|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-603 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1156.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 1 MALRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFG 80
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHADFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 81 GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFAALDATDEQLDFPI 160
Cdd:COG1217 84 GEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDFPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 161 LYGSGRSGWMNVNPEGPTdEGLAPLLDLVVKHVPEPKVE-EGPFRMIGTILEANNFLGRIITGRIASGSIKPNQAVKVLG 239
Cdd:COG1217 164 VYASARNGWASLDLDDPG-EDLTPLFDTILEHVPAPEVDpDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 240 QDGKlIENGRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPAVMEPMQAQPIDPPTVTMSFIVNDSPLAG 319
Cdd:COG1217 243 RDGK-VEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 320 TEGDKVTSRVIRDRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRREGFELAVSRPRVVMhKDENGQLMEP 399
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIF-KEIDGKKLEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 400 VEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQPYKGEI 479
Cdd:COG1217 401 IEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYKGEI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 480 GGRVNGVLLSNESGEAVAYALFNLEDRGPMIIDAGEKVYAGMIIGIHSRDNDLDVNVLKGKKLTNIRAAGKDEAVKLTPP 559
Cdd:COG1217 481 PGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 490578840 560 IKFTLERALSWIQDDELVEVTPKSIRLRKLYLDPNDRKRFEKAK 603
Cdd:COG1217 561 RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKK 604
|
|
| 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: 994.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFAALDATDEQLDFPILY 162
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 163 GSGRSGWMNVNPEGPTDEgLAPLLDLVVKHVPEPKVE-EGPFRMIGTILEANNFLGRIITGRIASGSIKPNQAVKVLGQD 241
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDN-MAPLFDAIVRHVPAPKGDlDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 242 GKlIENGRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPAVMEPMQAQPIDPPTVTMSFIVNDSPLAGTE 321
Cdd:TIGR01394 240 GT-IENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 322 GDKVTSRVIRDRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRREGFELAVSRPRVVMhKDENGQLMEPVE 401
Cdd:TIGR01394 319 GKKVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIY-KEIDGKKLEPIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 402 EVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQPYKGEIGG 481
Cdd:TIGR01394 398 ELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGEIET 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 482 RVNGVLLSNESGEAVAYALFNLEDRGPMIIDAGEKVYAGMIIGIHSRDNDLDVNVLKGKKLTNIRAAGKDEAVKLTPPIK 561
Cdd:TIGR01394 478 RRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRK 557
|
570 580 590
....*....|....*....|....*....|....*..
gi 490578840 562 FTLERALSWIQDDELVEVTPKSIRLRKLYLDPNDRKR 598
Cdd:TIGR01394 558 LSLEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
3-598 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 670.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:PRK10218 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFAALDATDEQLDFPILY 162
Cdd:PRK10218 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 163 GSGRSGWMNVNPEGpTDEGLAPLLDLVVKHVPEPKVE-EGPFRMIGTILEANNFLGRIITGRIASGSIKPNQAVKVLGQD 241
Cdd:PRK10218 165 ASALNGIAGLDHED-MAEDMTPLYQAIVDHVPAPDVDlDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 242 GKlIENGRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPAVMEPMQAQPIDPPTVTMSFIVNDSPLAGTE 321
Cdd:PRK10218 244 GK-TRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 322 GDKVTSRVIRDRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRREGFELAVSRPRVVMhKDENGQLMEPVE 401
Cdd:PRK10218 323 GKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIF-REIDGRKQEPYE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 402 EVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQPYK-GEIG 480
Cdd:PRK10218 402 NVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 481 GRVNGVLLSNESGEAVAYALFNLEDRGPMIIDAGEKVYAGMIIGIHSRDNDLDVNVLKGKKLTNIRAAGKDEAVKLTPPI 560
Cdd:PRK10218 482 QRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPI 561
|
570 580 590
....*....|....*....|....*....|....*...
gi 490578840 561 KFTLERALSWIQDDELVEVTPKSIRLRKLYLDPNDRKR 598
Cdd:PRK10218 562 RMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRR 599
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
3-196 |
8.45e-131 |
|
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: 381.17 E-value: 8.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:cd01891 2 IRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFAALDATDEQLDFPILY 162
Cdd:cd01891 82 VERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIVY 161
|
170 180 190
....*....|....*....|....*....|....
gi 490578840 163 GSGRSGWMNVNPEGPTDEgLAPLLDLVVKHVPEP 196
Cdd:cd01891 162 ASAKNGWASLNLDDPSED-LDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
3-194 |
2.49e-73 |
|
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: 232.80 E-value: 2.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVM---ERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADF 79
Cdd:pfam00009 3 HRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 80 GGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPD-ARHEEVVNEVFDLFAALDATDEqLDF 158
Cdd:pfam00009 83 VKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELLEKYGEDG-EFV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 490578840 159 PILYGSGRSGWmnvnpegptdeGLAPLLDLVVKHVP 194
Cdd:pfam00009 162 PVVPGSALKGE-----------GVQTLLDALDEYLP 186
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
4-387 |
5.76e-58 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 207.02 E-value: 5.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSI--EWKDTR--INIVDTPGHADF 79
Cdd:PRK07560 21 RNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMvhEYEGKEylINLIDTPGHVDF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 80 GGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDR--------PD---ARHEEVVNEVFDLFAA 148
Cdd:PRK07560 101 GGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPQemqQRLLKIIKDVNKLIKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 149 -----------LDATDEQLDFpilyGSGRSGW-----------------MNVNPEGPTDE--GLAPL----LDLVVKHVP 194
Cdd:PRK07560 181 mapeefkekwkVDVEDGTVAF----GSALYNWaisvpmmqktgikfkdiIDYYEKGKQKElaEKAPLhevvLDMVVKHLP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 195 EPKV--------------------------EEGPFRMIGTILEANNFLGRIITGRIASGSIKPNQAVKVLGQDGKlienG 248
Cdd:PRK07560 257 NPIEaqkyripkiwkgdlnsevgkamlncdPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKK----N 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 249 RISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPAVMEPMQA-QPIDPPTVTMSfI----VNDSPlagtegd 323
Cdd:PRK07560 333 RVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESlKHISEPVVTVA-IeaknPKDLP------- 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490578840 324 KVTSrVIRDrLFKEaEGNVALKIEEsaDKDSFFVSGRGELQLAVLIENMRRE-GFELAVSRPRVV 387
Cdd:PRK07560 405 KLIE-VLRQ-LAKE-DPTLVVKINE--ETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVV 464
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
3-386 |
5.58e-55 |
|
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: 198.35 E-value: 5.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSfreNQRVME-----RVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHA 77
Cdd:COG0480 9 IRNIGIVAHIDAGKTTLTERILFYTGA---IHRIGEvhdgnTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 78 DFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNE---------------- 141
Cdd:COG0480 86 DFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQlkerlganpvplqlpi 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 142 --------VFDLF-------------------------------------AALDATDEQLD------------------- 157
Cdd:COG0480 166 gaeddfkgVIDLVtmkayvyddelgakyeeeeipaelkeeaeeareelieAVAETDDELMEkylegeelteeeikaglrk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 158 -------FPILYGSGRSGWmnvnpegptdeGLAPLLDLVVKHVPEPkVEEGPFRMI----GTILE--------------- 211
Cdd:COG0480 246 atlagkiVPVLCGSAFKNK-----------GVQPLLDAVVDYLPSP-LDVPAIKGVdpdtGEEVErkpdddepfsalvfk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 212 --ANNFLGRIITGRIASGSIKPNQAVKVLGQDGKliEngRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCD 289
Cdd:COG0480 314 tmTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKK--E--RIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 290 PAvmEPMQAQPIDPPTVTMSFIVNdsplAGTEGDkvtsrviRDRLF----KEAEGNVALKIEESADKDSFFVSGRGELQL 365
Cdd:COG0480 390 ED--HPIVLEPIEFPEPVISVAIE----PKTKAD-------EDKLStalaKLAEEDPTFRVETDEETGQTIISGMGELHL 456
|
490 500
....*....|....*....|..
gi 490578840 366 AVLIENMRRE-GFELAVSRPRV 386
Cdd:COG0480 457 EIIVDRLKREfGVEVNVGKPQV 478
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
5-196 |
1.33e-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: 183.65 E-value: 1.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGEVE 84
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPD-ARHEEVVNEVFDLFAALDAT-DEQLDFPILY 162
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|....
gi 490578840 163 GSGRSGwmnvnpegptdEGLAPLLDLVVKHVPEP 196
Cdd:cd00881 161 ISALTG-----------EGIEELLDAIVEHLPPP 183
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-433 |
2.01e-54 |
|
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: 197.04 E-value: 2.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSI----EWKDTRINIVDTPGHAD 78
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyEGNEYLINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDR--------PDARHE---EVVNEVFDLFA 147
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltPQELQErfiKIITEVNKLIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 148 AL---DATDEQL----DFPILYGSGRSGWMNVNP-----------------EGPTDE--GLAPL----LDLVVKHVPEPK 197
Cdd:TIGR00490 179 AMapeEFRDKWKvrveDGSVAFGSAYYNWAISVPsmkktgigfkdiykyckEDKQKElaKKSPLhqvvLDMVIRHLPSPI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 198 VE--------------------------EGPFRMIGTILEANNFLGRIITGRIASGSIKPNQAVKVLGQDGKlienGRIS 251
Cdd:TIGR00490 259 EAqkyripviwkgdlnsevgkamlncdpKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAK----ARIQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 252 KILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPA-VMEPMQA-QPIDPPTVTMSFIVNDSplagtegdKVTSRV 329
Cdd:TIGR00490 335 QVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVeNITPFESiKHISEPVVTVAIEAKNT--------KDLPKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 330 IrDRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRRE-GFELAVSRPRVVMHKDENGQ------------- 395
Cdd:TIGR00490 407 I-EVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTspvvegkspnkhn 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 490578840 396 ----LMEPVEEVVIDVDEEhsGVVVQKMSERKAEMVELRPSG 433
Cdd:TIGR00490 486 rfyiVVEPLEESVIQAFKE--GKIVDMKMKKKERRRLLIEAG 525
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-387 |
1.03e-53 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 194.78 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 1 MALRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVME--RVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHAD 78
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNE----------------- 141
Cdd:PRK13351 86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDieerfgkrplplqlpig 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 142 -------VFDLF--------------------------------------AALDATDEQLD------------------- 157
Cdd:PRK13351 166 sedgfegVVDLItepelhfsegdggstveegpipeelleeveeareklieALAEFDDELLElylegeelsaeqlraplre 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 158 -------FPILYGSGRsgwmnvnpegpTDEGLAPLLDLVVKHVPEPK-------------------VEEGPFRMIGTILE 211
Cdd:PRK13351 246 gtrsghlVPVLFGSAL-----------KNIGIEPLLDAVVDYLPSPLevppprgskdngkpvkvdpDPEKPLLALVFKVQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 212 ANNFLGRIITGRIASGSIKPNQAVkVLGQDGKLIengRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPA 291
Cdd:PRK13351 315 YDPYAGKLTYLRVYSGTLRAGSQL-YNGTGGKRE---KVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 292 vmEPMQAQPIDPPTVTMSFIVndSPLAGTEGDKVTSRVirDRLFKEAEGnvaLKIEESADKDSFFVSGRGELQLAVLIEN 371
Cdd:PRK13351 391 --DPVLLELLTFPEPVVSLAV--EPERRGDEQKLAEAL--EKLVWEDPS---LRVEEDEETGQTILSGMGELHLEVALER 461
|
490
....*....|....*..
gi 490578840 372 MRRE-GFELAVSRPRVV 387
Cdd:PRK13351 462 LRREfKLEVNTGKPQVA 478
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
3-474 |
2.40e-50 |
|
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: 183.68 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFreNQRVM-ERVMDSNDIEKERGITILAKATSIEWKDT-----RINIVDTPGH 76
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAI--SEREMrEQVLDSMDLERERGITIKAQAVRLNYKAKdgetyVLNLIDTPGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 77 ADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFaALDATDeql 156
Cdd:TIGR01393 81 VDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVI-GLDASE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 157 dfpILYGSGRSGwmnvnpegptdEGLAPLLDLVVKHVPEPKVE-EGPFRMIgtILEA--NNFLGRIITGRIASGSIKPNQ 233
Cdd:TIGR01393 157 ---AILASAKTG-----------IGIEEILEAIVKRVPPPKGDpDAPLKAL--IFDShyDNYRGVVALVRVFEGTIKPGD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 234 AVKVL--GQDGKLIENGriskILAFRGIERTSIEEAHAGDIVA-IAGLSKGTVADTF--CDPAVMEPMQA-QPIDPptvt 307
Cdd:TIGR01393 221 KIRFMstGKEYEVDEVG----VFTPKLTKTDELSAGEVGYIIAgIKDVSDVRVGDTIthVKNPAKEPLPGfKEVKP---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 308 MSFivndSPLAGTEGDKVtsRVIRDRLFKEAEGNVALKIE-ESADKDSF-FVSG-RGELQLAVLIENMRREgFELAV--S 382
Cdd:TIGR01393 293 MVF----AGLYPIDTEDY--EDLRDALEKLKLNDASLTYEpESSPALGFgFRCGfLGLLHMEIIQERLERE-FNLDLitT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 383 RPRVVMH-KDENGQLM------------------EPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFA 443
Cdd:TIGR01393 366 APSVIYRvYLTNGEVIevdnpsdlpdpgkiehveEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIYEM 445
|
490 500 510
....*....|....*....|....*....|..
gi 490578840 444 P-TRGLIGYQSELLTDTRGTAVMNRLFHDYQP 474
Cdd:TIGR01393 446 PlAEIVYDFFDKLKSISRGYASFDYELIGYRP 477
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
9-387 |
6.10e-49 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 181.09 E-value: 6.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 9 IAHVDHGKTTLVDELLKQSGSFRENQRVME--RVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGEVERI 86
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 87 LSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNE------------------------V 142
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQlqeklgapvvplqlpigegddftgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 143 FDL-------------FAALDATDEQLD------------------------------------------------FPIL 161
Cdd:PRK12740 161 VDLlsmkayrydeggpSEEIEIPAELLDraeeareellealaefddelmekylegeelseeeikaglrkatlageiVPVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 162 YGSGRSGWmnvnpegptdeGLAPLLDLVVKHVPEP---KVEEGPFRMIGTILEANN---------------FLGRIITGR 223
Cdd:PRK12740 241 CGSALKNK-----------GVQRLLDAVVDYLPSPlevPPVDGEDGEEGAELAPDPdgplvalvfktmddpFVGKLSLVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 224 IASGSIKPNQAVKVLGQDGKlienGRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPAvmEPMQAQPIDP 303
Cdd:PRK12740 310 VYSGTLKKGDTLYNSGTGKK----ERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKG--DPILLEPMEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 304 PTVTMSFIVndSPLAGTEGDKVtSRVIRdRLfkeAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRRE-GFELAVS 382
Cdd:PRK12740 384 PEPVISLAI--EPKDKGDEEKL-SEALG-KL---AEEDPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEVETG 456
|
....*
gi 490578840 383 RPRVV 387
Cdd:PRK12740 457 PPQVP 461
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
4-196 |
9.40e-48 |
|
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: 166.64 E-value: 9.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITIlaKATSI-----------EWKDTRINIVD 72
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIslyfeyeeekmDGNDYLINLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 73 TPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDR--------PDARHE------EV 138
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklsPEEAYQrllrivED 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490578840 139 VNEVFDLFAALDATDEQLDFP-----ILYGSGRSGW-MNVNpegpTDEGLAPLLDLVVKHVPEP 196
Cdd:cd01885 159 VNAIIETYAPEEFKQEKWKFSpqkgnVAFGSALDGWgFTII----KFADIYAVLEMVVKHLPSP 218
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
3-386 |
6.35e-45 |
|
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: 169.60 E-value: 6.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVM--ERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFG 80
Cdd:TIGR00484 10 FRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHdgAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGHVDFT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 81 GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNE------------------- 141
Cdd:TIGR00484 90 VEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQikqrlganavpiqlpigae 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 142 -----VFDLF-------------------------------------AALDATDE---------QLDFPILYGSGRSGWM 170
Cdd:TIGR00484 170 dnfigVIDLVemkayffngdkgtkaiekeipsdlleqakelrenlveAVAEFDEElmekylegeELTIEEIKNAIRKGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 171 NVN------PEGPTDEGLAPLLDLVVKHVPEP--------------------KVEEGPFRMIGTILEANNFLGRIITGRI 224
Cdd:TIGR00484 250 NCEffpvlcGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidpdtekeierkASDDEPFSALAFKVATDPFVGQLTFVRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 225 ASGSIKPNQAVKVLGQDGKLiengRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCDPAVMEPMQAQPIDPP 304
Cdd:TIGR00484 330 YSGVLKSGSYVKNSRKNKKE----RVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPEP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 305 TVTMSFivndSPLAGTEGDKVTSrvirdRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRRE-GFELAVSR 383
Cdd:TIGR00484 406 VISLAV----EPKTKADQEKMGI-----ALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREfKVEANVGA 476
|
...
gi 490578840 384 PRV 386
Cdd:TIGR00484 477 PQV 479
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
4-272 |
4.03e-44 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 166.35 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSG--SFRENQrvmERVMDSNDIEKERGITILAKATSIEWK-----DTRINIVDTPGH 76
Cdd:COG0481 7 RNFSIIAHIDHGKSTLADRLLELTGtlSEREMK---EQVLDSMDLERERGITIKAQAVRLNYKakdgeTYQLNLIDTPGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 77 ADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFaALDATDeql 156
Cdd:COG0481 84 VDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 157 dfpILYGSGRSGwmnvnpegptdEGLAPLLDLVVKHVPEPK-VEEGPFRMIgtILEA--NNFLGRIITGRIASGSIKPNQ 233
Cdd:COG0481 160 ---AILVSAKTG-----------IGIEEILEAIVERIPPPKgDPDAPLQAL--IFDSwyDSYRGVVVYVRVFDGTLKKGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490578840 234 AVKVLGqdgklieNGRISKIL---AFRgIERTSIEEAHAGDI 272
Cdd:COG0481 224 KIKMMS-------TGKEYEVDevgVFT-PKMTPVDELSAGEV 257
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
304-382 |
1.44e-43 |
|
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: 150.15 E-value: 1.44e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 304 PTVTMSFIVNDSPLAGTEGDKVTSRVIRDRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRREGFELAVS 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 |
1.51e-42 |
|
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: 153.16 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVME--RVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKgtTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKfVVGKAL-KVGLRPIVAINKIDRPDARHEEVVNEV 142
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTR-ILFRLLrKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
4-196 |
2.19e-42 |
|
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: 150.38 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRvMERVMDSNDIEKERGITILAKATSIEWKDTR-----INIVDTPGHAD 78
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFaALDATDeqldf 158
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVL-GLDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 490578840 159 pILYGSGRSGwmnvnpegptdEGLAPLLDLVVKHVPEP 196
Cdd:cd01890 154 -AILVSAKTG-----------LGVEDLLEAIVERIPPP 179
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
398-476 |
7.46e-41 |
|
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: 142.64 E-value: 7.46e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 398 EPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQPYK 476
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
5-142 |
3.41e-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: 139.16 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMER--VMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEV 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 ... |
203-296 |
3.03e-35 |
|
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: 127.69 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 203 FRMIGTILEANNFLGRIITGRIASGSIKPNQAVKVLGQDGKlIENGRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGT 282
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGK-IEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDIT 79
|
90
....*....|....
gi 490578840 283 VADTFCDPAVMEPM 296
Cdd:cd03691 80 IGDTICDPEVPEPL 93
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-169 |
2.05e-31 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 130.17 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITIlaKATSI----EW--------KDTRINI 70
Cdd:PTZ00416 19 IRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyEHdledgddkQPFLINL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 71 VDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRP--DARHE------------ 136
Cdd:PTZ00416 97 IDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAilELQLDpeeiyqnfvkti 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 490578840 137 EVVNEVFDLFAALDATDEQLDfP----ILYGSGRSGW 169
Cdd:PTZ00416 177 ENVNVIIATYNDELMGDVQVY-PekgtVAFGSGLQGW 212
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
4-196 |
3.78e-31 |
|
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: 120.45 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVM---ERVMDSNDIEKERGITILAKATSIEWKDTR-----INIVDTPG 75
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGwkpLRYTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 76 HADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDR-------P--DARHE--EVVNEVFD 144
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRlilelklPptDAYYKlrHTIDEINN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 145 LFAALDATDEQLDFP----ILYGSGRSGWMNvnpegpTDEGLA---PLLDLVVKHVPEP 196
Cdd:cd04167 161 YIASFSTTEGFLVSPelgnVLFASSKFGFCF------TLESFAkkyGLVDSILSHIPSP 213
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
4-131 |
2.05e-28 |
|
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: 114.62 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMER------VMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHA 77
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARksrkhaTSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490578840 78 DFGGEVERILSMVDGAIVLVDAAEGPMPQTKfvvgKALKVG-LR--PIVA-INKIDRP 131
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTR----KLFEVCrLRgiPIITfINKLDRE 136
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
3-130 |
3.38e-27 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 117.13 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITIlaKATSI------------------EWK 64
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGIslyyemtdeslkdfkgerDGN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490578840 65 DTRINIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDR 130
Cdd:PLN00116 97 EYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
5-322 |
4.40e-27 |
|
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: 113.87 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVMER-----------------VMDSNDIEKERGITILAKATSIEWKDTR 67
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAI--DEHIIEKyeeeaekkgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 68 INIVDTPGHADFggeVERIL---SMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRP-IVAINKIDRPD---ARHEEVVN 140
Cdd:COG5256 87 FTIIDAPGHRDF---VKNMItgaSQADAAILVVSAKDGVMGQTREHAFLARTLGINQlIVAVNKMDAVNyseKRYEEVKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 141 EVFDLFAALDATDEQLDF-PIlygsgrSGWMNVN--------P--EGPTdegLAPLLDLVVkhVPEPKVEEgPFRM---- 205
Cdd:COG5256 164 EVSKLLKMVGYKVDKIPFiPV------SAWKGDNvvkksdnmPwyNGPT---LLEALDNLK--EPEKPVDK-PLRIpiqd 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 206 ------IGTileannflgrIITGRIASGSIKPNQAVKVL--GQDGKLiengriskilafRGIE--RTSIEEAHAGDIV-- 273
Cdd:COG5256 232 vysisgIGT----------VPVGRVETGVLKVGDKVVFMpaGVVGEV------------KSIEmhHEELEQAEPGDNIgf 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490578840 274 AIAGLSKGTvadtfcdpaVMEPMQAQPID-PPTVTMSF----IVNDSPLAGTEG 322
Cdd:COG5256 290 NVRGVEKND---------IKRGDVAGHPDnPPTVAEEFtaqiVVLQHPSAITVG 334
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-146 |
3.39e-26 |
|
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: 108.06 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVME--RVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLF 146
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
5-287 |
5.80e-26 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 110.79 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMER---------------VMDSNDIEKERGITILAKATSIEWKDTRIN 69
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELReeakekgkesfkfawVMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 70 IVDTPGHADFggeVERIL---SMVDGAIVLVDA--AEGPMPQTKFVVGKALKVGLRP-IVAINKIDRPD---ARHEEVVN 140
Cdd:PRK12317 88 IVDCPGHRDF---VKNMItgaSQADAAVLVVAAddAGGVMPQTREHVFLARTLGINQlIVAINKMDAVNydeKRYEEVKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 141 EVFDLFAALDATDEQLDF-PI--LYG------SGRSGWMNvnpeGPTdegLAPLLDLVVkhVPEPKVEEgPFRM------ 205
Cdd:PRK12317 165 EVSKLLKMVGYKPDDIPFiPVsaFEGdnvvkkSENMPWYN----GPT---LLEALDNLK--PPEKPTDK-PLRIpiqdvy 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 206 ----IGTileannflgrIITGRIASGSIKPNQAVKVL--GQDG--KLIEngriskilafrgIERTSIEEAHAGDIVAIA- 276
Cdd:PRK12317 235 sisgVGT----------VPVGRVETGVLKVGDKVVFMpaGVVGevKSIE------------MHHEELPQAEPGDNIGFNv 292
|
330 340
....*....|....*....|....*..
gi 490578840 277 -GLSKG---------------TVADTF 287
Cdd:PRK12317 293 rGVGKKdikrgdvcghpdnppTVAEEF 319
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-295 |
6.87e-26 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 111.07 E-value: 6.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGEVE 84
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVA-INKIDRPDARH--EEVVNEVFDLFAALDATDEqlDFPIL 161
Cdd:PLN03127 143 TGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEEllELVEMELRELLSFYKFPGD--EIPII 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 162 YGSGRSGWMNVNPEGPTDEGLApLLDLVVKHVPEPK-VEEGPFRMigTILEANNFLGR--IITGRIASGSIKPNQAVKVL 238
Cdd:PLN03127 221 RGSALSALQGTNDEIGKNAILK-LMDAVDEYIPEPVrVLDKPFLM--PIEDVFSIQGRgtVATGRVEQGTIKVGEEVEIV 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490578840 239 GqdgkLIENGRISKILAfrGIE--RTSIEEAHAGDIVA--IAGLSKGTV--ADTFCDPAVMEP 295
Cdd:PLN03127 298 G----LRPGGPLKTTVT--GVEmfKKILDQGQAGDNVGllLRGLKREDVqrGQVICKPGSIKT 354
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
395-479 |
4.41e-25 |
|
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: 99.16 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 395 QLMEPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQP 474
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*
gi 490578840 475 YKGEI 479
Cdd:pfam00679 81 VPGDI 85
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
5-275 |
1.35e-24 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 106.18 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITIlakATS-IEWK-DTR-INIVDTPGHADFgg 81
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITI---NTAhVEYEtEKRhYAHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 82 everILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLRPI-VAINKIDRPDArhEEVVN----EVFDLFAALD 150
Cdd:PRK12736 89 ----VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLvVFLNKVDLVDD--EELLElvemEVRELLSEYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 151 ATDEqlDFPILYGSGRSGwmnVNPEGPTDEGLAPLLDLVVKHVPEPKVE-EGPFRM----IGTIleannfLGR--IITGR 223
Cdd:PRK12736 163 FPGD--DIPVIRGSALKA---LEGDPKWEDAIMELMDAVDEYIPTPERDtDKPFLMpvedVFTI------TGRgtVVTGR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490578840 224 IASGSIKPNQAVKVLGQdgkliengRISKILAFRGIE--RTSIEEAHAGDIVAI 275
Cdd:PRK12736 232 VERGTVKVGDEVEIVGI--------KETQKTVVTGVEmfRKLLDEGQAGDNVGV 277
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
5-275 |
1.46e-24 |
|
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: 106.00 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGsfrenQRVMERVMDSNDI-----EKERGITIlakATS-IEWK-DTR-INIVDTPGH 76
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITKVLA-----KKGGAKAKAYDQIdkapeEKERGITI---NTShVEYEtEKRhYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 77 ADFggeverILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLRPI-VAINKIDRPDarHEEVVN----EVFDL 145
Cdd:COG0050 86 ADY------VKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEELLElvemEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 146 FAALDATDEqlDFPILYGSGrSGWMNVNPEGPTDEGLAPLLDLVVKHVPEPKVE-EGPFRM----IGTIleannfLGR-- 218
Cdd:COG0050 158 LSKYGFPGD--DTPIIRGSA-LKALEGDPDPEWEKKILELMDAVDSYIPEPERDtDKPFLMpvedVFSI------TGRgt 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 219 IITGRIASGSIKPNQAVKVLGqdgklIENGRISKIlafRGIE--RTSIEEAHAGDIVAI 275
Cdd:COG0050 229 VVTGRVERGIIKVGDEVEIVG-----IRDTQKTVV---TGVEmfRKLLDEGEAGDNVGL 279
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-295 |
4.61e-24 |
|
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: 106.92 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 8 IIA---HVDHGKTTLV--------DELlkqsgsfREnqrvmervmdsndiEKERGITI--------LAKatsiewkDTRI 68
Cdd:COG3276 2 IIGtagHIDHGKTTLVkaltgidtDRL-------KE--------------EKKRGITIdlgfaylpLPD-------GRRL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 69 NIVDTPGHADFggeverILSMVDGA----IVL--VDAAEGPMPQTK--FVVGKALKVGlRPIVAINKIDR-PDARHEEVV 139
Cdd:COG3276 54 GFVDVPGHEKF------IKNMLAGAggidLVLlvVAADEGVMPQTRehLAILDLLGIK-RGIVVLTKADLvDEEWLELVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 140 NEVFDLFAAL---DAtdeqldfPILYGSGRSGwmnvnpegptdEGLAPL---LDLVVKHVPePKVEEGPFRM-------- 205
Cdd:COG3276 127 EEIRELLAGTfleDA-------PIVPVSAVTG-----------EGIDELraaLDALAAAVP-ARDADGPFRLpidrvfsi 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 206 --IGTileannflgrIITGRIASGSIKPNQAVKVLGQdgklienGRISKIlafRGIER--TSIEEAHAGDIVAI--AGLS 279
Cdd:COG3276 188 kgFGT----------VVTGTLLSGTVRVGDELELLPS-------GKPVRV---RGIQVhgQPVEEAYAGQRVALnlAGVE 247
|
330
....*....|....*...
gi 490578840 280 KGTVA--DTFCDPAVMEP 295
Cdd:COG3276 248 KEEIErgDVLAAPGALRP 265
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-275 |
1.51e-23 |
|
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: 102.93 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQ-SGSFRENQRVMERVmDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGEV 83
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITTVlAKEGGAAARAYDQI-DNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 84 ERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGL-RPIVAINKIDRPDARH--EEVVNEVFDLFAALDATDEqlDFPI 160
Cdd:TIGR00485 93 ITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVpYIVVFLNKCDMVDDEEllELVEMEVRELLSQYDFPGD--DTPI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 161 LYGSGRSGwmnVNPEGPTDEGLAPLLDLVVKHVPEPKVE-EGPFRMigTILEANNFLGR--IITGRIASGSIKPNQAVKV 237
Cdd:TIGR00485 171 IRGSALKA---LEGDAEWEAKILELMDAVDEYIPTPEREiDKPFLL--PIEDVFSITGRgtVVTGRVERGIIKVGEEVEI 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 490578840 238 LGQdgKLIENGRISKILAFRGIertsIEEAHAGDIVAI 275
Cdd:TIGR00485 246 VGL--KDTRKTTVTGVEMFRKE----LDEGRAGDNVGL 277
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-275 |
5.61e-23 |
|
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: 101.70 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 1 MALRNIAIIAHVDHGKTTLVDELLKQSGSFRENQ----------RVMERV-----MDSNDIEKERGITI-LAK---ATsi 61
Cdd:COG2895 15 KDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQlaalerdskkRGTQEIdlallTDGLQAEREQGITIdVAYryfST-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 62 ewkDTR--InIVDTPGHADFggevERilSMVDGA------IVLVDAAEGPMPQTK---FVVgkALkVGLRP-IVAINKID 129
Cdd:COG2895 93 ---PKRkfI-IADTPGHEQY----TR--NMVTGAstadlaILLIDARKGVLEQTRrhsYIA--SL-LGIRHvVVAVNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 130 RPD---ARHEEVVNEVFDLFAALDATDEQLdFPIlygSGRSGWMNVNP-------EGPTdegLAPLLDLVvkhVPEPKVE 199
Cdd:COG2895 160 LVDyseEVFEEIVADYRAFAAKLGLEDITF-IPI---SALKGDNVVERsenmpwyDGPT---LLEHLETV---EVAEDRN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 200 EGPFRM-IGTILEAN-NFlgRIITGRIASGSIKPNQAVKVLGqdgklieNGRISKIlafRGIER--TSIEEAHAGDIVAI 275
Cdd:COG2895 230 DAPFRFpVQYVNRPNlDF--RGYAGTIASGTVRVGDEVVVLP-------SGKTSTV---KSIVTfdGDLEEAFAGQSVTL 297
|
|
| tufA |
CHL00071 |
elongation factor Tu |
5-275 |
6.32e-23 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 101.57 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFggeve 84
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADY----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 85 rILSM------VDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVA-INKIDRPDarHEEVVN----EVFDLfaaLDATD 153
Cdd:CHL00071 89 -VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVD--DEELLElvelEVREL---LSKYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 154 EQLDF-PILYGSGRSGWMNVNPEGPTDEGLAP-------LLDLVVKHVPEPKVE-EGPFRMigTILEANNFLGR--IITG 222
Cdd:CHL00071 163 FPGDDiPIVSGSALLALEALTENPKIKRGENKwvdkiynLMDAVDSYIPTPERDtDKPFLM--AIEDVFSITGRgtVATG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490578840 223 RIASGSIKPNQAVKVLGqdgklienGRISKILAFRGIE--RTSIEEAHAGDIVAI 275
Cdd:CHL00071 241 RIERGTVKVGDTVEIVG--------LRETKTTTVTGLEmfQKTLDEGLAGDNVGI 287
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
5-275 |
1.68e-22 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 99.88 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGsfrenQRVMERVMDSNDI-----EKERGITIlakATS-IEWK-DTR-INIVDTPGH 76
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITKVLA-----KKGGAEAKAYDQIdkapeEKARGITI---NTAhVEYEtEKRhYAHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 77 ADFggeverILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLRPI-VAINKIDRPDarHEE----VVNEVFDL 145
Cdd:PRK00049 86 ADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEEllelVEMEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 146 FAALDATDEqlDFPILYGSGRsGWMNVNPEGPTDEGLAPLLDLVVKHVPEPKVE-EGPFRM----IGTIleannfLGR-- 218
Cdd:PRK00049 158 LSKYDFPGD--DTPIIRGSAL-KALEGDDDEEWEKKILELMDAVDSYIPTPERAiDKPFLMpiedVFSI------SGRgt 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 219 IITGRIASGSIKPNQAVKVLGqdgklIENGRISKIlafRGIE--RTSIEEAHAGDIVAI 275
Cdd:PRK00049 229 VVTGRVERGIIKVGEEVEIVG-----IRDTQKTTV---TGVEmfRKLLDEGQAGDNVGA 279
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
5-173 |
2.91e-22 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 95.25 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVMER-----------------VMDSNDIEKERGITILAKATSIEWKDTR 67
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGV--DKRTIEKyekeakemgkesfkyawVLDKLKEERERGVTIDVGLAKFETEKYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 68 INIVDTPGHADFggeverILSMVDG------AIVLVDAAEG-------PMPQTK--FVVGKALKVGlRPIVAINKIDRPD 132
Cdd:cd01883 79 FTIIDAPGHRDF------VKNMITGasqadvAVLVVSARKGefeagfeKGGQTRehALLARTLGVK-QLIVAVNKMDDVT 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490578840 133 -----ARHEEVVNEVFDLFAALDATDEQLDF-PIlygsgrSGWMNVN 173
Cdd:cd01883 152 vnwsqERYDEIKKKVSPFLKKVGYNPKDVPFiPI------SGFTGDN 192
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
4-131 |
8.03e-22 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 99.44 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELL------KQSGSF--RENQRV-----MErvmdsndIEKERGITIlakATSI---EWKDTR 67
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVkgRKSGRHatsdwME-------MEKQRGISV---TSSVmqfPYRDCL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490578840 68 INIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKfvvgKALKV-GLR--PIVA-INKIDRP 131
Cdd:PRK00741 81 INLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMEVcRLRdtPIFTfINKLDRD 144
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
398-476 |
1.46e-21 |
|
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: 88.69 E-value: 1.46e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 398 EPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQPYK 476
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
5-275 |
1.77e-21 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 97.76 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERVMDSNDIEKERGITILAKATSIEWKDTRINIVDTPGHADFGGEVE 84
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVA-INKIDRPDARH--EEVVNEVFDLFAALDATDEqlDFPIL 161
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRELLSSYEFPGD--DIPII 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 162 YGSGRSGW--MNVNPEGPTDEG-----LAPLLDLVVKHVPEPKVE-EGPFRMigTILEANNFLGR--IITGRIASGSIKP 231
Cdd:PLN03126 241 SGSALLALeaLMENPNIKRGDNkwvdkIYELMDAVDSYIPIPQRQtDLPFLL--AVEDVFSITGRgtVATGRVERGTVKV 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490578840 232 NQAVKVLGQdgKLIENGRISKILAFRGIertsIEEAHAGDIVAI 275
Cdd:PLN03126 319 GETVDIVGL--RETRSTTVTGVEMFQKI----LDEALAGDNVGL 356
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
6-190 |
1.79e-20 |
|
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: 88.68 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvmervmdSNDIEKE-RGIT--ILAKATSIEWKDTRINIVDTPGHADFGGE 82
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK-----------------TNVAAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEvVNEVFDLFAALDATDEQL--DFPI 160
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEAD-PERVKNELSELGLVGEEWggDVSI 144
|
170 180 190
....*....|....*....|....*....|
gi 490578840 161 LYGSGRSGwmnvnpegptdEGLAPLLDLVV 190
Cdd:cd01887 145 VPISAKTG-----------EGIDDLLEAIL 163
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
5-275 |
2.76e-20 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 93.36 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLK-QSGSFRENQRVMERVmDSNDIEKERGITIlakATS-IEWK-DTR-INIVDTPGHADFg 80
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITKvLAKKGGGEAKAYDQI-DNAPEEKARGITI---NTShVEYEtANRhYAHVDCPGHADY- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 81 geverILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLRPI-VAINKIDRPDARH--EEVVNEVFDLFAALDA 151
Cdd:PRK12735 89 -----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMVDDEEllELVEMEVRELLSKYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 152 TDEqlDFPILYGSGRsGWMNVNPEGPTDEGLAPLLDLVVKHVPEPKVE-EGPFRM----IGTIleannfLGR--IITGRI 224
Cdd:PRK12735 164 PGD--DTPIIRGSAL-KALEGDDDEEWEAKILELMDAVDSYIPEPERAiDKPFLMpiedVFSI------SGRgtVVTGRV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490578840 225 ASGSIKPNQAVKVLGqdgklIENGRISKIlafRGIE--RTSIEEAHAGDIVAI 275
Cdd:PRK12735 235 ERGIVKVGDEVEIVG-----IKETQKTTV---TGVEmfRKLLDEGQAGDNVGV 279
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
5-196 |
2.56e-18 |
|
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: 83.40 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSgsfreNQRVMERVMDSNDI-----EKERGITIlaKATSIEWK-DTRINI-VDTPGHA 77
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITKVL-----AKKGGAKAKKYDEIdkapeEKARGITI--NTAHVEYEtANRHYAhVDCPGHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 78 DFggeverILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGL-RPIVAINKIDRPDarHEEVVN----EVFDLf 146
Cdd:cd01884 77 DY------IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVpYIVVFLNKADMVD--DEELLElvemEVREL- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490578840 147 aaLDATDEQLD-FPILYGSGRSGWMNVNPEGPTDeGLAPLLDLVVKHVPEP 196
Cdd:cd01884 148 --LSKYGFDGDdTPIVRGSALKALEGDDPNKWVD-KILELLDALDSYIPTP 195
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
5-276 |
5.56e-18 |
|
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: 87.62 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSfrenqRVMErvmdsndiEKERGITILAKATSIEWKDTRINIVDTPGHADFGGEVE 84
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAAD-----RLPE--------EKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 85 RILSMVDGAIVLVDAAEGPMPQTK--FVVGKALKVGLRpIVAINKIDRPDarhEEVVNEV-FDLFAALDATDEQLDFPIL 161
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGehLAVLDLLGIPHT-IVVITKADRVN---EEEIKRTeMFMKQILNSYIFLKNAKIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 162 YGSGRSGwmnvnpEGPTD--EGLAPLLDLVvkhvpEPKVEEGPFRM-IGTILEANNFlGRIITGRIASGSIKPNQAVKVL 238
Cdd:TIGR00475 145 KTSAKTG------QGIGElkKELKNLLESL-----DIKRIQKPLRMaIDRAFKVKGA-GTVVTGTAFSGEVKVGDNLRLL 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 490578840 239 GQDGKLiengRISKILAFrgieRTSIEEAHAGDIVAIA 276
Cdd:TIGR00475 213 PINHEV----RVKAIQAQ----NQDVEIAYAGQRIALN 242
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-287 |
8.85e-18 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 87.20 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvmervmdSNDIEKERG-IT--ILAKATSIEWKDTRINIV--DTPGHADFG 80
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGgITqkIGAYEVEFEYKDENQKIVflDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 81 GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVfdlfAALDATDEQL--DF 158
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL----AKYNLIPEKWggDT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 159 PILYGSGRSGWmNVNPEGPTDEGLAPLLDLvvKHVPEPKVEegpfrmiGTILEA--NNFLGRIITGRIASGSIKPNQAVk 236
Cdd:CHL00189 386 PMIPISASQGT-NIDKLLETILLLAEIEDL--KADPTQLAQ-------GIILEAhlDKTKGPVATILVQNGTLHIGDII- 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490578840 237 VLGQdgkliENGRISKILAFRGIErtsIEEAHAGDIVAIAGLSK----GTVADTF 287
Cdd:CHL00189 455 VIGT-----SYAKIRGMINSLGNK---INLATPSSVVEIWGLSSvpatGEHFQVF 501
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
4-144 |
3.57e-17 |
|
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: 78.95 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMERvMDSNDIEKERGITIlakatsiewkdtRINIVDTPGHADF---- 79
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTY------------KFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490578840 80 ---GGEVERILSMVDGAIVLVDAAEGPMPQTKfVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFD 144
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDLKDADLKTHVASEFA 135
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
5-292 |
3.87e-16 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 80.95 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVMER-----------------VMDSNDIEKERGITILAKATSIEWKDTR 67
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGI--DKRTIEKfekeaaemgkgsfkyawVLDKLKAERERGITIDIALWKFETPKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 68 INIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMP-------QTKFVVGKALKVGLRP-IVAINKIDRP-----DAR 134
Cdd:PTZ00141 87 FTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQmIVCINKMDDKtvnysQER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 135 HEEVVNEVFDLFAALDATDEQLDF-PIlygsgrSGWMNVNP----------EGPTdegLAPLLDLVvkhVPEPKVEEGPF 203
Cdd:PTZ00141 167 YDEIKKEVSAYLKKVGYNPEKVPFiPI------SGWQGDNMieksdnmpwyKGPT---LLEALDTL---EPPKRPVDKPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 204 RM-------IGTIleannflGRIITGRIASGSIKPNQAVkvlgqdgKLIENGRISKIlafRGIE--RTSIEEAHAGDIV- 273
Cdd:PTZ00141 235 RLplqdvykIGGI-------GTVPVGRVETGILKPGMVV-------TFAPSGVTTEV---KSVEmhHEQLAEAVPGDNVg 297
|
330 340
....*....|....*....|....*.
gi 490578840 274 ------AIAGLSKGTVA-DTFCDPAV 292
Cdd:PTZ00141 298 fnvknvSVKDIKRGYVAsDSKNDPAK 323
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-168 |
4.87e-15 |
|
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: 73.02 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 11 HVDHGKTTLVDELLKQSGsfrenqrvmervmDSNDIEKERGITILAKATSIEWKD-TRINIVDTPGHADFggeverILSM 89
Cdd:cd04171 7 HIDHGKTTLIKALTGIET-------------DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKF------VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 90 V------DGAIVLVDAAEGPMPQTK--FVVGKALKVGlRPIVAINKIDRPD-ARHEEVVNEVFDLFAALDATDEqldfPI 160
Cdd:cd04171 68 LagaggiDAVLLVVAADEGIMPQTRehLEILELLGIK-KGLVVLTKADLVDeDRLELVEEEILELLAGTFLADA----PI 142
|
....*...
gi 490578840 161 LYGSGRSG 168
Cdd:cd04171 143 FPVSSVTG 150
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
6-279 |
9.73e-15 |
|
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: 77.50 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvmervmdSNDIEKER-GITILAKATSIEWKDTR-INIVDTPGHADFGGEV 83
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSIRK-----------------TKVAQGEAgGITQHIGAYHVENEDGKmITFLDTPGHEAFTSMR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 84 ERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLfaALDATDEQLDFPILYG 163
Cdd:TIGR00487 153 ARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEY--GLVPEDWGGDTIFVPV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 164 SGRSGwmnvnpegptdEGLAPLLD--LVVKHVPEPK-VEEGpfRMIGTILEANNFLGR--IITGRIASGSIKPNQAVkVL 238
Cdd:TIGR00487 231 SALTG-----------DGIDELLDmiLLQSEVEELKaNPNG--QASGVVIEAQLDKGRgpVATVLVQSGTLRVGDIV-VV 296
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490578840 239 GQdgkliENGRISKILAFRGierTSIEEAHAGDIVAIAGLS 279
Cdd:TIGR00487 297 GA-----AYGRVRAMIDENG---KSVKEAGPSKPVEILGLS 329
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
5-178 |
2.86e-14 |
|
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: 71.83 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQR--VMER--------------VMDSNDIEKERGITI--------LAKATS 60
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLaaLERSkssgtqgekldlalLVDGLQAEREQGITIdvayryfsTPKRKF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 61 IewkdtrinIVDTPGHADFggeverILSMVDGA------IVLVDAAEGPMPQTK---FVVgkALkVGLRPIV-AINKIDR 130
Cdd:cd04166 81 I--------IADTPGHEQY------TRNMVTGAstadlaILLVDARKGVLEQTRrhsYIA--SL-LGIRHVVvAVNKMDL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 131 PD---ARHEEVVNEVFDLFAALDATDEQLdFPI--LYG------SGRSGWMnvnpEGPT 178
Cdd:cd04166 144 VDydeEVFEEIKADYLAFAASLGIEDITF-IPIsaLEGdnvvsrSENMPWY----KGPT 197
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
5-291 |
1.86e-13 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 72.82 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVMER-----------------VMDSNDIEKERGITILAKATSIEWKDTR 67
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGI--DKRVIERfekeaaemnkrsfkyawVLDKLKAERERGITIDIALWKFETTKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 68 INIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMP-------QTKFVVGKALKVGLRPIV-AINKIDR-----PDAR 134
Cdd:PLN00043 87 CTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkySKAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 135 HEEVVNEVFDLFAALDATDEQLDF-PIlygSGRSGWMNVNPEGPTDEGLAPLLDLVVKHVPEPK-VEEGPFRMIGTILEA 212
Cdd:PLN00043 167 YDEIVKEVSSYLKKVGYNPDKIPFvPI---SGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKrPSDKPLRLPLQDVYK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 213 NNFLGRIITGRIASGSIKPNQAVkvlgqdgKLIENGRISKILAFRgIERTSIEEAHAGD-------IVAIAGLSKGTVA- 284
Cdd:PLN00043 244 IGGIGTVPVGRVETGVIKPGMVV-------TFGPTGLTTEVKSVE-MHHESLQEALPGDnvgfnvkNVAVKDLKRGYVAs 315
|
....*..
gi 490578840 285 DTFCDPA 291
Cdd:PLN00043 316 NSKDDPA 322
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
6-141 |
4.30e-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: 71.97 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvmervmdSNDIEKE-RGIT--IlaKATSIEWKDTRINIVDTPGHADF--- 79
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAIRK-----------------TNVAAGEaGGITqhI--GAYQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 80 ---GGEVERIlsmvdgaIVLVDAA-EGPMPQTKFVVG--KALKVglrPI-VAINKIDRPDARHEEVVNE 141
Cdd:COG0532 68 rarGAQVTDI-------VILVVAAdDGVMPQTIEAINhaKAAGV---PIiVAINKIDKPGANPDRVKQE 126
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
5-129 |
2.57e-12 |
|
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: 65.85 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKQSGSfrenqrvmeRVMDSNDIEKERGITI--------------LAKATSIEWKDTRINI 70
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKALSEIAST---------AAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490578840 71 VDTPGHADFggeVERILS---MVDGAIVLVDAAEGPMPQTK--FVVGKALKVGLrpIVAINKID 129
Cdd:cd01889 73 VDCPGHASL---IRTIIGgaqIIDLMLLVVDAKKGIQTQTAecLVIGELLCKPL--IVVLNKID 131
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
217-288 |
5.01e-11 |
|
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: 58.82 E-value: 5.01e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490578840 217 GRIITGRIASGSIKPNQAVKVLGQD-GKLIENGRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFC 288
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
5-287 |
6.42e-11 |
|
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: 64.69 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvmervMDSNDIEKERGITI-LAKATSIEWKDT----------------- 66
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVW----------TDTHSEELKRGISIrLGYADAEIYKCPecdgpecyttepvcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 67 --------RINIVDTPGHADFggeVERILS---MVDGAIVLVDAAEG-PMPQTKFVVgKALK-VGLRPIV-AINKIDRPD 132
Cdd:TIGR03680 73 gsetellrRVSFVDAPGHETL---MATMLSgaaLMDGALLVIAANEPcPQPQTKEHL-MALEiIGIKNIViVQNKIDLVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 133 arHEEVVNEVFDLFAALDATDEQlDFPILygsGRSGWMNVNpegptdegLAPLLDLVVKHVPEPKVEEG-PFRMI----- 206
Cdd:TIGR03680 149 --KEKALENYEEIKEFVKGTVAE-NAPII---PVSALHNAN--------IDALLEAIEKFIPTPERDLDkPPLMYvarsf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 207 -----GTilEANNFLGRIITGRIASGSIKPNQAVKVLgqDGKLIENGR-------ISKILAFRgIERTSIEEAHAGDIVA 274
Cdd:TIGR03680 215 dvnkpGT--PPEKLKGGVIGGSLIQGKLKVGDEIEIR--PGIKVEKGGktkwepiYTEITSLR-AGGYKVEEARPGGLVG 289
|
330
....*....|...
gi 490578840 275 IaglskGTVADTF 287
Cdd:TIGR03680 290 V-----GTKLDPA 297
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
12-310 |
1.25e-10 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 64.18 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 12 VDHGKTTLVDELLKQSGSFRENQ-RVMER----------------VMDSNDIEKERGITI-LAK---ATsiewkDTRINI 70
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIFEDQlAALERdskkvgtqgdeidlalLVDGLAAEREQGITIdVAYryfAT-----PKRKFI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 71 V-DTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTK---FVVgkALkVGLRPIV-AINKIDRPD---ARHEEVVNEv 142
Cdd:PRK05506 108 VaDTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRrhsFIA--SL-LGIRHVVlAVNKMDLVDydqEVFDEIVAD- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 143 FDLFAA-LDATDEQLdFPI--LYG------SGRSGWMnvnpEGPTdegLAPLLDLVvkHVpEPKVEEGPFRM-IGTILEA 212
Cdd:PRK05506 184 YRAFAAkLGLHDVTF-IPIsaLKGdnvvtrSARMPWY----EGPS---LLEHLETV--EI-ASDRNLKDFRFpVQYVNRP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 213 N-NFLGriITGRIASGSIKPNQAVKVLgQDGKlieNGRISKILAFRGiertSIEEAHAGDIVAIaglskgTVADtfcdpa 291
Cdd:PRK05506 253 NlDFRG--FAGTVASGVVRPGDEVVVL-PSGK---TSRVKRIVTPDG----DLDEAFAGQAVTL------TLAD------ 310
|
330 340
....*....|....*....|....*
gi 490578840 292 vmE------PMQAQPIDPPTVTMSF 310
Cdd:PRK05506 311 --EidisrgDMLARADNRPEVADQF 333
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
215-289 |
1.73e-10 |
|
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: 57.53 E-value: 1.73e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490578840 215 FLGRIITGRIASGSIKPNQAVKVLGQDGKLiengRISKILAFRGIERTSIEEAHAGDIVAIAGLSKGTVADTFCD 289
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNSTKGKKE----RVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
7-169 |
2.11e-10 |
|
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: 59.78 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 7 AIIAHVDHGKTTLVDELLKQSGSFRENqrvmervmdsndiekERGITILAKATSIEWKDTR--INIVDTPGHADFGG--- 81
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSD---------------VPGTTRDPDVYVKELDKGKvkLVLVDTPGLDEFGGlgr 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 82 --EVERILSMVDGAIVLVDAAEGPMP--QTKFVVGKALKVGLRPIVAINKIDRPDARHEEVVNEVFDLFaaldatdEQLD 157
Cdd:cd00882 66 eeLARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-------KILG 138
|
170
....*....|..
gi 490578840 158 FPILYGSGRSGW 169
Cdd:cd00882 139 VPVFEVSAKTGE 150
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
12-275 |
5.95e-10 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 61.85 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 12 VDHGKTTLVDELLKQSGSFRENQ-RVMERvmDSNDI------------------EKERGITI--------LAKATSIewk 64
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIYEDQlASLHN--DSKRHgtqgekldlallvdglqaEREQGITIdvayryfsTEKRKFI--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 65 dtrinIVDTPGHADF------GGeverilSMVDGAIVLVDAAEGPMPQTK---FVvgkALKVGLRP-IVAINKIDRPD-- 132
Cdd:PRK05124 111 -----IADTPGHEQYtrnmatGA------STCDLAILLIDARKGVLDQTRrhsFI---ATLLGIKHlVVAVNKMDLVDys 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 133 -ARHEEVVNEVFDlFAALDATDEQLDF-PI--LYG------SGRSGWMnvnpEGPTdeglapLLDLVVKHVPEPKVEEGP 202
Cdd:PRK05124 177 eEVFERIREDYLT-FAEQLPGNLDIRFvPLsaLEGdnvvsqSESMPWY----SGPT------LLEVLETVDIQRVVDAQP 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490578840 203 FRM-IGTILEAN-NFLGriITGRIASGSIKPNQAVKVL--GQDGKliengrISKILAFRGiertSIEEAHAGDIVAI 275
Cdd:PRK05124 246 FRFpVQYVNRPNlDFRG--YAGTLASGVVKVGDRVKVLpsGKESN------VARIVTFDG----DLEEAFAGEAITL 310
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
5-129 |
1.19e-09 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 60.64 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvmervMDSNDIEKERGITI--------LAKATSIEWKDT---------- 66
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVW----------TDRHSEELKRGITIrlgyadatIRKCPDCEEPEAyttepkcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 67 --------RINIVDTPGHadfggEV--ERILS---MVDGAIVLVDAAEG-PMPQTK--FVvgkALK-VGLRPIV-AINKI 128
Cdd:PRK04000 78 gsetellrRVSFVDAPGH-----ETlmATMLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALDiIGIKNIViVQNKI 149
|
.
gi 490578840 129 D 129
Cdd:PRK04000 150 D 150
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
6-130 |
1.79e-09 |
|
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: 60.60 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKQSGSFRE----NQRVMERVMDSNDIEKERGItiLAKATSIEWKDTRINIVDTPGHADFGG 81
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEaggiTQHIGASEVPTDVIEKICGD--LLKSFKIKLKIPGLLFIDTPGHEAFTN 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490578840 82 EVERILSMVDGAIVLVDAAEGPMPQTKFVVgKALKVGLRP-IVAINKIDR 130
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEAL-NILRSRKTPfVVAANKIDR 133
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
1-130 |
5.41e-09 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 59.04 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 1 MALRN--IAIIAHVDHGKTTLVDELLKQSGSFRE----NQRVMERVMDSNDIEKERGitilakaTSIEWKDTRINI---- 70
Cdd:PRK04004 2 KKLRQpiVVVLGHVDHGKTTLLDKIRGTAVAAKEaggiTQHIGATEVPIDVIEKIAG-------PLKKPLPIKLKIpgll 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490578840 71 -VDTPGHADF------GGeverilSMVDGAIVLVDAAEGPMPQTKfvvgKALKVgLR----P-IVAINKIDR 130
Cdd:PRK04004 75 fIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTI----EAINI-LKrrktPfVVAANKIDR 135
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
304-382 |
6.62e-09 |
|
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: 52.74 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 304 PTVTMSFIVNDSplagtegdkVTSRVIRDRLFKEAEGNVALKIEESADKDSFFVSGRGELQLAVLIENMRRE-GFELAVS 382
Cdd:cd16257 1 PVVFVTVEVKNP---------LDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
6-169 |
1.07e-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: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKQsgsfrenqrvmERVMDSNdiekERGITILAKATSIEWKDTRINIVDTPG-----HADFG 80
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 81 GE------VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINK---IDRPDARHEEVVNEVFDLFAalda 151
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170
....*....|....*....
gi 490578840 152 tdeQLDF-PILYGSGRSGW 169
Cdd:cd01895 146 ---FLDYaPIVFISALTGQ 161
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
6-167 |
8.08e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 55.44 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVdellkQSGSFRENQRVMErvmdsndiEKERGITI-LAKATsieW--KDTR-INIVDTPGHADFgg 81
Cdd:PRK10512 3 IATAGHVDHGKTTLL-----QAITGVNADRLPE--------EKKRGMTIdLGYAY---WpqPDGRvLGFIDVPGHEKF-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 82 eVERILSMVDG---AIVLVDAAEGPMPQTKFVVGkALKVGLRP--IVAINKIDRPD-ARHEEVVNEVFDLFAALDATDEQ 155
Cdd:PRK10512 65 -LSNMLAGVGGidhALLVVACDDGVMAQTREHLA-ILQLTGNPmlTVALTKADRVDeARIAEVRRQVKAVLREYGFAEAK 142
|
170
....*....|..
gi 490578840 156 LdFPILYGSGRS 167
Cdd:PRK10512 143 L-FVTAATEGRG 153
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
5-129 |
8.16e-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: 52.66 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvmervMDSNDIEKERGITIL-----AKATSIEWKDT------------- 66
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVW----------TVRHKEELKRNITIKlgyanAKIYKCPNCGCprpydtpececpg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 67 ---------RINIVDTPGHadfggeveRIL--------SMVDGAIVLVDAAEG-PMPQTK--FVvgkALKV-GLRPIV-A 124
Cdd:cd01888 69 cggetklvrHVSFVDCPGH--------EILmatmlsgaAVMDGALLLIAANEPcPQPQTSehLA---ALEImGLKHIIiL 137
|
....*
gi 490578840 125 INKID 129
Cdd:cd01888 138 QNKID 142
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
5-129 |
4.70e-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: 52.53 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvmervMDSNDIEKERGITI---LAKAT-------------SIEWKDT-- 66
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVW----------TDRHSEELKRGITIrlgYADATfykcpnceppeayTTEPKCPnc 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 67 --------RINIVDTPGHadfggEV--ERILS---MVDGAIVLVDAAEG-PMPQTK--FVvgkALK-VGLRPIVAI-NKI 128
Cdd:COG5257 74 gsetellrRVSFVDAPGH-----ETlmATMLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALDiIGIKNIVIVqNKI 145
|
.
gi 490578840 129 D 129
Cdd:COG5257 146 D 146
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
213-283 |
5.39e-07 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 47.64 E-value: 5.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490578840 213 NNFLGRIITGRIASGSIKPNQAVKVLGQDGKlienGRISKILAFrgieRTSIEEAHAGDIVAIAGLSKGTV 283
Cdd:cd01342 11 IPGRGRVAGGRVESGTLKVGDEIRILPKGIT----GRVTSIERF----HEEVDEAKAGDIVGIGILGVKDI 73
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
398-474 |
1.77e-06 |
|
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. 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. 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 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. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.
Pssm-ID: 239683 [Multi-domain] Cd Length: 78 Bit Score: 45.98 E-value: 1.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490578840 398 EPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVrLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQP 474
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKV-IKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
51-127 |
2.49e-06 |
|
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: 46.46 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 51 GITILAKATSIEWKDTRINIVDTPG----HADFGGEVERILSM--VDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVA 124
Cdd:pfam01926 31 GTTRDPNEGRLELKGKQIILVDTPGliegASEGEGLGRAFLAIieADLILFVVDSEEGITPLDEELLELLRENKKPIILV 110
|
...
gi 490578840 125 INK 127
Cdd:pfam01926 111 LNK 113
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
6-191 |
2.92e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 50.05 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 6 IAIIAHVDHGKTTLVDELLKQsgsfrenqrvmERVMDSNdiekERGITILAKATSIEWKDTRINIVDTPG-------HAD 78
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 79 fggeVE--------RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKID-RPDARHEEVVNEVFDLFAal 149
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDlVDEKTMEEFKKELRRRLP-- 314
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490578840 150 datdeQLDF-PILYGSGRSGwmnvnpegptdEGLAPLLDLVVK 191
Cdd:PRK00093 315 -----FLDYaPIVFISALTG-----------QGVDKLLEAIDE 341
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
15-137 |
1.03e-05 |
|
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: 46.08 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 15 GKTTLVDELLKQsgsfrenqrvmervmDSNDIEKERGITILAKATSIEWKDTR-INIVDTPGHADFGGE----VERILSM 89
Cdd:cd00880 9 GKSSLLNALLGQ---------------NVGIVSPIPGTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGLgrerVEEARQV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490578840 90 ---VDGAIVLVDAAEGPMPQtKFVVGKALKVGLRPIVAINKIDRPDARHEE 137
Cdd:cd00880 74 adrADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEE 123
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
71-195 |
2.08e-05 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 46.52 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 71 VDTPG-----HAdFG----GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRpdARHEEvvne 141
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKKEE---- 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490578840 142 vfdLFAALDATDEQLDF----PIlygSGRSGwmnvnpegptdEGLAPLLDLVVKHVPE 195
Cdd:COG1159 129 ---LLPLLAEYSELLDFaeivPI---SALKG-----------DNVDELLDEIAKLLPE 169
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
61-200 |
6.68e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 45.79 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 61 IEWKDTRINIVDTPG-----HADFGGE----VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGlRP-IVAINKIDR 130
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490578840 131 PDarHEEVVNEvfdlFAALDatdeqLD--FPIlygSGRSGwmnvnpegptdEGLAPLLDLVVKHVPEPKVEE 200
Cdd:COG1160 124 PK--READAAE----FYSLG-----LGepIPI---SAEHG-----------RGVGDLLDAVLELLPEEEEEE 170
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-141 |
6.82e-05 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 43.82 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 1 MALRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVMervmdsndiekerGITILAKATSIEWKDTRINIVDTPGHADF- 79
Cdd:COG1100 1 MGEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTN-------------GVTIDKKELKLDGLDVDLVIWDTPGQDEFr 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 80 --GGEVERILSMVDGAIVLVDAAegpMPQT----KFVVGKALKVGLRP--IVAINKIDRPDArhEEVVNE 141
Cdd:COG1100 68 etRQFYARQLTGASLYLFVVDGT---REETlqslYELLESLRRLGKKSpiILVLNKIDLYDE--EEIEDE 132
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
71-195 |
8.62e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 44.65 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 71 VDTPG-HADfggevERIL--SMVDGA----------IVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRpdarhee 137
Cdd:PRK00089 58 VDTPGiHKP-----KRALnrAMNKAAwsslkdvdlvLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL------- 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490578840 138 vVNEVFDLFAALDATDEQLDF----PIlygSGRSGwmnvnpegptdEGLAPLLDLVVKHVPE 195
Cdd:PRK00089 126 -VKDKEELLPLLEELSELMDFaeivPI---SALKG-----------DNVDELLDVIAKYLPE 172
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
5-162 |
9.89e-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: 43.30 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 5 NIAIIAHVDHGKTTLVDELLKqsgsfrenqrvmERVMDSndiekerGITIL-AKAT--SIEWKDTrINIVDTPG------ 75
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLG------------EEVLPT-------GVTPTtAVITvlRYGLLKG-VVLVDTPGlnstie 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 76 -HADfggEVERILSMVDGAIVLVDAAEgpmPQTK----FVVGKALKVGLRPIVAINKIDRpdARHEEVVNEVFDLFAALD 150
Cdd:cd09912 62 hHTE---ITESFLPRADAVIFVLSADQ---PLTEsereFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREELG 133
|
170
....*....|..
gi 490578840 151 ATDEQLDFPILY 162
Cdd:cd09912 134 VLELGGGEPRIF 145
|
|
| EF2_II_snRNP |
cd04090 |
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ... |
222-280 |
1.30e-04 |
|
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This subfamily includes domain II of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. This domain is homologous to domain II of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase which is a component of the spliceosome complex which processes precursor mRNAs to produce mature mRNAs.
Pssm-ID: 293907 [Multi-domain] Cd Length: 94 Bit Score: 41.07 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490578840 222 GRIASGSIKPNQAVKVLG-----QDGKLIENGRISKILAFRGIERTSIEEAHAGDIVAIAGLSK 280
Cdd:cd04090 21 GRIYSGTLRKGQKVKVLGenyslEDEEDMTVCTVGRLWILGARYKYEVNSAPAGNWVLIKGIDQ 84
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
61-192 |
1.97e-04 |
|
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: 42.04 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 61 IEWKDTRINIVDTPGHADFGGE--------VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRPD 132
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIK 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 133 arHEEVVNEvfdlFAALDATDEqldFPIlygSGRSGwmnvnpegptdEGLAPLLDLVVKH 192
Cdd:cd01894 120 --EEEEAAE----FYSLGFGEP---IPI---SAEHG-----------RGIGDLLDAILEL 156
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
398-476 |
7.35e-04 |
|
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 239682 [Multi-domain] Cd Length: 78 Bit Score: 38.37 E-value: 7.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490578840 398 EPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRpSGGNRVRLVFFAPTRGLIGYQSELLTDTRGTAVMNRLFHDYQPYK 476
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQ-IKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
15-191 |
9.12e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.93 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 15 GKTTLVDELLKQsgsfrenqrvmERVMDSNdiekERGITILAKATSIEWKDTRINIVDTPG-----HADFGGE---VERI 86
Cdd:COG1160 187 GKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGKKYTLIDTAGirrkgKVDEGIEkysVLRT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 87 LSMVDGA---IVLVDAAEGPMPQTKFVVGKALKVGlRPIV-AINK---IDRPDARHEEVVNEVFDLFAaldatdeQLDF- 158
Cdd:COG1160 252 LRAIERAdvvLLVIDATEGITEQDLKIAGLALEAG-KALViVVNKwdlVEKDRKTREELEKEIRRRLP-------FLDYa 323
|
170 180 190
....*....|....*....|....*....|...
gi 490578840 159 PILYGSGRSGWmnvnpegptdeGLAPLLDLVVK 191
Cdd:COG1160 324 PIVFISALTGQ-----------GVDKLLEAVDE 345
|
|
| CysN_NodQ_II |
cd03695 |
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ... |
218-275 |
1.54e-03 |
|
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.
Pssm-ID: 293896 [Multi-domain] Cd Length: 81 Bit Score: 37.55 E-value: 1.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490578840 218 RIITGRIASGSIKPNQAVKVLgQDGKlieNGRISKILAFRGiertSIEEAHAGDIVAI 275
Cdd:cd03695 16 RGYAGTIASGSIRVGDEVTVL-PSGK---TSRVKSIVTFDG----ELDSAGAGEAVTL 65
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
219-278 |
1.83e-03 |
|
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. 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. This translocation step is catalyzed by EF-2_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.
Pssm-ID: 293913 [Multi-domain] Cd Length: 96 Bit Score: 37.97 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490578840 219 IITGRIASGSIKPNQAVKVLGQD-----GKLIENGRISKILAFRGIERTSIEEAHAGDIVAIAGL 278
Cdd:cd16268 19 VAFGRVFSGTVRRGQEVYILGPKyvpgkKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGL 83
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
197-289 |
2.03e-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: 37.27 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 197 KVEEGPFrmigtileannflGRIITGRIASGSIKPNQAVKVLgQDGKLIengRISKILAFRGIERTSIEEAHAGDIVAIA 276
Cdd:cd04091 7 KLEEGRF-------------GQLTYMRVYQGVLRKGDTIYNV-RTGKKV---RVPRLVRMHSDEMEDIEEVYAGDICALF 69
|
90
....*....|...
gi 490578840 277 GLsKGTVADTFCD 289
Cdd:cd04091 70 GI-DCASGDTFTD 81
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
70-130 |
2.42e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.02 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490578840 70 IVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVgKALKVGLRP-IVAINKIDR 130
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAI-NILRQYKTPfVVAANKIDL 590
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
64-165 |
3.59e-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: 38.60 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 64 KDTRINIVDTPG-HADFGG-------EVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLRPIVAINKIDRpdARH 135
Cdd:cd04163 49 DDAQIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL--VKD 126
|
90 100 110
....*....|....*....|....*....|...
gi 490578840 136 EEvvnEVFDLFAALDATDEQLD-FPI--LYGSG 165
Cdd:cd04163 127 KE---DLLPLLEKLKELHPFAEiFPIsaLKGEN 156
|
|
| RF3_II |
cd03689 |
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ... |
218-288 |
5.48e-03 |
|
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial Release Factor 3 (RF3). Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.
Pssm-ID: 293890 [Multi-domain] Cd Length: 87 Bit Score: 36.48 E-value: 5.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490578840 218 RIITGRIASGSIKPNQAVKvLGQDGKLIengRISKILAFRGIERTSIEEAHAGDIVAIagLSKGTVA--DTFC 288
Cdd:cd03689 19 RIAFLRVCSGKFERGMKVK-HVRTGKEV---RLSNATTFMAQDRETVEEAYPGDIIGL--PNHGTFQigDTFT 85
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| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
398-474 |
9.52e-03 |
|
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized in the cytoplasmic membrane. LepA is ubiquitous in Bacteria and Eukaryota (e.g. Saccharomyces cerevisiae GUF1p), but is missing from Archaea. LepA exhibits significant homology to elongation factors (EFs) Tu and G. The function(s) of the proteins in this family are unknown. The N-terminal domain of LepA is homologous to a domain of similar size found in initiation factor 2 (IF2), and in EF-Tu and EF-G (factors required for translation in Escherichia coli). Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including S. cerevisiae GUF1) originated within the bacterial LepA family. LepA has never been observed in archaea, and eukaryl LepA is organellar. LepA is therefore a true bacterial GTPase, found only in the bacterial lineage.
Pssm-ID: 239680 [Multi-domain] Cd Length: 80 Bit Score: 35.55 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578840 398 EPVEEVVIDVDEEHSGVVVQKMSERKAEMVELRPSGGNRVRLVFFAPTrgligyqSELLTD--------TRGTAVMNRLF 469
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPL-------AEIVYDffdklksiSKGYASLDYEL 73
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....*
gi 490578840 470 HDYQP 474
Cdd:cd03709 74 IGYRE 78
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