|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-605 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1102.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 1 MSLRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFG 80
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHADFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 81 GEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFANLDATDEQLDFPI 160
Cdd:COG1217 84 GEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDFPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 161 LYGSGRDGWMNVNPEGPKDqGLTPLLDLVLKHVPEPTVH-EGPFTMIGTILEANPFLGRIITGRINSGSIKPNQAVKVLH 239
Cdd:COG1217 164 VYASARNGWASLDLDDPGE-DLTPLFDTILEHVPAPEVDpDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 240 ADGKtIETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITIPLPAQPIDPPTVTMSFIVNDSPLAG 319
Cdd:COG1217 243 RDGK-VEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 320 TEGDKVTSRVIRDRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRREGFELAVSRPRVVMhKDENGQLLEP 399
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIF-KEIDGKKLEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 400 VEEVVVDVDEEHSGVVVQKMSERKAEMVELRPSGGNRLRLRFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYKGVI 479
Cdd:COG1217 401 IEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYKGEI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 480 GGRVNGVLLANAPGEAVAYAMFNLEDRGPMIIEPGEKVYAGMIIGIHSRDNDLEVNVLKGKQLTNIRAAGKDEAVKLTPP 559
Cdd:COG1217 481 PGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 502309546 560 IRMTLDRALSWIQDDELMEVTPKNIRLRKMYLDANDRKRFEKTKAA 605
Cdd:COG1217 561 RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK 606
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
3-598 |
0e+00 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 950.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGE 82
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 83 VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFANLDATDEQLDFPILY 162
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 163 GSGRDGWMNVNPEGPKDQgLTPLLDLVLKHVPEPTV-HEGPFTMIGTILEANPFLGRIITGRINSGSIKPNQAVKVLHAD 241
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDN-MAPLFDAIVRHVPAPKGdLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 242 GkTIETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITIPLPAQPIDPPTVTMSFIVNDSPLAGTE 321
Cdd:TIGR01394 240 G-TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 322 GDKVTSRVIRDRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRREGFELAVSRPRVVMhKDENGQLLEPVE 401
Cdd:TIGR01394 319 GKKVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIY-KEIDGKKLEPIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 402 EVVVDVDEEHSGVVVQKMSERKAEMVELRPSGGNRLRLRFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYKGVIGG 481
Cdd:TIGR01394 398 ELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGEIET 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 482 RVNGVLLANAPGEAVAYAMFNLEDRGPMIIEPGEKVYAGMIIGIHSRDNDLEVNVLKGKQLTNIRAAGKDEAVKLTPPIR 561
Cdd:TIGR01394 478 RRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRK 557
|
570 580 590
....*....|....*....|....*....|....*..
gi 502309546 562 MTLDRALSWIQDDELMEVTPKNIRLRKMYLDANDRKR 598
Cdd:TIGR01394 558 LSLEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
2-598 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 634.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 2 SLRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGG 81
Cdd:PRK10218 4 KLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 EVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFANLDATDEQLDFPIL 161
Cdd:PRK10218 84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 162 YGSGRDGWMNVNPEGPKDQgLTPLLDLVLKHVPEPTVH-EGPFTMIGTILEANPFLGRIITGRINSGSIKPNQAVKVLHA 240
Cdd:PRK10218 164 YASALNGIAGLDHEDMAED-MTPLYQAIVDHVPAPDVDlDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 241 DGKTiETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITIPLPAQPIDPPTVTMSFIVNDSPLAGT 320
Cdd:PRK10218 243 EGKT-RNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 321 EGDKVTSRVIRDRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRREGFELAVSRPRVVMhKDENGQLLEPV 400
Cdd:PRK10218 322 EGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIF-REIDGRKQEPY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 401 EEVVVDVDEEHSGVVVQKMSERKAEMVELRPSGGNRLRLRFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK-GVI 479
Cdd:PRK10218 401 ENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 480 GGRVNGVLLANAPGEAVAYAMFNLEDRGPMIIEPGEKVYAGMIIGIHSRDNDLEVNVLKGKQLTNIRAAGKDEAVKLTPP 559
Cdd:PRK10218 481 GQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPP 560
|
570 580 590
....*....|....*....|....*....|....*....
gi 502309546 560 IRMTLDRALSWIQDDELMEVTPKNIRLRKMYLDANDRKR 598
Cdd:PRK10218 561 IRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRR 599
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
2-196 |
1.25e-130 |
|
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: 380.79 E-value: 1.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 2 SLRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGG 81
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 EVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFANLDATDEQLDFPIL 161
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....*
gi 502309546 162 YGSGRDGWMNVNPEGPKDQgLTPLLDLVLKHVPEP 196
Cdd:cd01891 161 YASAKNGWASLNLDDPSED-LDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
3-194 |
9.51e-72 |
|
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: 228.95 E-value: 9.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVA---ERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADF 79
Cdd:pfam00009 3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 80 GGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDG-RHEEVINEVFDLFANLDATDEqLDF 158
Cdd:pfam00009 83 VKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGaELEEVVEEVSRELLEKYGEDG-EFV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 502309546 159 PILYGSGRDGWmnvnpegpkdqGLTPLLDLVLKHVP 194
Cdd:pfam00009 162 PVVPGSALKGE-----------GVQTLLDALDEYLP 186
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
3-386 |
2.47e-56 |
|
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: 201.81 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSfreNQRVAE-----RVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHA 77
Cdd:COG0480 9 IRNIGIVAHIDAGKTTLTERILFYTGA---IHRIGEvhdgnTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 78 DFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINE---------------- 141
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQlkerlganpvplqlpi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 142 --------VFDLFAN---------------------------------LDA---TDEQL------------D-------- 157
Cdd:COG0480 166 gaeddfkgVIDLVTMkayvyddelgakyeeeeipaelkeeaeeareelIEAvaeTDDELmekylegeelteEeikaglrk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 158 -------FPILYGSGRdgwmnvnpegpKDQGLTPLLDLVLKHVPEPTVH--------------------EGPF------T 204
Cdd:COG0480 246 atlagkiVPVLCGSAF-----------KNKGVQPLLDAVVDYLPSPLDVpaikgvdpdtgeeverkpddDEPFsalvfkT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 205 MigtileANPFLGRIITGRINSGSIKPNQAVKVLHADGKtiEtgRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVA 284
Cdd:COG0480 315 M------TDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKK--E--RIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 285 DTFCDPSITIPLPaqPIDPPTVTMSFIVNdsplAGTEGDkvtsrviRDRLFKeaegnvAL-KI-EEaegkD-SFYV---- 357
Cdd:COG0480 385 DTLCDEDHPIVLE--PIEFPEPVISVAIE----PKTKAD-------EDKLST------ALaKLaEE----DpTFRVetde 441
|
490 500 510
....*....|....*....|....*....|....*..
gi 502309546 358 -------SGRGELQLAVLIETMRRE-GFELAVSRPRV 386
Cdd:COG0480 442 etgqtiiSGMGELHLEIIVDRLKREfGVEVNVGKPQV 478
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
4-387 |
1.45e-54 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 197.78 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSGSFREnqRVA--ERVMDSNDLEKERGITILAKATS----VEWKGVRINIVDTPGHA 77
Cdd:PRK07560 21 RNIGIIAHIDHGKTTLSDNLLAGAGMISE--ELAgeQLALDFDEEEQARGITIKAANVSmvheYEGKEYLINLIDTPGHV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 78 DFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR--------PD---GRHEEVINEVFDLF 146
Cdd:PRK07560 99 DFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPQemqQRLLKIIKDVNKLI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 147 AN-----------LDATDEQLDFpilyGSGRDGWMNVNP----------------EGPKDQGL---TPL----LDLVLKH 192
Cdd:PRK07560 179 KGmapeefkekwkVDVEDGTVAF----GSALYNWAISVPmmqktgikfkdiidyyEKGKQKELaekAPLhevvLDMVVKH 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 193 VPEPTV--------------------------HEGPFTMIGTILEANPFLGRIITGRINSGSIKPNQAVKVLHADGKtie 246
Cdd:PRK07560 255 LPNPIEaqkyripkiwkgdlnsevgkamlncdPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKK--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 247 tGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITIPLPA-QPIDPPTVTMSfI----VNDSPlagte 321
Cdd:PRK07560 332 -NRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESlKHISEPVVTVA-IeaknPKDLP----- 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309546 322 gdKVTSrVIRDrLFKEaEGNVALKIEEAEGKdsFYVSGRGELQLAVLIETMRRE-GFELAVSRPRVV 387
Cdd:PRK07560 405 --KLIE-VLRQ-LAKE-DPTLVVKINEETGE--HLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVV 464
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
5-196 |
8.12e-54 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 181.34 E-value: 8.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGEVE 84
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 85 RILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPD-GRHEEVINEVFDLFANLDAT-DEQLDFPILY 162
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|....
gi 502309546 163 GSGRDGWmnvnpegpkdqGLTPLLDLVLKHVPEP 196
Cdd:cd00881 161 ISALTGE-----------GIEELLDAIVEHLPPP 183
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-395 |
1.69e-51 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 188.95 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSV--EWKGVR--INIVDTPGHAD 78
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvhEYEGNEylINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 79 FGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR--------PDGRHE---EVINEVFDLFA 147
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltPQELQErfiKIITEVNKLIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 148 NL---DATDEQL----DFPILYGSGRDGWMnVNPEGPKDQGLT--------------------PL----LDLVLKHVPEP 196
Cdd:TIGR00490 179 AMapeEFRDKWKvrveDGSVAFGSAYYNWA-ISVPSMKKTGIGfkdiykyckedkqkelakksPLhqvvLDMVIRHLPSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 197 --------------------------TVHEGPFTMIGTILEANPFLGRIITGRINSGSIKPNQAVKVLHADGKtietGRI 250
Cdd:TIGR00490 258 ieaqkyripviwkgdlnsevgkamlnCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAK----ARI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 251 SKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITI-PLPA-QPIDPPTVTMSFIVNDSplagtegdKVTSR 328
Cdd:TIGR00490 334 QQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVENItPFESiKHISEPVVTVAIEAKNT--------KDLPK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309546 329 VIrDRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRRE-GFELAVSRPRVVMHKDENGQ 395
Cdd:TIGR00490 406 LI-EVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGT 472
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-387 |
3.74e-51 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 187.47 E-value: 3.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 1 MSLRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRV--AERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHAD 78
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVedGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 79 FGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR-------------------------PDG 133
Cdd:PRK13351 86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRvgadlfkvledieerfgkrplplqlPIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 134 -------------------------------------------RHEEVINEV--FD------LFANLDATDEQLD----- 157
Cdd:PRK13351 166 sedgfegvvdlitepelhfsegdggstveegpipeelleeveeAREKLIEALaeFDdellelYLEGEELSAEQLRaplre 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 158 -------FPILYGSGRdgwmnvnpegpKDQGLTPLLDLVLKHVPEPT-------------------VHEGPFTMIGTILE 211
Cdd:PRK13351 246 gtrsghlVPVLFGSAL-----------KNIGIEPLLDAVVDYLPSPLevppprgskdngkpvkvdpDPEKPLLALVFKVQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 212 ANPFLGRIITGRINSGSIkpNQAVKVLHADGKTIEtgRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPS 291
Cdd:PRK13351 315 YDPYAGKLTYLRVYSGTL--RAGSQLYNGTGGKRE--KVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 292 ITIPLPAQPIDPPTVTMSFivndSPLAGTEGDKVTSRVirDRLFKEAEGnvaLKIEEAEGKDSFYVSGRGELQLAVLIET 371
Cdd:PRK13351 391 DPVLLELLTFPEPVVSLAV----EPERRGDEQKLAEAL--EKLVWEDPS---LRVEEDEETGQTILSGMGELHLEVALER 461
|
490
....*....|....*..
gi 502309546 372 MRRE-GFELAVSRPRVV 387
Cdd:PRK13351 462 LRREfKLEVNTGKPQVA 478
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
9-387 |
7.67e-49 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 180.71 E-value: 7.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 9 IAHVDHGKTTLVDELLKQSGSFRENQRVAE--RVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGEVERI 86
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 87 LSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINE------------------------V 142
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQlqeklgapvvplqlpigegddftgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 143 FDL-------------FANLDATDEQLD------------------------------------------------FPIL 161
Cdd:PRK12740 161 VDLlsmkayrydeggpSEEIEIPAELLDraeeareellealaefddelmekylegeelseeeikaglrkatlageiVPVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 162 YGSGRdgwmnvnpegpKDQGLTPLLDLVLKHVPEPT---VHEGPFTMIGTILEAN---------------PFLGRIITGR 223
Cdd:PRK12740 241 CGSAL-----------KNKGVQRLLDAVVDYLPSPLevpPVDGEDGEEGAELAPDpdgplvalvfktmddPFVGKLSLVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 224 INSGSIKPNQAVKVlhadGKTIETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITIPLPaqPIDP 303
Cdd:PRK12740 310 VYSGTLKKGDTLYN----SGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLE--PMEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 304 PTVTMSFIVndSPLAGTEGDKVtSRVIRdRLfkeAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRRE-GFELAVS 382
Cdd:PRK12740 384 PEPVISLAI--EPKDKGDEEKL-SEALG-KL---AEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEVETG 456
|
....*
gi 502309546 383 RPRVV 387
Cdd:PRK12740 457 PPQVP 461
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
3-386 |
9.72e-48 |
|
translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]
Pssm-ID: 129575 [Multi-domain] Cd Length: 689 Bit Score: 177.69 E-value: 9.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRV--AERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFG 80
Cdd:TIGR00484 10 FRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVhdGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGHVDFT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 81 GEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINE------------------- 141
Cdd:TIGR00484 90 VEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQikqrlganavpiqlpigae 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 142 -----VFDLFA----NLDATD------------------------------------------EQLDFPILYGSGRDGWM 170
Cdd:TIGR00484 170 dnfigVIDLVEmkayFFNGDKgtkaiekeipsdlleqakelrenlveavaefdeelmekylegEELTIEEIKNAIRKGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 171 NVN------PEGPKDQGLTPLLDLVLKHVPEPT-----------------VH---EGPFTMIGTILEANPFLGRIITGRI 224
Cdd:TIGR00484 250 NCEffpvlcGSAFKNKGVQLLLDAVVDYLPSPTdvpaikgidpdtekeieRKasdDEPFSALAFKVATDPFVGQLTFVRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 225 NSGSIKPNQAVKVLHADGKTietgRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCDPSITIPLPAQPIDPP 304
Cdd:TIGR00484 330 YSGVLKSGSYVKNSRKNKKE----RVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPEP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 305 TVTMSFivndSPLAGTEGDKVTSrvirdRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRRE-GFELAVSR 383
Cdd:TIGR00484 406 VISLAV----EPKTKADQEKMGI-----ALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREfKVEANVGA 476
|
...
gi 502309546 384 PRV 386
Cdd:TIGR00484 477 PQV 479
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
4-196 |
4.59e-46 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 162.02 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlaKATSV-----------EWKGVRINIVD 72
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIslyfeyeeekmDGNDYLINLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 73 TPGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR--------PDGRHE------EV 138
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklsPEEAYQrllrivED 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309546 139 INEVFDLFANLDATDEQLDFP-----ILYGSGRDGWmnvnpegpkdqGLT--------PLLDLVLKHVPEP 196
Cdd:cd01885 159 VNAIIETYAPEEFKQEKWKFSpqkgnVAFGSALDGW-----------GFTiikfadiyAVLEMVVKHLPSP 218
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
304-382 |
4.73e-44 |
|
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios. It is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 293920 [Multi-domain] Cd Length: 79 Bit Score: 151.31 E-value: 4.73e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309546 304 PTVTMSFIVNDSPLAGTEGDKVTSRVIRDRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRREGFELAVS 382
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
5-142 |
4.80e-41 |
|
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: 148.92 E-value: 4.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAE--RVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGE 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKgtTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 83 VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEV 142
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
3-474 |
3.94e-40 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 154.79 E-value: 3.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQrVAERVMDSNDLEKERGITILAKATSVEWK-----GVRINIVDTPGHA 77
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAISERE-MREQVLDSMDLERERGITIKAQAVRLNYKakdgeTYVLNLIDTPGHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 78 DFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFAnLDATDeqld 157
Cdd:TIGR01393 82 DFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIG-LDASE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 158 fpILYGSGRDGwmnvnpegpkdQGLTPLLDLVLKHVPEPTvhegpfTMIGTILEA-------NPFLGRIITGRINSGSIK 230
Cdd:TIGR01393 157 --AILASAKTG-----------IGIEEILEAIVKRVPPPK------GDPDAPLKAlifdshyDNYRGVVALVRVFEGTIK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 231 PNQAVKVLHAdGKTIEtgrISKILAFRgIERTAIDEAHQGD----IIAIAGLSKGTVADTF--CDPSITIPLPA-QPIDP 303
Cdd:TIGR01393 218 PGDKIRFMST-GKEYE---VDEVGVFT-PKLTKTDELSAGEvgyiIAGIKDVSDVRVGDTIthVKNPAKEPLPGfKEVKP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 304 ptvtMSFivndSPLAGTEGDKVtsRVIRDRLFKEAEGNVALKIE----EAEGKdSFYVSGRGELQLAVLIETMRREgFEL 379
Cdd:TIGR01393 293 ----MVF----AGLYPIDTEDY--EDLRDALEKLKLNDASLTYEpessPALGF-GFRCGFLGLLHMEIIQERLERE-FNL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 380 AV--SRPRVVMH-KDENGQLLEPVEEVVVDVDEE------------------HSGVVVQKMSERKAEMVELRPSGGNRLR 438
Cdd:TIGR01393 361 DLitTAPSVIYRvYLTNGEVIEVDNPSDLPDPGKiehveepyvkatiitpteYLGPIMTLCQEKRGVQTNMEYLDPNRVE 440
|
490 500 510
....*....|....*....|....*....|....*..
gi 502309546 439 LRFYAP-TRGLIGYQSELLTDTRGTAIMNRLFHDYQP 474
Cdd:TIGR01393 441 LIYEMPlAEIVYDFFDKLKSISRGYASFDYELIGYRP 477
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
4-297 |
3.98e-40 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 154.79 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSG--SFRENQrvaERVMDSNDLEKERGITILAKATSVEWK---GV--RINIVDTPGH 76
Cdd:COG0481 7 RNFSIIAHIDHGKSTLADRLLELTGtlSEREMK---EQVLDSMDLERERGITIKAQAVRLNYKakdGEtyQLNLIDTPGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 77 ADFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFaNLDATDeql 156
Cdd:COG0481 84 VDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 157 dfpILYGSGRDGwmnvnpegpkdQGLTPLLDLVLKHVPEPT-VHEGPftmigtiLEA-------NPFLGRIITGRINSGS 228
Cdd:COG0481 160 ---AILVSAKTG-----------IGIEEILEAIVERIPPPKgDPDAP-------LQAlifdswyDSYRGVVVYVRVFDGT 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309546 229 IKPNQAVKVLhADGKTIEtgrISKILAFRgIERTAIDEAHQGD---IIA-IAGLSKGTVADTFCDPS--ITIPLP 297
Cdd:COG0481 219 LKKGDKIKMM-STGKEYE---VDEVGVFT-PKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKnpAAEPLP 288
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
4-196 |
3.50e-39 |
|
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: 141.90 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRvAERVMDSNDLEKERGITILAKATSVEWKGVR-----INIVDTPGHAD 78
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 79 FGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFAnLDATDeqldf 158
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLG-LDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 502309546 159 pILYGSGRDGwmnvnpegpkdQGLTPLLDLVLKHVPEP 196
Cdd:cd01890 154 -AILVSAKTG-----------LGVEDLLEAIVERIPPP 179
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
5-142 |
7.74e-37 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 138.39 E-value: 7.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAER--VMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGE 82
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 83 VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEV 142
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
203-297 |
1.10e-34 |
|
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.
Pssm-ID: 293892 [Multi-domain] Cd Length: 94 Bit Score: 126.15 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 203 FTMIGTILEANPFLGRIITGRINSGSIKPNQAVKVLHADGKtIETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGT 282
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGK-IEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDIT 79
|
90
....*....|....*
gi 502309546 283 VADTFCDPSITIPLP 297
Cdd:cd03691 80 IGDTICDPEVPEPLP 94
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-169 |
1.55e-31 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 130.55 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlaKATSV---------EWKGVR---INI 70
Cdd:PTZ00416 19 IRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehdleDGDDKQpflINL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 71 VDTPGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRP------DG--------RHE 136
Cdd:PTZ00416 97 IDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAilelqlDPeeiyqnfvKTI 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 502309546 137 EVINEVFDLFANLDATDEQLDfP----ILYGSGRDGW 169
Cdd:PTZ00416 177 ENVNVIIATYNDELMGDVQVY-PekgtVAFGSGLQGW 212
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
411-476 |
4.10e-30 |
|
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of the elongation factors EF-G and EF-2. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and plants. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and, is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 239681 [Multi-domain] Cd Length: 79 Bit Score: 112.98 E-value: 4.10e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309546 411 HSGVVVQKMSERKAEMVELRPSGGNRLRLRFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK 476
Cdd:cd03710 14 YSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
3-130 |
4.79e-27 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 116.75 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlaKATSVE------------WKGVR--- 67
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGISlyyemtdeslkdFKGERdgn 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502309546 68 ---INIVDTPGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR 130
Cdd:PLN00116 97 eylINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
4-196 |
4.04e-26 |
|
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: 106.20 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSGS---FRENQRVAERVMDSNDLEKERGITIlaKATSV-------EWKGVRINIVDT 73
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKrtpSVKLGWKPLRYTDTRKDEQERGISI--KSNPIslvledsKGKSYLINIIDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 74 PGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR-------P--DGRHE--EVINEV 142
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRlilelklPptDAYYKlrHTIDEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502309546 143 FDLFANLDATDEQLDFP----ILYGSGRDGWMNVNPEGPKdqgLTPLLDLVLKHVPEP 196
Cdd:cd04167 159 NNYIASFSTTEGFLVSPelgnVLFASSKFGFCFTLESFAK---KYGLVDSILSHIPSP 213
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
4-131 |
1.22e-25 |
|
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: 106.53 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAER------VMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHA 77
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARksrkhaTSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 502309546 78 DFGGEVERILSMVDGAIVLVDSSEGPMPQTKfvvsKALKVG-LR--PIVA-INKIDRP 131
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTR----KLFEVCrLRgiPIITfINKLDRE 136
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-146 |
4.65e-25 |
|
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: 104.98 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAE--RVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGE 82
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309546 83 VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLF 146
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-280 |
5.40e-24 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 105.29 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlaKATSVEWKGVRINI--VDTPGHADFGGE 82
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITI--ATAHVEYETAKRHYahVDCPGHADYVKN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 83 VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVA-INKIDRPDGRH--EEVINEVFDLFANLDATDEqlDFP 159
Cdd:PLN03127 141 MITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEEllELVEMELRELLSFYKFPGD--EIP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 160 ILYGSGRDGWMNVNPEGPKDQGLTpLLDLVLKHVPEPT-VHEGPFTMigTILEANPFLGR--IITGRINSGSIKPNQAVK 236
Cdd:PLN03127 219 IIRGSALSALQGTNDEIGKNAILK-LMDAVDEYIPEPVrVLDKPFLM--PIEDVFSIQGRgtVATGRVEQGTIKVGEEVE 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309546 237 VL----HADGKTIETG--RISKILAF-----------RGIERtaiDEAHQGDIIAIAGLSK 280
Cdd:PLN03127 296 IVglrpGGPLKTTVTGveMFKKILDQgqagdnvglllRGLKR---EDVQRGQVICKPGSIK 353
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
5-275 |
6.40e-24 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 104.26 E-value: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlakATS-VEWKGVRINI--VDTPGHADFgg 81
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITI---NTAhVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 everILSMV------DGAIVLVDSSEGPMPQTKFVVSKALKVGLRPI-VAINKIDRPDGrhEEVIN----EVFDLFANLD 150
Cdd:PRK12736 89 ----VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLvVFLNKVDLVDD--EELLElvemEVRELLSEYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 151 ATDEqlDFPILYGS------GRDGWMNVNPEgpkdqgltpLLDLVLKHVPEPTVH-EGPFTM----IGTIleanpfLGR- 218
Cdd:PRK12736 163 FPGD--DIPVIRGSalkaleGDPKWEDAIME---------LMDAVDEYIPTPERDtDKPFLMpvedVFTI------TGRg 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309546 219 -IITGRINSGSIKPNQAVKV--LHADGKTIETgriskilafrGIE--RTAIDEAHQGDIIAI 275
Cdd:PRK12736 226 tVVTGRVERGTVKVGDEVEIvgIKETQKTVVT----------GVEmfRKLLDEGQAGDNVGV 277
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
5-322 |
1.50e-23 |
|
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: 103.47 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGS-----FRENQRVAER----------VMDSNDLEKERGITILAKATSVEWKGVRIN 69
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAidehiIEKYEEEAEKkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 70 IVDTPGHADFggeVERIL---SMVDGAIVLVDSSEGPMPQTK--FVVSKALKVGlRPIVAINKIDRPD---GRHEEVINE 141
Cdd:COG5256 89 IIDAPGHRDF---VKNMItgaSQADAAILVVSAKDGVMGQTRehAFLARTLGIN-QLIVAVNKMDAVNyseKRYEEVKEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 142 VFDLFANLDATDEQLDF-PIlygsgrDGWMNVN-----PEGPKDQGLTPL--LDLvLKHVPEPTvhEGPF---------- 203
Cdd:COG5256 165 VSKLLKMVGYKVDKIPFiPV------SAWKGDNvvkksDNMPWYNGPTLLeaLDN-LKEPEKPV--DKPLripiqdvysi 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 204 TMIGTileanpflgrIITGRINSGSIKPNQAVKVLHA----DGKTIETgriskilafrgiERTAIDEAHQGDII--AIAG 277
Cdd:COG5256 236 SGIGT----------VPVGRVETGVLKVGDKVVFMPAgvvgEVKSIEM------------HHEELEQAEPGDNIgfNVRG 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502309546 278 LSK-----GTVAdtfcdpsitiplpAQPIDPPTVTMSF----IVNDSPLAGTEG 322
Cdd:COG5256 294 VEKndikrGDVA-------------GHPDNPPTVAEEFtaqiVVLQHPSAITVG 334
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
5-287 |
6.39e-23 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 101.54 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQ-----RVAER----------VMDSNDLEKERGITILAKATSVEWKGVRIN 69
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIieelrEEAKEkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 70 IVDTPGHADFggeverILSMVDGA--------IVLVDSSEGPMPQTKFVVSKALKVGLRP-IVAINKIDRPD---GRHEE 137
Cdd:PRK12317 88 IVDCPGHRDF------VKNMITGAsqadaavlVVAADDAGGVMPQTREHVFLARTLGINQlIVAINKMDAVNydeKRYEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 138 VINEVFDLFANLDATDEQLDF-PI--LYG------SGRDGWMNvnpeGPKdqgLTPLLDLvLKHVPEPTvhEGP------ 202
Cdd:PRK12317 162 VKEEVSKLLKMVGYKPDDIPFiPVsaFEGdnvvkkSENMPWYN----GPT---LLEALDN-LKPPEKPT--DKPlripiq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 203 --FTMIGtileanpfLGRIITGRINSGSIKPNQAVKVLHADG----KTIETgriskilafrgiERTAIDEAHQGDIIAIA 276
Cdd:PRK12317 232 dvYSISG--------VGTVPVGRVETGVLKVGDKVVFMPAGVvgevKSIEM------------HHEELPQAEPGDNIGFN 291
|
330 340
....*....|....*....|....*...
gi 502309546 277 --GLSKG---------------TVADTF 287
Cdd:PRK12317 292 vrGVGKKdikrgdvcghpdnppTVAEEF 319
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
4-287 |
9.12e-23 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 102.13 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELL------KQSGSF--RENQRVAERvmDSNDLEKERGITIlakATSV---EWKGVRINIVD 72
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVkgRKSGRHATS--DWMEMEKQRGISV---TSSVmqfPYRDCLINLLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 73 TPGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTKfvvsKALKV-GLR--PIVA-INKIDRpDGRHE-EVINE------ 141
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMEVcRLRdtPIFTfINKLDR-DGREPlELLDEieevlg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 142 ------------------VFDL---------------------FANLDatDEQLDFPI---LYGSGRDGWMNVNPEGPK- 178
Cdd:PRK00741 161 iacapitwpigmgkrfkgVYDLyndevelyqpgeghtiqeveiIKGLD--NPELDELLgedLAEQLREELELVQGASNEf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 179 DQ------GLTP--------------LLDLVLKHVPEPTVHEgpfTMIGTILEANP-FLG---------------RIITG 222
Cdd:PRK00741 239 DLeaflagELTPvffgsalnnfgvqeFLDAFVEWAPAPQPRQ---TDEREVEPTEEkFSGfvfkiqanmdpkhrdRIAFV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502309546 223 RINSGsiKPNQAVKVLHA-DGKTIetgRISKILAFRGIERTAIDEAHQGDIIaiaGL-SKGTVA--DTF 287
Cdd:PRK00741 316 RVCSG--KFEKGMKVRHVrTGKDV---RISNALTFMAQDREHVEEAYAGDII---GLhNHGTIQigDTF 376
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
5-275 |
2.88e-22 |
|
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: 99.07 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlakATS-VEWKGVRINI--VDTPGHADFgg 81
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITI---NTShVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 everILSMV------DGAIVLVDSSEGPMPQTKFVVSKALKVGLRPI-VAINKIDRPDgrHEEVIN----EVFDLFANLD 150
Cdd:COG0050 89 ----VKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEELLElvemEVRELLSKYG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 151 ATDEqlDFPILYGSGRdGWMNVNPEGPKDQGLTPLLDLVLKHVPEPT-VHEGPFTM----IGTIleanpfLGR--IITGR 223
Cdd:COG0050 163 FPGD--DTPIIRGSAL-KALEGDPDPEWEKKILELMDAVDSYIPEPErDTDKPFLMpvedVFSI------TGRgtVVTGR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502309546 224 INSGSIKPNQAVKV--LHADGKTIETGriskILAFRGIertaIDEAHQGDIIAI 275
Cdd:COG0050 234 VERGIIKVGDEVEIvgIRDTQKTVVTG----VEMFRKL----LDEGEAGDNVGL 279
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
5-275 |
4.75e-22 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 98.72 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlakATS-VEWKGVRINI--VDTPGHADFgg 81
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITI---NTAhVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 everILSMV------DGAIVLVDSSEGPMPQTKFVVSKALKVGLRPI-VAINKIDRPDgrHEEVIN----EVFDLFANLD 150
Cdd:PRK00049 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEELLElvemEVRELLSKYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 151 ATDEqlDFPILYGSGRdGWMNVNPEGPKDQGLTPLLDLVLKHVPEPT-VHEGPFTM----IGTIleanpfLGR--IITGR 223
Cdd:PRK00049 163 FPGD--DTPIIRGSAL-KALEGDDDEEWEKKILELMDAVDSYIPTPErAIDKPFLMpiedVFSI------SGRgtVVTGR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309546 224 INSGSIKPNQAVKV--LHADGKTIETgriskilafrGIE--RTAIDEAHQGDIIAI 275
Cdd:PRK00049 234 VERGIIKVGEEVEIvgIRDTQKTTVT----------GVEmfRKLLDEGQAGDNVGA 279
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-271 |
3.21e-21 |
|
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: 96.00 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGEVE 84
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 85 RILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGL-RPIVAINKIDRPDGRH--EEVINEVFDLFANLDATDEqlDFPIL 161
Cdd:TIGR00485 94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVpYIVVFLNKCDMVDDEEllELVEMEVRELLSQYDFPGD--DTPII 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 162 YGSGRDGWMNVNPEGPKdqgLTPLLDLVLKHVPEPT-VHEGPFTMigTILEANPFLGR--IITGRINSGSIKPNQAVKV- 237
Cdd:TIGR00485 172 RGSALKALEGDAEWEAK---ILELMDAVDEYIPTPErEIDKPFLL--PIEDVFSITGRgtVVTGRVERGIIKVGEEVEIv 246
|
250 260 270
....*....|....*....|....*....|....*
gi 502309546 238 -LHADGKTIETGriskILAFRGIertaIDEAHQGD 271
Cdd:TIGR00485 247 gLKDTRKTTVTG----VEMFRKE----LDEGRAGD 273
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
5-275 |
2.63e-20 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 93.36 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlakATS-VEWKGVRINI--VDTPGHADFgg 81
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITI---NTShVEYETANRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 everILSMV------DGAIVLVDSSEGPMPQTKFVVSKALKVGLRPI-VAINKIDRPDgrHEEVIN----EVFDLFANLD 150
Cdd:PRK12735 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEELLElvemEVRELLSKYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 151 ATDEqlDFPILYGSGRdGWMNVNPEGPKDQGLTPLLDLVLKHVPEPT-VHEGPFTM----IGTIleanpfLGR--IITGR 223
Cdd:PRK12735 163 FPGD--DTPIIRGSAL-KALEGDDDEEWEAKILELMDAVDSYIPEPErAIDKPFLMpiedVFSI------SGRgtVVTGR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502309546 224 INSGSIKPNQAVKV--LHADGKTIETGriskILAFRGIertaIDEAHQGDIIAI 275
Cdd:PRK12735 234 VERGIVKVGDEVEIvgIKETQKTTVTG----VEMFRKL----LDEGQAGDNVGV 279
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
5-275 |
2.26e-19 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 91.22 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFGGEVE 84
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 85 RILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVA-INKIDRPDgrHEEVIN----EVFDLFANLDATDEqlDFP 159
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVD--DEELLElvelEVRELLSSYEFPGD--DIP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 160 ILYGSGRDGW--MNVNPEGPKDQG-----LTPLLDLVLKHVPEPTVH-EGPFTMigTILEANPFLGR--IITGRINSGSI 229
Cdd:PLN03126 239 IISGSALLALeaLMENPNIKRGDNkwvdkIYELMDAVDSYIPIPQRQtDLPFLL--AVEDVFSITGRgtVATGRVERGTV 316
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502309546 230 KPNQAVKVLHAdgKTIETGRISKILAFRGIertaIDEAHQGDIIAI 275
Cdd:PLN03126 317 KVGETVDIVGL--RETRSTTVTGVEMFQKI----LDEALAGDNVGL 356
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-282 |
4.00e-19 |
|
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: 91.13 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 8 IIA---HVDHGKTTLVDELlkqSGsfRENQRVAErvmdsndlEKERGITI--------LAkatsvewKGVRINIVDTPGH 76
Cdd:COG3276 2 IIGtagHIDHGKTTLVKAL---TG--IDTDRLKE--------EKKRGITIdlgfaylpLP-------DGRRLGFVDVPGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 77 ADFggeverILSMVDGA----IVL--VDSSEGPMPQTK--FVVSKALKVGlRPIVAINKIDR-PDGRHEEVINEVFDLFA 147
Cdd:COG3276 62 EKF------IKNMLAGAggidLVLlvVAADEGVMPQTRehLAILDLLGIK-RGIVVLTKADLvDEEWLELVEEEIRELLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 148 NL---DAtdeqldfPILYGSGRDGwmnvnpegpkdQGLTPL---LDLVLKHVPEPTVHEGP-------FTMIGTileanp 214
Cdd:COG3276 135 GTfleDA-------PIVPVSAVTG-----------EGIDELraaLDALAAAVPARDADGPFrlpidrvFSIKGF------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 215 flGRIITGRINSGSIK---------PNQAVKV--LHADGKTIETG----RISkiLAFRGIERTAIdeaHQGDIIAIAGLS 279
Cdd:COG3276 191 --GTVVTGTLLSGTVRvgdelellpSGKPVRVrgIQVHGQPVEEAyagqRVA--LNLAGVEKEEI---ERGDVLAAPGAL 263
|
...
gi 502309546 280 KGT 282
Cdd:COG3276 264 RPT 266
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
5-142 |
4.05e-19 |
|
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: 86.39 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVAER-----------------VMDSNDLEKERGITILAKATSVEWKGVR 67
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGV--DKRTIEKyekeakemgkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 68 INIVDTPGHADFggeverILSMVDG------AIVLVDSSEG-------PMPQTK--FVVSKALKVGlRPIVAINKIDRPD 132
Cdd:cd01883 79 FTIIDAPGHRDF------VKNMITGasqadvAVLVVSARKGefeagfeKGGQTRehALLARTLGVK-QLIVAVNKMDDVT 151
|
170
....*....|....*
gi 502309546 133 -----GRHEEVINEV 142
Cdd:cd01883 152 vnwsqERYDEIKKKV 166
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
6-138 |
4.70e-19 |
|
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: 84.83 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELlkqsgsfRENQRVAERVmdsndlekeRGITILAKATSVEW--KGVRINIVDTPGHADFGGEV 83
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKI-------RKTNVAAGEA---------GGITQHIGAYQVPIdvKIPGITFIDTPGHEAFTNMR 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502309546 84 ERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEV 138
Cdd:cd01887 67 ARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEADP 121
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-275 |
2.10e-18 |
|
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: 87.84 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 1 MSLRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVA------ERVMDSNDL---------EKERGITI--------LAK 57
Cdd:COG2895 15 KDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAAlerdskKRGTQEIDLalltdglqaEREQGITIdvayryfsTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 58 atsvewkgvR--InIVDTPGHADFggevERilSMVDGA------IVLVDSSEGPMPQTK---FVVSkaLkVGLRP-IVAI 125
Cdd:COG2895 95 ---------RkfI-IADTPGHEQY----TR--NMVTGAstadlaILLIDARKGVLEQTRrhsYIAS--L-LGIRHvVVAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 126 NKIDRPD---GRHEEVINEVFDLFANLDATDEQLdFPIlygSGRDGWMNVNP-------EGPkdqgltPLLDLvLKHVP- 194
Cdd:COG2895 156 NKMDLVDyseEVFEEIVADYRAFAAKLGLEDITF-IPI---SALKGDNVVERsenmpwyDGP------TLLEH-LETVEv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 195 EPTVHEGPFTM-IGTILEANP-FlgRIITGRINSGSIKPNQAVKVLHAdGKtieTGRISKILAFRGiertAIDEAHQGDI 272
Cdd:COG2895 225 AEDRNDAPFRFpVQYVNRPNLdF--RGYAGTIASGTVRVGDEVVVLPS-GK---TSTVKSIVTFDG----DLEEAFAGQS 294
|
...
gi 502309546 273 IAI 275
Cdd:COG2895 295 VTL 297
|
|
| tufA |
CHL00071 |
elongation factor Tu |
5-275 |
3.03e-18 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 87.32 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRINIVDTPGHADFggeve 84
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADY----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 85 rILSM------VDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVA-INKIDRPDgrHEEVIN----EVFDLFANLD-AT 152
Cdd:CHL00071 89 -VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVD--DEELLElvelEVRELLSKYDfPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 153 DeqlDFPILYGSGRDGwMNVNPEGPK-DQGLTP-------LLDLVLKHVPEPTVH-EGPFTMigTILEANPFLGR--IIT 221
Cdd:CHL00071 166 D---DIPIVSGSALLA-LEALTENPKiKRGENKwvdkiynLMDAVDSYIPTPERDtDKPFLM--AIEDVFSITGRgtVAT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309546 222 GRINSGSIKPNQAVKVLhadgktieTGRISKILAFRGIE--RTAIDEAHQGDIIAI 275
Cdd:CHL00071 240 GRIERGTVKVGDTVEIV--------GLRETKTTTVTGLEmfQKTLDEGLAGDNVGI 287
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
5-196 |
6.64e-17 |
|
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: 79.16 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSNDLEKERGITIlaKATSVEWKGVRINI--VDTPGHADFgge 82
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITI--NTAHVEYETANRHYahVDCPGHADY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 83 verILSMV------DGAIVLVDSSEGPMPQTKFVVSKALKVGL-RPIVAINKIDRPDGR--HEEVINEVFDLfanLDATD 153
Cdd:cd01884 79 ---IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVpYIVVFLNKADMVDDEelLELVEMEVREL---LSKYG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502309546 154 EQLD-FPILYGSGRDGWMNVNPEGPKDQgLTPLLDLVLKHVPEP 196
Cdd:cd01884 153 FDGDdTPIVRGSALKALEGDDPNKWVDK-ILELLDALDSYIPTP 195
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
4-149 |
3.27e-16 |
|
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: 76.26 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERvMDSNDLEKERGITIlakatsvewkgvRINIVDTPGHADF---- 79
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTY------------KFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309546 80 ---GGEVERILSMVDGAIVLVDSSEGPMPQTKfVVSKALKVGLRPIVAINKIDRPDGRHEEvinEVFDLFANL 149
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDLKDADLKT---HVASEFAKL 137
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-287 |
6.73e-16 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 81.42 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvaervmdSNDLEKER-GITILAKATSVEW--KGVRINIV--DTPGHADFG 80
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAgGITQKIGAYEVEFeyKDENQKIVflDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 81 GEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVfdLFANLDATDEQLDFPI 160
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL--AKYNLIPEKWGGDTPM 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 161 LYGSGRDGwmnvnpegpkdQGLTPLLDLV--------LKHVPEPTVHegpftmiGTILEA--NPFLGRIITGRINSGSik 230
Cdd:CHL00189 388 IPISASQG-----------TNIDKLLETIlllaeiedLKADPTQLAQ-------GIILEAhlDKTKGPVATILVQNGT-- 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309546 231 pnqavkvLHAdGKTIETG-RISKILAFRGIERTAIDEAHQGDIIAIAGLSK----GTVADTF 287
Cdd:CHL00189 448 -------LHI-GDIIVIGtSYAKIRGMINSLGNKINLATPSSVVEIWGLSSvpatGEHFQVF 501
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-168 |
1.41e-14 |
|
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: 71.87 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 11 HVDHGKTTLVDELlkqSGsfRENQRVAErvmdsndlEKERGITI-LAKATSVEWKGVRINIVDTPGHADFggeverILSM 89
Cdd:cd04171 7 HIDHGKTTLIKAL---TG--IETDRLPE--------EKKRGITIdLGFAYLDLPDGKRLGFIDVPGHEKF------VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 90 V------DGAIVLVDSSEGPMPQTK--FVVSKALKVGlRPIVAINKIDRPD-GRHEEVINEVFDLFANLDATDEqldfPI 160
Cdd:cd04171 68 LagaggiDAVLLVVAADEGIMPQTRehLEILELLGIK-KGLVVLTKADLVDeDRLELVEEEILELLAGTFLADA----PI 142
|
....*...
gi 502309546 161 LYGSGRDG 168
Cdd:cd04171 143 FPVSSVTG 150
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
402-479 |
2.62e-14 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 68.34 E-value: 2.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309546 402 EVVVDVDEEHSGVVVQKMSERKAEMVELRPSGGNRLRLRFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYKGVI 479
Cdd:pfam00679 8 KVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQPVPGDI 85
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
6-141 |
3.50e-14 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 75.57 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELlkqsgsfrENQRVAERvmdsndleKERGITILAKATSVEWK-GVRINIVDTPGHADFGGEVE 84
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI--------RKTKVAQG--------EAGGITQHIGAYHVENEdGKMITFLDTPGHEAFTSMRA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 502309546 85 RILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINE 141
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQE 210
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
5-291 |
7.23e-14 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 74.01 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVAER-----------------VMDSNDLEKERGITILAKATSVEWKGVR 67
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGI--DKRTIEKfekeaaemgkgsfkyawVLDKLKAERERGITIDIALWKFETPKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 68 INIVDTPGHADFGGEVERILSMVDGAIVLVDSSEGPMP-------QTKFVVSKALKVGLRP-IVAINKIDRP-----DGR 134
Cdd:PTZ00141 87 FTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQmIVCINKMDDKtvnysQER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 135 HEEVINEVFDLFANLDATDEQLDFPILYGSGRDGWMNVNPEGP--KDQGLTPLLDLVlkhVPEPTVHEGPFTM------- 205
Cdd:PTZ00141 167 YDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPwyKGPTLLEALDTL---EPPKRPVDKPLRLplqdvyk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 206 IGTIleanpflGRIITGRINSGSIKPNQAVKV----LHADGKTIEtgriskilafrgIERTAIDEAHQGDI-------IA 274
Cdd:PTZ00141 244 IGGI-------GTVPVGRVETGILKPGMVVTFapsgVTTEVKSVE------------MHHEQLAEAVPGDNvgfnvknVS 304
|
330
....*....|....*...
gi 502309546 275 IAGLSKGTVA-DTFCDPS 291
Cdd:PTZ00141 305 VKDIKRGYVAsDSKNDPA 322
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
5-142 |
8.85e-14 |
|
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: 74.14 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKqsgsfrenqrvaervMDSNDL--EKERGITILAKATSVEWKGVRINIVDTPGHADFGGE 82
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTG---------------IAADRLpeEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309546 83 VERILSMVDGAIVLVDSSEGPMPQTK--FVVSKALKVGLRpIVAINKIDRPDgrhEEVINEV 142
Cdd:TIGR00475 67 AIAGGGGIDAALLVVDADEGVMTQTGehLAVLDLLGIPHT-IVVITKADRVN---EEEIKRT 124
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
6-141 |
2.49e-13 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 72.74 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDellkqsgSFReNQRVAErvmdsndleKE-RGIT--IlaKATSVEWKGVRINIVDTPGHADF--- 79
Cdd:COG0532 7 VTVMGHVDHGKTSLLD-------AIR-KTNVAA---------GEaGGITqhI--GAYQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309546 80 ---GGEVERIlsmvdgAIVLVDSSEGPMPQTKFVVS--KALKVglrPI-VAINKIDRPDGRHEEVINE 141
Cdd:COG0532 68 rarGAQVTDI------VILVVAADDGVMPQTIEAINhaKAAGV---PIiVAINKIDKPGANPDRVKQE 126
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
5-168 |
4.66e-13 |
|
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: 68.37 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVA-ER---------------VMDSNDLEKERGITI--------LAKATS 60
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAAlERskssgtqgekldlalLVDGLQAEREQGITIdvayryfsTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 61 VewkgvrinIVDTPGHADFggeverILSMVDGA------IVLVDSSEGPMPQTK---FVVSkalKVGLRPIV-AINKIDR 130
Cdd:cd04166 81 I--------IADTPGHEQY------TRNMVTGAstadlaILLVDARKGVLEQTRrhsYIAS---LLGIRHVVvAVNKMDL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502309546 131 PD---GRHEEVINEVFDLFANLDATDEQLdFPIlygSGRDG 168
Cdd:cd04166 144 VDydeEVFEEIKADYLAFAASLGIEDITF-IPI---SALEG 180
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
7-169 |
1.78e-12 |
|
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: 65.56 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 7 AIIAHVDHGKTTLVDELLKQSGSFRENqrvaervmdsndlekERGITILAKATSVEW--KGVRINIVDTPGHADFGG--- 81
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSD---------------VPGTTRDPDVYVKELdkGKVKLVLVDTPGLDEFGGlgr 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 82 --EVERILSMVDGAIVLVDSSEGPMP--QTKFVVSKALKVGLRPIVAINKIDRPDGRHEEVINEVFDLFANldatdeqLD 157
Cdd:cd00882 66 eeLARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKI-------LG 138
|
170
....*....|..
gi 502309546 158 FPILYGSGRDGW 169
Cdd:cd00882 139 VPVFEVSAKTGE 150
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
404-476 |
2.10e-12 |
|
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.
Pssm-ID: 238772 [Multi-domain] Cd Length: 79 Bit Score: 62.88 E-value: 2.10e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309546 404 VVDVDEEHSGVVVQKMSERKAEMVELRPSGGNRLRLRFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK 476
Cdd:cd01514 7 EITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
217-288 |
2.78e-12 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 62.28 E-value: 2.78e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502309546 217 GRIITGRINSGSIKPNQAVKVLHAD-GKTIETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFC 288
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
5-291 |
6.59e-12 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 67.81 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVAER-----------------VMDSNDLEKERGITILAKATSVEWKGVR 67
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGI--DKRVIERfekeaaemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 68 INIVDTPGHADFGGEVERILSMVDGAIVLVDSSEGPMP-------QTKFVVSKALKVGLRPIV-AINKIDR-----PDGR 134
Cdd:PLN00043 87 CTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 135 HEEVINEVFDLFANLDATDEQLDF-PIlygSGRDGWMNVNPEGPKDQGLTPLLDLVLKHVPEPT-VHEGPFTMIGTILEA 212
Cdd:PLN00043 167 YDEIVKEVSSYLKKVGYNPDKIPFvPI---SGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKrPSDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 213 NPFLGRIITGRINSGSIKPNQAVkVLHADGKTIETGRISkilafrgIERTAIDEAHQGD-------IIAIAGLSKGTVA- 284
Cdd:PLN00043 244 IGGIGTVPVGRVETGVIKPGMVV-TFGPTGLTTEVKSVE-------MHHESLQEALPGDnvgfnvkNVAVKDLKRGYVAs 315
|
....*..
gi 502309546 285 DTFCDPS 291
Cdd:PLN00043 316 NSKDDPA 322
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
5-129 |
4.76e-11 |
|
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: 62.38 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELlkqsgsfRENQRVAerVMDSNDLEKERGITI--------------LAKATSVEWKGVRINI 70
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL-------SEIASTA--AFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502309546 71 VDTPGHADFggeVERILS---MVDGAIVLVDSSEGPMPQTK--FVVSKALKVGLrpIVAINKID 129
Cdd:cd01889 73 VDCPGHASL---IRTIIGgaqIIDLMLLVVDAKKGIQTQTAecLVIGELLCKPL--IVVLNKID 131
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
210-289 |
6.21e-11 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 58.69 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 210 LEANPFLGRIITGRINSGSIKPNQAVKvlhaDGKTIETGRISKILAFRGIERTAIDEAHQGDIIAIAGLSKGTVADTFCD 289
Cdd:cd04088 8 TMADPFVGKLTFFRVYSGTLKSGSTVY----NSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
6-133 |
6.53e-10 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 61.75 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERVMDSndlekERGITILAKATSVEWKGVRINI-------VDTPGHAD 78
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLLKSFKIKLkipgllfIDTPGHEA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 502309546 79 FGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSkALKVGLRP-IVAINKIDRPDG 133
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEALN-ILRSRKTPfVVAANKIDRIPG 136
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
1-130 |
8.45e-10 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 61.73 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 1 MSLRN--IAIIAHVDHGKTTLVDellKQSGSfrenqRVAervmdsndlEKERG-ITILAKATSVEW-----------KGV 66
Cdd:PRK04004 2 KKLRQpiVVVLGHVDHGKTTLLD---KIRGT-----AVA---------AKEAGgITQHIGATEVPIdviekiagplkKPL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 67 RINI-------VDTPGHADF------GGeverilSMVDGAIVLVDSSEGPMPQTKfvvsKALKVgLR----P-IVAINKI 128
Cdd:PRK04004 65 PIKLkipgllfIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTI----EAINI-LKrrktPfVVAANKI 133
|
..
gi 502309546 129 DR 130
Cdd:PRK04004 134 DR 135
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
5-129 |
1.07e-09 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 60.64 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaervMDSNDLEKERGITI---LAKAT---------------------- 59
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVW----------TDRHSEELKRGITIrlgYADATirkcpdceepeayttepkcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 60 SVEWKGVR-INIVDTPGHadfggEV--ERILS---MVDGAIVLVDSSEG-PMPQTK--FVvskALK-VGLRPIV-AINKI 128
Cdd:PRK04000 78 GSETELLRrVSFVDAPGH-----ETlmATMLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALDiIGIKNIViVQNKI 149
|
.
gi 502309546 129 D 129
Cdd:PRK04000 150 D 150
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
5-293 |
1.76e-09 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 60.07 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaervMDSNDLEKERGITI-LAKATSVEWKGV----------------- 66
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVW----------TDTHSEELKRGISIrLGYADAEIYKCPecdgpecyttepvcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 67 --------RINIVDTPGHADFggeVERILS---MVDGAIVLVDSSEG-PMPQTKFVVSKALKVGLRPIV-AINKIDRPDg 133
Cdd:TIGR03680 73 gsetellrRVSFVDAPGHETL---MATMLSgaaLMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIViVQNKIDLVS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 134 rHEEVINEVFDLFANLDATDEQlDFPILYGSGRDgwmNVNpegpkdqgLTPLLDLVLKHVPEPTVHEG-PFTMI------ 206
Cdd:TIGR03680 149 -KEKALENYEEIKEFVKGTVAE-NAPIIPVSALH---NAN--------IDALLEAIEKFIPTPERDLDkPPLMYvarsfd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 207 ----GTilEANPFLGRIITGRINSGSIKPNQAVKVL-----HADGKTIETGRISKILAFRgIERTAIDEAHQGDIIAIAg 277
Cdd:TIGR03680 216 vnkpGT--PPEKLKGGVIGGSLIQGKLKVGDEIEIRpgikvEKGGKTKWEPIYTEITSLR-AGGYKVEEARPGGLVGVG- 291
|
330
....*....|....*.
gi 502309546 278 lskgtvadTFCDPSIT 293
Cdd:TIGR03680 292 --------TKLDPALT 299
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
6-191 |
1.34e-08 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 54.75 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELLKQsgsfrenqrvaERVMDSNdlekERGITILAKATSVEWKGVRINIVDTPG-----HADFG 80
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 81 GE------VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINK---IDRPDGRHEEVINEVFDLFAnlda 151
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502309546 152 tdeQLDF-PILYGSGRDGwmnvnpegpkdQGLTPLLDLVLK 191
Cdd:cd01895 146 ---FLDYaPIVFISALTG-----------QGVDKLFDAIKE 172
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
6-166 |
5.75e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 55.83 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVdellkQSGSFRENQRVAErvmdsndlEKERGITI-LAKATSVEWKGVRINIVDTPGHADFggeVE 84
Cdd:PRK10512 3 IATAGHVDHGKTTLL-----QAITGVNADRLPE--------EKKRGMTIdLGYAYWPQPDGRVLGFIDVPGHEKF---LS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 85 RILSMVDG---AIVLVDSSEGPMPQTKFVVSkALKVGLRP--IVAINKIDRPD-GRHEEVINEVFDLFANLDATDEQLdF 158
Cdd:PRK10512 67 NMLAGVGGidhALLVVACDDGVMAQTREHLA-ILQLTGNPmlTVALTKADRVDeARIAEVRRQVKAVLREYGFAEAKL-F 144
|
....*...
gi 502309546 159 PILYGSGR 166
Cdd:PRK10512 145 VTAATEGR 152
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
5-129 |
7.14e-08 |
|
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: 53.04 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaervMDSNDLEKERGITI-LAKATS----------------------- 60
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVW----------TVRHKEELKRNITIkLGYANAkiykcpncgcprpydtpececpg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 61 --VEWKGVR-INIVDTPGHadfggeveRIL--------SMVDGAIVLVDSSEG-PMPQTK--FVvskALKV-GLRPIV-A 124
Cdd:cd01888 69 cgGETKLVRhVSFVDCPGH--------EILmatmlsgaAVMDGALLLIAANEPcPQPQTSehLA---ALEImGLKHIIiL 137
|
....*
gi 502309546 125 INKID 129
Cdd:cd01888 138 QNKID 142
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
304-382 |
7.56e-08 |
|
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G (EF-G) and related proteins play a role in translation and share a similar domain architecture. Elongation factor EFG participates in the elongation phase during protein biosynthesis on the ribosome by stimulating translocation. Its functional cycles depend on GTP binding and its hydrolysis. Domain III is involved in the activation of GTP hydrolysis. This domain III, which is different from domain III in EF-TU and related elongation factors, is found in several translation factors, like bacterial release factors RF3, elongation factor 4, elongation factor 2, GTP-binding protein BipA and tetracycline resistance protein Tet.
Pssm-ID: 293914 [Multi-domain] Cd Length: 71 Bit Score: 49.65 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 304 PTVTMSFIVNDSplagtegdkVTSRVIRDRLFKEAEGNVALKIEEAEGKDSFYVSGRGELQLAVLIETMRRE-GFELAVS 382
Cdd:cd16257 1 PVVFVTVEVKNP---------LDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
5-127 |
3.39e-07 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 49.15 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKqsgsfrENQRVAERVmdsndlekerGITILAKATSVEWKGVRINIVDTPG----HADFG 80
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTG------AKAIVSDYP----------GTTRDPNEGRLELKGKQIILVDTPGliegASEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 502309546 81 GEVERILSM--VDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINK 127
Cdd:pfam01926 65 GLGRAFLAIieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
5-129 |
6.15e-07 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 52.15 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaervMDSNDLEKERGITI---LAKAT-------------SVEWK---- 64
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVW----------TDRHSEELKRGITIrlgYADATfykcpnceppeayTTEPKcpnc 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 65 GV------RINIVDTPGHadfggEV--ERILS---MVDGAIVLVDSSEG-PMPQTK--FVvskALK-VGLRPIVAI-NKI 128
Cdd:COG5257 74 GSetellrRVSFVDAPGH-----ETlmATMLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALDiIGIKNIVIVqNKI 145
|
.
gi 502309546 129 D 129
Cdd:COG5257 146 D 146
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
12-310 |
6.30e-07 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 52.24 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 12 VDHGKTTLVDELLKQSGSFRENQRVA-ER----------------VMDSNDLEKERGITI------LAKATsvewkgvRI 68
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIFEDQLAAlERdskkvgtqgdeidlalLVDGLAAEREQGITIdvayryFATPK-------RK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 69 NIV-DTPGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTK---FVVSkalKVGLRPIV-AINKIDRPD---GRHEEVIN 140
Cdd:PRK05506 106 FIVaDTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRrhsFIAS---LLGIRHVVlAVNKMDLVDydqEVFDEIVA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 141 EVFDLFANLDATDEQLdFPIlygSGRDGWMNVNP-------EGPkdqgltPLLDLvLKHVP-EPTVHEGPFTMigTILEA 212
Cdd:PRK05506 183 DYRAFAAKLGLHDVTF-IPI---SALKGDNVVTRsarmpwyEGP------SLLEH-LETVEiASDRNLKDFRF--PVQYV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 213 N-PFLG-RIITGRINSGSIKPNQAVKVLHAdGKtieTGRISKILAFRGiertAIDEAHQGDIIAIaglskgTVADtfcdp 290
Cdd:PRK05506 250 NrPNLDfRGFAGTVASGVVRPGDEVVVLPS-GK---TSRVKRIVTPDG----DLDEAFAGQAVTL------TLAD----- 310
|
330 340
....*....|....*....|...
gi 502309546 291 SITIP---LPAQPIDPPTVTMSF 310
Cdd:PRK05506 311 EIDISrgdMLARADNRPEVADQF 333
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
15-139 |
1.64e-06 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 48.40 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 15 GKTTLVDELLKQsgsfreNQRVAERVMdsndlekerGITILAKATSVEWKGVR-INIVDTPGHADFGGE----VERILSM 89
Cdd:cd00880 9 GKSSLLNALLGQ------NVGIVSPIP---------GTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGLgrerVEEARQV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 502309546 90 ---VDGAIVLVDSSEGPMPQtKFVVSKALKVGLRPIVAINKIDRPDGRHEEVI 139
Cdd:cd00880 74 adrADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEEEL 125
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
6-191 |
2.43e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 50.05 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELLKQsgsfrenqrvaERVMDSNdlekERGITILAKATSVEWKGVRINIVDTPG-------HAD 78
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 79 fggeVE--------RILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKID-RPDGRHEEVINEVFDLFANL 149
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDlVDEKTMEEFKKELRRRLPFL 316
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502309546 150 DatdeqlDFPILYGSGRDGwmnvnpegpkdQGLTPLLDLVLK 191
Cdd:PRK00093 317 D------YAPIVFISALTG-----------QGVDKLLEAIDE 341
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
213-283 |
4.73e-06 |
|
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: 44.95 E-value: 4.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309546 213 NPFLGRIITGRINSGSIKPNQAVKVLhadgKTIETGRISKILAFrgieRTAIDEAHQGDIIAIAGLSKGTV 283
Cdd:cd01342 11 IPGRGRVAGGRVESGTLKVGDEIRIL----PKGITGRVTSIERF----HEEVDEAKAGDIVGIGILGVKDI 73
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-168 |
5.30e-06 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 47.28 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 1 MSLRNIAIIAHVDHGKTTLVDELLkqsgsfreNQRVAERVMDSndlekERGITILAKATSVEWKGVRINIVDTPGHADF- 79
Cdd:COG1100 1 MGEKKIVVVGTGGVGKTSLVNRLV--------GDIFSLEKYLS-----TNGVTIDKKELKLDGLDVDLVIWDTPGQDEFr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 80 --GGEVERILSMVDGAIVLVDSSegpMPQT----KFVVSKALKVGLRP--IVAINKIDRPDgrhEEVINEVFDLfanLDA 151
Cdd:COG1100 68 etRQFYARQLTGASLYLFVVDGT---REETlqslYELLESLRRLGKKSpiILVLNKIDLYD---EEEIEDEERL---KEA 138
|
170
....*....|....*..
gi 502309546 152 TDEQLDFPILYGSGRDG 168
Cdd:COG1100 139 LSEDNIVEVVATSAKTG 155
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
12-275 |
1.08e-05 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 48.37 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 12 VDHGKTTLVDELLKQSGSFRENQRVAERvMDSN---------DL---------EKERGITIlakatSVEWKGVRIN---- 69
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIYEDQLASLH-NDSKrhgtqgeklDLallvdglqaEREQGITI-----DVAYRYFSTEkrkf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 70 -IVDTPGHADF------GGeverilSMVDGAIVLVDSSEGPMPQTK---FVVSkalKVGLRP-IVAINKIDRPDGRHE-- 136
Cdd:PRK05124 110 iIADTPGHEQYtrnmatGA------STCDLAILLIDARKGVLDQTRrhsFIAT---LLGIKHlVVAVNKMDLVDYSEEvf 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 137 EVINEVFDLFANLDATDEQLDF-PIlygSGRDGWMNVNP-------EGPkdqgltPLLDlVLKHVPEPTVHE-GPFTM-I 206
Cdd:PRK05124 181 ERIREDYLTFAEQLPGNLDIRFvPL---SALEGDNVVSQsesmpwySGP------TLLE-VLETVDIQRVVDaQPFRFpV 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 207 GTILEAN-PFLGriITGRINSGSIKPNQAVKVLHAdGKtieTGRISKILAFRGIertaIDEAHQGDIIAI 275
Cdd:PRK05124 251 QYVNRPNlDFRG--YAGTLASGVVKVGDRVKVLPS-GK---ESNVARIVTFDGD----LEEAFAGEAITL 310
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
61-192 |
4.68e-05 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 43.96 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 61 VEWKGVRINIVDTPGHADFGGE--------VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPD 132
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIK 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 133 grHEEVINEvfdlFANLDATDEqldFPIlygSGRDGwmnvnpegpkdQGLTPLLDLVLKH 192
Cdd:cd01894 120 --EEEEAAE----FYSLGFGEP---IPI---SAEHG-----------RGIGDLLDAILEL 156
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
5-162 |
8.82e-05 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 43.69 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 5 NIAIIAHVDHGKTTLVDELLKqsgsfrenqrvaERVMDSndlekerGITIL-AKATSVEW---KGVRinIVDTPG----- 75
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLG------------EEVLPT-------GVTPTtAVITVLRYgllKGVV--LVDTPGlnsti 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 76 --HADfggEVERILSMVDGAIVLVDSSEgpmPQTK----FVVSKALKVGLRPIVAINKIDRPdgRHEEVINEVFDLFANL 149
Cdd:cd09912 61 ehHTE---ITESFLPRADAVIFVLSADQ---PLTEsereFLKEILKWSGKKIFFVLNKIDLL--SEEELEEVLEYSREEL 132
|
170
....*....|...
gi 502309546 150 DATDEQLDFPILY 162
Cdd:cd09912 133 GVLELGGGEPRIF 145
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
61-227 |
2.69e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.89 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 61 VEWKGVRINIVDTPG----HADFGGEV----ERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDRPD 132
Cdd:PRK00093 44 AEWLGREFILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 133 GrhEEVINEvfdlFANLDATDEqldFPIlygSGRDGwmnvnpegpkdQGLTPLLDLVLKHVPEPTVHEGPFTMIgtilea 212
Cdd:PRK00093 124 E--EADAYE----FYSLGLGEP---YPI---SAEHG-----------RGIGDLLDAILEELPEEEEEDEEDEPI------ 174
|
170
....*....|....*.
gi 502309546 213 npflgRI-ITGRINSG 227
Cdd:PRK00093 175 -----KIaIIGRPNVG 185
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
71-195 |
2.85e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 43.05 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 71 VDTPG-----HAdFG----GEVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR-PDGRHEEVIN 140
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLvKKEELLPLLA 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502309546 141 EVFDLFANLDAtdeqldFPIlygSGRDGwmnvnpegpkdQGLTPLLDLVLKHVPE 195
Cdd:COG1159 135 EYSELLDFAEI------VPI---SALKG-----------DNVDELLDEIAKLLPE 169
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
71-195 |
3.54e-04 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 42.73 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 71 VDTPG-HADfggevERIL--SMVDGA----------IVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR--PDGRH 135
Cdd:PRK00089 58 VDTPGiHKP-----KRALnrAMNKAAwsslkdvdlvLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLvkDKEEL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502309546 136 EEVINEVFDLFANLDAtdeqldFPI--LYGSGRDGwmnvnpegpkdqgltpLLDLVLKHVPE 195
Cdd:PRK00089 133 LPLLEELSELMDFAEI------VPIsaLKGDNVDE----------------LLDVIAKYLPE 172
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
61-200 |
4.13e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 43.09 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 61 VEWKGVRINIVDTPG-----HADFGGE----VERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGlRP-IVAINKIDR 130
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502309546 131 PDgrHEEVINEVFDL-FANLdatdeqldFPIlygSGRDGwmnvnpegpkdQGLTPLLDLVLKHVPEPTVHE 200
Cdd:COG1160 124 PK--READAAEFYSLgLGEP--------IPI---SAEHG-----------RGVGDLLDAVLELLPEEEEEE 170
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
70-133 |
5.86e-04 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 42.95 E-value: 5.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502309546 70 IVDTPGHADFGGEVERILSMVDGAIVLVDSSEGPMPQTKFVVSkALKVGLRP-IVAINKIDRPDG 133
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAIN-ILRQYKTPfVVAANKIDLIPG 593
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
6-131 |
2.43e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 40.93 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqRVAERVMDSNDLEKERgITILAkatsvEWKGVRINIVDTPG--------HA 77
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILG---------RREAVVEDTPGVTRDR-VSYDA-----EWAGTDFKLVDTGGweadvegiDS 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502309546 78 DFGGEVERILSMVDGAIVLVDSSEGPMpQTKFVVSKALKVGLRPI-VAINKIDRP 131
Cdd:PRK09518 343 AIASQAQIAVSLADAVVFVVDGQVGLT-STDERIVRMLRRAGKPVvLAVNKIDDQ 396
|
|
| Septin |
pfam00735 |
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
15-79 |
2.67e-03 |
|
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.
Pssm-ID: 395596 Cd Length: 272 Bit Score: 39.98 E-value: 2.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502309546 15 GKTTLVDELLkqsgsfrENQRVAERVMDSNDLEKERGITILAKATSVEWKGVRIN--IVDTPGHADF 79
Cdd:pfam00735 15 GKTTFINTLF-------LTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNltVIDTPGFGDA 74
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
15-191 |
2.88e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 40.39 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 15 GKTTLVDELLKQsgsfrenqrvaERVMDSNdlekERGITILAKATSVEWKGVRINIVDTPG-----HADFGGE---VERI 86
Cdd:COG1160 187 GKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkgKVDEGIEkysVLRT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 87 LSMVDGA---IVLVDSSEGPMPQTKFVVSKALKVGlRPIV-AINK---IDRPDGRHEEVINEVFDLFANLDatdeqlDFP 159
Cdd:COG1160 252 LRAIERAdvvLLVIDATEGITEQDLKIAGLALEAG-KALViVVNKwdlVEKDRKTREELEKEIRRRLPFLD------YAP 324
|
170 180 190
....*....|....*....|....*....|..
gi 502309546 160 ILYGSGRDGwmnvnpegpkdQGLTPLLDLVLK 191
Cdd:COG1160 325 IVFISALTG-----------QGVDKLLEAVDE 345
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
210-289 |
3.09e-03 |
|
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.
Pssm-ID: 293908 [Multi-domain] Cd Length: 81 Bit Score: 36.88 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502309546 210 LEANPFlGRIITGRINSGSIKPNQAVKVLHaDGKTIetgRISKILAFRGIERTAIDEAHQGDIIAIAGLsKGTVADTFCD 289
Cdd:cd04091 8 LEEGRF-GQLTYMRVYQGVLRKGDTIYNVR-TGKKV---RVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFTD 81
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
71-130 |
4.45e-03 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 38.21 E-value: 4.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502309546 71 VDTPG-HADFGG-------EVERILSMVDGAIVLVDSSEGPMPQTKFVVSKALKVGLRPIVAINKIDR 130
Cdd:cd04163 56 VDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL 123
|
|
| |
