|
Name |
Accession |
Description |
Interval |
E-value |
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
69-498 |
3.39e-148 |
|
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: 430.51 E-value: 3.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 69 APKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFE 148
Cdd:COG5256 2 ASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 149 TEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEfetgfekGGQTREHAMLAKTAGVKHLIVLINKMDDptVN 228
Cdd:COG5256 82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDA--VN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 229 WSSERYEECKEKLVPFLKKVGFNPkKDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPIVD 308
Cdd:COG5256 153 YSEKRYEEVKEEVSKLLKMVGYKV-DKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 309 KY--KDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDPNNL 386
Cdd:COG5256 232 VYsiSGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 387 CHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLE 466
Cdd:COG5256 312 PTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIE 391
|
410 420 430
....*....|....*....|....*....|..
gi 2131067815 467 TFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEK 498
Cdd:COG5256 392 KFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
76-292 |
4.65e-147 |
|
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: 419.59 E-value: 4.65e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 156 ILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSSERYE 235
Cdd:cd01883 81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131067815 236 ECKEKLVPFLKKVGFNPkKDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLP 292
Cdd:cd01883 161 EIKKKVSPFLKKVGYNP-KDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLE 216
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
69-498 |
1.94e-141 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 413.17 E-value: 1.94e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 69 APKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFE 148
Cdd:PRK12317 1 AKEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 149 TEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEfetGFEkgGQTREHAMLAKTAGVKHLIVLINKMDdpTVN 228
Cdd:PRK12317 81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAG---GVM--PQTREHVFLARTLGINQLIVAINKMD--AVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 229 WSSERYEECKEKLVPFLKKVGFNPkKDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPIVD 308
Cdd:PRK12317 154 YDEKRYEEVKEEVSKLLKMVGYKP-DDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 309 KY--KDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDPNNL 386
Cdd:PRK12317 233 VYsiSGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 387 CHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLE 466
Cdd:PRK12317 313 PTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIE 392
|
410 420 430
....*....|....*....|....*....|..
gi 2131067815 467 TFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEK 498
Cdd:PRK12317 393 KVKEIPQLGRFAIRDMGQTIAAGMVIDVKPAK 424
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
72-499 |
2.19e-128 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 380.63 E-value: 2.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 72 KEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEK 151
Cdd:PTZ00141 5 KTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSS 231
Cdd:PTZ00141 85 YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 232 ERYEECKEKLVPFLKKVGFNPKKdIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPIVDKYK 311
Cdd:PTZ00141 165 ERYDEIKKEVSAYLKKVGYNPEK-VPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 312 --DMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDPNNLCHS 389
Cdd:PTZ00141 244 igGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 390 G-RTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETF 468
Cdd:PTZ00141 324 EcADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVF 403
|
410 420 430
....*....|....*....|....*....|.
gi 2131067815 469 KDFPQMGRFTLRDEGKTIAIGkVLKLVPEKD 499
Cdd:PTZ00141 404 NEYPPLGRFAVRDMKQTVAVG-VIKSVEKKE 433
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
71-499 |
2.03e-103 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 317.03 E-value: 2.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 71 KKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETE 150
Cdd:PLN00043 4 EKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 151 KKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWS 230
Cdd:PLN00043 84 KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 231 SERYEECKEKLVPFLKKVGFNPKKdIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPIVDKY 310
Cdd:PLN00043 164 KARYDEIVKEVSSYLKKVGYNPDK-IPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 311 K--DMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDP-NNLC 387
Cdd:PLN00043 243 KigGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSkDDPA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 388 HSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLET 467
Cdd:PLN00043 323 KEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVET 402
|
410 420 430
....*....|....*....|....*....|..
gi 2131067815 468 FKDFPQMGRFTLRDEGKTIAIGkVLKLVPEKD 499
Cdd:PLN00043 403 FSEYPPLGRFAVRDMRQTVAVG-VIKSVEKKD 433
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
69-482 |
1.09e-70 |
|
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: 231.52 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 69 APKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMV--DKrtLEKYEREAKEKNREtwYLSWAL--DTNQEERDKGKTVEVGR 144
Cdd:COG2895 12 HENKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQ--EIDLALltDGLQAEREQGITIDVAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 145 AYFETEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDd 224
Cdd:COG2895 88 RYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 225 pTVNWSSERYEECKEKLVPFLKKVGFnpkKDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRL 304
Cdd:COG2895 160 -LVDYSEEVFEEIVADYRAFAAKLGL---EDITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 305 PI--VDKYKD-----MGTVvlgklESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLkgieEEEI--L 375
Cdd:COG2895 236 PVqyVNRPNLdfrgyAGTI-----ASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTL----EDEIdiS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 376 PGFILCDPNNLCHSGRTFDAQIVIIEHKSIIcPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPrfVKQDQVCIA 455
Cdd:COG2895 307 RGDVIVAADAPPEVADQFEATLVWMDEEPLL-PGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAADS--LELNDIGRV 383
|
410 420
....*....|....*....|....*..
gi 2131067815 456 RLRTAGTICLETFKDFPQMGRFTLRDE 482
Cdd:COG2895 384 TLRLAEPIAFDPYADNRATGSFILIDR 410
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
72-271 |
2.93e-64 |
|
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: 206.61 E-value: 2.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 72 KEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAkeknretwylswALDTNQEERDKGKTVEVGRAYFETEK 151
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGefetgfeKGGQTREHAMLAKTAGVKhLIVLINKMDDPTvnwsS 231
Cdd:pfam00009 69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRVD----G 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2131067815 232 ERYEECKEKLV-PFLKKVGFNPKKdIHFMPCSGLTGANLKE 271
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDGEF-VPVVPGSALKGEGVQT 176
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
81-491 |
7.15e-63 |
|
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: 210.31 E-value: 7.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 81 GHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWAL--DTNQEERDKGKTVEVGRAYFETEKKHFTILD 158
Cdd:TIGR02034 7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTQGGEIDLALlvDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 159 APGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDdpTVNWSSERYEECK 238
Cdd:TIGR02034 87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMD--LVDYDEEVFENIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 239 EKLVPFLKKVGFnpkKDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPI--VDKYKDMGTV 316
Cdd:TIGR02034 158 KDYLAFAEQLGF---RDVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVqyVNRPNLDFRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 317 VLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKgiEEEEILPGFILCDPNNLCHSGRTFDAQ 396
Cdd:TIGR02034 235 YAGTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLD--DEIDISRGDLLAAADSAPEVADQFAAT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 397 IVIIEHKSIIcPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTrPRFVKQDqVCIARLRTAGTICLETFKDFPQMGR 476
Cdd:TIGR02034 313 LVWMAEEPLL-PGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA-KSLELNE-IGRVNLSLDEPIAFDPYAENRTTGA 389
|
410
....*....|....*..
gi 2131067815 477 FTL--RDEGKTIAIGKV 491
Cdd:TIGR02034 390 FILidRLSNRTVGAGMI 406
|
|
| eRF3_C_III |
cd03704 |
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ... |
388-494 |
2.02e-62 |
|
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: 198.93 E-value: 2.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 388 HSGRTFDAQIVIIEH-KSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLE 466
Cdd:cd03704 1 PVVTEFEAQIVILDLlKSIITAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLE 80
|
90 100
....*....|....*....|....*...
gi 2131067815 467 TFKDFPQMGRFTLRDEGKTIAIGKVLKL 494
Cdd:cd03704 81 TFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
76-292 |
2.89e-58 |
|
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: 191.63 E-value: 2.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETwYLSWAL--DTNQEERDKGKTVEVGRAYFETEKKH 153
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAALERSKSSGTQGE-KLDLALlvDGLQAEREQGITIDVAYRYFSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 154 FTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDdpTVNWSSER 233
Cdd:cd04166 80 FIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMD--LVDYDEEV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131067815 234 YEECKEKLVPFLKKVGFNpkkDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLP 292
Cdd:cd04166 151 FEEIKADYLAFAASLGIE---DITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVE 206
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
81-489 |
1.03e-54 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 193.99 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 81 GHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWAL--DTNQEERDKGKTVEVGRAYFETEKKHFTILD 158
Cdd:PRK05506 31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGTQGDEIDLALlvDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 159 APGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDdpTVNWSSERYEECK 238
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMD--LVDYDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 239 EKLVPFLKKVGFNpkkDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPI-------VDKYK 311
Cdd:PRK05506 182 ADYRAFAAKLGLH---DVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVEIASDRNLKDFRFPVqyvnrpnLDFRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 312 DMGTVVlgkleSGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKgiEEEEILPGFILCDPNNLCHSGR 391
Cdd:PRK05506 259 FAGTVA-----SGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLARADNRPEVAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 392 TFDAQIVIIEHKSIIcPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPrfVKQDQVCIARLRTAGTICLETFKDF 471
Cdd:PRK05506 332 QFDATVVWMAEEPLL-PGRPYLLKHGTRTVPASVAAIKYRVDVNTLERLAAKT--LELNEIGRCNLSTDAPIAFDPYARN 408
|
410 420
....*....|....*....|
gi 2131067815 472 PQMGRFTLRDE--GKTIAIG 489
Cdd:PRK05506 409 RTTGSFILIDRltNATVGAG 428
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
81-398 |
2.81e-53 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 186.66 E-value: 2.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 81 GHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWAL--DTNQEERDKGKTVEVGRAYFETEKKHFTILD 158
Cdd:PRK05124 34 GSVDDGKSTLIGRLLHDTKQIYEDQLASLHNDSKRHGTQGEKLDLALlvDGLQAEREQGITIDVAYRYFSTEKRKFIIAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 159 APGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDdpTVNWSSERYEECK 238
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMD--LVDYSEEVFERIR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 239 EKLVPFLKKVGFNPkkDIHFMPCSGLTGANLKEQSDFCPWYTGLPFIPYLDNLPNFNRSVDGPIRLPIvdKYkdmgtvVL 318
Cdd:PRK05124 185 EDYLTFAEQLPGNL--DIRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPV--QY------VN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 319 ----------GKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKgiEEEEILPGFILCDPNNLCH 388
Cdd:PRK05124 255 rpnldfrgyaGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLE--DEIDISRGDLLVAADEALQ 332
|
330
....*....|
gi 2131067815 389 SGRTFDAQIV 398
Cdd:PRK05124 333 AVQHASADVV 342
|
|
| eRF3_II |
cd04089 |
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ... |
301-382 |
6.52e-48 |
|
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: 159.96 E-value: 6.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 301 PIRLPIVDKYKDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFIL 380
Cdd:cd04089 1 PLRMPILDKYKDMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFVL 80
|
..
gi 2131067815 381 CD 382
Cdd:cd04089 81 CS 82
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
76-266 |
6.42e-39 |
|
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: 139.74 E-value: 6.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYereakeknretwylsWALDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 156 ILDAPGHKSFVPNMIGGASQADLAVLVISARKGEfetgfekGGQTREHAMLAKtAGVKHLIVLINKMDDPtvnwSSERYE 235
Cdd:cd00881 66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFD 133
|
170 180 190
....*....|....*....|....*....|...
gi 2131067815 236 ECKEKLVPFLKKVGFN--PKKDIHFMPCSGLTG 266
Cdd:cd00881 134 EVLREIKELLKLIGFTflKGKDVPIIPISALTG 166
|
|
| eRF3_II_like |
cd03698 |
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ... |
301-382 |
2.19e-36 |
|
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: 129.54 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 301 PIRLPIVDKYKDM-GTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSD-DVETDSVAPGENLKIRLKGIEEEEILPGF 378
Cdd:cd03698 1 PFRLSIDDKYKSPrGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPGD 80
|
....
gi 2131067815 379 ILCD 382
Cdd:cd03698 81 ILSS 84
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
71-400 |
5.93e-36 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 137.60 E-value: 5.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 71 KKEHVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNRetwylswaLDTNQEERDKGKTVEVGRAYFETE 150
Cdd:TIGR00485 9 TKPHVNVGTIGHVDHGKTT-------LTAAITTVLAKEGGAAARAYDQ--------IDNAPEEKARGITINTAHVEYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 151 KKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDDPTvnwS 230
Cdd:TIGR00485 74 TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD---D 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 231 SERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGLTGANLKEQsdfcpWYTG-LPFIPYLD-NLPNFNRSVDGPIRLPIVD 308
Cdd:TIGR00485 144 EELLELVEMEVRELLSQYDF-PGDDTPIIRGSALKALEGDAE-----WEAKiLELMDAVDeYIPTPEREIDKPFLLPIED 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 309 KY--KDMGTVVLGKLESGSICKGQ--QLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDPN 384
Cdd:TIGR00485 218 VFsiTGRGTVVTGRVERGIIKVGEevEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPG 297
|
330
....*....|....*.
gi 2131067815 385 NlCHSGRTFDAQIVII 400
Cdd:TIGR00485 298 S-IKPHTKFEAEVYVL 312
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
72-400 |
4.74e-35 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 135.07 E-value: 4.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 72 KEHVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNRetwylswaLDTNQEERDKGKTVEVGRAYFETEK 151
Cdd:PRK12736 10 KPHVNIGTIGHVDHGKTT-------LTAAITKVLAERGLNQAKDYDS--------IDAAPEEKERGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINK---MDDPtvn 228
Cdd:PRK12736 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKvdlVDDE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 229 wssERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGLTGANLKEqsdfcPWYTG-LPFIPYLDN-LPNFNRSVDGPIRLPI 306
Cdd:PRK12736 145 ---ELLELVEMEVRELLSEYDF-PGDDIPVIRGSALKALEGDP-----KWEDAiMELMDAVDEyIPTPERDTDKPFLMPV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 307 VDKY--KDMGTVVLGKLESGSICKGQQlvmmpnkhnVEVLGIlSDDVET------------DSVAPGENLKIRLKGIEEE 372
Cdd:PRK12736 216 EDVFtiTGRGTVVTGRVERGTVKVGDE---------VEIVGI-KETQKTvvtgvemfrkllDEGQAGDNVGVLLRGVDRD 285
|
330 340
....*....|....*....|....*....
gi 2131067815 373 EILPGFILCDPNNLC-HsgRTFDAQIVII 400
Cdd:PRK12736 286 EVERGQVLAKPGSIKpH--TKFKAEVYIL 312
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
71-495 |
5.90e-35 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 136.67 E-value: 5.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 71 KKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEReakeknretwylswaLDTNQEERDKGKTVEVGRAYFETE 150
Cdd:PLN03126 78 KKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYETE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 151 KKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDDPTvnwS 230
Cdd:PLN03126 143 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD---D 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 231 SERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGL-------TGANLKEQSDfcPWYTGLpfIPYLDNLPNF----NRSVD 299
Cdd:PLN03126 213 EELLELVELEVRELLSSYEF-PGDDIPIISGSALlalealmENPNIKRGDN--KWVDKI--YELMDAVDSYipipQRQTD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 300 GPIRLPIVDKYK--DMGTVVLGKLESGSICKGQ--QLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEIL 375
Cdd:PLN03126 288 LPFLLAVEDVFSitGRGTVATGRVERGTVKVGEtvDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 376 PGFILCDPNNLC-HSgrTFDAQIVIIEHK-----SIICPGYNAVLHIHTcieeVEITALICLVDKKSGEKSKTrprFVKQ 449
Cdd:PLN03126 368 RGMVLAKPGSITpHT--KFEAIVYVLKKEeggrhSPFFAGYRPQFYMRT----TDVTGKVTSIMNDKDEESKM---VMPG 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2131067815 450 DQVCIArLRTAGTICLEtfkdfpQMGRFTLRDEGKTIAIGKVLKLV 495
Cdd:PLN03126 439 DRVKMV-VELIVPVACE------QGMRFAIREGGKTVGAGVIQSII 477
|
|
| tufA |
CHL00071 |
elongation factor Tu |
71-400 |
7.07e-35 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 135.09 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 71 KKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEReakeknretwylswaLDTNQEERDKGKTVEVGRAYFETE 150
Cdd:CHL00071 9 KKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINTAHVEYETE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 151 KKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINK---MDDPtv 227
Cdd:CHL00071 74 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKedqVDDE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 228 nwssERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGLTGAN-LKEQSDFCPWYTglpfiPYLDNLPNFNRSVDGPIRLPI 306
Cdd:CHL00071 145 ----ELLELVELEVRELLSKYDF-PGDDIPIVSGSALLALEaLTENPKIKRGEN-----KWVDKIYNLMDAVDSYIPTPE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 307 VDKYKDM-------------GTVVLGKLESGSICKGQ--QLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEE 371
Cdd:CHL00071 215 RDTDKPFlmaiedvfsitgrGTVATGRIERGTVKVGDtvEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQK 294
|
330 340 350
....*....|....*....|....*....|
gi 2131067815 372 EEILPGFILCDPNNLC-HSgrTFDAQIVII 400
Cdd:CHL00071 295 EDIERGMVLAKPGTITpHT--KFEAQVYIL 322
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
81-498 |
9.92e-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: 137.74 E-value: 9.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 81 GHVDAGKSTIggqIMYLTGMvdkrtlekyereakeknrETwylswalDTNQEERDKGKTVEVGRAYFETEK-KHFTILDA 159
Cdd:COG3276 7 GHIDHGKTTL---VKALTGI------------------DT-------DRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 160 PGHKSFVPNMIGGASQADLAVLVISARkgEfetgfekgG---QTREHamLA--KTAGVKHLIVLINKMD--DPtvnwssE 232
Cdd:COG3276 59 PGHEKFIKNMLAGAGGIDLVLLVVAAD--E--------GvmpQTREH--LAilDLLGIKRGIVVLTKADlvDE------E 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 233 RYEECKEKLVPFLKKVGFnpkKDIHFMPCSGLTGANLKEqsdfcpwytglpFIPYLDNLPN--FNRSVDGPIRLPI--VD 308
Cdd:COG3276 121 WLELVEEEIRELLAGTFL---EDAPIVPVSAVTGEGIDE------------LRAALDALAAavPARDADGPFRLPIdrVF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 309 KYKDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDPNNLcH 388
Cdd:COG3276 186 SIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGAL-R 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 389 SGRTFDAQIVII--EHKSIicpGYNAVLHIHtcIEEVEITALICLVDKKSgeksktrprfVKQDQVCIARLRTAGTICLe 466
Cdd:COG3276 265 PTDRIDVRLRLLpsAPRPL---KHWQRVHLH--HGTAEVLARVVLLDREE----------LAPGEEALAQLRLEEPLVA- 328
|
410 420 430
....*....|....*....|....*....|....
gi 2131067815 467 TFKDfpqmgRFTLRDEG--KTIAIGKVLKLVPEK 498
Cdd:COG3276 329 ARGD-----RFILRDYSprRTIGGGRVLDPNPPK 357
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
72-399 |
1.36e-34 |
|
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: 133.74 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 72 KEHVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNRetwylswaLDTNQEERDKGKTVEVGRAYFETEK 151
Cdd:COG0050 10 KPHVNIGTIGHVDHGKTT-------LTAAITKVLAKKGGAKAKAYDQ--------IDKAPEEKERGITINTSHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMD---DPtvn 228
Cdd:COG0050 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDmvdDE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 229 wssERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGLtGAnlKEQSDFCPWYTG-LPFIPYLDN-LPNFNRSVDGPIRLPI 306
Cdd:COG0050 145 ---ELLELVEMEVRELLSKYGF-PGDDTPIIRGSAL-KA--LEGDPDPEWEKKiLELMDAVDSyIPEPERDTDKPFLMPV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 307 VDKY--KDMGTVVLGKLESGSICKGqqlvmmpnkHNVEVLGIlSDDVET------------DSVAPGENLKIRLKGIEEE 372
Cdd:COG0050 218 EDVFsiTGRGTVVTGRVERGIIKVG---------DEVEIVGI-RDTQKTvvtgvemfrkllDEGEAGDNVGLLLRGIKRE 287
|
330 340
....*....|....*....|....*..
gi 2131067815 373 EILPGFILCDPNNLcHSGRTFDAQIVI 399
Cdd:COG0050 288 DVERGQVLAKPGSI-TPHTKFEAEVYV 313
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
72-399 |
1.17e-32 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 128.38 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 72 KEHVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNretwylswALDTNQEERDKGKTVEVGRAYFETEK 151
Cdd:PRK00049 10 KPHVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGAEAKAYD--------QIDKAPEEKARGITINTAHVEYETEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINK---MDDPtvn 228
Cdd:PRK00049 75 RHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKcdmVDDE--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 229 wssERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGLTGAnlkEQSDFCPWYTG-LPFIPYLDN-LPNFNRSVDGPIRLPI 306
Cdd:PRK00049 145 ---ELLELVEMEVRELLSKYDF-PGDDTPIIRGSALKAL---EGDDDEEWEKKiLELMDAVDSyIPTPERAIDKPFLMPI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 307 VDKY--KDMGTVVLGKLESGSICKGQQlvmmpnkhnVEVLGIlSDDVET------------DSVAPGENLKIRLKGIEEE 372
Cdd:PRK00049 218 EDVFsiSGRGTVVTGRVERGIIKVGEE---------VEIVGI-RDTQKTtvtgvemfrkllDEGQAGDNVGALLRGIKRE 287
|
330 340
....*....|....*....|....*...
gi 2131067815 373 EILPGFILCDPNNL-CHsgRTFDAQIVI 399
Cdd:PRK00049 288 DVERGQVLAKPGSItPH--TKFEAEVYV 313
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
72-400 |
1.51e-32 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 129.17 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 72 KEHVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNRetwylswaLDTNQEERDKGKTVEVGRAYFETEK 151
Cdd:PLN03127 59 KPHVNVGTIGHVDHGKTT-------LTAAITKVLAEEGKAKAVAFDE--------IDKAPEEKARGITIATAHVEYETAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMD---DPTVn 228
Cdd:PLN03127 124 RHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDvvdDEEL- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 229 wsSERYEECKEKLVPFLKkvgFnPKKDIHFMPCSGLtgANLKEQSDFCPWYTGLPFIPYLDN-LPNFNRSVDGPIRLPIV 307
Cdd:PLN03127 196 --LELVEMELRELLSFYK---F-PGDEIPIIRGSAL--SALQGTNDEIGKNAILKLMDAVDEyIPEPVRVLDKPFLMPIE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 308 DKY--KDMGTVVLGKLESGSICKGQQlvmmpnkhnVEVLGILSDD--------VET-----DSVAPGENLKIRLKGIEEE 372
Cdd:PLN03127 268 DVFsiQGRGTVATGRVEQGTIKVGEE---------VEIVGLRPGGplkttvtgVEMfkkilDQGQAGDNVGLLLRGLKRE 338
|
330 340
....*....|....*....|....*...
gi 2131067815 373 EILPGFILCDPNNlCHSGRTFDAQIVII 400
Cdd:PLN03127 339 DVQRGQVICKPGS-IKTYKKFEAEIYVL 365
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
71-384 |
1.52e-32 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 128.03 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 71 KKEHVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNretwylswALDTNQEERDKGKTVEVGRAYFETE 150
Cdd:PRK12735 9 TKPHVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGGEAKAYD--------QIDNAPEEKARGITINTSHVEYETA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 151 KKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINK---MDDPtv 227
Cdd:PRK12735 74 NRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKcdmVDDE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 228 nwssERYEECKEKLVPFLKKVGFnPKKDIHFMPCSGLTGANLKEQSDFCPWYTGLpfIPYLDN-LPNFNRSVDGPIRLPI 306
Cdd:PRK12735 145 ----ELLELVEMEVRELLSKYDF-PGDDTPIIRGSALKALEGDDDEEWEAKILEL--MDAVDSyIPEPERAIDKPFLMPI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 307 VDKY--KDMGTVVLGKLESGSICKGQQlvmmpnkhnVEVLGIlSDDVET------------DSVAPGENLKIRLKGIEEE 372
Cdd:PRK12735 218 EDVFsiSGRGTVVTGRVERGIVKVGDE---------VEIVGI-KETQKTtvtgvemfrkllDEGQAGDNVGVLLRGTKRE 287
|
330
....*....|..
gi 2131067815 373 EILPGFILCDPN 384
Cdd:PRK12735 288 DVERGQVLAKPG 299
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
75-438 |
1.86e-30 |
|
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: 124.60 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 75 VNVVFIGHVDAGKSTIggqIMYLTGMvdkrtlekyereakeknretwylswALDTNQEERDKGKTVEVGRAYFETEKKHF 154
Cdd:TIGR00475 1 MIIATAGHVDHGKTTL---LKALTGI-------------------------AADRLPEEKKRGMTIDLGFAYFPLPDYRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 155 TILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMDdpTVNwsSERY 234
Cdd:TIGR00475 53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKAD--RVN--EEEI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 235 EECKEKLVPFLKKVGFNpkKDIHFMPCSGLTGANLKEQSDfcpwytglpfipYLDNLPNF--NRSVDGPIRLPI--VDKY 310
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFL--KNAKIFKTSAKTGQGIGELKK------------ELKNLLESldIKRIQKPLRMAIdrAFKV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 311 KDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILCDPNNlchsg 390
Cdd:TIGR00475 188 KGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPED----- 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2131067815 391 rTFDAQIVIIEHKSIICPGYnaVLHIHTCIEEVeiTALICLVDKKSGE 438
Cdd:TIGR00475 263 -PKLRVVVKFIAEVPLLELQ--PYHIAHGMSVT--TGKISLLDKGIAL 305
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
74-223 |
1.60e-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: 111.91 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 74 HVNVVFIGHVDAGKSTiggqimyLTGMVDKRTLEKYEREAKEKNretwylswALDTNQEERDKGKTVEVGRAYFETEKKH 153
Cdd:cd01884 2 HVNVGTIGHVDHGKTT-------LTAAITKVLAKKGGAKAKKYD--------EIDKAPEEKARGITINTAHVEYETANRH 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 154 FTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMD 223
Cdd:cd01884 67 YAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
|
|
| HBS1_C_III |
cd04093 |
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ... |
391-494 |
7.60e-27 |
|
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: 104.16 E-value: 7.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 391 RTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKD 470
Cdd:cd04093 6 SKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKD 85
|
90 100
....*....|....*....|....
gi 2131067815 471 FPQMGRFTLRDEGKTIAIGKVLKL 494
Cdd:cd04093 86 NKELGRFVLRRGGETIAAGIVTEI 109
|
|
| EF1_alpha_III |
cd03705 |
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ... |
392-491 |
1.87e-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: 94.57 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 392 TFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDF 471
Cdd:cd03705 5 SFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETFSEY 84
|
90 100
....*....|....*....|
gi 2131067815 472 PQMGRFTLRDEGKTIAIGKV 491
Cdd:cd03705 85 PPLGRFAVRDMRQTVAVGVI 104
|
|
| GTP_EFTU_D3 |
pfam03143 |
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ... |
391-494 |
1.89e-23 |
|
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: 94.64 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 391 RTFDAQIVIIEH-----KSIICPGYNAVLHIHTCIEEVEITALICLVDkkSGEKSKtRPRFVKQDQVCIARLRTAGTICL 465
Cdd:pfam03143 6 TKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELIKPIAL 82
|
90 100
....*....|....*....|....*....
gi 2131067815 466 ETFKdfpqmgRFTLRDEGKTIAIGKVLKL 494
Cdd:pfam03143 83 EKGQ------RFAIREGGRTVAAGVVTEI 105
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
81-271 |
1.43e-21 |
|
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: 91.51 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 81 GHVDAGKSTIggqIMYLTGMvdkrtlekyereakeknrETwylswalDTNQEERDKGKTVEVGRAYFETEK-KHFTILDA 159
Cdd:cd04171 6 GHIDHGKTTL---IKALTGI------------------ET-------DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 160 PGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHLIVLINKMD--DPtvnwssERYEEC 237
Cdd:cd04171 58 PGHEKFVKNMLAGAGGIDAVLLVVAADEGIMP-------QTREHLEILELLGIKKGLVVLTKADlvDE------DRLELV 124
|
170 180 190
....*....|....*....|....*....|....
gi 2131067815 238 KEKLVPFLKKVGFNPKKdihFMPCSGLTGANLKE 271
Cdd:cd04171 125 EEEILELLAGTFLADAP---IFPVSSVTGEGIEE 155
|
|
| Translation_factor_III |
cd01513 |
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ... |
393-491 |
5.11e-19 |
|
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: 82.06 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 393 FDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKtrPRFVKQDQVCIARLRTAGTICLETFKDFP 472
Cdd:cd01513 6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKP--PDSLQPGENGTVEVELQKPVVLERGKEFP 83
|
90
....*....|....*....
gi 2131067815 473 QMGRFTLRDEGKTIAIGKV 491
Cdd:cd01513 84 TLGRFALRDGGRTVGAGLI 102
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
75-251 |
1.14e-14 |
|
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: 72.69 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 75 VNVVFIGHVDAGKSTIggqIMYLTGMVDKRTLEKYEREAKEKnretwyLSWAlDT------NQEERDKGKTVEVGRAYFE 148
Cdd:cd01888 1 INIGTIGHVAHGKTTL---VKALSGVWTVRHKEELKRNITIK------LGYA-NAkiykcpNCGCPRPYDTPECECPGCG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 149 TEKK---HFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETgfekggQTREHAMLAKTAGVKHLIVLINKMDDP 225
Cdd:cd01888 71 GETKlvrHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQP------QTSEHLAALEIMGLKHIIILQNKIDLV 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 2131067815 226 TVNWSSERYEECKE----------KLVPFLKKVGFN 251
Cdd:cd01888 145 KEEQALENYEQIKEfvkgtiaenaPIIPISAQLKYN 180
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
77-271 |
6.76e-14 |
|
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: 69.42 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 77 VVFIGHVDAGKSTIggqimyltgmvdkrtlekyereakeknretwylswaLD----TNQEERDKGK-TVEVGRAYFETEK 151
Cdd:cd01887 3 VTVMGHVDHGKTTL------------------------------------LDkirkTNVAAGEAGGiTQHIGAYQVPIDV 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KH--FTILDAPGHKSFVpNM-IGGASQADLAVLVISArkgefETGFEKggQTREHAMLAKTAGVKhLIVLINKMD-DPTV 227
Cdd:cd01887 47 KIpgITFIDTPGHEAFT-NMrARGASVTDIAILVVAA-----DDGVMP--QTIEAINHAKAANVP-IIVAINKIDkPYGT 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2131067815 228 NWSSER-YEECKEKLVpflkkVGFNPKKDIHFMPCSGLTGANLKE 271
Cdd:cd01887 118 EADPERvKNELSELGL-----VGEEWGGDVSIVPISAKTGEGIDD 157
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
76-386 |
1.75e-13 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 72.82 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRTlEKYEReakeknretwylswALDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:PRK10218 7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 156 ILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTREHAMLAKTAGVKHlIVLINKMDDPTV--NWSSER 233
Cdd:PRK10218 72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKP-IVVINKVDRPGArpDWVVDQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 234 YEECkeklvpFLKKVGFNPKKDIHFMPCSGLTG-ANLKEQ---SDFCPWYTGLpfipyLDNLPNFNRSVDGPIRLPI--V 307
Cdd:PRK10218 144 VFDL------FVNLDATDEQLDFPIVYASALNGiAGLDHEdmaEDMTPLYQAI-----VDHVPAPDVDLDGPFQMQIsqL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 308 DKYKDMGTVVLGKLESGSICKGQQLVMMPNK---HNVEVLGILS----DDVETDSVAPGENLKIrlKGIEEEEIlpGFIL 380
Cdd:PRK10218 213 DYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEgktRNAKVGKVLGhlglERIETDLAEAGDIVAI--TGLGELNI--SDTV 288
|
....*.
gi 2131067815 381 CDPNNL 386
Cdd:PRK10218 289 CDTQNV 294
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
75-266 |
2.18e-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: 68.55 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 75 VNVVFIGHVDAGKSTIGgqimyltgmvdkRTLEKYEREAkeknretwylswALDTNQEERDKGKTVEVGRAYFETEKK-- 152
Cdd:cd01889 1 VNVGLLGHVDSGKTSLA------------KALSEIASTA------------AFDKNPQSQERGITLDLGFSSFEVDKPkh 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 153 ------------HFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGeFETgfekggQTREHAMLAKTAGVKhLIVLIN 220
Cdd:cd01889 57 lednenpqienyQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-IQT------QTAECLVIGELLCKP-LIVVLN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131067815 221 KMDDPTVNWSSERYEECKEKLVPFLKKVGFnpkKDIHFMPCSGLTG 266
Cdd:cd01889 129 KIDLIPEEERKRKIEKMKKRLQKTLEKTRL---KDSPIIPVSAKPG 171
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
82-253 |
8.17e-13 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 68.03 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 82 HVDAGKSTIGGQIMYLTGMVDKRTlekyerEAKEKNRETwylswalDTNQEERDKGKTVEVGRAYFETEKKHFTILDAPG 161
Cdd:cd04168 7 HVDAGKTTLTESLLYTSGAIRELG------SVDKGTTRT-------DSMELERQRGITIFSAVASFQWEDTKVNIIDTPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 162 HKSFVPNMIGGASQADLAVLVISARKGefetgfeKGGQTREHAMLAKTAGVKhLIVLINKMDDPTVNwSSERYEECKEKL 241
Cdd:cd04168 74 HMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTRILFRLLRKLNIP-TIIFVNKIDRAGAD-LEKVYQEIKEKL 144
|
170
....*....|....*
gi 2131067815 242 VP---FLKKVGFNPK 253
Cdd:cd04168 145 SPdivPMQKVGLYPN 159
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
75-246 |
1.65e-12 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 69.11 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 75 VNVVFIGHVDAGKSTIggqIMYLTGmvdkrtlekyereakeknretwylSWAlDTNQEERDKGKTVEVGRA--------- 145
Cdd:PRK04000 10 VNIGMVGHVDHGKTTL---VQALTG------------------------VWT-DRHSEELKRGITIRLGYAdatirkcpd 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 146 -----YFETEKK------------HFTILDAPGHKSFVPNMIGGASQADLAVLVISARkgefetgfEK--GGQTREHAML 206
Cdd:PRK04000 62 ceepeAYTTEPKcpncgsetellrRVSFVDAPGHETLMATMLSGAALMDGAILVIAAN--------EPcpQPQTKEHLMA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2131067815 207 AKTAGVKHLIVLINKMDDPTVNWSSERYEECKEklvpFLK 246
Cdd:PRK04000 134 LDIIGIKNIVIVQNKIDLVSKERALENYEQIKE----FVK 169
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
81-374 |
2.04e-12 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 69.31 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 81 GHVDAGKSTIggqIMYLTGmVDKRTLEkyereakeknretwylswaldtnqEERDKGKTVEVGRAYF-ETEKKHFTILDA 159
Cdd:PRK10512 7 GHVDHGKTTL---LQAITG-VNADRLP------------------------EEKKRGMTIDLGYAYWpQPDGRVLGFIDV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 160 PGHKSFVPNMIGGASQADLAVLVISARKGEFetgfekgGQTREHAMLAKTAGVKHLIVLINKMDdpTVnwSSERYEECKE 239
Cdd:PRK10512 59 PGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHLAILQLTGNPMLTVALTKAD--RV--DEARIAEVRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 240 KLVPFLKKVGFNpkkDIHFMPCSGLTGANLKEQSDfcpwytglpfipYLDNLPNFNRSVDGPIRLPIvDK---YKDMGTV 316
Cdd:PRK10512 128 QVKAVLREYGFA---EAKLFVTAATEGRGIDALRE------------HLLQLPEREHAAQHRFRLAI-DRaftVKGAGLV 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131067815 317 VLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKG-IEEEEI 374
Cdd:PRK10512 192 VTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQI 250
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
76-243 |
2.13e-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: 67.23 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKrtLEKYEREakeknretwylSWALDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDR--LGRVEDG-----------NTVSDYDPEEKKRKMSIETSVAPLEWNGHKIN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 156 ILDAPGHKSFVPNMIGGASQADLAVLVISArkgefETGFEkgGQTREHAMLAKTAGVKHLIVlINKMDDPTVNWsSERYE 235
Cdd:cd04170 68 LIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRIIF-INKMDRARADF-DKTLA 138
|
170
....*....|..
gi 2131067815 236 ECKE----KLVP 243
Cdd:cd04170 139 ALREafgrPVVP 150
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
301-382 |
2.85e-12 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 62.15 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 301 PIRLPIVDKYKDMGTVVL--GKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGF 378
Cdd:cd16267 1 PFRLSVSDVFKGQGSGFTvsGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80
|
....
gi 2131067815 379 ILCD 382
Cdd:cd16267 81 ILCD 84
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
80-241 |
5.21e-12 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 68.23 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 80 IGHVDAGKSTIGGQIMYLTGMVDKRTlekyerEAKEKNRetwylswALDTNQEERDKGKTVEVGRAYFETEKKHFTILDA 159
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIG------EVEDGTT-------TMDFMPEERERGISITSAATTCEWKGHKINLIDT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 160 PGHKSFVPNMIGGASQADLAVLVISArkgefETGFEkgGQTREHAMLAKTAGVKHLIVlINKMDDPTVNWsSERYEECKE 239
Cdd:PRK12740 68 PGHVDFTGEVERALRVLDGAVVVVCA-----VGGVE--PQTETVWRQAEKYGVPRIIF-VNKMDRAGADF-FRVLAQLQE 138
|
..
gi 2131067815 240 KL 241
Cdd:PRK12740 139 KL 140
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
76-241 |
8.13e-12 |
|
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: 67.76 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRtlekyeREAKEKNRETwylswalDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:COG0480 11 NIGIVAHIDAGKTTLTERILFYTGAIHRI------GEVHDGNTVM-------DWMPEEQERGITITSAATTCEWKGHKIN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 156 ILDAPGHKSFVPNMIGGASQADLAVLVISARKGefetgfeKGGQTREHAMLAKTAGVKHlIVLINKMDDPTVNWssER-Y 234
Cdd:COG0480 78 IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG-------VEPQTETVWRQADKYGVPR-IVFVNKMDREGADF--DRvL 147
|
....*..
gi 2131067815 235 EECKEKL 241
Cdd:COG0480 148 EQLKERL 154
|
|
| GTPBP_III |
cd03708 |
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ... |
391-494 |
7.40e-11 |
|
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: 58.30 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 391 RTFDAQIVIIEHKSIICPGYNAVLHIHTcieeVEITALICLVDK---KSGEKSKTRPRFVKQDQVciarLRtAGTiclet 467
Cdd:cd03708 4 WEFEAEVLVLHHPTTISPGYQPVVHCGT----IRQTARIISIDKevlRTGDRALVRFRFLYRPEY----LR-EGQ----- 69
|
90 100
....*....|....*....|....*..
gi 2131067815 468 fkdfpqmgRFTLRdEGKTIAIGKVLKL 494
Cdd:cd03708 70 --------RLIFR-EGRTKGIGTVTKV 87
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
76-223 |
2.86e-10 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 62.66 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRTlekyerEAKEKNRETwylswalDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:PRK13351 10 NIGILAHIDAGKTTLTERILFYTGKIHKMG------EVEDGTTVT-------DWMPQEQERGITIESAATSCDWDNHRIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131067815 156 ILDAPGHKSFVPNMIGGASQADLAVLVISARkgefeTGFEKggQTREHAMLAKTAGVKHLIVlINKMD 223
Cdd:PRK13351 77 LIDTPGHIDFTGEVERSLRVLDGAVVVFDAV-----TGVQP--QTETVWRQADRYGIPRLIF-INKMD 136
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
298-385 |
5.09e-10 |
|
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: 56.04 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 298 VDGPIRLPIVDKYK--DMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEIL 375
Cdd:cd03693 1 TDKPLRLPIQDVYKigGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
|
90
....*....|
gi 2131067815 376 PGFILCDPNN 385
Cdd:cd03693 81 RGDVAGDSKN 90
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
314-381 |
5.76e-10 |
|
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: 55.35 E-value: 5.76e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131067815 314 GTVVLGKLESGSICKGQQLVMMPN-----KHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFILC 381
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
303-382 |
7.83e-10 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 55.23 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 303 RLPIvDKY---KDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFI 379
Cdd:cd03696 2 RLPI-DHVfsiKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
|
...
gi 2131067815 380 LCD 382
Cdd:cd03696 81 LSE 83
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
75-336 |
3.88e-08 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 55.40 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 75 VNVVFIGHVDAGKSTIggqIMYLTGMvdkrTLEKYEREaKEKN-------------------RETWYLSWAldTNQEERD 135
Cdd:PTZ00327 35 INIGTIGHVAHGKSTV---VKALSGV----KTVRFKRE-KVRNitiklgyanakiykcpkcpRPTCYQSYG--SSKPDNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 136 K----GKTVEVgrayfeteKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETgfekggQTREHAMLAKTAG 211
Cdd:PTZ00327 105 PcpgcGHKMTL--------KRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQP------QTSEHLAAVEIMK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 212 VKHLIVLINKMDDPTVNWSSERYEECKEklvpFLKKvgfNPKKDIHFMPCSgltgANLKEQSDFCPWY--TGLPfIPYLD 289
Cdd:PTZ00327 171 LKHIIILQNKIDLVKEAQAQDQYEEIRN----FVKG---TIADNAPIIPIS----AQLKYNIDVVLEYicTQIP-IPKRD 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2131067815 290 -NLP---NFNRSVDgpIRLPIVDKYKDMGTVVLGKLESGSICKGQQLVMMP 336
Cdd:PTZ00327 239 lTSPprmIVIRSFD--VNKPGEDIENLKGGVAGGSILQGVLKVGDEIEIRP 287
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
76-271 |
2.15e-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: 51.00 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKrtlekyeREAKEKnretwylswALDTNQEERDKGKTVEVG--RAYFETEKKH 153
Cdd:cd01890 2 NFSIIAHIDHGKSTLADRLLELTGTVSE-------REMKEQ---------VLDSMDLERERGITIKAQavRLFYKAKDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 154 FTIL---DAPGHKSF---VPNMIgGASQAdlAVLVISARKG-EfetgfekgGQTREHAMLAKTAGVKhLIVLINKMDDPT 226
Cdd:cd01890 66 EYLLnliDTPGHVDFsyeVSRSL-AACEG--ALLVVDATQGvE--------AQTLANFYLALENNLE-IIPVINKIDLPA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2131067815 227 VNwsserYEECKEKLVPFLkkvGFNPKKDIHfmpCSGLTGANLKE 271
Cdd:cd01890 134 AD-----PDRVKQEIEDVL---GLDASEAIL---VSAKTGLGVED 167
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
77-271 |
5.11e-07 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 52.53 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 77 VVFIGHVDAGKSTIGGQImyltgmvdkrtlekyereakeknRETwylswalDTNQEERDkGKTVEVGrAY-----FETEK 151
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKI-----------------------RKT-------QIAQKEAG-GITQKIG-AYevefeYKDEN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 152 KHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGefetgfeKGGQTREHAMLAKTAGVKhLIVLINKMDDPTVNWSS 231
Cdd:CHL00189 295 QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIEAINYIQAANVP-IIVAINKIDKANANTER 366
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2131067815 232 ERYEECKEKLVPflKKVGfnpkKDIHFMPCSGLTGANLKE 271
Cdd:CHL00189 367 IKQQLAKYNLIP--EKWG----GDTPMIPISASQGTNIDK 400
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
303-381 |
7.36e-07 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 46.87 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 303 RLPIVDKYKD--MGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDSVAPGENLKIRLKGIeeEEILPGFIL 380
Cdd:cd01342 2 VMQVFKVFYIpgRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTGDTL 79
|
.
gi 2131067815 381 C 381
Cdd:cd01342 80 T 80
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
148-228 |
7.45e-07 |
|
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: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 148 ETEKKHFTILDAPGHKSFVpNM-IGGASQADLAVLVISARKGEFEtgfekggQTRE---HamlAKTAGVKhLIVLINKMD 223
Cdd:COG0532 47 ETNGGKITFLDTPGHEAFT-AMrARGAQVTDIVILVVAADDGVMP-------QTIEainH---AKAAGVP-IIVAINKID 114
|
....*
gi 2131067815 224 DPTVN 228
Cdd:COG0532 115 KPGAN 119
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
76-223 |
7.21e-06 |
|
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: 46.88 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIggqimyltgmVDkrTLEKYEREAKEKNRETWYLSWALDTNQEERDKG---KTVEVGRAYFETEKK 152
Cdd:cd04167 2 NVCIAGHLHHGKTSL----------LD--MLIEQTHKRTPSVKLGWKPLRYTDTRKDEQERGisiKSNPISLVLEDSKGK 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131067815 153 H--FTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFEtgfekggQTRE---HAMLAKtagvKHLIVLINKMD 223
Cdd:cd04167 70 SylINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTS-------VTERlirHAIQEG----LPMVLVINKID 134
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
76-225 |
9.29e-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: 46.43 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 76 NVVFIGHVDAGKSTIGGQIMYLTGMVDKRTlEKYEReakeknretwylswALDTNQEERDKGKTVEVGRAYFETEKKHFT 155
Cdd:cd01891 4 NIAIIAHVDHGKTTLVDALLKQSGTFRENE-EVGER--------------VMDSNDLERERGITILAKNTAITYKDTKIN 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131067815 156 ILDAPGHKSFvpnmiGGA-----SQADLAVLVISARKGEFEtgfekggQTRehAMLAKT--AGVKhLIVLINKMDDP 225
Cdd:cd01891 69 IIDTPGHADF-----GGEvervlSMVDGVLLLVDASEGPMP-------QTR--FVLKKAleAGLK-PIVVINKIDRP 130
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
80-226 |
1.28e-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: 46.82 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 80 IGHVDAGKSTI-------GGQImYLTGMVDKRTLEKYEREakeknretwylswalDTNQEERDKGKTVEVGRAYFETEKK 152
Cdd:cd04169 8 ISHPDAGKTTLteklllfGGAI-QEAGAVKARKSRKHATS---------------DWMEIEKQRGISVTSSVMQFEYKGC 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131067815 153 HFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGeFETgfekggQTREHAMLAKTAGVKhLIVLINKMDDPT 226
Cdd:cd04169 72 VINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG-VEP------QTRKLFEVCRLRGIP-IITFINKLDREG 137
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
75-269 |
1.32e-05 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 45.44 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 75 VNVVFIGHVDAGKSTIggqimyltgmvdkrtLEKYereAKEKNRETwylswaldtnqeERDKGKTVEVGRAYFET--EKK 152
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTL---------------LNSL---LGNKGSIT------------EYYPGTTRNYVTTVIEEdgKTY 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 153 HFTILDAPGHKSF-------VPNMIGGASQADLAVLVISARKGefetgfeKGGQTREHAMLAKTaGVKhLIVLINKMDDP 225
Cdd:TIGR00231 52 KFNLLDTAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEI-------LEKQTKEIIHHADS-GVP-IILVGNKIDLK 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2131067815 226 TvnwsseryEECKEKLVPFLKKVGFNPkkdihFMPCSGLTGANL 269
Cdd:TIGR00231 123 D--------ADLKTHVASEFAKLNGEP-----IIPLSAETGKNI 153
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
78-271 |
2.49e-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: 44.75 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 78 VFIGHVDAGKSTIggqIMYLTGmvdkrtlekyereakeknretwylSWALDTNQEErdkGKTVE--VGRAYFETEKKHFT 155
Cdd:cd00882 1 VVVGRGGVGKSSL---LNALLG------------------------GEVGEVSDVP---GTTRDpdVYVKELDKGKVKLV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131067815 156 ILDAPGHKSFVPNMIGG-----ASQADLAVLVISARKGEFEtgfekGGQTREHAMLAKTAGvKHLIVLINKMDDPTVnwS 230
Cdd:cd00882 51 LVDTPGLDEFGGLGREElarllLRGADLILLVVDSTDRESE-----EDAKLLILRRLRKEG-IPIILVGNKIDLLEE--R 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2131067815 231 SERYEECKEKLvpflkkvgfNPKKDIHFMPCSGLTGANLKE 271
Cdd:cd00882 123 EVEELLRLEEL---------AKILGVPVFEVSAKTGEGVDE 154
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
311-380 |
1.61e-04 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 40.28 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131067815 311 KDMGTVVLGKLESGSICKGQQLVMMPNK----HNVEVLGILSDDVETDSVAPGENLKIRLKGIEEEEILPGFIL 380
Cdd:cd03694 12 PGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMVL 85
|
|
| |
