|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
1-615 |
0e+00 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 1230.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALL 80
Cdd:PRK10512 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 81 VVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEVLAALDNYGFADTVLFVTAANEGRGIAELRAH 160
Cdd:PRK10512 81 VVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLREYGFAEAKLFVTAATEGRGIDALREH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 161 LQQLPARSHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALN 240
Cdd:PRK10512 161 LLQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 241 IAGDAEKEQLNRGDWLLSDAPMgEAFSRVIVSLALHAQLSQWQPLHIHHAASHVTGRVSLLEGGLAELIFDTPLWLADND 320
Cdd:PRK10512 241 IAGDAEKEQINRGDWLLADAPP-EPFTRVIVELQTHTPLTQWQPLHIHHAASHVTGRVSLLEDNLAELVLDTPLWLADND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 321 RLVLRDISARATLAGARVVTLKAPRRGKRKPDYLHWLSTLAAAQDDSAALAIHLERGAVNLPDFGWARQLNPLGMRQLIE 400
Cdd:PRK10512 320 RLVLRDISARNTLAGARVVMLNPPRRGKRKPEYLQWLAALARAQDDAEALALHLERGAVNLADFAWARQLNGEGMRALLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 401 QHGFIQAGDNLLSAPVAARWQRKILDTLATYHEQHRDEPGPGRERLRRMALPMEDEALVLMLIERMRDDGLIHSHHGWLH 480
Cdd:PRK10512 400 QPGYIQAGDSLLSAPVAARWQRKLLDTLATYHEQHRDEPGPGRERLRRMALPMEDEALVLLLIEKMRESGDIHSHHGWLH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 481 LPDHKAGFSDEQQAVWQKVEPLFGDEPWWVRDLAKETGTEEQLMRLVLRQAAQQGIITAIVKDRYYRNDRIVAFANMIRE 560
Cdd:PRK10512 480 LPDHKAGFSEEQQALWQKAEPLFGDEPWWVRDLAKETGTDEQAMRLTLRQAAQQGIITAIVKDRYYRNDRIVQFANMIRE 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 446504538 561 LDQERGSTCAADFRDRLNVGRKLAIQILEYFDRIGFTRRRGNDHLLRDALLFPQK 615
Cdd:PRK10512 560 LDQECGSTCAADFRDRLGVGRKLAIQILEYFDRIGFTRRRGNDHLLRDALLFPEK 614
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
1-608 |
0e+00 |
|
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: 789.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAGVGGIDHALL 80
Cdd:TIGR00475 1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAYFPLPD-YRLGFIDVPGHEKFISNAIAGGGGIDAALL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 81 VVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEVLAALDNYGFADTV-LFVTAANEGRGIAELRA 159
Cdd:TIGR00475 80 VVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAkIFKTSAKTGQGIGELKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 160 HLQQLPARSHAA--QHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRI 237
Cdd:TIGR00475 160 ELKNLLESLDIKriQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 238 ALNIAgDAEKEQLNRGdwLLSDAPMgEAFSRVIVSLALHAQLSQWQPLHIHHAASHVTGRVSLLEGGLAELIFDTPLWLA 317
Cdd:TIGR00475 240 ALNLM-DVEPESLKRG--LLILTPE-DPKLRVVVKFIAEVPLLELQPYHIAHGMSVTTGKISLLDKGIALLTLDAPLILA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 318 DNDRLVLRDiSARATLAGARVVTLkaPRRGKRKpdylHWLSTLAAAQDDSAALAIHLERGAVNLpDFGWARQLNPLGMRQ 397
Cdd:TIGR00475 316 KGDKLVLRD-SSGNFLAGARVLEP--PVRVKRK----AFIAELIKAGDSCYCIFLLLERGAVDL-GLEWFKQLTGILIMR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 398 LIEQHGFIQAGDNLLSAPVAARWQRKILDTLATyhEQHrDEPGPGRERLRRMALPMedEALVLMLIERMRDdglIHSHHG 477
Cdd:TIGR00475 388 LLLPPTTIRICGFGENIDFGEVEVKKILVKLGT--EQH-DVKGVDKERLERMASLN--EELLKTAIEKLIG---TYKIGG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 478 WLHLPDHKAGFSDEQQaVWQKVEPLFGDEPWWVRDLAKETGTEEQLMRLVLRQAAQQGIITAIVKDRYYRndrivafaNM 557
Cdd:TIGR00475 460 WLHIPDHKSDFEKEED-IWQKIKGTFGTKGAWVREFAEEVNGDEKVMLKRVRKAGHRGGETLIVKDRLLK--------KY 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 446504538 558 IRELDQERGSTCAADFRDRLNVGRKLAIQILEYFDRIGFTRRRGNDHLLRD 608
Cdd:TIGR00475 531 INELKEEGGTFNVQQARDKLGLGRKLLIQLLEYFDRLGFTRREGNDHRLRD 581
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
1-609 |
0e+00 |
|
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: 739.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALL 80
Cdd:COG3276 1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPLPDGRRLGFVDVPGHEKFIKNMLAGAGGIDLVLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 81 VVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEVLAALDNYGFADTVLFVTAANEGRGIAELRAH 160
Cdd:COG3276 81 VVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 161 LQQLPARSHA--AQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIA 238
Cdd:COG3276 161 LDALAAAVPArdADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 239 LNIAGdAEKEQLNRGDWLLSDAPMgEAFSRVIVSLAL----HAQLSQWQPLHIHHAASHVTGRVSLLEG--------GLA 306
Cdd:COG3276 241 LNLAG-VEKEEIERGDVLAAPGAL-RPTDRIDVRLRLlpsaPRPLKHWQRVHLHHGTAEVLARVVLLDReelapgeeALA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 307 ELIFDTPLWLADNDRLVLRDISARATLAGARVVTLKAPRRGKRKPDYLHWLSTLAAAQDDSA-ALAIHLERGAVNLPDFG 385
Cdd:COG3276 319 QLRLEEPLVAARGDRFILRDYSPRRTIGGGRVLDPNPPKRKRRSPERLAWLEALAKGDPAELlAALLALAPGGLSLAELA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 386 WARQLNPLGMRQLIEQ--HGFIQAGDN---LLSAPVAARWQRKILDTLATYHEQHRDEPGPGRERLRRMALPMEDEALVL 460
Cdd:COG3276 399 RLTGLSEEELAALLEElgARVVVLGGGdrlLVSAAALEALKERLLAALAEFHEKNPLRPGLSREELRRRLLPRLPEKLFD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 461 MLIERMRDDGLIHSHHGWLHLPDHKAGFSDEQQAVWQKVEPLFGDE---PWWVRDLAKETGTEEQLMRLVLRQAAQQGII 537
Cdd:COG3276 479 ALLEELLAEGELVLTGGWLHLPGHKVTLSAEEEALWQRLLPLLAAGgfpPPWLRELAAELGLEEEAVRELLRLLLRLGEL 558
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446504538 538 TAIVKDRYYRNDRIVAFANMIRELDQERGSTCAADFRDRLNVGRKLAIQILEYFDRIGFTRRRGNDHLLRDA 609
Cdd:COG3276 559 VKVVDDLFYLAAALAALAALLAALLAETGAAAAADRRDLLGGRRKLLLLLLEFFDRRRRRRRRGRRRRLRRD 630
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
2-171 |
7.95e-92 |
|
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: 280.65 E-value: 7.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALLV 81
Cdd:cd04171 1 IIGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPDGKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 82 VACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEVLAALDNYGFADTVLFVTAANEGRGIAELRAHL 161
Cdd:cd04171 81 VAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
|
170
....*....|
gi 446504538 162 QQLPARSHAA 171
Cdd:cd04171 161 DELAEPQSKD 170
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
2-167 |
6.84e-48 |
|
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: 165.55 E-value: 6.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNM 68
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGaidrrgtrketflDTLKEERERGITIKTGVVEFEWPK-RRINFIDTPGHEDFSKET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 69 LAGVGGIDHALLVVACDDGVMAQTREHLQILQLtGNLQLTVALTKADRVDEARIGEVREEVLAALDNYGF-----ADTVL 143
Cdd:cd00881 80 VRGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPI 158
|
170 180
....*....|....*....|....*
gi 446504538 144 FVTAANEGRGIAELRAHL-QQLPAR 167
Cdd:cd00881 159 IPISALTGEGIEELLDAIvEHLPPP 183
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
1-253 |
3.20e-41 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 157.02 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQA-ITG----------VNADRLPEEKKRGMTIDLGYA-YWPQPDG------------------ 50
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTlVTGklddgnggtrSFLDVQPHEVERGLSADLSYAvYGFDDDGpvrmknplrktdrarvve 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 51 ---RVLGFIDVPGHEKFLSNMLAGVGG--IDHALLVVACDDGVMAQTREHLQILQLTGnLQLTVALTKADRVDEARIGEV 125
Cdd:COG5258 203 esdKLVSFVDTVGHEPWLRTTIRGLVGqkLDYGLLVVAADDGPTHTTREHLGILLAMD-LPVIVAITKIDKVDDERVEEV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 126 REEVLAAL--------------DNYGFADTV------LFVTAANEGRGIAELRAHLQQLPARSHAAQHRFRLAIDRAFTV 185
Cdd:COG5258 282 EREIENLLrivgrtplevesrhDVDAAIEEIngrvvpILKTSAVTGEGLDLLDELFERLPKRATDEDEPFLMYIDRIYNV 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446504538 186 KGAGLVVTGTALSGEVNVGDTLWL----TGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:COG5258 362 TGVGTVVSGTVKSGKVEAGDELLIgptkDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKG-VEEEELERG 432
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
1-254 |
8.91e-38 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 145.07 E-value: 8.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAI---TGVNA-------------------------DRLPEEKKRGMTIDLGYAYWPQPDgRV 52
Cdd:PRK12317 7 LNLAVIGHVDHGKSTLVGRLlyeTGAIDehiieelreeakekgkesfkfawvmDRLKEERERGVTIDLAHKKFETDK-YY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 53 LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDD--GVMAQTREHLQILQLTGNLQLTVALTKADRV--DEARIGEVREE 128
Cdd:PRK12317 86 FTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVnyDEKRYEEVKEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 129 VLAALDNYGF-ADTVLFV-TAANEGRGIAE------------LRAHLQQLPARSHAAQHRFRLAIDRAFTVKGAGLVVTG 194
Cdd:PRK12317 166 VSKLLKMVGYkPDDIPFIpVSAFEGDNVVKksenmpwyngptLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVG 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 195 TALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRGD 254
Cdd:PRK12317 246 RVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRG-VGKKDIKRGD 304
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
1-239 |
1.71e-37 |
|
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: 144.04 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA---------------YWPQPDG----------RVLGF 55
Cdd:TIGR03680 5 VNIGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYAdaeiykcpecdgpecYTTEPVCpncgsetellRRVSF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 56 IDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEVLAALD 134
Cdd:TIGR03680 85 VDAPGHETLMATMLSGAALMDGALLVIAANEPCpQPQTKEHLMALEIIGIKNIVIVQNKIDLVSKEKALENYEEIKEFVK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 135 NYGFADTVLFVTAANEGRGIAELRAHLQ-QLPARSHAAQHRFRLAIDRAFTV--------KGAGLVVTGTALSGEVNVGD 205
Cdd:TIGR03680 165 GTVAENAPIIPVSALHNANIDALLEAIEkFIPTPERDLDKPPLMYVARSFDVnkpgtppeKLKGGVIGGSLIQGKLKVGD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446504538 206 TLWLT-GVN---------TPM--RVRSLHAQNQPTDHAYAGQRIAL 239
Cdd:TIGR03680 245 EIEIRpGIKvekggktkwEPIytEITSLRAGGYKVEEARPGGLVGV 290
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
1-157 |
2.53e-37 |
|
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: 136.89 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAI---TGVNA-------------DRLPEEKKRGMTIDLGYAYWPqPDGRVLGFIDVPGHEKF 64
Cdd:pfam00009 4 RNIGIIGHVDHGKTTLTDRLlyyTGAISkrgevkgegeaglDNLPEERERGITIKSAAVSFE-TKDYLINLIDTPGHVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 65 LSNMLAGVGGIDHALLVVACDDGVMAQTREHL-QILQLtgNLQLTVALTKADRVDEARIGEVREEVLAAL-DNYGFADTV 142
Cdd:pfam00009 83 VKEVIRGLAQADGAILVVDAVEGVMPQTREHLrLARQL--GVPIIVFINKMDRVDGAELEEVVEEVSRELlEKYGEDGEF 160
|
170
....*....|....*..
gi 446504538 143 LFV--TAANEGRGIAEL 157
Cdd:pfam00009 161 VPVvpGSALKGEGVQTL 177
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
1-254 |
7.78e-37 |
|
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: 142.38 E-value: 7.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAI---TGV-----------NA--------------DRLPEEKKRGMTIDLGYAYWpQPDGRV 52
Cdd:COG5256 8 LNLVVIGHVDHGKSTLVGRLlyeTGAidehiiekyeeEAekkgkesfkfawvmDRLKEERERGVTIDLAHKKF-ETDKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 53 LGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRV--DEARIGEVREEVL 130
Cdd:COG5256 87 FTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVnySEKRYEEVKEEVS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 131 AALDNYGF-ADTVLFV-TAANEGRGIAELRAH------------LQQLPARSHAAQHRFRLAIDRAFTVKGAGLVVTGTA 196
Cdd:COG5256 167 KLLKMVGYkVDKIPFIpVSAWKGDNVVKKSDNmpwyngptlleaLDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRV 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446504538 197 LSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRGD 254
Cdd:COG5256 247 ETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRG-VEKNDIKRGD 303
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
3-253 |
2.01e-35 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 137.77 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
Cdd:PRK12736 15 IGTIGHVDHGKTTLTAAITKVLAerglnqakdydsiDAAPEEKERGITINTAHVEY-ETEKRHYAHVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGF-ADTVLFV-- 145
Cdd:PRK12736 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLElVEMEVRELLSEYDFpGDDIPVIrg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 146 --TAANEGR-----GIAELRAHLQQ-LPARSHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMR 217
Cdd:PRK12736 174 saLKALEGDpkwedAIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQK 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 446504538 218 --VRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:PRK12736 254 tvVTGVEMFRKLLDEGQAGDNVGVLLRG-VDRDEVERG 290
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
3-253 |
3.56e-35 |
|
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: 137.22 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
Cdd:TIGR00485 15 VGTIGHVDHGKTTLTAAITTVLAkeggaaaraydqiDNAPEEKARGITINTAHVEY-ETETRHYAHVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGF-ADTVLFVTA 147
Cdd:TIGR00485 94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSQYDFpGDDTPIIRG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 148 ----ANEGRG-----IAELRAHLQQ-LPARSHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGV--NTP 215
Cdd:TIGR00485 174 salkALEGDAeweakILELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLkdTRK 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 446504538 216 MRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:TIGR00485 254 TTVTGVEMFRKELDEGRAGDNVGLLLRG-IKREEIERG 290
|
|
| tufA |
CHL00071 |
elongation factor Tu |
3-253 |
2.23e-34 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 135.09 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
Cdd:CHL00071 15 IGTIGHVDHGKTTLTAAITMTLAakggakakkydeiDSAPEEKARGITINTAHVEY-ETENRHYAHVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGFA-DTVLFVTA 147
Cdd:CHL00071 94 TGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLElVELEVRELLSKYDFPgDDIPIVSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 148 A------------NEGRG-------IAELRAHLQQ---LPARShaAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGD 205
Cdd:CHL00071 174 SallalealtenpKIKRGenkwvdkIYNLMDAVDSyipTPERD--TDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGD 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446504538 206 TLWLTGVN--TPMRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:CHL00071 252 TVEIVGLRetKTTTVTGLEMFQKTLDEGLAGDNVGILLRG-IQKEDIERG 300
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
1-136 |
9.42e-34 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 133.44 E-value: 9.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA---------------YWPQP----DG------RVLGF 55
Cdd:PRK04000 10 VNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYAdatirkcpdceepeaYTTEPkcpnCGsetellRRVSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 56 IDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLQILQLTGNLQLTVALTKADRVDearigevREEvlaALD 134
Cdd:PRK04000 90 VDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKIDLVS-------KER---ALE 159
|
..
gi 446504538 135 NY 136
Cdd:PRK04000 160 NY 161
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
3-253 |
1.44e-33 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 133.41 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
Cdd:PLN03127 64 VGTIGHVDHGKTTLTAAITKVLAeegkakavafdeiDKAPEEKARGITIATAHVEY-ETAKRHYAHVDCPGHADYVKNMI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVRE-EVLAALDNYGF-ADTVLFVT- 146
Cdd:PLN03127 143 TGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEmELRELLSFYKFpGDEIPIIRg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 147 ---AANEGR-------GIAELRAHLQQ-LPARSHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTP 215
Cdd:PLN03127 223 salSALQGTndeigknAILKLMDAVDEyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPG 302
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446504538 216 MRVRS----LHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:PLN03127 303 GPLKTtvtgVEMFKKILDQGQAGDNVGLLLRG-LKREDVQRG 343
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
3-253 |
8.56e-33 |
|
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: 130.27 E-value: 8.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYA-YwpQPDGRVLGFIDVPGHEKFLSNM 68
Cdd:COG0050 15 IGTIGHVDHGKTTLTAAITKVLAkkggakakaydqiDKAPEEKERGITINTSHVeY--ETEKRHYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 69 LAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGF-ADTVLFV- 145
Cdd:COG0050 93 ITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSKYGFpGDDTPIIr 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 146 ---TAANEGRGIAELRAHLQQL----------PARshAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGV 212
Cdd:COG0050 173 gsaLKALEGDPDPEWEKKILELmdavdsyipePER--DTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGI 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446504538 213 NTPMR--VRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:COG0050 251 RDTQKtvVTGVEMFRKLLDEGEAGDNVGLLLRG-IKREDVERG 292
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
3-212 |
1.18e-32 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 129.92 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNADRL-------------PEEKKRGMTIDLGYA-YwpQPDGRVLGFIDVPGHEKFLSNM 68
Cdd:PRK00049 15 VGTIGHVDHGKTTLTAAITKVLAKKGgaeakaydqidkaPEEKARGITINTAHVeY--ETEKRHYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 69 LAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGF-ADTVLFVT 146
Cdd:PRK00049 93 ITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSKYDFpGDDTPIIR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 147 ----AANEGRG-------IAELRAHLQQ---LPARshAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGV 212
Cdd:PRK00049 173 gsalKALEGDDdeewekkILELMDAVDSyipTPER--AIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI 250
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
3-239 |
8.15e-32 |
|
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: 127.65 E-value: 8.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA---YW-----PQPDG-----------------RVLGFID 57
Cdd:COG5257 8 IGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYAdatFYkcpncEPPEAyttepkcpncgsetellRRVSFVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 58 VPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEVLAALDNY 136
Cdd:COG5257 88 APGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 137 GFADTVLFVTAANEGRGIAELRAHLQQL---PARSHAAQhrFRLAIDRAFTV--------KGAGLVVTGTALSGEVNVGD 205
Cdd:COG5257 168 VAENAPIIPVSAQHKVNIDALIEAIEEEiptPERDLSKP--PRMLVARSFDVnkpgtppkDLKGGVIGGSLIQGVLKVGD 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446504538 206 TL-WLTGVNTP-----------MRVRSLHAQNQPTDHAYAGQRIAL 239
Cdd:COG5257 246 EIeIRPGIKVEkggktkyepitTTVVSLRAGGEEVEEAKPGGLVAV 291
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
3-138 |
3.31e-31 |
|
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: 120.38 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTID---LGYaywpQPDGRVLGFIDVPGHEKFLS 66
Cdd:cd01884 5 VGTIGHVDHGKTTLTAAITKVLAkkggakakkydeiDKAPEEKARGITINtahVEY----ETANRHYAHVDCPGHADYIK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446504538 67 NMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGF 138
Cdd:cd01884 81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLElVEMEVRELLSKYGF 153
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
175-257 |
7.67e-31 |
|
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: 115.32 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 175 FRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDaEKEQLNRGD 254
Cdd:cd03696 1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGV-DAKELERGF 79
|
...
gi 446504538 255 WLL 257
Cdd:cd03696 80 VLS 82
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
3-212 |
8.07e-31 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 124.57 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
Cdd:PRK12735 15 VGTIGHVDHGKTTLTAAITKVLAkkgggeakaydqiDNAPEEKARGITINTSHVEY-ETANRHYAHVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGE-VREEVLAALDNYGF-ADTVLFVT- 146
Cdd:PRK12735 94 TGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSKYDFpGDDTPIIRg 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446504538 147 ---AANEGRGIAELRAHLQQL----------PARshAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGV 212
Cdd:PRK12735 174 salKALEGDDDEEWEAKILELmdavdsyipePER--AIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGI 250
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
3-253 |
1.75e-30 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 125.11 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSNML 69
Cdd:PLN03126 84 IGTIGHVDHGKTTLTAALTMALAsmggsapkkydeiDAAPEERARGITINTATVEY-ETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVRE-EVLAALDNYGF---------A 139
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVElEVRELLSSYEFpgddipiisG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 140 DTVLFVTAANEG----RG-------IAELRAHLQQ-LPARSHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTL 207
Cdd:PLN03126 243 SALLALEALMENpnikRGdnkwvdkIYELMDAVDSyIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV 322
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446504538 208 WLTGVNTPMR--VRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:PLN03126 323 DIVGLRETRSttVTGVEMFQKILDEALAGDNVGLLLRG-IQKADIQRG 369
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
1-138 |
1.16e-28 |
|
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: 113.13 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 1 MIIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA----------YWPQPDG----------------RVLG 54
Cdd:cd01888 1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYAnakiykcpncGCPRPYDtpececpgcggetklvRHVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 55 FIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLQILQLTGNLQLTVALTKADRVDEARigevreevlaAL 133
Cdd:cd01888 81 FVDCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQ----------AL 150
|
....*
gi 446504538 134 DNYGF 138
Cdd:cd01888 151 ENYEQ 155
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
7-161 |
3.40e-25 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 103.21 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 7 GHVDHGKTTLLQAITGVNA----DRLPEEKKRGMTIDLGYA--YWPQPDGRVLG-----------FIDVPGHEKFLSNML 69
Cdd:cd01889 7 GHVDSGKTSLAKALSEIAStaafDKNPQSQERGITLDLGFSsfEVDKPKHLEDNenpqienyqitLVDCPGHASLIRTII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNlQLTVALTKADRVD----EARIGEVREEVLAALDNYGFADTVLFV 145
Cdd:cd01889 87 GGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCK-PLIVVLNKIDLIPeeerKRKIEKMKKRLQKTLEKTRLKDSPIIP 165
|
170
....*....|....*.
gi 446504538 146 TAANEGRGIAELRAHL 161
Cdd:cd01889 166 VSAKPGEGEAELGGEL 181
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
2-157 |
2.04e-24 |
|
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: 100.24 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAITGVNadrLPEEKKRGMTIDLGyAY---WPQPDGRVLgFIDVPGHEKFlSNMLA-GVGGIDH 77
Cdd:cd01887 2 VVTVMGHVDHGKTTLLDKIRKTN---VAAGEAGGITQHIG-AYqvpIDVKIPGIT-FIDTPGHEAF-TNMRArGASVTDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 78 ALLVVACDDGVMAQTREHLQILQlTGNLQLTVALTKADR--VDEARIGEVREEvLAALDNYG--FADTVLFV-TAANEGR 152
Cdd:cd01887 76 AILVVAADDGVMPQTIEAINHAK-AANVPIIVAINKIDKpyGTEADPERVKNE-LSELGLVGeeWGGDVSIVpISAKTGE 153
|
....*
gi 446504538 153 GIAEL 157
Cdd:cd01887 154 GIDDL 158
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
3-145 |
4.95e-22 |
|
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: 94.87 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLGYAYWpQPDGRVLG 54
Cdd:cd01883 2 LVVIGHVDAGKSTltghLLYKLGGVDKrtiekyekeakemgkesfkyawvlDKLKEERERGVTIDVGLAKF-ETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 55 FIDVPGHEKFLSNMLAGVGGIDHALLVVACDDG-------VMAQTREHLQILQLTGNLQLTVALTKADRV----DEARIG 123
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVtvnwSQERYD 160
|
170 180
....*....|....*....|...
gi 446504538 124 EVREEVLAALDNYGF-ADTVLFV 145
Cdd:cd01883 161 EIKKKVSPFLKKVGYnPKDVPFI 183
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
3-161 |
5.16e-22 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 94.56 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTL---------------LQAIT-----GVNA---------DRLPEEKKRGMTIDLGYAYWPQPDgRVL 53
Cdd:cd04166 2 FITCGSVDDGKSTLigrllydsksifedqLAALErskssGTQGekldlallvDGLQAEREQGITIDVAYRYFSTPK-RKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVD--EARIGEVREEVLA 131
Cdd:cd04166 81 IIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDydEEVFEEIKADYLA 160
|
170 180 190
....*....|....*....|....*....|
gi 446504538 132 ALDNYGFADTVLFVTAANEGRGIAELRAHL 161
Cdd:cd04166 161 FAASLGIEDITFIPISALEGDNVVSRSENM 190
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
3-256 |
6.57e-22 |
|
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: 98.62 E-value: 6.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTL---------------LQAITGVNADR-------------LPEEKKRGMTIDLGYAYWpQPDGRvlG 54
Cdd:COG2895 20 FITCGSVDDGKSTLigrllydtksifedqLAALERDSKKRgtqeidlalltdgLQAEREQGITIDVAYRYF-STPKR--K 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 55 FI--DVPGHEKFLSNMLAGVGGIDHALLVVacdD---GVMAQTREHLQILQLTGNLQLTVALTKADRVD--EARIGEVRE 127
Cdd:COG2895 97 FIiaDTPGHEQYTRNMVTGASTADLAILLI---DarkGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDysEEVFEEIVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 128 EVLAALDNYGFADTVLFVTAANEGRGIAE------------LRAHLQQLPARSHAAQHRFRLAI--------D-RAFtvk 186
Cdd:COG2895 174 DYRAFAAKLGLEDITFIPISALKGDNVVErsenmpwydgptLLEHLETVEVAEDRNDAPFRFPVqyvnrpnlDfRGY--- 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 187 gaglvvTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDAEkeqLNRGDWL 256
Cdd:COG2895 251 ------AGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEDEID---ISRGDVI 311
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
2-207 |
3.04e-20 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 95.28 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAITGVNADrlpEEKKRGMTIDLGyAY---WPQPD-GRVLGFIDVPGHEKFLSNMLAGVGGIDH 77
Cdd:CHL00189 246 IVTILGHVDHGKTTLLDKIRKTQIA---QKEAGGITQKIG-AYeveFEYKDeNQKIVFLDTPGHEAFSSMRSRGANVTDI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 78 ALLVVACDDGVMAQTREHLQILQlTGNLQLTVALTKADRvDEARIGEVREEVLA---ALDNYGfADTVLFVTAANEGRGI 154
Cdd:CHL00189 322 AILIIAADDGVKPQTIEAINYIQ-AANVPIIVAINKIDK-ANANTERIKQQLAKynlIPEKWG-GDTPMIPISASQGTNI 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 155 AEL------RAHLQQLPAR-SHAAQHrfrlAIDRAFTVKGAGLVVTGTALSGEVNVGDTL 207
Cdd:CHL00189 399 DKLletillLAEIEDLKADpTQLAQG----IILEAHLDKTKGPVATILVQNGTLHIGDII 454
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
3-238 |
8.58e-20 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 92.37 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYA---------------YWP----QPDG------------- 50
Cdd:PTZ00327 37 IGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYAnakiykcpkcprptcYQSygssKPDNppcpgcghkmtlk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 51 RVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGV-MAQTREHLQILQLTGNLQLTVALTKADRVDEARIGEVREEV 129
Cdd:PTZ00327 117 RHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 130 LAALDNYGFADTVLFVTAANEGRGIAELRAHL-QQLPARSHAAQHRFRLAIDRAFTVKGAGL--------VVTGTALSGE 200
Cdd:PTZ00327 197 RNFVKGTIADNAPIIPISAQLKYNIDVVLEYIcTQIPIPKRDLTSPPRMIVIRSFDVNKPGEdienlkggVAGGSILQGV 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446504538 201 VNVGDTLWL-TGVN----------TPMRVR--SLHAQNQPTDHAYAGQRIA 238
Cdd:PTZ00327 277 LKVGDEIEIrPGIIskdsggeftcRPIRTRivSLFAENNELQYAVPGGLIG 327
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
5-302 |
9.96e-20 |
|
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: 91.67 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 5 TAGHVDHGKTTL---------------LQAITGVNADR---------------LPEEKKRGMTIDLGYAYWpQPDGRVLG 54
Cdd:TIGR02034 5 TCGSVDDGKSTLigrllhdtkqiyedqLAALERDSKKHgtqggeidlallvdgLQAEREQGITIDVAYRYF-STDKRKFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 55 FIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRV--DEARIGEVREEVLAA 132
Cdd:TIGR02034 84 VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVdyDEEVFENIKKDYLAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 133 LDNYGFADTVLFVTAANEGRGIAE------------LRAHLQQLPARSHAAQHRFRLAID---------RAFtvkgaglv 191
Cdd:TIGR02034 164 AEQLGFRDVTFIPLSALKGDNVVSrsesmpwysgptLLEILETVEVERDAQDLPLRFPVQyvnrpnldfRGY-------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 192 vTGTALSGEVNVGDTL--WLTGVNTpmRVRSLHAQNQPTDHAYAGQRIALNIAGDAEkeqLNRGDWLL---SDAPMGEAF 266
Cdd:TIGR02034 236 -AGTIASGSVHVGDEVvvLPSGRSS--RVARIVTFDGDLEQARAGQAVTLTLDDEID---ISRGDLLAaadSAPEVADQF 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 446504538 267 SRVIVSLALHAqLSQWQPLHIHHAASHVTGRVSLLE 302
Cdd:TIGR02034 310 AATLVWMAEEP-LLPGRSYDLKLGTRKVRASVAAIK 344
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
2-225 |
1.58e-18 |
|
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: 89.44 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAI--TGVNAdrlpeEKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHAL 79
Cdd:TIGR00487 89 VVTIMGHVDHGKTSLLDSIrkTKVAQ-----GEAGGITQHIGAYHVENEDGKMITFLDTPGHEAFTSMRARGAKVTDIVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 80 LVVACDDGVMAQTREHLQILQlTGNLQLTVALTKADRvDEARIGEVREEvlaaLDNYGF------ADTVLFVTAANEGRG 153
Cdd:TIGR00487 164 LVVAADDGVMPQTIEAISHAK-AANVPIIVAINKIDK-PEANPDRVKQE----LSEYGLvpedwgGDTIFVPVSALTGDG 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446504538 154 IAEL------RAHLQQLPARSHAaqhRFRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLwLTGvNTPMRVRSLHAQN 225
Cdd:TIGR00487 238 IDELldmillQSEVEELKANPNG---QASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIV-VVG-AAYGRVRAMIDEN 310
|
|
| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
279-338 |
4.50e-17 |
|
Domain III of selenocysteine-specific translation elongation factor; This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.
Pssm-ID: 294012 [Multi-domain] Cd Length: 87 Bit Score: 76.33 E-value: 4.50e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446504538 279 LSQWQPLHIHHAASHVTGRVSLLEG--------GLAELIFDTPLWLADNDRLVLRDISARATLAGARV 338
Cdd:cd15491 20 LKHRTRVRLHLGTSEVLGRVVLLDRdelapgeeALAQLRLEEPVVAKRGDRFILRSYSPMRTIGGGRV 87
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
7-271 |
1.66e-16 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 82.10 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 7 GHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGR-VLGFID 57
Cdd:PTZ00141 14 GHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETPKyYFTIID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 58 VPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLQILQLTGNLQLTVALTKADRV----DEARIGEVR 126
Cdd:PTZ00141 92 APGHRDFIKNMITGTSQADVAILVVASTAGEFeagiskdGQTREHALLAFTLGVKQMIVCINKMDDKtvnySQERYDEIK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 127 EEVLAALDNYGF-ADTVLFV-TAANEGRGIAE------------LRAHLQQLPARSHAAQHRFRLAIDRAFTVKGAGLVV 192
Cdd:PTZ00141 172 KEVSAYLKKVGYnPEKVPFIpISGWQGDNMIEksdnmpwykgptLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 193 TGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDAEKEqLNRGdWLLSDA---PMGEAFS-- 267
Cdd:PTZ00141 252 VGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKD-IKRG-YVASDSkndPAKECADft 329
|
....*
gi 446504538 268 -RVIV 271
Cdd:PTZ00141 330 aQVIV 334
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
7-157 |
1.15e-15 |
|
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: 80.06 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 7 GHVDHGKTTLLQAI--TGVNADrlpEEkkRGMTIDLGyAYWPQPDGRVLGFIDVPGHEKFlSNMLA-GVGGIDHALLVVA 83
Cdd:COG0532 11 GHVDHGKTSLLDAIrkTNVAAG---EA--GGITQHIG-AYQVETNGGKITFLDTPGHEAF-TAMRArGAQVTDIVILVVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 84 CDDGVMAQTRE---HLQilqlTGNLQLTVALTKADRvDEARIGEVREEvLAALD----NYGfADTVlFV-TAANEGRGIA 155
Cdd:COG0532 84 ADDGVMPQTIEainHAK----AAGVPIIVAINKIDK-PGANPDRVKQE-LAEHGlvpeEWG-GDTI-FVpVSAKTGEGID 155
|
..
gi 446504538 156 EL 157
Cdd:COG0532 156 EL 157
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
3-299 |
1.24e-15 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 80.36 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTL---------------LQAITGVNADR---------------LPEEKKRGMTIDLGYAYWPQPDGRv 52
Cdd:PRK05506 27 FITCGSVDDGKSTLigrllydskmifedqLAALERDSKKVgtqgdeidlallvdgLAAEREQGITIDVAYRYFATPKRK- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 53 lgFI--DVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVD--EARIGEVREE 128
Cdd:PRK05506 106 --FIvaDTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDydQEVFDEIVAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 129 VLAALDNYGFADTVLFVTAANEGRGIAE------------LRAHLQQLPARSHAAQHRFRLAID---------RAFtvkg 187
Cdd:PRK05506 184 YRAFAAKLGLHDVTFIPISALKGDNVVTrsarmpwyegpsLLEHLETVEIASDRNLKDFRFPVQyvnrpnldfRGF---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 188 aglvvTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDAEkeqLNRGDWLL-SDAP--MGE 264
Cdd:PRK05506 260 -----AGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADEID---ISRGDMLArADNRpeVAD 331
|
330 340 350
....*....|....*....|....*....|....*
gi 446504538 265 AFSRVIVSLALHAQLSQwQPLHIHHAASHVTGRVS 299
Cdd:PRK05506 332 QFDATVVWMAEEPLLPG-RPYLLKHGTRTVPASVA 365
|
|
| SelB-wing_2 |
pfam09106 |
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with ... |
425-481 |
2.04e-14 |
|
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.
Pssm-ID: 430412 [Multi-domain] Cd Length: 57 Bit Score: 67.92 E-value: 2.04e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446504538 425 LDTLATYHEQHRDEPGPGRERLRRMALPMEDEALVLMLIERMRDDGLIHSHHGWLHL 481
Cdd:pfam09106 1 LAALAEYHAKNPLRPGMPKEELRSRLLPRLPPKLFDALLEELVAEGRLKLEGNWVRL 57
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
3-253 |
4.56e-14 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 74.74 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWP-QPDGRVL 53
Cdd:PLN00043 10 IVVIGHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDI--ALWKfETTKYYC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLQILQLTGNLQLTVALTKAD----RVDEARI 122
Cdd:PLN00043 88 TVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFeagiskdGQTREHALLAFTLGVKQMICCCNKMDattpKYSKARY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 123 GEVREEVLAALDNYGF-ADTVLFVTAAN-EGRGIAE------------LRAHLQQLPARSHAAQHRFRLAIDRAFTVKGA 188
Cdd:PLN00043 168 DEIVKEVSSYLKKVGYnPDKIPFVPISGfEGDNMIErstnldwykgptLLEALDQINEPKRPSDKPLRLPLQDVYKIGGI 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446504538 189 GLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDAEKEqLNRG 253
Cdd:PLN00043 248 GTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKD-LKRG 311
|
|
| SelB-wing_3 |
pfam09107 |
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with ... |
563-606 |
5.04e-14 |
|
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.
Pssm-ID: 430413 [Multi-domain] Cd Length: 46 Bit Score: 66.29 E-value: 5.04e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446504538 563 QERGSTCAADFRDRLNVGRKLAIQILEYFDRIGFTRRRGNDHLL 606
Cdd:pfam09107 3 KENGEITVAEFRDLLGTSRKYAIPLLEYLDRIGITRRVGDKRVL 46
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
2-221 |
1.28e-13 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 73.68 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAITG--------------VNADRLPEEKKRGMTIDLgyayWPQPDGRV----LGFIDVPGHEK 63
Cdd:PRK04004 8 IVVVLGHVDHGKTTLLDKIRGtavaakeaggitqhIGATEVPIDVIEKIAGPL----KKPLPIKLkipgLLFIDTPGHEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 64 FlSNMLAGVGGI-DHALLVVACDDGVMAQTREHLQILQLTGnlqlT---VALTKADRV-------DE---ARIGEVREEV 129
Cdd:PRK04004 84 F-TNLRKRGGALaDIAILVVDINEGFQPQTIEAINILKRRK----TpfvVAANKIDRIpgwksteDApflESIEKQSQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 130 LAALDN-----------YGF-AD----------TVLFV-TAANEGRGIAELRAHLQQLparshaAQhRF---RLAIDR-- 181
Cdd:PRK04004 159 QQELEEklyeligqlseLGFsADrfdrvkdftkTVAIVpVSAKTGEGIPDLLMVLAGL------AQ-RYleeRLKIDVeg 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446504538 182 --AFTV------KGAGLVVTGTALSGEVNVGDTLWLTGVNTPM--RVRSL 221
Cdd:PRK04004 232 pgKGTVlevkeeRGLGTTIDVILYDGTLRKGDTIVVGGKDGPIvtKVRAL 281
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
2-130 |
4.02e-13 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 68.39 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTLLQAI---TGV---NA-------DRLPEEKKRGMTI---DLGYAYwpqpDGRVLGFIDVPGHEKFL 65
Cdd:cd01891 7 IIA---HVDHGKTTLVDALlkqSGTfreNEevgervmDSNDLERERGITIlakNTAITY----KDTKINIIDTPGHADFG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446504538 66 SNMLAGVGGIDHALLVVACDDGVMAQTREHLQiLQLTGNLQLTVALTKADRVDeARIGEVREEVL 130
Cdd:cd01891 80 GEVERVLSMVDGVLLLVDASEGPMPQTRFVLK-KALEAGLKPIVVINKIDRPD-ARPEEVVDEVF 142
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
2-136 |
4.56e-13 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 68.80 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTL---LQAITGV----NA------DRLPEEKKRGMTID-----LGYAYWPQ---PDGRVLGFIDVPG 60
Cdd:cd01885 5 IIA---HVDHGKTTLsdsLLASAGIisekLAgkarylDTREDEQERGITIKssaisLYFEYEEEkmdGNDYLINLIDSPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 61 HEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHL-QILQltGNLQLTVALTKADRV--------DEA--RIGEVREEV 129
Cdd:cd01885 82 HVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLrQALE--ERVKPVLVINKIDRLilelklspEEAyqRLLRIVEDV 159
|
....*..
gi 446504538 130 LAALDNY 136
Cdd:cd01885 160 NAIIETY 166
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
2-166 |
8.78e-13 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 66.79 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTL----LQAITGVNA--------DRLPEEKKRGMTIDLGYA--YWPQPDGR--VLGFIDVPGHEKF- 64
Cdd:cd01890 5 IIA---HIDHGKSTLadrlLELTGTVSEremkeqvlDSMDLERERGITIKAQAVrlFYKAKDGEeyLLNLIDTPGHVDFs 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 65 --LSNMLAGVGGidhALLVVACDDGVMAQTREHLQiLQLTGNLQLTVALTKADrVDEARIGEVREEVlaaLDNYGF-ADT 141
Cdd:cd01890 82 yeVSRSLAACEG---ALLVVDATQGVEAQTLANFY-LALENNLEIIPVINKID-LPAADPDRVKQEI---EDVLGLdASE 153
|
170 180
....*....|....*....|....*.
gi 446504538 142 VLFVTaANEGRGIAE-LRAHLQQLPA 166
Cdd:cd01890 154 AILVS-AKTGLGVEDlLEAIVERIPP 178
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
175-253 |
1.87e-12 |
|
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: 63.39 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 175 FRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWL----TGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDaEKEQL 250
Cdd:cd03694 1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKI-KRESL 79
|
...
gi 446504538 251 NRG 253
Cdd:cd03694 80 RKG 82
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
3-243 |
2.13e-12 |
|
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: 70.02 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTT-----LLQAITGVNADRLPE--------EKKRGMTI---DLGYAYwpqpDGRVLGFIDVPGHEKFLS 66
Cdd:TIGR01394 4 IAIIAHVDHGKTTlvdalLKQSGTFRANEAVAErvmdsndlERERGITIlakNTAIRY----NGTKINIVDTPGHADFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 67 NMLAGVGGIDHALLVVACDDGVMAQTREHLQiLQLTGNLQLTVALTKADRVDeARIGEVREEVLAALDNYGFAD-----T 141
Cdd:TIGR01394 80 EVERVLGMVDGVLLLVDASEGPMPQTRFVLK-KALELGLKPIVVINKIDRPS-ARPDEVVDEVFDLFAELGADDeqldfP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 142 VLFVTA---------ANEGRGIAEL-RAHLQQLPARSHAAQHRFRL---AIDRAFTVkgaGLVVTGTALSGEVNVGDTL- 207
Cdd:TIGR01394 158 IVYASGragwasldlDDPSDNMAPLfDAIVRHVPAPKGDLDEPLQMlvtNLDYDEYL---GRIAIGRVHRGTVKKGQQVa 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446504538 208 WLT--GVNTPMRVRSLHA----QNQPTDHAYAGQRIAlnIAG 243
Cdd:TIGR01394 235 LMKrdGTIENGRISKLLGfeglERVEIDEAGAGDIVA--VAG 274
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
6-163 |
1.34e-11 |
|
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: 63.24 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 6 AGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRVLgFIDVPGHEKF-----LSNMLAGVGGIDHALL 80
Cdd:cd00882 3 VGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVKLV-LVDTPGLDEFgglgrEELARLLLRGADLILL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 81 VVACDDGVMAQTREHLQILQL-TGNLQLTVALTKADRVDEarigEVREEVLAALDNYGFADTVLFVTAANEGRGIAELRA 159
Cdd:cd00882 82 VVDSTDRESEEDAKLLILRRLrKEGIPIILVGNKIDLLEE----REVEELLRLEELAKILGVPVFEVSAKTGEGVDELFE 157
|
....
gi 446504538 160 HLQQ 163
Cdd:cd00882 158 KLIE 161
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
2-221 |
2.71e-11 |
|
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: 66.38 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIATAGHVDHGKTTLLQAITG--------------VNADRLPEEKKRGMTIDLgyayWPQPDGRV----LGFIDVPGHEK 63
Cdd:TIGR00491 6 IVVVLGHVDHGKTTLLDKIRGtavvkkeaggitqhIGASEVPTDVIEKICGDL----LKSFKIKLkipgLLFIDTPGHEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 64 FLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQlTGNLQLTVALTKADRVDEARIGE------------------- 124
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEALNILR-SRKTPFVVAANKIDRIPGWKSHEgypflesinkqeqrvrqnl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 125 --VREEVLAALDNYGF-----------ADTVLFV-TAANEGRGIAELRAHLQQLPARShaAQHRFRLAID-----RAFTV 185
Cdd:TIGR00491 161 dkQVYNLVIQLAEQGFnaerfdrirdfTKTVAIIpVSAKTGEGIPELLAILAGLAQNY--LENKLKLAIEgpakgTILEV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446504538 186 K---GAGLVVTGTALSGEVNVGDTLWLTGVNTPM--RVRSL 221
Cdd:TIGR00491 239 KeeqGLGYTIDAVIYDGILRKGDIIVLAGIDDVIvtRVRAI 279
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
3-167 |
3.54e-11 |
|
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: 63.46 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITG-----------VNADRLPEEKKRGMTID-----LGY------AYWPQP------------ 48
Cdd:cd04165 2 VAVVGNVDAGKSTLLGVLTQgeldngrgkarLNLFRHKHEVESGRTSSvsndiLGFdsdgevVNYPDNhlgeldveicek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 49 DGRVLGFIDVPGHEKFLSNMLAGVGG--IDHALLVVACDDGVMAQTREHLQI-LQLtgNLQLTVALTKADRVDEARIGEV 125
Cdd:cd04165 82 SSKVVTFIDLAGHERYLKTTVFGMTGyaPDYAMLVVGANAGIIGMTKEHLGLaLAL--KVPVFVVVTKIDMTPANVLQET 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446504538 126 REE-----------------------VLAALDnyGFADTV--LFVTAANEGRGIAELRAHLQQLPAR 167
Cdd:cd04165 160 LKDlkrllkspgvrklpvpvkskddvVLSASN--LSSGRVvpIFQVSNVTGEGLDLLRRFLNLLPPR 224
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
5-207 |
7.73e-11 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 64.55 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 5 TAGHVDHGKTTLL-------------QAITGVN-----------------ADRLPEEKKRGMTIDLGYAYWpQPDGRvlG 54
Cdd:PRK05124 32 TCGSVDDGKSTLIgrllhdtkqiyedQLASLHNdskrhgtqgekldlallVDGLQAEREQGITIDVAYRYF-STEKR--K 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 55 FI--DVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGNLQLTVALTKADRVD--EARIGEVREEVL 130
Cdd:PRK05124 109 FIiaDTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDysEEVFERIREDYL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 131 AALDNYGFADTVLFV-TAANEGRGIAELRAH------------LQQLPARSHAAQHRFRLAID---------RAFtvkga 188
Cdd:PRK05124 189 TFAEQLPGNLDIRFVpLSALEGDNVVSQSESmpwysgptllevLETVDIQRVVDAQPFRFPVQyvnrpnldfRGY----- 263
|
250
....*....|....*....
gi 446504538 189 glvvTGTALSGEVNVGDTL 207
Cdd:PRK05124 264 ----AGTLASGVVKVGDRV 278
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
3-92 |
7.49e-10 |
|
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: 61.99 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAI---TGVNaDRL-------------PEEKKRGMTIDLG--YAYWpqpDGRVLGFIDVPGHEKF 64
Cdd:COG0480 12 IGIVAHIDAGKTTLTERIlfyTGAI-HRIgevhdgntvmdwmPEEQERGITITSAatTCEW---KGHKINIIDTPGHVDF 87
|
90 100
....*....|....*....|....*...
gi 446504538 65 LSNMLAGVGGIDHALLVVACDDGVMAQT 92
Cdd:COG0480 88 TGEVERSLRVLDGAVVVFDAVAGVEPQT 115
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
2-130 |
1.32e-09 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 61.19 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTLLQAI---TGV------NADRL----PEEKKRGMTIdlgYA-----YWpqpDGRVLGFIDVPGHEK 63
Cdd:COG1217 11 IIA---HVDHGKTTLVDALlkqSGTfrenqeVAERVmdsnDLERERGITI---LAkntavRY---KGVKINIVDTPGHAD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446504538 64 FlsnmlagvGG--------IDHALLVVACDDGVMAQTREHLQ-ILQLtgNLQLTVALTKADRvDEARIGEVREEVL 130
Cdd:COG1217 82 F--------GGevervlsmVDGVLLLVDAFEGPMPQTRFVLKkALEL--GLKPIVVINKIDR-PDARPDEVVDEVF 146
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-92 |
2.77e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 60.26 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTL---LQAITGVNADRL----------PEEKKRGMTID-----LGYAYwpQPDGRVLGFIDVPGHEKF 64
Cdd:PRK07560 23 IGIIAHIDHGKTTLsdnLLAGAGMISEELageqlaldfdEEEQARGITIKaanvsMVHEY--EGKEYLINLIDTPGHVDF 100
|
90 100
....*....|....*....|....*...
gi 446504538 65 LSNMLAGVGGIDHALLVVACDDGVMAQT 92
Cdd:PRK07560 101 GGDVTRAMRAVDGAIVVVDAVEGVMPQT 128
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
189-256 |
4.34e-09 |
|
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: 53.04 E-value: 4.34e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446504538 189 GLVVTGTALSGEVNVGDTLWLTGVNT-----PMRVRSLHAQNQPTDHAYAGQRIALNIAGDaEKEQLNRGDWL 256
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGV-GLEDIRVGDTL 72
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
2-92 |
5.51e-09 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 59.29 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTLLQA-------ITGVNA------DRLPEEKKRGMTIDLG----YAYWPQPDGR-----VLGFIDVP 59
Cdd:PTZ00416 24 VIA---HVDHGKSTLTDSlvckagiISSKNAgdarftDTRADEQERGITIKSTgislYYEHDLEDGDdkqpfLINLIDSP 100
|
90 100 110
....*....|....*....|....*....|...
gi 446504538 60 GHEKFLSNMLAGVGGIDHALLVVACDDGVMAQT 92
Cdd:PTZ00416 101 GHVDFSSEVTAALRVTDGALVVVDCVEGVCVQT 133
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
7-133 |
7.19e-09 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 58.60 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 7 GHVDHGKTTLLQAI---TGVN------------ADRLPEEKKRGMTIDLGYA--YWpqpDGRVLGFIDVPGHEKFLSNML 69
Cdd:PRK12740 2 GHSGAGKTTLTEAIlfyTGAIhrigevedgtttMDFMPEERERGISITSAATtcEW---KGHKINLIDTPGHVDFTGEVE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTRehlQILQLTGNLQL--TVALTKADRvDEARIgevrEEVLAAL 133
Cdd:PRK12740 79 RALRVLDGAVVVVCAVGGVEPQTE---TVWRQAEKYGVprIIFVNKMDR-AGADF----FRVLAQL 136
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
3-133 |
1.28e-08 |
|
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: 56.45 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAI---TGV------------NADRLPEEKKRGMTIDLGYAYWpQPDGRVLGFIDVPGHEKFLSN 67
Cdd:cd04170 2 IALVGHSGSGKTTLAEALlyaTGAidrlgrvedgntVSDYDPEEKKRKMSIETSVAPL-EWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446504538 68 MLAGVGGIDHALLVVACDDGVMAQTRehlQILQLTGNLQL--TVALTKADRvDEARIgevrEEVLAAL 133
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTE---KVWEFLDDAKLprIIFINKMDR-ARADF----DKTLAAL 140
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
3-116 |
1.54e-08 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 55.35 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNADRLPE----------------EKKRGMTIDLGyaywP--------QPDGRVLGFIDV 58
Cdd:cd04167 3 VCIAGHLHHGKTSLLDMLIEQTHKRTPSvklgwkplrytdtrkdEQERGISIKSN----PislvledsKGKSYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446504538 59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQTREHLQILQLTGnLQLTVALTKADR 116
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEG-LPMVLVINKIDR 135
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
3-93 |
2.24e-08 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 57.27 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAI---TGVN------------ADRLPEEKKRGMTIDLGYA--YWpqpDGRVLGFIDVPGHEKFL 65
Cdd:PRK13351 11 IGILAHIDAGKTTLTERIlfyTGKIhkmgevedgttvTDWMPQEQERGITIESAATscDW---DNHRINLIDTPGHIDFT 87
|
90 100
....*....|....*....|....*...
gi 446504538 66 SNMLAGVGGIDHALLVVACDDGVMAQTR 93
Cdd:PRK13351 88 GEVERSLRVLDGAVVVFDAVTGVQPQTE 115
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
175-254 |
1.06e-07 |
|
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: 49.57 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 175 FRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGDAEkeqLNRGD 254
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVKD---ILTGD 77
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
2-92 |
1.08e-07 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 55.12 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTL---LQAITGVNA----------DRLPEEKKRGMTI-------------DLGYAYWPQPDGR--VL 53
Cdd:PLN00116 24 VIA---HVDHGKSTLtdsLVAAAGIIAqevagdvrmtDTRADEAERGITIkstgislyyemtdESLKDFKGERDGNeyLI 100
|
90 100 110
....*....|....*....|....*....|....*....
gi 446504538 54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVMAQT 92
Cdd:PLN00116 101 NLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQT 139
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
175-259 |
1.08e-07 |
|
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: 49.43 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 175 FRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRGD 254
Cdd:cd16267 2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTG-IDPNHLRVGS 80
|
....*
gi 446504538 255 wLLSD 259
Cdd:cd16267 81 -ILCD 84
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
2-100 |
2.52e-07 |
|
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: 51.85 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTLLQAI---TGV----------NA--DRLPEEKKRGMTIDLGYAYWPQPDGRVlGFIDVPGHEKFLS 66
Cdd:cd04168 4 ILA---HVDAGKTTLTESLlytSGAirelgsvdkgTTrtDSMELERQRGITIFSAVASFQWEDTKV-NIIDTPGHMDFIA 79
|
90 100 110
....*....|....*....|....*....|....
gi 446504538 67 NMLAGVGGIDHALLVVACDDGVMAQTREHLQILQ 100
Cdd:cd04168 80 EVERSLSVLDGAILVISAVEGVQAQTRILFRLLR 113
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
3-119 |
5.68e-07 |
|
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: 49.68 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVnaDRLPEEKKRGMTIDlgyaYWPQP---DGR--VLGFIDVPGHEKFLS----NMLAGVG 73
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLGN--KGSITEYYPGTTRN----YVTTVieeDGKtyKFNLLDTAGQEDYDAirrlYYPQVER 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446504538 74 GI---DHALLVVACDDGVMAQTREhlQILQLTGNLQLTVALTKADRVDE 119
Cdd:TIGR00231 78 SLrvfDIVILVLDVEEILEKQTKE--IIHHADSGVPIILVGNKIDLKDA 124
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
4-164 |
3.68e-06 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 47.24 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 4 ATAGHVDHGKTTLLQAITGvnADRLPEEKKRGMTIDLGYAYWPQPDGRVLGFIDVPG-------HEKFLSNMLAGVGGID 76
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLG--QNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 77 HALLVVACDDGvmaQTREHLQILQL-TGNLQLTVALTKADRVDEARigevREEVLAALDNYGFADTVLFVTAANEGRGIA 155
Cdd:cd00880 79 LVLLVVDSDLT---PVEEEAKLGLLrERGKPVLLVLNKIDLVPESE----EEELLRERKLELLPDLPVIAVSALPGEGID 151
|
....*....
gi 446504538 156 ELRAHLQQL 164
Cdd:cd00880 152 ELRKKIAEL 160
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
3-157 |
1.32e-05 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 48.17 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTL----LQAITGVNA---------DRLPEEKKRGMTIDLGYAYWPQPDGRVlGFIDVPGHEKFLSNML 69
Cdd:PRK10218 8 IAIIAHVDHGKTTLvdklLQQSGTFDSraetqervmDSNDLEKERGITILAKNTAIKWNDYRI-NIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVGGIDHALLVVACDDGVMAQTReHLQILQLTGNLQLTVALTKADRvDEARIGEVREEVLAALDNYGFADT-----VLF 144
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTR-FVTKKAFAYGLKPIVVINKVDR-PGARPDWVVDQVFDLFVNLDATDEqldfpIVY 164
|
170
....*....|...
gi 446504538 145 VTAANegrGIAEL 157
Cdd:PRK10218 165 ASALN---GIAGL 174
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
175-256 |
1.45e-04 |
|
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: 40.96 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 175 FRLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWLTGVNTPMR--VRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNR 252
Cdd:cd03697 1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKttVTGIEMFRKTLDEAEAGDNVGVLLRG-VKKEDVER 79
|
....
gi 446504538 253 GDWL 256
Cdd:cd03697 80 GMVL 83
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
176-254 |
2.67e-04 |
|
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: 40.25 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 176 RLAIDRAFTVKGAGLVVTGTALSGEVNVGDTLWL--TGVNTpmRVRSLHAQNQPTDHAYAGQRIALNIAGdAEKEQLNRG 253
Cdd:cd03693 6 RLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVTG--EVKSVEMHHEPLEEAIPGDNVGFNVKG-VSVKDIKRG 82
|
.
gi 446504538 254 D 254
Cdd:cd03693 83 D 83
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
53-117 |
1.03e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 42.18 E-value: 1.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446504538 53 LGFIDVPGHEKFLSnmLAGVGG--IDHALLVVACDDGVMAQTREHLQILQlTGNLQLTVALTKADRV 117
Cdd:PRK14845 528 LLFIDTPGHEAFTS--LRKRGGslADLAVLVVDINEGFKPQTIEAINILR-QYKTPFVVAANKIDLI 591
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
75-162 |
1.43e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.46 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 75 IDHALLVVACDDG-----------VMAQtrehlqilqlTGNLQLTVALTKADRVDEARIgevrEEVLAALDNYGFAdtvL 143
Cdd:cd01854 3 VDQVLIVFSLKEPffnlrlldrylVAAE----------ASGIEPVIVLNKADLVDDEEL----EELLEIYEKLGYP---V 65
|
90
....*....|....*....
gi 446504538 144 FVTAANEGRGIAELRAHLQ 162
Cdd:cd01854 66 LAVSAKTGEGLDELRELLK 84
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
104-164 |
1.95e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 39.42 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446504538 104 NLQLTVALTKADRVDEARIGEVREEVLAALDNYGFADTVLFVTAANeGRGIAELRAHLQQL 164
Cdd:cd01876 110 GIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKK-GTGIDELRALIAEW 169
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
3-189 |
2.00e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.52 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 3 IATAGHVDHGKTTLLQAITGVNA----DRLPEekkrgmTIDLGYAYWPQPDGRVLGFIDVPGHE---------KFLSNML 69
Cdd:COG3596 42 IALVGKTGAGKSSLINALFGAEVaevgVGRPC------TREIQRYRLESDGLPGLVLLDTPGLGevnerdreyRELRELL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 70 AGVggiDHALLVVACDDGVMAQTREHLQ-ILQLTGNLQLTVALTKADRVDEARI-------------GEVREEVLA-ALD 134
Cdd:COG3596 116 PEA---DLILWVVKADDRALATDEEFLQaLRAQYPDPPVLVVLTQVDRLEPEREwdppynwpsppkeQNIRRALEAiAEQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446504538 135 NYGFADTVLFVTAA--NEGRGIAELRAHLQQL--PARSHAAQHRFRLAIDRAFTVKGAG 189
Cdd:COG3596 193 LGVPIDRVIPVSAAedRTGYGLEELVDALAEAlpEAKRSRLARLLRAKAIDRYTLLAAA 251
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
2-64 |
9.08e-03 |
|
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: 38.24 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446504538 2 IIAtagHVDHGKTTLLQAI---TGVNA------------DRLPEEKKRGMTIDLG--YAYWpqpDGRVLGFIDVPGHEKF 64
Cdd:cd01886 4 IIA---HIDAGKTTTTERIlyyTGRIHkigevhgggatmDWMEQERERGITIQSAatTCFW---KDHRINIIDTPGHVDF 77
|
|
| |
