|
Name |
Accession |
Description |
Interval |
E-value |
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
179-398 |
7.44e-138 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 399.94 E-value: 7.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFETGFDRGGQTREHAMLAKTAGVKHLVVLVNKMDDPTVNWDEARYN 338
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 339 ECKDKILPYLKKLGFNPaKDLTFMPCSGLSGAGLrdIIPDSICPWYSGPAFIPFIDLLPS 398
Cdd:cd01883 161 EIKKKVSPFLKKVGYNP-KDVPFIPISGFTGDNL--IEKSENMPWYKGPTLLEALDSLEP 217
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
173-599 |
9.54e-134 |
|
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: 397.38 E-value: 9.54e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 173 SKKEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFET 252
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 253 ERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEfetgfdrGGQTREHAMLAKTAGVKHLVVLVNKMDDptVNW 332
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDA--VNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 333 DEARYNECKDKILPYLKKLGFNPAkDLTFMPCSGLSGAGLrdIIPDSICPWYSGPAFIPFIDLLPSLNRKADGPFIMPIV 412
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVD-KIPFIPVSAWKGDNV--VKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 413 DKY--KDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDASN 490
Cdd:COG5256 231 DVYsiSGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICL 570
Cdd:COG5256 311 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVI 390
|
410 420
....*....|....*....|....*....
gi 1937271225 571 EQFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:COG5256 391 EKFKEFPQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
173-599 |
4.00e-127 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 380.43 E-value: 4.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 173 SKKEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFET 252
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 253 ERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEfetgfDRGGQTREHAMLAKTAGVKHLVVLVNKMDdpTVNW 332
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG-----GVMPQTREHVFLARTLGINQLIVAINKMD--AVNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 333 DEARYNECKDKILPYLKKLGFNPAkDLTFMPCSGLSGAGLRDIIPDSicPWYSGPAFIPFIDLLPSLNRKADGPFIMPIV 412
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPD-DIPFIPVSAFEGDNVVKKSENM--PWYNGPTLLEALDNLKPPEKPTDKPLRIPIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 413 DKY--KDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDASN 490
Cdd:PRK12317 232 DVYsiSGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICL 570
Cdd:PRK12317 312 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVI 391
|
410 420
....*....|....*....|....*....
gi 1937271225 571 EQFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:PRK12317 392 EKVKEIPQLGRFAIRDMGQTIAAGMVIDV 420
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
175-376 |
8.22e-61 |
|
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: 200.06 E-value: 8.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAReksreswylswaLDTNQEERDKGKTVEVGRAYFETER 254
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAG------------LDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGefetgfdRGGQTREHAMLAKTAGVKhLVVLVNKMDDPtvnwDE 334
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937271225 335 ARYNECKDKIL-PYLKKLGFNPaKDLTFMPCSGLSGAGLRDII 376
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDG-EFVPVVPGSALKGEGVQTLL 178
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
493-599 |
2.39e-60 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 294003 [Multi-domain] Cd Length: 108 Bit Score: 195.85 E-value: 2.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 493 KTGKVFDAQVVILEH-KSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICLE 571
Cdd:cd03704 1 PVVTEFEAQIVILDLlKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLE 80
|
90 100
....*....|....*....|....*...
gi 1937271225 572 QFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:cd03704 81 TFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
184-596 |
5.83e-54 |
|
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: 189.12 E-value: 5.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWAL--DTNQEERDKGKTVEVGRAYFETERKHFTILD 261
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEIDLALlvDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 262 APGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVNWDEARYNECK 341
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 342 DKILPYLKKLGFnpaKDLTFMPCSGLSGAGLRDiiPDSICPWYSGPAFIPFIDLLPSLNRKADGPFIMPI-------VDK 414
Cdd:TIGR02034 158 KDYLAFAEQLGF---RDVTFIPLSALKGDNVVS--RSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVqyvnrpnLDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 415 YKDMGTVVMGKVEsgtarKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKgiEEEDVSPGFVLCDASNPIKT 494
Cdd:TIGR02034 233 RGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSAPEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 495 GKVFDAQVVILEHKSIIcAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSrPRFVKQDqVAIMRIECSGMICLEQFK 574
Cdd:TIGR02034 306 ADQFAATLVWMAEEPLL-PGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA-KSLELNE-IGRVNLSLDEPIAFDPYA 382
|
410 420
....*....|....*....|....
gi 1937271225 575 LFPQMGRFTL--RDENKTIAIGKV 596
Cdd:TIGR02034 383 ENRTTGAFILidRLSNRTVGAGMI 406
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
406-487 |
2.15e-52 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 173.83 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 406 PFIMPIVDKYKDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVL 485
Cdd:cd04089 1 PLRMPILDKYKDMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFVL 80
|
..
gi 1937271225 486 CD 487
Cdd:cd04089 81 CS 82
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
491-599 |
8.81e-31 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 115.82 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEH-----KSIICAGYSAVMHIHCAAEEVTVKALICLVDkkTGDKSKsRPRFVKQDQVAIMRIECS 565
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 1937271225 566 GMICLEQFKlfpqmgRFTLRDENKTIAIGKVLKV 599
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
419-486 |
7.16e-12 |
|
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: 61.13 E-value: 7.16e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937271225 419 GTVVMGKVESGTARKGQNLLVMPNRTQ-----VAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLC 486
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGkkkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
1-135 |
5.77e-05 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 45.40 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 1 MA-QDNAEmstkfstLNVNAAEFVPSFTSFSAAASTTPLSSDNTPAAATIAHMDTASVPASASGTPATTPNSEASGSGST 79
Cdd:PRK10856 146 MAdQSSAE-------LSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVD 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937271225 80 NALNQadVPPAESPMQTSPIKTAAAAApveniNTADKIAANNGNENDPADSW-DVED 135
Cdd:PRK10856 219 TAATP--APAAPATPDGAAPLPTDQAG-----VSTPAADPNALVMNFTADCWlEVTD 268
|
|
| PAM2 |
pfam07145 |
Ataxin-2 C-terminal region; The PABP-interacting motif PAM2 has been identified in various ... |
11-27 |
5.75e-04 |
|
Ataxin-2 C-terminal region; The PABP-interacting motif PAM2 has been identified in various eukaryotic proteins as an important binding site for pfam00658. It has been found in a wide range of eukaryotic proteins. Strikingly, this motif appears to occur solely outside of globular domains.
Pssm-ID: 429316 Cd Length: 17 Bit Score: 37.21 E-value: 5.75e-04
|
| SP4_N |
cd22536 |
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ... |
5-99 |
2.28e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.
Pssm-ID: 411773 [Multi-domain] Cd Length: 623 Bit Score: 41.06 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 5 NAEMSTKFSTLNVNAAEFVPSFTSFSAAASTTPLSSDNTPAAAT---IAHMDTASVPASASGTPATTPNSEASGSGSTNA 81
Cdd:cd22536 274 NQLVSTPITTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSSAetgQYASTAASSERTEEEPQTSAAESEAQSSSQLQS 353
|
90
....*....|....*...
gi 1937271225 82 LNQADVPPAESPMQTSPI 99
Cdd:cd22536 354 NGLQNVQDQSNSLQQVQI 371
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
179-398 |
7.44e-138 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 399.94 E-value: 7.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFETGFDRGGQTREHAMLAKTAGVKHLVVLVNKMDDPTVNWDEARYN 338
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 339 ECKDKILPYLKKLGFNPaKDLTFMPCSGLSGAGLrdIIPDSICPWYSGPAFIPFIDLLPS 398
Cdd:cd01883 161 EIKKKVSPFLKKVGYNP-KDVPFIPISGFTGDNL--IEKSENMPWYKGPTLLEALDSLEP 217
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
173-599 |
9.54e-134 |
|
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: 397.38 E-value: 9.54e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 173 SKKEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFET 252
Cdd:COG5256 3 SEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 253 ERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEfetgfdrGGQTREHAMLAKTAGVKHLVVLVNKMDDptVNW 332
Cdd:COG5256 83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDA--VNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 333 DEARYNECKDKILPYLKKLGFNPAkDLTFMPCSGLSGAGLrdIIPDSICPWYSGPAFIPFIDLLPSLNRKADGPFIMPIV 412
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVD-KIPFIPVSAWKGDNV--VKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 413 DKY--KDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDASN 490
Cdd:COG5256 231 DVYsiSGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICL 570
Cdd:COG5256 311 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVI 390
|
410 420
....*....|....*....|....*....
gi 1937271225 571 EQFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:COG5256 391 EKFKEFPQLGRFAIRDMGQTVAAGVVLDV 419
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
173-599 |
4.00e-127 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 380.43 E-value: 4.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 173 SKKEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFET 252
Cdd:PRK12317 2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 253 ERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEfetgfDRGGQTREHAMLAKTAGVKHLVVLVNKMDdpTVNW 332
Cdd:PRK12317 82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG-----GVMPQTREHVFLARTLGINQLIVAINKMD--AVNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 333 DEARYNECKDKILPYLKKLGFNPAkDLTFMPCSGLSGAGLRDIIPDSicPWYSGPAFIPFIDLLPSLNRKADGPFIMPIV 412
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPD-DIPFIPVSAFEGDNVVKKSENM--PWYNGPTLLEALDNLKPPEKPTDKPLRIPIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 413 DKY--KDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDASN 490
Cdd:PRK12317 232 DVYsiSGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICL 570
Cdd:PRK12317 312 PPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVI 391
|
410 420
....*....|....*....|....*....
gi 1937271225 571 EQFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:PRK12317 392 EKVKEIPQLGRFAIRDMGQTIAAGMVIDV 420
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
175-601 |
9.00e-123 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 369.85 E-value: 9.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFETER 254
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFETGFDRGGQTREHAMLAKTAGVKHLVVLVNKMDDPTVNWDE 334
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 335 ARYNECKDKILPYLKKLGFNPAKdLTFMPCSGLSGaglRDIIPDSI-CPWYSGPAFIPFIDLLPSLNRKADGPFIMPIVD 413
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEK-VPFIPISGWQG---DNMIEKSDnMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 414 KYK--DMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDASN- 490
Cdd:PTZ00141 241 VYKigGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVM-----HIHCAAEEVTVKaliclVDKKTGDKSKSRPRFVKQDQVAIMRIECS 565
Cdd:PTZ00141 321 PAKECADFTAQVIVLNHPGQIKNGYTPVLdchtaHIACKFAEIESK-----IDRRSGKVLEENPKAIKSGDAAIVKMVPT 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 1937271225 566 GMICLEQFKLFPQMGRFTLRDENKTIAIGkVLKVIE 601
Cdd:PTZ00141 396 KPMCVEVFNEYPPLGRFAVRDMKQTVAVG-VIKSVE 430
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
174-601 |
8.74e-95 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 297.77 E-value: 8.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 174 KKEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWALDTNQEERDKGKTVEVGRAYFETE 253
Cdd:PLN00043 4 EKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 254 RKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFETGFDRGGQTREHAMLAKTAGVKHLVVLVNKMDDPTVNWD 333
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 334 EARYNECKDKILPYLKKLGFNPAKdLTFMPCSGLSGAGLrdIIPDSICPWYSGPAFIPFIDLLPSLNRKADGPFIMPIVD 413
Cdd:PLN00043 164 KARYDEIVKEVSSYLKKVGYNPDK-IPFVPISGFEGDNM--IERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 414 KYK--DMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDASN- 490
Cdd:PLN00043 241 VYKigGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICL 570
Cdd:PLN00043 321 PAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVV 400
|
410 420 430
....*....|....*....|....*....|.
gi 1937271225 571 EQFKLFPQMGRFTLRDENKTIAIGkVLKVIE 601
Cdd:PLN00043 401 ETFSEYPPLGRFAVRDMRQTVAVG-VIKSVE 430
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
170-601 |
1.77e-67 |
|
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: 225.74 E-value: 1.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 170 ESRSKKEHVNVVFIGHVDAGKSTIGGQIMSLTGMV--DKrtLEKYEREAREKSREswYLSWAL--DTNQEERDKGKTVEV 245
Cdd:COG2895 10 AQHENKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQ--EIDLALltDGLQAEREQGITIDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 246 GRAYFETERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKM 325
Cdd:COG2895 86 AYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 326 DdpTVNWDEARYNECKDKILPYLKKLGFnpaKDLTFMPCSGLSGaglrdiipDSI------CPWYSGPAFIPFIDLLPSL 399
Cdd:COG2895 159 D--LVDYSEEVFEEIVADYRAFAAKLGL---EDITFIPISALKG--------DNVversenMPWYDGPTLLEHLETVEVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 400 NRKADGPFIMPI--VDKYKDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLkgiEEE 477
Cdd:COG2895 226 EDRNDAPFRFPVqyVNRPNLDFRGYAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 478 -DVSPGFVLCDASNPIKTGKVFDAQVVILEHKSIIcAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPrfVKQDQ 556
Cdd:COG2895 303 iDISRGDVIVAADAPPEVADQFEATLVWMDEEPLL-PGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAADS--LELND 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1937271225 557 VAIMRIECSGMICLEQFKLFPQMGRFTLRDE--NKTIAIGKVLKVIE 601
Cdd:COG2895 380 IGRVTLRLAEPIAFDPYADNRATGSFILIDRltNATVGAGMIRGALR 426
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
175-376 |
8.22e-61 |
|
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: 200.06 E-value: 8.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAReksreswylswaLDTNQEERDKGKTVEVGRAYFETER 254
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAG------------LDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGefetgfdRGGQTREHAMLAKTAGVKhLVVLVNKMDDPtvnwDE 334
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937271225 335 ARYNECKDKIL-PYLKKLGFNPaKDLTFMPCSGLSGAGLRDII 376
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDG-EFVPVVPGSALKGEGVQTLL 178
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
493-599 |
2.39e-60 |
|
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 294003 [Multi-domain] Cd Length: 108 Bit Score: 195.85 E-value: 2.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 493 KTGKVFDAQVVILEH-KSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICLE 571
Cdd:cd03704 1 PVVTEFEAQIVILDLlKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLE 80
|
90 100
....*....|....*....|....*...
gi 1937271225 572 QFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:cd03704 81 TFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
184-596 |
5.83e-54 |
|
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: 189.12 E-value: 5.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWAL--DTNQEERDKGKTVEVGRAYFETERKHFTILD 261
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEIDLALlvDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 262 APGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVNWDEARYNECK 341
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 342 DKILPYLKKLGFnpaKDLTFMPCSGLSGAGLRDiiPDSICPWYSGPAFIPFIDLLPSLNRKADGPFIMPI-------VDK 414
Cdd:TIGR02034 158 KDYLAFAEQLGF---RDVTFIPLSALKGDNVVS--RSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVqyvnrpnLDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 415 YKDMGTVVMGKVEsgtarKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKgiEEEDVSPGFVLCDASNPIKT 494
Cdd:TIGR02034 233 RGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSAPEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 495 GKVFDAQVVILEHKSIIcAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSrPRFVKQDqVAIMRIECSGMICLEQFK 574
Cdd:TIGR02034 306 ADQFAATLVWMAEEPLL-PGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA-KSLELNE-IGRVNLSLDEPIAFDPYA 382
|
410 420
....*....|....*....|....
gi 1937271225 575 LFPQMGRFTL--RDENKTIAIGKV 596
Cdd:TIGR02034 383 ENRTTGAFILidRLSNRTVGAGMI 406
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
406-487 |
2.15e-52 |
|
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.
Pssm-ID: 293906 [Multi-domain] Cd Length: 82 Bit Score: 173.83 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 406 PFIMPIVDKYKDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVL 485
Cdd:cd04089 1 PLRMPILDKYKDMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFVL 80
|
..
gi 1937271225 486 CD 487
Cdd:cd04089 81 CS 82
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
179-397 |
1.78e-51 |
|
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: 175.84 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESwYLSWAL--DTNQEERDKGKTVEVGRAYFETERKH 256
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERSKSSGTQGE-KLDLALlvDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 257 FTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVNWDEAR 336
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD--LVDYDEEV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937271225 337 YNECKDKILPYLKKLGFNpakDLTFMPCSGLSGAGLRDIIPDSicPWYSGPAFIPFIDLLP 397
Cdd:cd04166 151 FEEIKADYLAFAASLGIE---DITFIPISALEGDNVVSRSENM--PWYKGPTLLEHLETVE 206
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
184-503 |
1.40e-50 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 184.75 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWAL--DTNQEERDKGKTVEVGRAYFETERKHFTILD 261
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQGDEIDLALlvDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 262 APGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVNWDEARYNECK 341
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMD--LVDYDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 342 DKILPYLKKLGFNpakDLTFMPCSGLSGAGLRDIIPDSicPWYSGPAFIPFIDLLPSLNRKADGPFIMPIvdKYkdmgtv 421
Cdd:PRK05506 182 ADYRAFAAKLGLH---DVTFIPISALKGDNVVTRSARM--PWYEGPSLLEHLETVEIASDRNLKDFRFPV--QY------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 422 VM----------GKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKgiEEEDVSPGFVLCDASNP 491
Cdd:PRK05506 249 VNrpnldfrgfaGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLARADNR 326
|
330
....*....|..
gi 1937271225 492 IKTGKVFDAQVV 503
Cdd:PRK05506 327 PEVADQFDATVV 338
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
184-503 |
9.32e-49 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 176.64 E-value: 9.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIGGQIMSLTGMVDKRTLEKYEREAREKSRESWYLSWAL--DTNQEERDKGKTVEVGRAYFETERKHFTILD 261
Cdd:PRK05124 34 GSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTQGEKLDLALlvDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 262 APGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVNWDEARYNECK 341
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMD--LVDYSEEVFERIR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 342 DKILPYLKKLGFNPakDLTFMPCSGLSGAGLRDiiPDSICPWYSGPAFIPFIDLLPSLNRKADGPFIMPI--VDK----- 414
Cdd:PRK05124 185 EDYLTFAEQLPGNL--DIRFVPLSALEGDNVVS--QSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVqyVNRpnldf 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 415 --YkdmgtvvMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKgiEEEDVSPGFVLCDASNPI 492
Cdd:PRK05124 261 rgY-------AGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLE--DEIDISRGDLLVAADEAL 331
|
330
....*....|.
gi 1937271225 493 KTGKVFDAQVV 503
Cdd:PRK05124 332 QAVQHASADVV 342
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
175-505 |
1.79e-38 |
|
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: 146.06 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTiggqimsLTGMVDKRTLEKYEREAREKSReswylswaLDTNQEERDKGKTVEVGRAYFETER 254
Cdd:COG0050 10 KPHVNIGTIGHVDHGKTT-------LTAAITKVLAKKGGAKAKAYDQ--------IDKAPEEKERGITINTSHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMD---DPtvn 331
Cdd:COG0050 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDmvdDE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 332 wdearynECKD----KILPYLKKLGFnPAKDLTFMPcsglsGAGLRDIIPDSICPWYSgpafiPFIDLL-------PSLN 400
Cdd:COG0050 145 -------ELLElvemEVRELLSKYGF-PGDDTPIIR-----GSALKALEGDPDPEWEK-----KILELMdavdsyiPEPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 401 RKADGPFIMPIVDKY--KDMGTVVMGKVESGTARKGQNL-LVMPNRTQVAVdqlwsdddeVTSVG----------PGENV 467
Cdd:COG0050 207 RDTDKPFLMPVEDVFsiTGRGTVVTGRVERGIIKVGDEVeIVGIRDTQKTV---------VTGVEmfrklldegeAGDNV 277
|
330 340 350
....*....|....*....|....*....|....*...
gi 1937271225 468 KIKLKGIEEEDVSPGFVLCdASNPIKTGKVFDAQVVIL 505
Cdd:COG0050 278 GLLLRGIKREDVERGQVLA-KPGSITPHTKFEAEVYVL 314
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
175-505 |
7.15e-38 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 144.32 E-value: 7.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTiggqimsLTGMVDKRTLEKYEREAREKSReswylswaLDTNQEERDKGKTVEVGRAYFETER 254
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTT-------LTAAITKVLAERGLNQAKDYDS--------IDAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDDPTvnwDE 334
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVD---DE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 335 ARYNECKDKILPYLKKLGFnPAKDLTFMPCSGLSGAGLRDIIPDSIcpwysgpafipfIDLL-------PSLNRKADGPF 407
Cdd:PRK12736 145 ELLELVEMEVRELLSEYDF-PGDDIPVIRGSALKALEGDPKWEDAI------------MELMdavdeyiPTPERDTDKPF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 408 IMPIVDKY--KDMGTVVMGKVESGTARKGQNLLVM---PNRTQVA--VDQLWSDDDEVTSvgpGENVKIKLKGIEEEDVS 480
Cdd:PRK12736 212 LMPVEDVFtiTGRGTVVTGRVERGTVKVGDEVEIVgikETQKTVVtgVEMFRKLLDEGQA---GDNVGVLLRGVDRDEVE 288
|
330 340
....*....|....*....|....*
gi 1937271225 481 PGFVLCdASNPIKTGKVFDAQVVIL 505
Cdd:PRK12736 289 RGQVLA-KPGSIKPHTKFKAEVYIL 312
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
174-505 |
9.21e-38 |
|
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: 144.15 E-value: 9.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 174 KKEHVNVVFIGHVDAGKSTiggqimsLTGMVDKRTLEKYEREAREKSReswylswaLDTNQEERDKGKTVEVGRAYFETE 253
Cdd:TIGR00485 9 TKPHVNVGTIGHVDHGKTT-------LTAAITTVLAKEGGAAARAYDQ--------IDNAPEEKARGITINTAHVEYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 254 RKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDDPTvnwD 333
Cdd:TIGR00485 74 TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD---D 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 334 EARYNECKDKILPYLKKLGFnPAKDltfmpCSGLSGAGLRDIIPDSIcpWYSGP-AFIPFID-LLPSLNRKADGPFIMPI 411
Cdd:TIGR00485 144 EELLELVEMEVRELLSQYDF-PGDD-----TPIIRGSALKALEGDAE--WEAKIlELMDAVDeYIPTPEREIDKPFLLPI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 412 VDKY--KDMGTVVMGKVESGTARKGQNLLVM---PNR--TQVAVDQLWSDDDEVTSvgpGENVKIKLKGIEEEDVSPGFV 484
Cdd:TIGR00485 216 EDVFsiTGRGTVVTGRVERGIIKVGEEVEIVglkDTRktTVTGVEMFRKELDEGRA---GDNVGLLLRGIKREEIERGMV 292
|
330 340
....*....|....*....|.
gi 1937271225 485 LCdASNPIKTGKVFDAQVVIL 505
Cdd:TIGR00485 293 LA-KPGSIKPHTKFEAEVYVL 312
|
|
| tufA |
CHL00071 |
elongation factor Tu |
174-601 |
2.37e-37 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 143.56 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 174 KKEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEReareksreswylswaLDTNQEERDKGKTVEVGRAYFETE 253
Cdd:CHL00071 9 KKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHVEYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 254 RKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDDPTvnwD 333
Cdd:CHL00071 74 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD---D 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 334 EARYNECKDKILPYLKKLGFnPAKDLTFMPCSGLsgAGLRDIIPDSIC-----PWYSgpAFIPFIDLL----PSLNRKAD 404
Cdd:CHL00071 144 EELLELVELEVRELLSKYDF-PGDDIPIVSGSAL--LALEALTENPKIkrgenKWVD--KIYNLMDAVdsyiPTPERDTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 405 GPFIMPIVDKYK--DMGTVVMGKVESGTARKGQNL-LVMPNRTQVAVdqlwsdddeVTSVG----------PGENVKIKL 471
Cdd:CHL00071 219 KPFLMAIEDVFSitGRGTVATGRIERGTVKVGDTVeIVGLRETKTTT---------VTGLEmfqktldeglAGDNVGILL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 472 KGIEEEDVSPGFVLcdaSNP--IKTGKVFDAQVVIL------EHKSIIcAGYSAVMHIHCAaeEVTVKaliclVDKKTGD 543
Cdd:CHL00071 290 RGIQKEDIERGMVL---AKPgtITPHTKFEAQVYILtkeeggRHTPFF-PGYRPQFYVRTT--DVTGK-----IESFTAD 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937271225 544 KSKSRPRFVKQDQVaIMRIECSGMICLEQfklfpQMgRFTLRDENKTIAIGKVLKVIE 601
Cdd:CHL00071 359 DGSKTEMVMPGDRI-KMTVELIYPIAIEK-----GM-RFAIREGGRTVGAGVVSKILK 409
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
179-375 |
3.01e-37 |
|
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: 136.66 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYereareksreswylsWALDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEfetgfdrGGQTREHAMLAKtAGVKHLVVLVNKMDDPtvnwDEARYN 338
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFD 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937271225 339 ECKDKILPYLKKLGFN--PAKDLTFMPCSGLSGAGLRDI 375
Cdd:cd00881 134 EVLREIKELLKLIGFTflKGKDVPIIPISALTGEGIEEL 172
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
175-505 |
5.12e-37 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 143.43 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTIGGQIMSLTGMVDKRTLEKYEReareksreswylswaLDTNQEERDKGKTVEVGRAYFETER 254
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDE---------------IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVNwDE 334
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVD--VVD-DE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 335 ARYNECKDKILPYLKKLGFnPAKDLTFMPCSGLSGAGLRD--IIPDSICpwysgpAFIPFID-LLPSLNRKADGPFIMPI 411
Cdd:PLN03127 194 ELLELVEMELRELLSFYKF-PGDEIPIIRGSALSALQGTNdeIGKNAIL------KLMDAVDeYIPEPVRVLDKPFLMPI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 412 VDKY--KDMGTVVMGKVESGTARKGQNLLVmpnrtqVAVDQLWSDDDEVTSV----------GPGENVKIKLKGIEEEDV 479
Cdd:PLN03127 267 EDVFsiQGRGTVATGRVEQGTIKVGEEVEI------VGLRPGGPLKTTVTGVemfkkildqgQAGDNVGLLLRGLKREDV 340
|
330 340
....*....|....*....|....*.
gi 1937271225 480 SPGFVLCDASNpIKTGKVFDAQVVIL 505
Cdd:PLN03127 341 QRGQVICKPGS-IKTYKKFEAEIYVL 365
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
174-505 |
1.35e-35 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 138.05 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 174 KKEHVNVVFIGHVDAGKSTiggqimsLTGMVDKRTLEKYEREAREKSreswylswALDTNQEERDKGKTVEVGRAYFETE 253
Cdd:PRK12735 9 TKPHVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGGEAKAYD--------QIDNAPEEKARGITINTSHVEYETA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 254 RKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNK---MDDPtv 330
Cdd:PRK12735 74 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKcdmVDDE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 331 nwdearynECKD----KILPYLKKLGFnPAKDLTFMPCSGLsgAGLRDiipDSICPWYsgPAFIPFIDLL----PSLNRK 402
Cdd:PRK12735 145 --------ELLElvemEVRELLSKYDF-PGDDTPIIRGSAL--KALEG---DDDEEWE--AKILELMDAVdsyiPEPERA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 403 ADGPFIMPIVDKY--KDMGTVVMGKVESGTARKGQNL-LVMPNRTQVAVdqlwsdddeVTSVG----------PGENVKI 469
Cdd:PRK12735 209 IDKPFLMPIEDVFsiSGRGTVVTGRVERGIVKVGDEVeIVGIKETQKTT---------VTGVEmfrklldegqAGDNVGV 279
|
330 340 350
....*....|....*....|....*....|....*.
gi 1937271225 470 KLKGIEEEDVSPGFVLCdASNPIKTGKVFDAQVVIL 505
Cdd:PRK12735 280 LLRGTKREDVERGQVLA-KPGSIKPHTKFEAEVYVL 314
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
174-601 |
1.37e-35 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 139.75 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 174 KKEHVNVVFIGHVDAGKSTIGGQI-MSLTGMVDKRTlEKYEReareksreswylswaLDTNQEERDKGKTVEVGRAYFET 252
Cdd:PLN03126 78 KKPHVNIGTIGHVDHGKTTLTAALtMALASMGGSAP-KKYDE---------------IDAAPEERARGITINTATVEYET 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 253 ERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDDPTvnw 332
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 333 DEARYNECKDKILPYLKKLGFnPAKDLTFMPCSGLSGA---------------------GLRDIIpDSICPwysgpafIP 391
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEF-PGDDIPIISGSALLALealmenpnikrgdnkwvdkiyELMDAV-DSYIP-------IP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 392 fidllpslNRKADGPFIMPIVDKYK--DMGTVVMGKVESGTARKGQNLLVM-----PNRTQVAVDQLWSDDDEVTSvgpG 464
Cdd:PLN03126 283 --------QRQTDLPFLLAVEDVFSitGRGTVATGRVERGTVKVGETVDIVglretRSTTVTGVEMFQKILDEALA---G 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 465 ENVKIKLKGIEEEDVSPGFVLCDASNpIKTGKVFDAQVVILEHK-----SIICAGYSAVMHIHcaAEEVTVKaliclVDK 539
Cdd:PLN03126 352 DNVGLLLRGIQKADIQRGMVLAKPGS-ITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMR--TTDVTGK-----VTS 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937271225 540 KTGDKSKSRPRFVKQDQVAiMRIECSGMICLEQfklfpQMgRFTLRDENKTIAIGKVLKVIE 601
Cdd:PLN03126 424 IMNDKDEESKMVMPGDRVK-MVVELIVPVACEQ-----GM-RFAIREGGKTVGAGVIQSIIE 478
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
175-505 |
1.45e-35 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 138.01 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 175 KEHVNVVFIGHVDAGKSTiggqimsLTGMVDKRTLEKYEREAREKSreswylswALDTNQEERDKGKTVEVGRAYFETER 254
Cdd:PRK00049 10 KPHVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGAEAKAYD--------QIDKAPEEKARGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 255 KHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNK---MDDPtvN 331
Cdd:PRK00049 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKcdmVDDE--E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 332 WDEARYNECKDkilpYLKKLGFnPAKDLTFMPCSGLsgAGLRDiipDSICPWYSgpafiPFIDLL-------PSLNRKAD 404
Cdd:PRK00049 146 LLELVEMEVRE----LLSKYDF-PGDDTPIIRGSAL--KALEG---DDDEEWEK-----KILELMdavdsyiPTPERAID 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 405 GPFIMPIVDKY--KDMGTVVMGKVESGTARKGQNL-LVMPNRTQVAVdqlwsdddeVTSVG----------PGENVKIKL 471
Cdd:PRK00049 211 KPFLMPIEDVFsiSGRGTVVTGRVERGIIKVGEEVeIVGIRDTQKTT---------VTGVEmfrklldegqAGDNVGALL 281
|
330 340 350
....*....|....*....|....*....|....
gi 1937271225 472 KGIEEEDVSPGFVLCdASNPIKTGKVFDAQVVIL 505
Cdd:PRK00049 282 RGIKREDVERGQVLA-KPGSITPHTKFEAEVYVL 314
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
184-597 |
9.73e-35 |
|
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: 139.28 E-value: 9.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIggqIMSLTGMvdkrtlekyereareksreswylswalDTN--QEERDKGKTVEVGRAYFETER-KHFTIL 260
Cdd:COG3276 7 GHIDHGKTTL---VKALTGI---------------------------DTDrlKEEKKRGITIDLGFAYLPLPDgRRLGFV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 261 DAPGHKSFVPNMIGGAAQADLAVLVISArkgefetgfDRG--GQTREHamLA--KTAGVKHLVVLVNKMDdpTVnwDEAR 336
Cdd:COG3276 57 DVPGHEKFIKNMLAGAGGIDLVLLVVAA---------DEGvmPQTREH--LAilDLLGIKRGIVVLTKAD--LV--DEEW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 337 YNECKDKILPYLKKLGFnpaKDLTFMPCSGLSGAG---LRDIIpdsicpwysgpafipfIDLLPSL-NRKADGPFIMPI- 411
Cdd:COG3276 122 LELVEEEIRELLAGTFL---EDAPIVPVSAVTGEGideLRAAL----------------DALAAAVpARDADGPFRLPId 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 412 -VDKYKDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLCDAsN 490
Cdd:COG3276 183 rVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAP-G 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHksiicAGYS----AVMHIHCAAEEVTVKALicLVDKKTgdksksrprfVKQDQVAIMRIEcsg 566
Cdd:COG3276 262 ALRPTDRIDVRLRLLPS-----APRPlkhwQRVHLHHGTAEVLARVV--LLDREE----------LAPGEEALAQLR--- 321
|
410 420 430
....*....|....*....|....*....|....
gi 1937271225 567 micLEQfKLFPQMG-RFTLRDEN--KTIAIGKVL 597
Cdd:COG3276 322 ---LEE-PLVAARGdRFILRDYSprRTIGGGRVL 351
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
491-599 |
8.81e-31 |
|
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.
Pssm-ID: 397314 [Multi-domain] Cd Length: 105 Bit Score: 115.82 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEH-----KSIICAGYSAVMHIHCAAEEVTVKALICLVDkkTGDKSKsRPRFVKQDQVAIMRIECS 565
Cdd:pfam03143 1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77
|
90 100 110
....*....|....*....|....*....|....
gi 1937271225 566 GMICLEQFKlfpqmgRFTLRDENKTIAIGKVLKV 599
Cdd:pfam03143 78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
491-599 |
1.73e-29 |
|
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.
Pssm-ID: 294008 [Multi-domain] Cd Length: 109 Bit Score: 112.25 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 491 PIKTGKVFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICL 570
Cdd:cd04093 1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
|
90 100
....*....|....*....|....*....
gi 1937271225 571 EQFKLFPQMGRFTLRDENKTIAIGKVLKV 599
Cdd:cd04093 81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
178-542 |
4.40e-29 |
|
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: 121.90 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 178 VNVVFIGHVDAGKSTIggqIMSLTGMvdkrtlekyereareksreswylswALDTNQEERDKGKTVEVGRAYFETERKHF 257
Cdd:TIGR00475 1 MIIATAGHVDHGKTTL---LKALTGI-------------------------AADRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 258 TILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDDPtvnwDEARY 337
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRV----NEEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 338 NECKDKILPYLKKLGFNpaKDLTFMPCSGLSGAGLRDIIPDsicpwysgpafipFIDLLPSLNRK-ADGPFIMPI--VDK 414
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFL--KNAKIFKTSAKTGQGIGELKKE-------------LKNLLESLDIKrIQKPLRMAIdrAFK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 415 YKDMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFvLCDASNPIKT 494
Cdd:TIGR00475 187 VKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGL-LILTPEDPKL 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1937271225 495 GKV--FDAQVVILEHKsiicagysaVMHIHCAAEEVTVKalICLVDKKTG 542
Cdd:TIGR00475 266 RVVvkFIAEVPLLELQ---------PYHIAHGMSVTTGK--ISLLDKGIA 304
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
177-326 |
5.66e-28 |
|
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: 111.14 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 177 HVNVVFIGHVDAGKSTiggqimsLTGMVDKRTLEKYEREAREKSreswylswALDTNQEERDKGKTVEVGRAYFETERKH 256
Cdd:cd01884 2 HVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGAKAKKYD--------EIDKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 257 FTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMD 326
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
406-487 |
8.57e-27 |
|
Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 293899 [Multi-domain] Cd Length: 84 Bit Score: 103.74 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 406 PFIMPIVDKYKDM-GTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDD-EVTSVGPGENVKIKLKGIEEEDVSPGF 483
Cdd:cd03698 1 PFRLSIDDKYKSPrGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDeETDWAIAGDTVTLRLRGIEVEDIQPGD 80
|
....
gi 1937271225 484 VLCD 487
Cdd:cd03698 81 ILSS 84
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
498-596 |
3.69e-23 |
|
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).
Pssm-ID: 294004 [Multi-domain] Cd Length: 104 Bit Score: 94.18 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 498 FDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKSRPRFVKQDQVAIMRIECSGMICLEQFKLFP 577
Cdd:cd03705 6 FTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETFSEYP 85
|
90
....*....|....*....
gi 1937271225 578 QMGRFTLRDENKTIAIGKV 596
Cdd:cd03705 86 PLGRFAVRDMRQTVAVGVI 104
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
184-372 |
3.48e-22 |
|
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: 93.82 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIggqIMSLTGMvdkrtlekyereareksreswylswALDTNQEERDKGKTVEVGRAYFETER-KHFTILDA 262
Cdd:cd04171 6 GHIDHGKTTL---IKALTGI-------------------------ETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 263 PGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVLVNKMDdpTVnwDEARYNECKD 342
Cdd:cd04171 58 PGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKAD--LV--DEDRLELVEE 126
|
170 180 190
....*....|....*....|....*....|
gi 1937271225 343 KILPYLKKLGFnpaKDLTFMPCSGLSGAGL 372
Cdd:cd04171 127 EILELLAGTFL---ADAPIFPVSSVTGEGI 153
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
498-596 |
4.53e-18 |
|
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).
Pssm-ID: 275447 [Multi-domain] Cd Length: 102 Bit Score: 79.74 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 498 FDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALICLVDKKTGDKSKsrPRFVKQDQVAIMRIECSGMICLEQFKLFP 577
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKP--PDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 1937271225 578 QMGRFTLRDENKTIAIGKV 596
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
184-529 |
2.69e-16 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 82.41 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 184 GHVDAGKSTIggqIMSLTGmVDKRTLEkyereareksreswylswaldtnqEERDKGKTVEVGRAYF-ETERKHFTILDA 262
Cdd:PRK10512 7 GHVDHGKTTL---LQAITG-VNADRLP------------------------EEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 263 PGHKSFVPNMIGGAAQADLAVLVISARKGEFetgfdrgGQTREHAMLAKTAGVKHLVVLVNKMDdpTVnwDEARYNECKD 342
Cdd:PRK10512 59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKAD--RV--DEARIAEVRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 343 KILPYLKKLGFNpakDLTFMPCSGLSGAG---LRDiipdsicpwysgpafipFIDLLPSLNRKADGPFIMPIvDK---YK 416
Cdd:PRK10512 128 QVKAVLREYGFA---EAKLFVTAATEGRGidaLRE-----------------HLLQLPEREHAAQHRFRLAI-DRaftVK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 417 DMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKG-IEEEDVSPG-FVLCDASNPikt 494
Cdd:PRK10512 187 GAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGdWLLADAPPE--- 263
|
330 340 350
....*....|....*....|....*....|....*
gi 1937271225 495 gkVFDAQVVILEHKSIICAGYSavMHIHCAAEEVT 529
Cdd:PRK10512 264 --PFTRVIVELQTHTPLTQWQP--LHIHHAASHVT 294
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
178-338 |
1.01e-13 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 69.99 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 178 VNVVFIGHVDAGKSTIggqIMSLTGMVDKRTLEKYEREAREKsreswyLSWAlDT------NQEERDKGKTVEVGRAYFE 251
Cdd:cd01888 1 INIGTIGHVAHGKTTL---VKALSGVWTVRHKEELKRNITIK------LGYA-NAkiykcpNCGCPRPYDTPECECPGCG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 252 TERK---HFTILDAPGHKSFVPNMIGGAAQADLAVLVISArkgefETGFDRgGQTREHAMLAKTAGVKHLVVLVNKMDdp 328
Cdd:cd01888 71 GETKlvrHVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----NEPCPQ-PQTSEHLAALEIMGLKHIIILQNKID-- 142
|
170
....*....|
gi 1937271225 329 TVNWDEARYN 338
Cdd:cd01888 143 LVKEEQALEN 152
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
406-487 |
1.13e-13 |
|
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: 66.38 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 406 PFIMPIVDKYKDMGT--VVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGF 483
Cdd:cd16267 1 PFRLSVSDVFKGQGSgfTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 1937271225 484 VLCD 487
Cdd:cd16267 81 ILCD 84
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
178-342 |
1.65e-13 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 72.58 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 178 VNVVFIGHVDAGKSTIggqIMSLTGmvdkrtlekyereareksreswylSWAlDTNQEERDKGKTVEVGRA--------- 248
Cdd:PRK04000 10 VNIGMVGHVDHGKTTL---VQALTG------------------------VWT-DRHSEELKRGITIRLGYAdatirkcpd 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 249 -----YFETERK------------HFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFETgfdrggQTREHAMLAK 311
Cdd:PRK04000 62 ceepeAYTTEPKcpncgsetellrRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEHLMALD 135
|
170 180 190
....*....|....*....|....*....|...
gi 1937271225 312 TAGVKHLVVLVNKMDdpTVNWDEAR--YNECKD 342
Cdd:PRK04000 136 IIGIKNIVIVQNKID--LVSKERALenYEQIKE 166
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
178-387 |
3.88e-13 |
|
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: 68.16 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 178 VNVVFIGHVDAGKSTIGGQIMSLTGmvdkrtlekyereareksreswylSWALDTNQEERDKGKTVEVGRAYF------- 250
Cdd:cd01889 1 VNVGLLGHVDSGKTSLAKALSEIAS------------------------TAAFDKNPQSQERGITLDLGFSSFevdkpkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 251 -------ETERKHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGeFETgfdrggQTREHAMLAKTAGVKhLVVLVN 323
Cdd:cd01889 57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQT------QTAECLVIGELLCKP-LIVVLN 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937271225 324 KMDDPTVNWDEARYNECKDKILPYLKKLGFnpaKDLTFMPCSGLSG---AGLRDIIPDSICPWYSGP 387
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKTRL---KDSPIIPVSAKPGegeAELGGELKNLIVLPLINL 192
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
404-491 |
4.49e-13 |
|
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: 64.90 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 404 DGPFIMPIVDKYK--DMGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSP 481
Cdd:cd03693 2 DKPLRLPIQDVYKigGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKR 81
|
90
....*....|
gi 1937271225 482 GFVLCDASNP 491
Cdd:cd03693 82 GDVAGDSKND 91
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
179-490 |
3.21e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 69.35 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKRTlEKYEReareksreswylswALDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTREHAMLAKTAGVKHLVVlVNKMDDPTvnwdeARYN 338
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDRPG-----ARPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 339 ECKDKILPYLKKLGFNPAK-DLTFMPCSGLSG-AGL-RDIIPDSICPWYSGpafipFIDLLPSLNRKADGPFIMPI--VD 413
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQlDFPIVYASALNGiAGLdHEDMAEDMTPLYQA-----IVDHVPAPDVDLDGPFQMQIsqLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 414 KYKDMGTVVMGKVESGTARKGQNLLVMPNR------------TQVAVDQLWSDDDEVTSVgpgenvkIKLKGIEEEDVSP 481
Cdd:PRK10218 214 YNSYVGVIGIGRIKRGKVKPNQQVTIIDSEgktrnakvgkvlGHLGLERIETDLAEAGDI-------VAITGLGELNISD 286
|
....*....
gi 1937271225 482 gfVLCDASN 490
Cdd:PRK10218 287 --TVCDTQN 293
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
180-376 |
3.82e-12 |
|
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: 64.80 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 180 VVFIGHVDAGKSTIggqimsltgmVDK-RTLEKYEREAReksreswylswaldtnqeerdkGKTVEVGrAYF---ETERK 255
Cdd:cd01887 3 VTVMGHVDHGKTTL----------LDKiRKTNVAAGEAG----------------------GITQHIG-AYQvpiDVKIP 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 256 HFTILDAPGHKSFVpNM-IGGAAQADLAVLVISArkgefetgfDRG--GQTREHAMLAKTAGVKhLVVLVNKMD-DPTVN 331
Cdd:cd01887 50 GITFIDTPGHEAFT-NMrARGASVTDIAILVVAA---------DDGvmPQTIEAINHAKAANVP-IIVAINKIDkPYGTE 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937271225 332 WDEARYNECKDKilpyLKKLGFNPAKDLTFMPCSGLSGAGLRDII 376
Cdd:cd01887 119 ADPERVKNELSE----LGLVGEEWGGDVSIVPISAKTGEGIDDLL 159
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
179-346 |
4.93e-12 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 66.46 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKrtLEKYEREareksreswylSWALDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDR--LGRVEDG-----------NTVSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAAQADLAVLVISARKGefetgfdRGGQTREHAMLAKTAGVKHLVVlVNKMDDPTVNWDEArYN 338
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMDRARADFDKT-LA 138
|
170
....*....|..
gi 1937271225 339 ECKD----KILP 346
Cdd:cd04170 139 ALREafgrPVVP 150
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
419-486 |
7.16e-12 |
|
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: 61.13 E-value: 7.16e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937271225 419 GTVVMGKVESGTARKGQNLLVMPNRTQ-----VAVDQLWSDDDEVTSVGPGENVKIKLKGIEEEDVSPGFVLC 486
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTGkkkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
183-343 |
1.11e-10 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 64.38 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 183 IGHVDAGKSTIGGQIMSLTGMVDKRTlekyerEAREKSRESwylswalDTNQEERDKGKTVEVGRAYFETERKHFTILDA 262
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIG------EVEDGTTTM-------DFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 263 PGHKSFVPNMIGGAAQADLAVLVISARKGefetgfdRGGQTREHAMLAKTAGVKHLVVlVNKMDDPTVNWDEArYNECKD 342
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTETVWRQAEKYGVPRIIF-VNKMDRAGADFFRV-LAQLQE 138
|
.
gi 1937271225 343 K 343
Cdd:PRK12740 139 K 139
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
179-396 |
5.35e-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: 62.37 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKRtlekyeREAREKSRESwylswalDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHRI------GEVHDGNTVM-------DWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAAQADLAVLVISARKGefetgfdRGGQTREHAMLAKTAGVKHLVVlVNKMDDPTVNWDEArYN 338
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQTETVWRQADKYGVPRIVF-VNKMDREGADFDRV-LE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937271225 339 ECKDkilpylkKLGFNPakdltfmpcsglsgaglrdiIPDSIcPWYSGPAFIPFIDLL 396
Cdd:COG0480 149 QLKE-------RLGANP--------------------VPLQL-PIGAEDDFKGVIDLV 178
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
497-599 |
1.01e-09 |
|
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 294007 [Multi-domain] Cd Length: 87 Bit Score: 55.60 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 497 VFDAQVVILEHKSIICAGYSAVMHIHCAAEEVTVKALiclvDK---KTGDKSKSRPRFVKQDQVaiMRIecsGMicleqf 573
Cdd:cd03708 5 EFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISI----DKevlRTGDRALVRFRFLYRPEY--LRE---GQ------ 69
|
90 100
....*....|....*....|....*.
gi 1937271225 574 klfpqmgRFTLRdENKTIAIGKVLKV 599
Cdd:cd03708 70 -------RLIFR-EGRTKGIGTVTKV 87
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
179-326 |
1.71e-08 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 57.65 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKR-TLEKYEREAreksreswylswalDTNQEERDKGKTVEVGRAYFETERKHF 257
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAATSCDWDNHRI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937271225 258 TILDAPGHKSFVPNMIGGAAQADLAVLVISARKGefetgfdRGGQTREHAMLAKTAGVKHLVVlVNKMD 326
Cdd:PRK13351 76 NLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-------VQPQTETVWRQADRYGIPRLIF-INKMD 136
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
407-486 |
1.83e-08 |
|
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: 51.50 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 407 FIMPIVDKYKD--MGTVVMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKGIeeEDVSPGFV 484
Cdd:cd01342 1 LVMQVFKVFYIpgRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTGDT 78
|
..
gi 1937271225 485 LC 486
Cdd:cd01342 79 LT 80
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
166-326 |
8.46e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 55.01 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 166 PKVEESRSKKEHVNVVFIGHVDAGKSTIggqIMSLTGMvdkrTLEKYEREAR------------------EKSRESWYLS 227
Cdd:PTZ00327 23 PLTPEVISRQATINIGTIGHVAHGKSTV---VKALSGV----KTVRFKREKVrnitiklgyanakiykcpKCPRPTCYQS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 228 WAldTNQEERDK----GKTVEVGRayfeterkHFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFETgfdrggQT 303
Cdd:PTZ00327 96 YG--SSKPDNPPcpgcGHKMTLKR--------HVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQP------QT 159
|
170 180
....*....|....*....|...
gi 1937271225 304 REHAMLAKTAGVKHLVVLVNKMD 326
Cdd:PTZ00327 160 SEHLAAVEIMKLKHIIILQNKID 182
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
179-377 |
5.11e-07 |
|
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: 50.22 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMVDKrtlekyeREAREKsreswylswALDTNQEERDKGKTVEVGRAYFETERKH-- 256
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSE-------REMKEQ---------VLDSMDLERERGITIKAQAVRLFYKAKDge 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 257 ---FTILDAPGHKSF---VPNMIgGAAQAdlAVLVISARKG-EfetgfdrgGQTREHAMLAKTAGVKHLVVLvNKMDDPT 329
Cdd:cd01890 66 eylLNLIDTPGHVDFsyeVSRSL-AACEG--ALLVVDATQGvE--------AQTLANFYLALENNLEIIPVI-NKIDLPA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937271225 330 VNWDEARyNECKDKIlpylkklGFNPAKdltFMPCSGLSGAGLRDIIP 377
Cdd:cd01890 134 ADPDRVK-QEIEDVL-------GLDASE---AILVSAKTGLGVEDLLE 170
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
157-439 |
7.18e-07 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 52.14 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 157 TPKVSKKKLPKVEESRSKKEHVNVVFIGHVDAGKSTIGGQImsltgmvdkrtlekyereareksRESwylswalDTNQEE 236
Cdd:CHL00189 224 NEKTSNLDNTSAFTENSINRPPIVTILGHVDHGKTTLLDKI-----------------------RKT-------QIAQKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 237 RDkGKTVEVGrAYfETERKH------FTILDAPGHKSFVPNMIGGAAQADLAVLVISArkgefetgfDRG--GQTREHAM 308
Cdd:CHL00189 274 AG-GITQKIG-AY-EVEFEYkdenqkIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA---------DDGvkPQTIEAIN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 309 LAKTAGVKhLVVLVNKMDDPTVNWDEARYNECKDKILPylKKLGfnpaKDLTFMPCSGLSGAGLRDIIpDSICpwysgpA 388
Cdd:CHL00189 342 YIQAANVP-IIVAINKIDKANANTERIKQQLAKYNLIP--EKWG----GDTPMIPISASQGTNIDKLL-ETIL------L 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1937271225 389 FIPFIDLLPSLNRKADGPFIMPIVDKYKdmGTVVMGKVESGTARKGQNLLV 439
Cdd:CHL00189 408 LAEIEDLKADPTQLAQGIILEAHLDKTK--GPVATILVQNGTLHIGDIIVI 456
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
251-372 |
1.09e-06 |
|
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: 51.55 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 251 ETERKHFTILDAPGHKSFVpNM-IGGAAQADLAVLVISArkgefetgfDRG--GQTRE---HamlAKTAGVKhLVVLVNK 324
Cdd:COG0532 47 ETNGGKITFLDTPGHEAFT-AMrARGAQVTDIVILVVAA---------DDGvmPQTIEainH---AKAAGVP-IIVAINK 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1937271225 325 MDDPTVNwdearynecKDKILPYLKKLGFNPAK---DLTFMPCSGLSGAGL 372
Cdd:COG0532 113 IDKPGAN---------PDRVKQELAEHGLVPEEwggDTIFVPVSAKTGEGI 154
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
179-369 |
5.40e-06 |
|
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: 47.20 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKSTIGGQIMSLTGMvdkrtlekyEREAREKSREswylswALDTNQEERDKGKTVEVGRAYFETERKHFT 258
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITILAKNTAITYKDTKIN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSF------VPNMiggaaqADLAVLVISARKGEFEtgfdrggQTRehAMLAKT--AGVKHLVVlVNKMDDPtv 330
Cdd:cd01891 69 IIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTR--FVLKKAleAGLKPIVV-INKIDRP-- 130
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937271225 331 nwdEARYNECKDKILPYLKKLGFNPAK-DLTFMPCSGLSG 369
Cdd:cd01891 131 ---DARPEEVVDEVFDLFLELNATDEQlDFPIVYASAKNG 167
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
183-329 |
1.02e-05 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 47.59 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 183 IGHVDAGKSTI-------GGQImSLTGMVDKRtlekyerEAREKSRESWYlswaldtnQEERDKGKTVEVGRAYFETERK 255
Cdd:cd04169 8 ISHPDAGKTTLteklllfGGAI-QEAGAVKAR-------KSRKHATSDWM--------EIEKQRGISVTSSVMQFEYKGC 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937271225 256 HFTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGeFETgfdrggQTREHAMLAKTAGVKhLVVLVNKMDDPT 329
Cdd:cd04169 72 VINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-VEP------QTRKLFEVCRLRGIP-IITFINKLDREG 137
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
179-326 |
1.38e-05 |
|
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: 46.49 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 179 NVVFIGHVDAGKStiggqimSLTGMvdkrtLEKYEREAREKSRESWYLSWALDTNQEERDKG---KTVEVGRAYFETERK 255
Cdd:cd04167 2 NVCIAGHLHHGKT-------SLLDM-----LIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGisiKSNPISLVLEDSKGK 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937271225 256 H--FTILDAPGHKSFVPNMIGGAAQADLAVLVISARKGEFEtgfdrggQTRE---HAMLAKtagvKHLVVLVNKMD 326
Cdd:cd04167 70 SylINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTS-------VTERlirHAIQEG----LPMVLVINKID 134
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
181-376 |
2.23e-05 |
|
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: 45.14 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 181 VFIGHVDAGKSTIggqIMSLTGmvdkrtlekyeREAREKSRESwylswaldtnqeerdkGKTVE--VGRAYFETERKHFT 258
Cdd:cd00882 1 VVVGRGGVGKSSL---LNALLG-----------GEVGEVSDVP----------------GTTRDpdVYVKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 259 ILDAPGHKSFVPNMIGGAA-----QADLAVLVISARKGEFetgFDRggQTREHAMLAKTAGVKHLVVLvNKMDdptvnwd 333
Cdd:cd00882 51 LVDTPGLDEFGGLGREELArlllrGADLILLVVDSTDRES---EED--AKLLILRRLRKEGIPIILVG-NKID------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937271225 334 eaRYNECKDKILPYLKKLGFNPakDLTFMPCSGLSGAGLRDII 376
Cdd:cd00882 118 --LLEEREVEELLRLEELAKIL--GVPVFEVSAKTGEGVDELF 156
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
1-135 |
5.77e-05 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 45.40 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 1 MA-QDNAEmstkfstLNVNAAEFVPSFTSFSAAASTTPLSSDNTPAAATIAHMDTASVPASASGTPATTPNSEASGSGST 79
Cdd:PRK10856 146 MAdQSSAE-------LSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVD 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937271225 80 NALNQadVPPAESPMQTSPIKTAAAAApveniNTADKIAANNGNENDPADSW-DVED 135
Cdd:PRK10856 219 TAATP--APAAPATPDGAAPLPTDQAG-----VSTPAADPNALVMNFTADCWlEVTD 268
|
|
| PAM2 |
pfam07145 |
Ataxin-2 C-terminal region; The PABP-interacting motif PAM2 has been identified in various ... |
11-27 |
5.75e-04 |
|
Ataxin-2 C-terminal region; The PABP-interacting motif PAM2 has been identified in various eukaryotic proteins as an important binding site for pfam00658. It has been found in a wide range of eukaryotic proteins. Strikingly, this motif appears to occur solely outside of globular domains.
Pssm-ID: 429316 Cd Length: 17 Bit Score: 37.21 E-value: 5.75e-04
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
407-475 |
1.38e-03 |
|
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: 37.88 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937271225 407 FIMPIVDKY--KDMGTVVMGKVESGTARKGqnllvmpnrtqvavdqlwsddDEVTSVGPGENVKIKLKGIE 475
Cdd:cd03697 1 FLMPIEDVFsiPGRGTVVTGRIERGVIKVG---------------------DEVEIVGFKETLKTTVTGIE 50
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
422-485 |
1.87e-03 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 37.55 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937271225 422 VMGKVESGTARKGQNLLVMPNRTQVAVDQLWSDDDEVTSVGPGENVKIKLKgiEEEDVSPGFVL 485
Cdd:cd03695 18 YAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLE--DEIDVSRGDLI 79
|
|
| SP4_N |
cd22536 |
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ... |
5-99 |
2.28e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.
Pssm-ID: 411773 [Multi-domain] Cd Length: 623 Bit Score: 41.06 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 5 NAEMSTKFSTLNVNAAEFVPSFTSFSAAASTTPLSSDNTPAAAT---IAHMDTASVPASASGTPATTPNSEASGSGSTNA 81
Cdd:cd22536 274 NQLVSTPITTASVSTMPESPSSSTTCTTTASTSLTSSDTLVSSAetgQYASTAASSERTEEEPQTSAAESEAQSSSQLQS 353
|
90
....*....|....*...
gi 1937271225 82 LNQADVPPAESPMQTSPI 99
Cdd:cd22536 354 NGLQNVQDQSNSLQQVQI 371
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
162-291 |
4.36e-03 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 40.23 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 162 KKKLPKVEESRSKKEHV-NVVFIGHVDAGKSTIGGQIMSLTGMVDkrtlEKYEREAReksreswylswALDTNQEERDKG 240
Cdd:PRK07560 4 KKMVEKILELMKNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMIS----EELAGEQL-----------ALDFDEEEQARG 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937271225 241 KTVEVGRA--YFETERKHFTI--LDAPGHKSFvpnmiGG----AAQA-DLAVLVISARKG 291
Cdd:PRK07560 69 ITIKAANVsmVHEYEGKEYLInlIDTPGHVDF-----GGdvtrAMRAvDGAIVVVDAVEG 123
|
|
| |
