdd:TIGR00491 162 kqvyNLVIQLAEQGFNAE 179
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
55-177 |
6.01e-07 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 51.72 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 55 GHVDHGKTTLTAAITKTLAAKG---------GANFLDYAAIDKapeerargitISTAHVEYETAKRHYS---HVDCPGHA 122
Cdd:PRK04004 13 GHVDHGKTTLLDKIRGTAVAAKeaggitqhiGATEVPIDVIEK----------IAGPLKKPLPIKLKIPgllFIDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6324761 123 DYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTI 177
Cdd:PRK04004 83 AFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKIDRI 136
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
50-238 |
1.64e-06 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 48.31 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAItktLaakgGANFLdyaaidkaPEerarGITISTA---HVEYETaKRHYSHVDCPG------ 120
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNAL---L----GEEVL--------PT----GVTPTTAvitVLRYGL-LKGVVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 121 -HADYIKNMItgaAQMDGAIIVVAAtdgQMPQT---REHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEmEMRELLNE 196
Cdd:cd09912 62 hHTEITESFL---PRADAVIFVLSA---DQPLTeseREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLE-YSREELGV 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324761 197 YGFDGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYI 238
Cdd:cd09912 135 LELGGGEPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHL 176
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
249-318 |
1.29e-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: 40.24 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324761 249 FLMPVEDI--FSISGRGtvVTGRVERGNLKKGEELEIVGHNSTplkTTVTGIEMFRKELDSAMAGDNAGVLL 318
Cdd:cd03695 1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTVLPSGKT---SRVKSIVTFDGELDSAGAGEAVTLTL 67
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
263-312 |
4.61e-04 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 39.09 E-value: 4.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6324761 263 GTVVTGRVERGNLKKGEELEIVGHNSTPLKTTVTGIEMFRK----ELDSAMAGD 312
Cdd:cd03691 15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGlervEVEEAEAGD 68
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
116-202 |
1.13e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.41 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 116 VDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVDTI-------DDPEMLE---- 184
Cdd:PRK14845 531 IDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILRQYKTP-FVVAANKIDLIpgwniseDEPFLLNfneq 609
|
90 100
....*....|....*....|....*..
gi 6324761 185 ----LVEMEMR--EL---LNEYGFDGD 202
Cdd:PRK14845 610 dqhaLTELEIKlyELigkLYELGFDAD 636
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
50-175 |
1.82e-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: 39.58 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 50 NIGTIGHVDHGKTTLTAAITKTLA--AKGGANfldyAAIDKAPEERARGIT--ISTAHVEYETAKR----HYSH------ 115
Cdd:cd04165 1 RVAVVGNVDAGKSTLLGVLTQGELdnGRGKAR----LNLFRHKHEVESGRTssVSNDILGFDSDGEvvnyPDNHlgeldv 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324761 116 ------------VDCPGHADYIKNMITG--AAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQhIVVFVNKVD 175
Cdd:cd04165 77 eiceksskvvtfIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKID 149
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
136-239 |
4.08e-03 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 38.82 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324761 136 DGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVfVNKVDTIDDPEMLELVEmEMRELLneygfdgDNAPIIMgsaLCAL 215
Cdd:COG1159 84 DVILFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA-EYSELL-------DFAEIVP---ISAL 151
|
90 100
....*....|....*....|....
gi 6324761 216 EGRQpeigeqaIMKLLDAVDEYIP 239
Cdd:COG1159 152 KGDN-------VDELLDEIAKLLP 168
|
|
| |
