|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-605 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1169.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 1 MELRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFG 80
Cdd:COG1217 4 EDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHADFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 81 GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFANLDATDEQLDFPI 160
Cdd:COG1217 84 GEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLDFPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 161 LYGSGRNGWMALSPEGPKDqGLAPLFDLVLKHVPAPKV-AEGPFRMIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLG 239
Cdd:COG1217 164 VYASARNGWASLDLDDPGE-DLTPLFDTILEHVPAPEVdPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 240 QDGSVlENGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPSVSEPLAAQPIDPPTVTMSFIVNDSPYAG 319
Cdd:COG1217 243 RDGKV-EKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 320 TEGDKVTSRVIRDRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRREGFELGVSRPRVVMKDgENGEKLEP 399
Cdd:COG1217 322 REGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKE-IDGKKLEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 400 VEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYKGEI 479
Cdd:COG1217 401 IEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEPYKGEI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 480 AGRNNGVLISNDQGEAVAYALFNLEDRGPMIIEAGVKVYQGMLIGIHSRDNDLEVNVLKGKKLTNIRAAGKDEAVKLTPP 559
Cdd:COG1217 481 PGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTPP 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 489055622 560 IKMTLERALSWIQDDELVEVTPKSIRLRKLYLDPNERKRFEKSKSS 605
Cdd:COG1217 561 RKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK 606
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
3-598 |
0e+00 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 1004.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGE 82
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFANLDATDEQLDFPILY 162
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 163 GSGRNGWMALSPEGPKDQgLAPLFDLVLKHVPAPKV-AEGPFRMIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQD 241
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDN-MAPLFDAIVRHVPAPKGdLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 242 GSVlENGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPSVSEPLAAQPIDPPTVTMSFIVNDSPYAGTE 321
Cdd:TIGR01394 240 GTI-ENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 322 GDKVTSRVIRDRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRREGFELGVSRPRVVMKDgENGEKLEPVE 401
Cdd:TIGR01394 319 GKKVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKE-IDGKKLEPIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 402 EVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYKGEIAG 481
Cdd:TIGR01394 398 ELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEPWKGEIET 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 482 RNNGVLISNDQGEAVAYALFNLEDRGPMIIEAGVKVYQGMLIGIHSRDNDLEVNVLKGKKLTNIRAAGKDEAVKLTPPIK 561
Cdd:TIGR01394 478 RRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRK 557
|
570 580 590
....*....|....*....|....*....|....*..
gi 489055622 562 MTLERALSWIQDDELVEVTPKSIRLRKLYLDPNERKR 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: 667.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGE 82
Cdd:PRK10218 5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFANLDATDEQLDFPILY 162
Cdd:PRK10218 85 VERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 163 GSGRNGWMALSPEGPKDQgLAPLFDLVLKHVPAPKV-AEGPFRMIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQD 241
Cdd:PRK10218 165 ASALNGIAGLDHEDMAED-MTPLYQAIVDHVPAPDVdLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 242 GSVlENGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPSVSEPLAAQPIDPPTVTMSFIVNDSPYAGTE 321
Cdd:PRK10218 244 GKT-RNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 322 GDKVTSRVIRDRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRREGFELGVSRPRVVMKDgENGEKLEPVE 401
Cdd:PRK10218 323 GKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFRE-IDGRKQEPYE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 402 EVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK-GEIA 480
Cdd:PRK10218 402 NVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRpGEVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 481 GRNNGVLISNDQGEAVAYALFNLEDRGPMIIEAGVKVYQGMLIGIHSRDNDLEVNVLKGKKLTNIRAAGKDEAVKLTPPI 560
Cdd:PRK10218 482 QRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPI 561
|
570 580 590
....*....|....*....|....*....|....*...
gi 489055622 561 KMTLERALSWIQDDELVEVTPKSIRLRKLYLDPNERKR 598
Cdd:PRK10218 562 RMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRR 599
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
2-196 |
3.14e-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: 382.33 E-value: 3.14e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 2 ELRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGG 81
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 EVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFANLDATDEQLDFPIL 161
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489055622 162 YGSGRNGWMALSPEGPKDQgLAPLFDLVLKHVPAP 196
Cdd:cd01891 161 YASAKNGWASLNLDDPSED-LDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
2-195 |
6.98e-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: 231.65 E-value: 6.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 2 ELRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVA---ERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHAD 78
Cdd:pfam00009 2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDG-RHEEVVNEVFDLFANLDATDEqLD 157
Cdd:pfam00009 82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGaELEEVVEEVSRELLEKYGEDG-EF 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 489055622 158 FPILYGSGRNGWmalspegpkdqGLAPLFDLVLKHVPA 195
Cdd:pfam00009 161 VPVVPGSALKGE-----------GVQTLLDALDEYLPS 187
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
4-430 |
1.23e-60 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 214.73 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSGSFREnqRVA--ERMMDSNDIEKERGITILAKATSVVW----KNTRINIVDTPGHA 77
Cdd:PRK07560 21 RNIGIIAHIDHGKTTLSDNLLAGAGMISE--ELAgeQLALDFDEEEQARGITIKAANVSMVHeyegKEYLINLIDTPGHV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 78 DFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR--------PD---GRHEEVVNEVFDLF 146
Cdd:PRK07560 99 DFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPQemqQRLLKIIKDVNKLI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 147 AN-----------LDATDEQLDFpilyGSGRNGWmALS-P----------------EGPKDQGLA---PL----FDLVLK 191
Cdd:PRK07560 179 KGmapeefkekwkVDVEDGTVAF----GSALYNW-AISvPmmqktgikfkdiidyyEKGKQKELAekaPLhevvLDMVVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 192 HVPAPKVAE--------------------------GPFRMIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQDGSvl 245
Cdd:PRK07560 254 HLPNPIEAQkyripkiwkgdlnsevgkamlncdpnGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKK-- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 246 enGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPSVSEPLAA-QPIDPPTVTMSfivndspyagtegdk 324
Cdd:PRK07560 332 --NRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESlKHISEPVVTVA--------------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 325 VTSRVIRD--------RLLKEAEGNVALKIEESTEKdsFFVSGRGELQLAVLIENMRRE-GFELGVSRPRVVMKDGENGE 395
Cdd:PRK07560 395 IEAKNPKDlpklievlRQLAKEDPTLVVKINEETGE--HLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGK 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489055622 396 -----------------KLEPVEEVVIDVDEEysGTVVQKMSERkaEMVELR 430
Cdd:PRK07560 473 sqvvegkspnkhnrfyiSVEPLEEEVIEAIKE--GEISEDMDKK--EAKILR 520
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
3-433 |
2.86e-56 |
|
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: 202.43 E-value: 2.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVW----KNTRINIVDTPGHAD 78
Cdd:TIGR00490 19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMVHeyegNEYLINLIDTPGHVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR--------PDGRHE---EVVNEVFDLFA 147
Cdd:TIGR00490 99 FGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltPQELQErfiKIITEVNKLIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 148 NL---DATDEQL----DFPILYGSGRNGWmALSPEGPKDQGL--------------------APLF----DLVLKHVPAP 196
Cdd:TIGR00490 179 AMapeEFRDKWKvrveDGSVAFGSAYYNW-AISVPSMKKTGIgfkdiykyckedkqkelakkSPLHqvvlDMVIRHLPSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 197 KVA--------------------------EGPFRMIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQDgsvlENGRI 250
Cdd:TIGR00490 258 IEAqkyripviwkgdlnsevgkamlncdpKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRK----AKARI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 251 SKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDP-SVSEPLAA-QPIDPPTVTMSFIVNDSpyagtegdKVTSR 328
Cdd:TIGR00490 334 QQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTvENITPFESiKHISEPVVTVAIEAKNT--------KDLPK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 329 VIrDRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRRE-GFELGVSRPRVVMKDGENGEK----------- 396
Cdd:TIGR00490 406 LI-EVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTSpvvegkspnkh 484
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489055622 397 ------LEPVEEVVIDVDEEysGTVVQKMSERKAEMVELRPSG 433
Cdd:TIGR00490 485 nrfyivVEPLEESVIQAFKE--GKIVDMKMKKKERRRLLIEAG 525
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
3-386 |
9.86e-56 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 200.27 E-value: 9.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGsfrenqrVAERM---------MDSNDIEKERGITILAKATSVVWKNTRINIVDT 73
Cdd:COG0480 9 IRNIGIVAHIDAGKTTLTERILFYTG-------AIHRIgevhdgntvMDWMPEEQERGITITSAATTCEWKGHKINIIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 74 PGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNE------------ 141
Cdd:COG0480 82 PGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQlkerlganpvpl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 142 ------------VFDLFAN---------------------------------LDA---TDEQL------------D---- 157
Cdd:COG0480 162 qlpigaeddfkgVIDLVTMkayvyddelgakyeeeeipaelkeeaeeareelIEAvaeTDDELmekylegeelteEeika 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 158 -----------FPILYGSgrngwmALspegpKDQGLAPLFDLVLKHVPAPKV--------------------AEGPFRMI 206
Cdd:COG0480 242 glrkatlagkiVPVLCGS------AF-----KNKGVQPLLDAVVDYLPSPLDvpaikgvdpdtgeeverkpdDDEPFSAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 207 GTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQDGSVlengRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADT 286
Cdd:COG0480 311 VFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKE----RIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 287 FCDPsvSEPLAAQPIDPPTVTMSFIVndspYAGTEGD--KVTSRVirDRLLKEaegNVALKIEESTEKDSFFVSGRGELQ 364
Cdd:COG0480 387 LCDE--DHPIVLEPIEFPEPVISVAI----EPKTKADedKLSTAL--AKLAEE---DPTFRVETDEETGQTIISGMGELH 455
|
490 500
....*....|....*....|...
gi 489055622 365 LAVLIENMRRE-GFELGVSRPRV 386
Cdd:COG0480 456 LEIIVDRLKREfGVEVNVGKPQV 478
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
3-474 |
1.48e-54 |
|
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: 195.23 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQrVAERMMDSNDIEKERGITILAKATSVVWK-----NTRINIVDTPGHA 77
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAISERE-MREQVLDSMDLERERGITIKAQAVRLNYKakdgeTYVLNLIDTPGHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 78 DFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFAnLDATDeqld 157
Cdd:TIGR01393 82 DFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEVIG-LDASE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 158 fpILYGSGRNGwmalspegpkdQGLAPLFDLVLKHVPAPKVA-EGPFRMIgtILEA--DPFLGRIITGRIHSGSIKPNQA 234
Cdd:TIGR01393 157 --AILASAKTG-----------IGIEEILEAIVKRVPPPKGDpDAPLKAL--IFDShyDNYRGVVALVRVFEGTIKPGDK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 235 VKVL--GQDGSVLENGriskilaFRGIERQAIDEAHAGD----IVAIAGLSKGTVADTF--CDPSVSEPLAA-QPIDPPT 305
Cdd:TIGR01393 222 IRFMstGKEYEVDEVG-------VFTPKLTKTDELSAGEvgyiIAGIKDVSDVRVGDTIthVKNPAKEPLPGfKEVKPMV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 306 VTMSFIVNDSPYagtegdkvtsRVIRDRLLKEAEGNVALKIE-ESTEKDSF-FVSG-RGELQLAVLIENMRREgFELGV- 381
Cdd:TIGR01393 295 FAGLYPIDTEDY----------EDLRDALEKLKLNDASLTYEpESSPALGFgFRCGfLGLLHMEIIQERLERE-FNLDLi 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 382 -SRP----RVVMKDGE-----NGEKL----------EPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVF 441
Cdd:TIGR01393 364 tTAPsviyRVYLTNGEvievdNPSDLpdpgkiehveEPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNRVELIY 443
|
490 500 510
....*....|....*....|....*....|....
gi 489055622 442 YAP-TRGLIGYQSELLTDTRGTAIMNRLFHDYQP 474
Cdd:TIGR01393 444 EMPlAEIVYDFFDKLKSISRGYASFDYELIGYRP 477
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
5-196 |
5.12e-53 |
|
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: 179.41 E-value: 5.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGEVE 84
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPD-GRHEEVVNEVFDLFANLDAT-DEQLDFPILY 162
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|....
gi 489055622 163 GSGRNGWmalspegpkdqGLAPLFDLVLKHVPAP 196
Cdd:cd00881 161 ISALTGE-----------GIEELLDAIVEHLPPP 183
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-387 |
6.90e-53 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 192.47 E-value: 6.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 1 MELRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRV--AERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHAD 78
Cdd:PRK13351 6 MQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVedGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR-------------------------PDG 133
Cdd:PRK13351 86 FTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRvgadlfkvledieerfgkrplplqlPIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 134 -------------------------------------------RHEEVVNEV--FD------LFANLDATDEQLD----- 157
Cdd:PRK13351 166 sedgfegvvdlitepelhfsegdggstveegpipeelleeveeAREKLIEALaeFDdellelYLEGEELSAEQLRaplre 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 158 -------FPILYGSgrngwmALspegpKDQGLAPLFDLVLKHVPAPK-------------------VAEGPFRMIGTILE 211
Cdd:PRK13351 246 gtrsghlVPVLFGS------AL-----KNIGIEPLLDAVVDYLPSPLevppprgskdngkpvkvdpDPEKPLLALVFKVQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 212 ADPFLGRIITGRIHSGSIkpNQAVKVLGQDGSVLEngRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPs 291
Cdd:PRK13351 315 YDPYAGKLTYLRVYSGTL--RAGSQLYNGTGGKRE--KVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHDS- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 292 vSEPLAAQPIDPPTVTMSFIVndSPYAGTEGDKVTSRVirDRLLKEAEGnvaLKIEESTEKDSFFVSGRGELQLAVLIEN 371
Cdd:PRK13351 390 -ADPVLLELLTFPEPVVSLAV--EPERRGDEQKLAEAL--EKLVWEDPS---LRVEEDEETGQTILSGMGELHLEVALER 461
|
490
....*....|....*..
gi 489055622 372 MRRE-GFELGVSRPRVV 387
Cdd:PRK13351 462 LRREfKLEVNTGKPQVA 478
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
9-387 |
5.37e-50 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 183.79 E-value: 5.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 9 IAHVDHGKTTLVDELLKQSGSFRENQRVAE--RMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGEVERI 86
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 87 LSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNE------------------------V 142
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQlqeklgapvvplqlpigegddftgV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 143 FDL-------------FANLDATDEQLD------------------------------------------------FPIL 161
Cdd:PRK12740 161 VDLlsmkayrydeggpSEEIEIPAELLDraeeareellealaefddelmekylegeelseeeikaglrkatlageiVPVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 162 YGSGRngwmalspegpKDQGLAPLFDLVLKHVPAPK------------------VAEGPFRMIGTILEADPFLGRIITGR 223
Cdd:PRK12740 241 CGSAL-----------KNKGVQRLLDAVVDYLPSPLevppvdgedgeegaelapDPDGPLVALVFKTMDDPFVGKLSLVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 224 IHSGSIKPNQAVKVLGQDGSVlengRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPsvSEPLAAQPIDP 303
Cdd:PRK12740 310 VYSGTLKKGDTLYNSGTGKKE----RVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDK--GDPILLEPMEF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 304 PTVTMSFIVndSPYAGTEGDKVtSRVIRdRLLKEaegNVALKIEESTEKDSFFVSGRGELQLAVLIENMRRE-GFELGVS 382
Cdd:PRK12740 384 PEPVISLAI--EPKDKGDEEKL-SEALG-KLAEE---DPTLRVERDEETGQTILSGMGELHLDVALERLKREyGVEVETG 456
|
....*
gi 489055622 383 RPRVV 387
Cdd:PRK12740 457 PPQVP 461
|
|
| EF-G |
TIGR00484 |
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ... |
3-386 |
1.76e-47 |
|
translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]
Pssm-ID: 129575 [Multi-domain] Cd Length: 689 Bit Score: 177.31 E-value: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRV--AERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFG 80
Cdd:TIGR00484 10 FRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVhdGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGHVDFT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 81 GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNE------------------- 141
Cdd:TIGR00484 90 VEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQikqrlganavpiqlpigae 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 142 -----VFDLFA----NLDATD------------------------------------------EQLDFPILYGSGRNGWM 170
Cdd:TIGR00484 170 dnfigVIDLVEmkayFFNGDKgtkaiekeipsdlleqakelrenlveavaefdeelmekylegEELTIEEIKNAIRKGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 171 ALS------PEGPKDQGLAPLFDLVLKHVPAP-KVA-------------------EGPFRMIGTILEADPFLGRIITGRI 224
Cdd:TIGR00484 250 NCEffpvlcGSAFKNKGVQLLLDAVVDYLPSPtDVPaikgidpdtekeierkasdDEPFSALAFKVATDPFVGQLTFVRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 225 HSGSIKPNQAVKVLGQDgsvlENGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCDPSVSEPLAAQPIDPP 304
Cdd:TIGR00484 330 YSGVLKSGSYVKNSRKN----KKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLCDPKIDVILERMEFPEP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 305 TVTMSFivndSPYAGTEGDKVTSrvirdRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRRE-GFELGVSR 383
Cdd:TIGR00484 406 VISLAV----EPKTKADQEKMGI-----ALGKLAEEDPTFRTFTDPETGQTIIAGMGELHLDIIVDRMKREfKVEANVGA 476
|
...
gi 489055622 384 PRV 386
Cdd:TIGR00484 477 PQV 479
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
4-196 |
2.64e-47 |
|
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: 165.10 E-value: 2.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTR---------INIVDTP 74
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITIKSSAISLYFEYEEekmdgndylINLIDSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 75 GHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR--------PDGRHE------EVVN 140
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklsPEEAYQrllrivEDVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055622 141 EVFDLFANLDATDEQLDFP-----ILYGSGRNGWmALSPEGPKDqgLAPLFDLVLKHVPAP 196
Cdd:cd01885 161 AIIETYAPEEFKQEKWKFSpqkgnVAFGSALDGW-GFTIIKFAD--IYAVLEMVVKHLPSP 218
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
4-474 |
6.63e-47 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 174.05 E-value: 6.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSG--SFRENQrvaERMMDSNDIEKERGITILAKATSVVWK----NT-RINIVDTPGH 76
Cdd:COG0481 7 RNFSIIAHIDHGKSTLADRLLELTGtlSEREMK---EQVLDSMDLERERGITIKAQAVRLNYKakdgETyQLNLIDTPGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 77 ADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFaNLDATDeql 156
Cdd:COG0481 84 VDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDASD--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 157 dfpILYGSGRNGwmalspegpkdQGLAPLFDLVLKHVPAPK-VAEGPFRMIgtILEA--DPFLGRIITGRIHSGSIKPNQ 233
Cdd:COG0481 160 ---AILVSAKTG-----------IGIEEILEAIVERIPPPKgDPDAPLQAL--IFDSwyDSYRGVVVYVRVFDGTLKKGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 234 AVKVL--GQDGSVLENGRISkilafrgIERQAIDEAHAGD---IVA-IAGLSKGTVADTFCDPS--VSEPLAA-QPIDPp 304
Cdd:COG0481 224 KIKMMstGKEYEVDEVGVFT-------PKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKnpAAEPLPGfKEVKP- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 305 tvtMsfiVndspYAG---TEGDKVTSrvIRDRLLK----------EAEGNVALkieestekdsffvsG---R----GELQ 364
Cdd:COG0481 296 ---M---V----FAGlypVDSDDYED--LRDALEKlqlndasltyEPETSAAL--------------GfgfRcgflGLLH 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 365 LAVLIENMRRE-GFELGVSRP----RVVMKDGE-----NGEKL----------EPVEEVVIDVDEEYSGTVVQKMSERKA 424
Cdd:COG0481 350 MEIIQERLEREfDLDLITTAPsvvyEVTLTDGEvievdNPSDLpdpgkieeieEPIVKATIITPSEYVGAVMELCQEKRG 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055622 425 EMVELRPSGGNRVRLVFYAPTrgligyqSELLTD--------TRGTAIMNRLFHDYQP 474
Cdd:COG0481 430 VQKNMEYLGENRVELTYELPL-------AEIVFDffdrlksiTRGYASLDYEFIGYRE 480
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
304-382 |
3.63e-42 |
|
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: 146.30 E-value: 3.63e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 304 PTVTMSFIVNDSPYAGTEGDKVTSRVIRDRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRREGFELGVS 382
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| 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 |
1.35e-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: 144.95 E-value: 1.35e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 398 EPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK 476
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
5-142 |
2.95e-41 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 149.31 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAE--RMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGE 82
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKgtTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055622 83 VERILSMVDGAIVLVDAAEGPMPQTKfVVGKAL-KVGLKPIVAINKIDRPDGRHEEVVNEV 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 |
4.58e-41 |
|
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: 146.91 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRvAERMMDSNDIEKERGITILAKATSVVWKNTR-----INIVDTPGHAD 78
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREM-KEQVLDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFAnLDATDeqldf 158
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLG-LDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 489055622 159 pILYGSGRNGwmalspegpkdQGLAPLFDLVLKHVPAP 196
Cdd:cd01890 154 -AILVSAKTG-----------LGVEDLLEAIVERIPPP 179
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
203-296 |
1.22e-36 |
|
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: 131.54 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 203 FRMIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQDGSVlENGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGT 282
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKI-EKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDIT 79
|
90
....*....|....
gi 489055622 283 VADTFCDPSVSEPL 296
Cdd:cd03691 80 IGDTICDPEVPEPL 93
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
5-142 |
1.98e-35 |
|
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: 134.54 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAER--MMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGE 82
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEV 142
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-169 |
1.36e-33 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 137.10 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTR----------INIVD 72
Cdd:PTZ00416 19 IRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITIKSTGISLYYEHDLedgddkqpflINLID 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 73 TPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRP------DG--------RHEEV 138
Cdd:PTZ00416 99 SPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAilelqlDPeeiyqnfvKTIEN 178
|
170 180 190
....*....|....*....|....*....|....*
gi 489055622 139 VNEVFDLFANLDATDEQLDfP----ILYGSGRNGW 169
Cdd:PTZ00416 179 VNVIIATYNDELMGDVQVY-PekgtVAFGSGLQGW 212
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
4-196 |
9.96e-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: 119.30 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSGS---FRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTR-----INIVDTPG 75
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKrtpSVKLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 76 HADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR-------P--DGRHE--EVVNEVFD 144
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRlilelklPptDAYYKlrHTIDEINN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055622 145 LFANLDATDEQLDFP----ILYGSGRNGW------MALspegpkdqgLAPLFDLVLKHVPAP 196
Cdd:cd04167 161 YIASFSTTEGFLVSPelgnVLFASSKFGFcftlesFAK---------KYGLVDSILSHIPSP 213
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
3-130 |
1.36e-27 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 118.29 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 3 LRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITIlaKATSV------------VWKNTR--- 67
Cdd:PLN00116 19 IRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGIslyyemtdeslkDFKGERdgn 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 68 ---INIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR 130
Cdd:PLN00116 97 eylINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
4-141 |
1.16e-26 |
|
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: 109.61 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAER------MMDSNDIEKERGITIlakATSVV---WKNTRINIVDTP 74
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARksrkhaTSDWMEIEKQRGISV---TSSVMqfeYKGCVINLLDTP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055622 75 GHADFGGEVERILSMVDGAIVLVDAAEGPMPQTK--FVVGKALKVglkPIVA-INKIDRPdGRH-----EEVVNE 141
Cdd:cd04169 80 GHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRklFEVCRLRGI---PIITfINKLDRE-GRDplellDEIENE 150
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
5-275 |
1.37e-26 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 111.96 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITIlakATSVVWKNT---RINIVDTPGHADFgg 81
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITI---NTAHVEYETekrHYAHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 everILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLKPI-VAINKIDRPDGrhEEVVN----EVFDLFANLD 150
Cdd:PRK12736 89 ----VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLvVFLNKVDLVDD--EELLElvemEVRELLSEYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 151 ATDEqlDFPILYGSGRngwMALSPEGPKDQGLAPLFDLVLKHVPAPKVA-EGPFRM----IGTIleadpfLGR--IITGR 223
Cdd:PRK12736 163 FPGD--DIPVIRGSAL---KALEGDPKWEDAIMELMDAVDEYIPTPERDtDKPFLMpvedVFTI------TGRgtVVTGR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489055622 224 IHSGSIKPNQAVKVLGQdgsvlengRISKILAFRGIE--RQAIDEAHAGDIVAI 275
Cdd:PRK12736 232 VERGTVKVGDEVEIVGI--------KETQKTVVTGVEmfRKLLDEGQAGDNVGV 277
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
395-482 |
3.06e-26 |
|
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: 102.24 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 395 EKLEPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQP 474
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
....*...
gi 489055622 475 YKGEIAGR 482
Cdd:pfam00679 81 VPGDILDR 88
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
5-283 |
2.50e-25 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 109.14 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGEVE 84
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVA-INKIDRPDGRH--EEVVNEVFDLFANLDATDEqlDFPIL 161
Cdd:PLN03127 143 TGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEEllELVEMELRELLSFYKFPGD--EIPII 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 162 YGSGRNGWMALSPEGPKDQGLApLFDLVLKHVPAPK-VAEGPFRMigTILEADPFLGR--IITGRIHSGSIKPNQAVKVL 238
Cdd:PLN03127 221 RGSALSALQGTNDEIGKNAILK-LMDAVDEYIPEPVrVLDKPFLM--PIEDVFSIQGRgtVATGRVEQGTIKVGEEVEIV 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489055622 239 GQDGSVLENGRISKILAFRGIerqaIDEAHAGDIVA--IAGLSKGTV 283
Cdd:PLN03127 298 GLRPGGPLKTTVTGVEMFKKI----LDQGQAGDNVGllLRGLKREDV 340
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-146 |
7.93e-25 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 104.21 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAE--RMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGE 82
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055622 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLF 146
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
5-322 |
1.10e-24 |
|
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: 106.94 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGS-----FRENQRVAERM----------MDSNDIEKERGITILAKATSVVWKNTRIN 69
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAidehiIEKYEEEAEKKgkesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 70 IVDTPGHADFggeVERIL---SMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKP-IVAINKIDRPD---GRHEEVVNEV 142
Cdd:COG5256 89 IIDAPGHRDF---VKNMItgaSQADAAILVVSAKDGVMGQTREHAFLARTLGINQlIVAVNKMDAVNyseKRYEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 143 FDLFANLDATDEQLDF-PIlygSGRNG--WMALSPEGP--KDQGLAPLFDLVlkhVPAPKVAEGPFRM----IGTIlead 213
Cdd:COG5256 166 SKLLKMVGYKVDKIPFiPV---SAWKGdnVVKKSDNMPwyNGPTLLEALDNL---KEPEKPVDKPLRIpiqdVYSI---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 214 PFLGRIITGRIHSGSIKPNQAVKVL--GQDGSVlengriskilafRGIE--RQAIDEAHAGDIV--AIAGLSKGTVA--D 285
Cdd:COG5256 236 SGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEV------------KSIEmhHEELEQAEPGDNIgfNVRGVEKNDIKrgD 303
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489055622 286 tfcdpsvsepLAAQPIDPPTVTMSF----IVNDSPYAGTEG 322
Cdd:COG5256 304 ----------VAGHPDNPPTVAEEFtaqiVVLQHPSAITVG 334
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
5-275 |
2.83e-24 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 105.27 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITIlakATSVVWKNTRIN---IVDTPGHADFgg 81
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITI---NTAHVEYETEKRhyaHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 everILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLKPI-VAINKIDRPDgrHEE----VVNEVFDLFANLD 150
Cdd:PRK00049 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEEllelVEMEVRELLSKYD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 151 ATDEqlDFPILYGSGRngwMALspEGPKD----QGLAPLFDLVLKHVPAPKVA-EGPFRM----IGTIleadpfLGR--I 219
Cdd:PRK00049 163 FPGD--DTPIIRGSAL---KAL--EGDDDeeweKKILELMDAVDSYIPTPERAiDKPFLMpiedVFSI------SGRgtV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055622 220 ITGRIHSGSIKPNQAVKVLGQdgsvlengRISKILAFRGIE--RQAIDEAHAGDIVAI 275
Cdd:PRK00049 230 VTGRVERGIIKVGEEVEIVGI--------RDTQKTTVTGVEmfRKLLDEGQAGDNVGA 279
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
5-275 |
3.52e-24 |
|
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: 104.86 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGEVE 84
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVA-INKIDRPDGRH--EEVVNEVFDLFANLDATDEqlDFPIL 161
Cdd:TIGR00485 94 TGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELLSQYDFPGD--DTPII 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 162 YGSgrnGWMALSPEGPKDQGLAPLFDLVLKHVPAP-KVAEGPFRMigTILEADPFLGR--IITGRIHSGSIKPNQAVKVL 238
Cdd:TIGR00485 172 RGS---ALKALEGDAEWEAKILELMDAVDEYIPTPeREIDKPFLL--PIEDVFSITGRgtVVTGRVERGIIKVGEEVEIV 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 489055622 239 GQdgsvlengRISKILAFRGIE--RQAIDEAHAGDIVAI 275
Cdd:TIGR00485 247 GL--------KDTRKTTVTGVEmfRKELDEGRAGDNVGL 277
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
5-275 |
5.72e-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: 104.46 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITIlakATSVVWKNTRIN---IVDTPGHADFgg 81
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITI---NTSHVEYETEKRhyaHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 everILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLKPI-VAINKIDRPDgrHEEVVN----EVFDLFANLD 150
Cdd:COG0050 89 ----VKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCDMVD--DEELLElvemEVRELLSKYG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 151 ATDEqlDFPILYGSGRngwMALspEGPKD-QGLAPLFDL---VLKHVPAPK-VAEGPFRM----IGTIleadpfLGR--I 219
Cdd:COG0050 163 FPGD--DTPIIRGSAL---KAL--EGDPDpEWEKKILELmdaVDSYIPEPErDTDKPFLMpvedVFSI------TGRgtV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489055622 220 ITGRIHSGSIKPNQAVKVLGqdgsvLENGRISKIlafRGIE--RQAIDEAHAGDIVAI 275
Cdd:COG0050 230 VTGRVERGIIKVGDEVEIVG-----IRDTQKTVV---TGVEmfRKLLDEGEAGDNVGL 279
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
8-348 |
7.49e-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: 106.15 E-value: 7.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 8 IIA---HVDHGKTTLVDELlkqSGsfRENQRVAErmmdsndiEKERGITI--------LAkatsvvwKNTRINIVDTPGH 76
Cdd:COG3276 2 IIGtagHIDHGKTTLVKAL---TG--IDTDRLKE--------EKKRGITIdlgfaylpLP-------DGRRLGFVDVPGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 77 ADFggeverILSMVDGA----IVL--VDAAEGPMPQTK--FVVGKALKVGlKPIVAINKIDR-PDGRHEEVVNEVFDLFA 147
Cdd:COG3276 62 EKF------IKNMLAGAggidLVLlvVAADEGVMPQTRehLAILDLLGIK-RGIVVLTKADLvDEEWLELVEEEIRELLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 148 NL---DAtdeqldfPILYGSGRNGwmalspegpkdQGLAPLFDLVLKHVPA--PKVAEGPFRM----------IGTilea 212
Cdd:COG3276 135 GTfleDA-------PIVPVSAVTG-----------EGIDELRAALDALAAAvpARDADGPFRLpidrvfsikgFGT---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 213 dpflgrIITGRIHSGSIKPNQAVKVLGQDGSVlengRIskilafRGIERQ--AIDEAHAGDIVAI--AGLSKGTVA--DT 286
Cdd:COG3276 193 ------VVTGTLLSGTVRVGDELELLPSGKPV----RV------RGIQVHgqPVEEAYAGQRVALnlAGVEKEEIErgDV 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 287 FCDPsvseplaaqpiDPPTVTMSFIV-----NDSPYAGTEGDKV-----TSRVI-------RDRLLKEAEGNVALKIEE 348
Cdd:COG3276 257 LAAP-----------GALRPTDRIDVrlrllPSAPRPLKHWQRVhlhhgTAEVLarvvlldREELAPGEEALAQLRLEE 324
|
|
| tufA |
CHL00071 |
elongation factor Tu |
5-275 |
2.02e-23 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 103.11 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFggeve 84
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADY----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 rILSM------VDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVA-INKIDRPDgrHEEVVN----EVFDLFANLD-AT 152
Cdd:CHL00071 89 -VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVD--DEELLElvelEVRELLSKYDfPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 153 DeqlDFPILYGSGRNGWMALSpEGPK-DQGLAP-------LFDLVLKHVPAPKV-AEGPFRMigTILEADPFLGR--IIT 221
Cdd:CHL00071 166 D---DIPIVSGSALLALEALT-ENPKiKRGENKwvdkiynLMDAVDSYIPTPERdTDKPFLM--AIEDVFSITGRgtVAT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 222 GRIHSGSIKPNQAVKVLGqdgsvLENGRISKILafrGIE--RQAIDEAHAGDIVAI 275
Cdd:CHL00071 240 GRIERGTVKVGDTVEIVG-----LRETKTTTVT---GLEmfQKTLDEGLAGDNVGI 287
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
5-287 |
2.69e-23 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 102.70 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQ-----RVAERM----------MDSNDIEKERGITILAKATSVVWKNTRIN 69
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIieelrEEAKEKgkesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 70 IVDTPGHADFggeVERIL---SMVDGAIVLVDA--AEGPMPQTKFVVGKALKVGLKP-IVAINKIDRPD---GRHEEVVN 140
Cdd:PRK12317 88 IVDCPGHRDF---VKNMItgaSQADAAVLVVAAddAGGVMPQTREHVFLARTLGINQlIVAINKMDAVNydeKRYEEVKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 141 EVFDLFANLDATDEQLDF-PILYGSGRNgWMALSPEGP--KDQGLAPLFDLVlkhVPAPKVAEGPFRM----------IG 207
Cdd:PRK12317 165 EVSKLLKMVGYKPDDIPFiPVSAFEGDN-VVKKSENMPwyNGPTLLEALDNL---KPPEKPTDKPLRIpiqdvysisgVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 208 TileadpflgrIITGRIHSGSIKPNQAVKVL--GQDGSVlengriskilafRGIE--RQAIDEAHAGDIVAIA--GLSKG 281
Cdd:PRK12317 241 T----------VPVGRVETGVLKVGDKVVFMpaGVVGEV------------KSIEmhHEELPQAEPGDNIGFNvrGVGKK 298
|
330 340
....*....|....*....|.
gi 489055622 282 ---------------TVADTF 287
Cdd:PRK12317 299 dikrgdvcghpdnppTVAEEF 319
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
398-476 |
7.25e-23 |
|
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: 92.55 E-value: 7.25e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 398 EPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK 476
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
5-275 |
7.48e-23 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 102.00 E-value: 7.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFGGEVE 84
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVA-INKIDRPDGRH--EEVVNEVFDLFANLDATDEqlDFPIL 161
Cdd:PLN03126 163 TGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRELLSSYEFPGD--DIPII 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 162 YGSGRNGWMALSPEGPKDQG-------LAPLFDLVLKHVPAP-KVAEGPFRMIGTILEADPFLGRIITGRIHSGSIKPNQ 233
Cdd:PLN03126 241 SGSALLALEALMENPNIKRGdnkwvdkIYELMDAVDSYIPIPqRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGE 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489055622 234 AVKVLGQdgsvlengRISKILAFRGIE--RQAIDEAHAGDIVAI 275
Cdd:PLN03126 321 TVDIVGL--------RETRSTTVTGVEmfQKILDEALAGDNVGL 356
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
4-142 |
4.05e-22 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 100.21 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELL------KQSGSF--RENQRVAERmmDSNDIEKERGITIlakATSVV---WKNTRINIVD 72
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVkgRKSGRHATS--DWMEMEKQRGISV---TSSVMqfpYRDCLINLLD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 73 TPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKfvvgKALKV----GLkPIVA-INKIDRpDGRHE-EVVNEV 142
Cdd:PRK00741 86 TPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMEVcrlrDT-PIFTfINKLDR-DGREPlELLDEI 155
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
5-275 |
9.67e-22 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 97.60 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITIlakATSVVWKNTRIN---IVDTPGHADFgg 81
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITI---NTSHVEYETANRhyaHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 everILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLKPI-VAINKIDRPDGRH--EEVVNEVFDLFANLDAT 152
Cdd:PRK12735 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIvVFLNKCDMVDDEEllELVEMEVRELLSKYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 153 DEqlDFPILYGSGRngwMALspEGPKDQGLAP----LFDLVLKHVPAPKVA-EGPFRM----IGTIleadpfLGR--IIT 221
Cdd:PRK12735 165 GD--DTPIIRGSAL---KAL--EGDDDEEWEAkileLMDAVDSYIPEPERAiDKPFLMpiedVFSI------SGRgtVVT 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 222 GRIHSGSIKPNQAVKVLGqdgsvLENGRISKIlafRGIE--RQAIDEAHAGDIVAI 275
Cdd:PRK12735 232 GRVERGIVKVGDEVEIVG-----IKETQKTTV---TGVEmfRKLLDEGQAGDNVGV 279
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
6-138 |
1.01e-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: 89.45 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvaermmdSNDIEKE-RGITILAKATSVVW--KNTRINIVDTPGHADFGGE 82
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK-----------------TNVAAGEaGGITQHIGAYQVPIdvKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 83 VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEV 138
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEADP 121
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
1-275 |
1.32e-19 |
|
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: 91.69 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 1 MELRNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVA-ERM-----MDSND---------IEKERGITIlakatSVVWK- 64
Cdd:COG2895 15 KDLLRFITCGSVDDGKSTLIGRLLYDTKSIFEDQLAAlERDskkrgTQEIDlalltdglqAEREQGITI-----DVAYRy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 65 ---NTR--InIVDTPGHADFggevERilSMVDGA------IVLVDAAEGPMPQTK---FVVgkALkVGLKP-IVAINKID 129
Cdd:COG2895 90 fstPKRkfI-IADTPGHEQY----TR--NMVTGAstadlaILLIDARKGVLEQTRrhsYIA--SL-LGIRHvVVAVNKMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 130 RPD---GRHEEVVNEVFDLFANLDATDEQLdFPIlygSGRNGWMALSP-------EGPkdqglaPLFDLvLKHVPAPK-V 198
Cdd:COG2895 160 LVDyseEVFEEIVADYRAFAAKLGLEDITF-IPI---SALKGDNVVERsenmpwyDGP------TLLEH-LETVEVAEdR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 199 AEGPFRM-IGTILEADP-FlgRIITGRIHSGSIKPNQAVKVLGqdgsvleNGRISKIlafRGIER--QAIDEAHAGDIVA 274
Cdd:COG2895 229 NDAPFRFpVQYVNRPNLdF--RGYAGTIASGTVRVGDEVVVLP-------SGKTSTV---KSIVTfdGDLEEAFAGQSVT 296
|
.
gi 489055622 275 I 275
Cdd:COG2895 297 L 297
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
5-142 |
8.02e-19 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 85.62 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSF-----RENQRVAERM----------MDSNDIEKERGITILAKATSVVWKNTRIN 69
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVdkrtiEKYEKEAKEMgkesfkyawvLDKLKEERERGVTIDVGLAKFETEKYRFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 70 IVDTPGHADFggeverILSMVDG------AIVLVDAAEG-------PMPQTK--FVVGKALKVGlKPIVAINKIDRPD-- 132
Cdd:cd01883 81 IIDAPGHRDF------VKNMITGasqadvAVLVVSARKGefeagfeKGGQTRehALLARTLGVK-QLIVAVNKMDDVTvn 153
|
170
....*....|...
gi 489055622 133 ---GRHEEVVNEV 142
Cdd:cd01883 154 wsqERYDEIKKKV 166
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
5-196 |
5.91e-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: 82.25 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSNDIEKERGITILAKATSVVWKNTRINIVDTPGHADFggeve 84
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 rILSMV------DGAIVLVDAAEGPMPQTKFVVGKALKVGLKPI-VAINKIDRPDgrHEEVVN----EVFDLfanLDATD 153
Cdd:cd01884 79 -IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVPYIvVFLNKADMVD--DEELLElvemEVREL---LSKYG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489055622 154 EQLD-FPILYGSgrnGWMALspEGPKD----QGLAPLFDLVLKHVPAP 196
Cdd:cd01884 153 FDGDdTPIVRGS---ALKAL--EGDDPnkwvDKILELLDALDSYIPTP 195
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
4-144 |
1.16e-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: 80.49 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 4 RNIAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERmMDSNDIEKERGITIlakatsvvwkntRINIVDTPGHADF---- 79
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTY------------KFNLLDTAGQEDYdair 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055622 80 ---GGEVERILSMVDGAIVLVDAAEGPMPQTKfVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFD 144
Cdd:TIGR00231 69 rlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDLKDADLKTHVASEFA 135
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
5-276 |
2.24e-17 |
|
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: 85.70 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSgsfrenqrvAERMMDsndiEKERGITILAKATSVVWKNTRINIVDTPGHADFGGEVE 84
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIA---------ADRLPE----EKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKP-IVAINKIDRPD----GRHEEVVNEVFDLFANLDATDEqldFP 159
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVNeeeiKRTEMFMKQILNSYIFLKNAKI---FK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 160 ILYGSGRnGWMALSPEGPKdqgLAPLFDLVLKHVPAPKVAEGPFRMIGTileadpflGRIITGRIHSGSIKPNQAVKVLG 239
Cdd:TIGR00475 146 TSAKTGQ-GIGELKKELKN---LLESLDIKRIQKPLRMAIDRAFKVKGA--------GTVVTGTAFSGEVKVGDNLRLLP 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 489055622 240 QDGSVlengRISKILAFrgieRQAIDEAHAGDIVAIA 276
Cdd:TIGR00475 214 INHEV----RVKAIQAQ----NQDVEIAYAGQRIALN 242
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
6-287 |
2.49e-16 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 82.57 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvaermmdSNDIEKERG-ITILAKATSVVWK----NTRINIVDTPGHADFG 80
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGgITQKIGAYEVEFEykdeNQKIVFLDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 81 GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVfdLFANLDATDEQLDFPI 160
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQL--AKYNLIPEKWGGDTPM 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 161 LYGSGRNGwmalspegpkdQGLAPLFDLV--------LKHVPAPKVAegpfrmiGTILEA--DPFLGRIITGRIHSGSIK 230
Cdd:CHL00189 388 IPISASQG-----------TNIDKLLETIlllaeiedLKADPTQLAQ-------GIILEAhlDKTKGPVATILVQNGTLH 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055622 231 PNQAVkVLGQdgsvlENGRISKILAFRGierQAIDEAHAGDIVAIAGLSK----GTVADTF 287
Cdd:CHL00189 450 IGDII-VIGT-----SYAKIRGMINSLG---NKINLATPSSVVEIWGLSSvpatGEHFQVF 501
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
11-168 |
1.83e-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: 74.56 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 11 HVDHGKTTLVDELlkqSGsfRENQRVAErmmdsndiEKERGITI-LAKATSVVWKNTRINIVDTPGHADFggeverILSM 89
Cdd:cd04171 7 HIDHGKTTLIKAL---TG--IETDRLPE--------EKKRGITIdLGFAYLDLPDGKRLGFIDVPGHEKF------VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 90 V------DGAIVLVDAAEGPMPQTK--FVVGKALKVGlKPIVAINKIDRPD-GRHEEVVNEVFDLFANLDATDEqldfPI 160
Cdd:cd04171 68 LagaggiDAVLLVVAADEGIMPQTRehLEILELLGIK-KGLVVLTKADLVDeDRLELVEEEILELLAGTFLADA----PI 142
|
....*...
gi 489055622 161 LYGSGRNG 168
Cdd:cd04171 143 FPVSSVTG 150
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
5-301 |
1.28e-14 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 76.32 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVAER-----------------MMDSNDIEKERGITIlakaTSVVWK--- 64
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGI--DKRTIEKfekeaaemgkgsfkyawVLDKLKAERERGITI----DIALWKfet 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 65 -NTRINIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMP-------QTKFVVGKALKVGLKP-IVAINKIDRP---- 131
Cdd:PTZ00141 83 pKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQmIVCINKMDDKtvny 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 132 -DGRHEEVVNEVFDLFANLDATDEQLDF-PIlygSGRNG--WMALSPEGP--KDQGLAPLFDLVlkhVPAPKVAEGPFRM 205
Cdd:PTZ00141 163 sQERYDEIKKEVSAYLKKVGYNPEKVPFiPI---SGWQGdnMIEKSDNMPwyKGPTLLEALDTL---EPPKRPVDKPLRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 206 -------IGTIleadpflGRIITGRIHSGSIKPnqavkvlgqdGSVLENGRISKILAFRGIE--RQAIDEAHAGDIV--- 273
Cdd:PTZ00141 237 plqdvykIGGI-------GTVPVGRVETGILKP----------GMVVTFAPSGVTTEVKSVEmhHEQLAEAVPGDNVgfn 299
|
330 340 350
....*....|....*....|....*....|....
gi 489055622 274 ----AIAGLSKGTVA-DTFCDPSV-SEPLAAQPI 301
Cdd:PTZ00141 300 vknvSVKDIKRGYVAsDSKNDPAKeCADFTAQVI 333
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
210-289 |
6.82e-14 |
|
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: 67.16 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 210 LEADPFLGRIITGRIHSGSIKPNQAVKVLGQDGSVlengRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFCD 289
Cdd:cd04088 8 TMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKE----RVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
5-154 |
1.03e-13 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 70.29 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFRENQRVA-ER---------------MMDSNDIEKERGITI-LAK---ATSvvwK 64
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEDQLAAlERskssgtqgekldlalLVDGLQAEREQGITIdVAYryfSTP---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 65 NTRInIVDTPGHADFggeverILSMVDGA------IVLVDAAEGPMPQTK---FVVgkALkVGLKPIV-AINKIDRPD-- 132
Cdd:cd04166 78 RKFI-IADTPGHEQY------TRNMVTGAstadlaILLVDARKGVLEQTRrhsYIA--SL-LGIRHVVvAVNKMDLVDyd 147
|
170 180
....*....|....*....|...
gi 489055622 133 -GRHEEVVNEVFDLFANLDATDE 154
Cdd:cd04166 148 eEVFEEIKADYLAFAASLGIEDI 170
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
6-279 |
1.49e-13 |
|
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: 73.65 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELlkqsgsfrENQRVAERmmdsndieKERGITILAKATSVVWKNTR-INIVDTPGHADFGGEVE 84
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSI--------RKTKVAQG--------EAGGITQHIGAYHVENEDGKmITFLDTPGHEAFTSMRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 85 RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLfaNLDATDEQLDFPILYGS 164
Cdd:TIGR00487 154 RGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEY--GLVPEDWGGDTIFVPVS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 165 GRNGwmalspegpkdQGLAPLFDLVLKHVPAPKVAEGPFRM-IGTILEADPFLGR--IITGRIHSGSIKPNQAVkVLGQd 241
Cdd:TIGR00487 232 ALTG-----------DGIDELLDMILLQSEVEELKANPNGQaSGVVIEAQLDKGRgpVATVLVQSGTLRVGDIV-VVGA- 298
|
250 260 270
....*....|....*....|....*....|....*...
gi 489055622 242 gsvlENGRISKILAFRGierQAIDEAHAGDIVAIAGLS 279
Cdd:TIGR00487 299 ----AYGRVRAMIDENG---KSVKEAGPSKPVEILGLS 329
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
5-129 |
2.81e-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: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELlkqsgsfRENQRVAErmMDSNDIEKERGITI--------------LAKATSVVWKNTRINI 70
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL-------SEIASTAA--FDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055622 71 VDTPGHADFggeVERILS---MVDGAIVLVDAAEGPMPQTK--FVVGKALKVglKPIVAINKID 129
Cdd:cd01889 73 VDCPGHASL---IRTIIGgaqIIDLMLLVVDAKKGIQTQTAecLVIGELLCK--PLIVVLNKID 131
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
217-288 |
3.52e-12 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 61.90 E-value: 3.52e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055622 217 GRIITGRIHSGSIKPNQAVKVLGQD-GSVLENGRISKILAFRGIERQAIDEAHAGDIVAIAGLSKGTVADTFC 288
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
6-141 |
4.40e-12 |
|
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: 68.50 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKqsgsfrenqrvaermmdSNDIEKE-RGIT--IlaKATSVVWKNTRINIVDTPGHADF--- 79
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAIRK-----------------TNVAAGEaGGITqhI--GAYQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 80 ---GGEVERIlsmvdgaIVLVDAA-EGPMPQTKFVVG--KALKVglkPI-VAINKIDRPDGRHEEVVNE 141
Cdd:COG0532 68 rarGAQVTDI-------VILVVAAdDGVMPQTIEAINhaKAAGV---PIiVAINKIDKPGANPDRVKQE 126
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
5-129 |
5.02e-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: 65.07 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaermMDSNDIEKERGITI-LAKATSVVWKNT----------------- 66
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVW----------TDTHSEELKRGISIrLGYADAEIYKCPecdgpecyttepvcpnc 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055622 67 --------RINIVDTPGHADFggeVERILS---MVDGAIVLVDAAEG-PMPQTKFVVgKALK-VGLKPIV-AINKID 129
Cdd:TIGR03680 73 gsetellrRVSFVDAPGHETL---MATMLSgaaLMDGALLVIAANEPcPQPQTKEHL-MALEiIGIKNIViVQNKID 145
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
7-191 |
8.40e-11 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 60.93 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 7 AIIAHVDHGKTTLVDELLKQSGSFRENqrvaermmdsndiekERGITILAKATSVVW--KNTRINIVDTPGHADFGG--- 81
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSD---------------VPGTTRDPDVYVKELdkGKVKLVLVDTPGLDEFGGlgr 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 --EVERILSMVDGAIVLVDAAEGPMP--QTKFVVGKALKVGLKPIVAINKIDRPDGRHEEVVNEVFDLFANldatdeqLD 157
Cdd:cd00882 66 eeLARLLLRGADLILLVVDSTDRESEedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKI-------LG 138
|
170 180 190
....*....|....*....|....*....|....
gi 489055622 158 FPILYGSGRNGWmalspegpkdqGLAPLFDLVLK 191
Cdd:cd00882 139 VPVFEVSAKTGE-----------GVDELFEKLIE 161
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
5-291 |
1.17e-10 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 63.96 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKQSGSFreNQRVAER-----------------MMDSNDIEKERGITI---LAKATSVVWK 64
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGGI--DKRVIERfekeaaemnkrsfkyawVLDKLKAERERGITIdiaLWKFETTKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 65 NTrinIVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMP-------QTKFVVGKALKVGLKPIV-AINKIDR-----P 131
Cdd:PLN00043 87 CT---VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpkyS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 132 DGRHEEVVNEVFDLFANLDATDEQLDF-PIlygSGRNGWMALSPEGPKDQGLAPLFDLVLKHVPAPK-VAEGPFRMIGTI 209
Cdd:PLN00043 164 KARYDEIVKEVSSYLKKVGYNPDKIPFvPI---SGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKrPSDKPLRLPLQD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 210 LEADPFLGRIITGRIHSGSIKPNQAVkvlgqdgSVLENGRISKILAFRgIERQAIDEAHAGD-------IVAIAGLSKGT 282
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVV-------TFGPTGLTTEVKSVE-MHHESLQEALPGDnvgfnvkNVAVKDLKRGY 312
|
330
....*....|
gi 489055622 283 VA-DTFCDPS 291
Cdd:PLN00043 313 VAsNSKDDPA 322
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
5-129 |
3.48e-10 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 62.18 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaermMDSNDIEKERGITI-LAKATSVVWKNT----------------- 66
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVW----------TDRHSEELKRGITIrLGYADATIRKCPdceepeayttepkcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 67 --------RINIVDTPGHadfggEV--ERILS---MVDGAIVLVDAAEG-PMPQTK--FVvgkALK-VGLKPIV-AINKI 128
Cdd:PRK04000 78 gsetellrRVSFVDAPGH-----ETlmATMLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALDiIGIKNIViVQNKI 149
|
.
gi 489055622 129 D 129
Cdd:PRK04000 150 D 150
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
6-130 |
1.11e-09 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 61.35 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKQSGSFRE----NQRVAERMMDSNDIEKERGitilakatsVVWKNTRINI-------VDTP 74
Cdd:PRK04004 9 VVVLGHVDHGKTTLLDKIRGTAVAAKEaggiTQHIGATEVPIDVIEKIAG---------PLKKPLPIKLkipgllfIDTP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055622 75 GHADF------GGeverilSMVDGAIVLVDAAEGPMPQTKfvvgKALKVgLK----P-IVAINKIDR 130
Cdd:PRK04004 80 GHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTI----EAINI-LKrrktPfVVAANKIDR 135
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
5-129 |
1.43e-09 |
|
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: 58.05 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaermMDSNDIEKERGITI-LAKATSVVWKNT----------------- 66
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVW----------TVRHKEELKRNITIkLGYANAKIYKCPncgcprpydtpececpg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 67 ---------RINIVDTPGHadfggeveRIL--------SMVDGAIVLVDAAEG-PMPQTK--FVvgkALKV-GLKPIV-A 124
Cdd:cd01888 69 cggetklvrHVSFVDCPGH--------EILmatmlsgaAVMDGALLLIAANEPcPQPQTSehLA---ALEImGLKHIIiL 137
|
....*
gi 489055622 125 INKID 129
Cdd:cd01888 138 QNKID 142
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
6-133 |
1.60e-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: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKQSGSFRENQRVAERMMDSndiekERGITILAKATSVVWKNTRINI-------VDTPGHAD 78
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLLKSFKIKLkipgllfIDTPGHEA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 79 FGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVgKALKVGLKP-IVAINKIDRPDG 133
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEAL-NILRSRKTPfVVAANKIDRIPG 136
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
12-310 |
3.42e-09 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 59.56 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 12 VDHGKTTLVDELLKQSGSFRENQRVA-ER----------------MMDSNDIEKERGITI-LAK---ATSvvwKNTRInI 70
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKMIFEDQLAAlERdskkvgtqgdeidlalLVDGLAAEREQGITIdVAYryfATP---KRKFI-V 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 71 VDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTK---FVVgkALkVGLKPIV-AINKIDRPD---GRHEEVVNEVF 143
Cdd:PRK05506 109 ADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRrhsFIA--SL-LGIRHVVlAVNKMDLVDydqEVFDEIVADYR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 144 DLFANLDATDEQLdFPIlygSGRNG--WMALSPEGPKDQGlAPLFDLvLKHVP-APKVAEGPFRMigtileadP------ 214
Cdd:PRK05506 186 AFAAKLGLHDVTF-IPI---SALKGdnVVTRSARMPWYEG-PSLLEH-LETVEiASDRNLKDFRF--------Pvqyvnr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 215 ----FLGriITGRIHSGSIKPNQAVKVL--GQdgsvleNGRISKILAFRGierqAIDEAHAGDIVAIaglskgTVADTFc 288
Cdd:PRK05506 252 pnldFRG--FAGTVASGVVRPGDEVVVLpsGK------TSRVKRIVTPDG----DLDEAFAGQAVTL------TLADEI- 312
|
330 340
....*....|....*....|..
gi 489055622 289 DPSVSEPLAAqPIDPPTVTMSF 310
Cdd:PRK05506 313 DISRGDMLAR-ADNRPEVADQF 333
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
304-382 |
5.84e-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: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 304 PTVTMSFIVNDSpyagtegdkVTSRVIRDRLLKEAEGNVALKIEESTEKDSFFVSGRGELQLAVLIENMRRE-GFELGVS 382
Cdd:cd16257 1 PVVFVTVEVKNP---------LDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
6-277 |
2.46e-08 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 56.98 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVdellkQSGSFRENQRVAErmmdsndiEKERGITI-LAKAtsvVWKNTR---INIVDTPGHADFgg 81
Cdd:PRK10512 3 IATAGHVDHGKTTLL-----QAITGVNADRLPE--------EKKRGMTIdLGYA---YWPQPDgrvLGFIDVPGHEKF-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 82 eVERILSMVDG---AIVLVDAAEGPMPQTKFVVGkALKVGLKP--IVAINKIDRPD-GRHEEVVNEVFDLFANLDATDEQ 155
Cdd:PRK10512 65 -LSNMLAGVGGidhALLVVACDDGVMAQTREHLA-ILQLTGNPmlTVALTKADRVDeARIAEVRRQVKAVLREYGFAEAK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 156 LdFPILYGSGRngwmalspegpkdqGLAPLFDLVLKHVPAPKVAEGPFRM----IGTILEAdpflGRIITGRIHSGSIKP 231
Cdd:PRK10512 143 L-FVTAATEGR--------------GIDALREHLLQLPEREHAAQHRFRLaidrAFTVKGA----GLVVTGTALSGEVKV 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489055622 232 NQAVKVLGQDGSVlengRIskilafRGI--ERQAIDEAHAGDIVA--IAG 277
Cdd:PRK10512 204 GDTLWLTGVNKPM----RV------RGLhaQNQPTEQAQAGQRIAlnIAG 243
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
5-129 |
5.31e-08 |
|
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: 55.23 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELlkqSGSFrenqrvaermMDSNDIEKERGITI-LAKATSVVWKNT----------------- 66
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVW----------TDRHSEELKRGITIrLGYADATFYKCPnceppeayttepkcpnc 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 67 --------RINIVDTPGHadfggEV--ERILS---MVDGAIVLVDAAEG-PMPQTK--FVvgkALK-VGLKPIVAI-NKI 128
Cdd:COG5257 74 gsetellrRVSFVDAPGH-----ETlmATMLSgaaLMDGAILVIAANEPcPQPQTKehLM---ALDiIGIKNIVIVqNKI 145
|
.
gi 489055622 129 D 129
Cdd:COG5257 146 D 146
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
6-191 |
9.29e-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: 52.05 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKQsgsfrenqrvaERMMDSNdiekERGITILAKATSVVWKNTRINIVDTPG-----HADFG 80
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 81 GE------VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINK---IDRPDGRHEEVVNEVFDLFAnlda 151
Cdd:cd01895 70 IEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRKLP---- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489055622 152 tdeQLDF-PILYGSGRNGwmalspegpkdQGLAPLFDLVLK 191
Cdd:cd01895 146 ---FLDYaPIVFISALTG-----------QGVDKLFDAIKE 172
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
213-283 |
2.92e-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: 48.41 E-value: 2.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055622 213 DPFLGRIITGRIHSGSIKPNQAVKVLGqdgsVLENGRISKILAFrgieRQAIDEAHAGDIVAIAGLSKGTV 283
Cdd:cd01342 11 IPGRGRVAGGRVESGTLKVGDEIRILP----KGITGRVTSIERF----HEEVDEAKAGDIVGIGILGVKDI 73
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
12-309 |
3.47e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 52.99 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 12 VDHGKTTLVDELLKQSGSFRENQ-----RVAERM------------MDSNDIEKERGITIlakatSVVWK----NTRINI 70
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIYEDQlaslhNDSKRHgtqgekldlallVDGLQAEREQGITI-----DVAYRyfstEKRKFI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 71 V-DTPGHADF------GGeverilSMVDGAIVLVDAAEGPMPQTK---FVvgkALKVGLKP-IVAINKIDRPD---GRHE 136
Cdd:PRK05124 111 IaDTPGHEQYtrnmatGA------STCDLAILLIDARKGVLDQTRrhsFI---ATLLGIKHlVVAVNKMDLVDyseEVFE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 137 EVVNEVFDLFANLDaTDEQLDF-PI--LYG------SGRNGWMalspEGPkdqglaPLFDlVLKHVPAPKVAE-GPFRMi 206
Cdd:PRK05124 182 RIREDYLTFAEQLP-GNLDIRFvPLsaLEGdnvvsqSESMPWY----SGP------TLLE-VLETVDIQRVVDaQPFRF- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 207 gtileadP----------FLGriITGRIHSGSIKPNQAVKVL--GQDGSVlengriSKILAFRGIerqaIDEAHAGDIVA 274
Cdd:PRK05124 249 -------PvqyvnrpnldFRG--YAGTLASGVVKVGDRVKVLpsGKESNV------ARIVTFDGD----LEEAFAGEAIT 309
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489055622 275 IA-----GLSKGtvaDTFCDPSvSEPLAAQPIDPPTVTMS 309
Cdd:PRK05124 310 LVledeiDISRG---DLLVAAD-EALQAVQHASADVVWMA 345
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
398-474 |
6.47e-07 |
|
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: 47.14 E-value: 6.47e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055622 398 EPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVrLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQP 474
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGWKV-IKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
5-127 |
8.32e-07 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 48.00 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLKqsgsfrENQRVAERMmdsndiekerGITILAKATSVVWKNTRINIVDTPG----HADFG 80
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTG------AKAIVSDYP----------GTTRDPNEGRLELKGKQIILVDTPGliegASEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489055622 81 GEVERILSM--VDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINK 127
Cdd:pfam01926 65 GLGRAFLAIieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
6-191 |
1.85e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 50.43 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 6 IAIIAHVDHGKTTLVDELLKQsgsfrenqrvaERMMDSNdiekERGITILAKATSVVWKNTRINIVDTPG-------HAD 78
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 79 fggeVE--------RILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKID-RPDGRHEEVVNEVFDLFANL 149
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDlVDEKTMEEFKKELRRRLPFL 316
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489055622 150 DatdeqlDFPILYGSGRNGwmalspegpkdQGLAPLFDLVLK 191
Cdd:PRK00093 317 D------YAPIVFISALTG-----------QGVDKLLEAIDE 341
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
205-278 |
1.13e-05 |
|
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: 44.13 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 205 MIGTILEADPFLGRIITGRIHSGSIKPNQAVKVLGQD-----GSVLENGRISKILAFRGIERQAIDEAHAGDIVAIAGL 278
Cdd:cd16268 5 YVSKMVPTDKGAGFVAFGRVFSGTVRRGQEVYILGPKyvpgkKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGL 83
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
15-137 |
1.55e-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: 45.31 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 15 GKTTLVDELLkqsgsfreNQRVAErmmdsndIEKERGITILAKATSVVWKNTR-INIVDTPGHADFGGE----VERILSM 89
Cdd:cd00880 9 GKSSLLNALL--------GQNVGI-------VSPIPGTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGLgrerVEEARQV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489055622 90 ---VDGAIVLVDAAEGPMPQtKFVVGKALKVGLKPIVAINKIDRPDGRHEE 137
Cdd:cd00880 74 adrADLVLLVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEE 123
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
398-476 |
8.52e-05 |
|
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: 41.07 E-value: 8.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055622 398 EPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRpSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQPYK 476
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQ-IKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
|
|
| EF2_II_snRNP |
cd04090 |
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ... |
222-280 |
1.34e-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: 1.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055622 222 GRIHSGSIKPNQAVKVLG--------QDGSVLEngrISKILAFRGIERQAIDEAHAGDIVAIAGLSK 280
Cdd:cd04090 21 GRIYSGTLRKGQKVKVLGenysledeEDMTVCT---VGRLWILGARYKYEVNSAPAGNWVLIKGIDQ 84
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-132 |
1.53e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 42.66 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 1 MELRNIAIIAHVDHGKTTLVDELLkqsgsfreNQRVAERMMDSndiekERGITILAKATSVVWKNTRINIVDTPGHADF- 79
Cdd:COG1100 1 MGEKKIVVVGTGGVGKTSLVNRLV--------GDIFSLEKYLS-----TNGVTIDKKELKLDGLDVDLVIWDTPGQDEFr 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055622 80 --GGEVERILSMVDGAIVLVDAAegpMPQT----KFVVGKALKVGLKP--IVAINKIDRPD 132
Cdd:COG1100 68 etRQFYARQLTGASLYLFVVDGT---REETlqslYELLESLRRLGKKSpiILVLNKIDLYD 125
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
398-474 |
1.55e-04 |
|
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: 40.55 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 398 EPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRPSGGNRVRLVFYAPTrgligyqSELLTD--------TRGTAIMNRLF 469
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPL-------AEIVYDffdklksiSKGYASLDYEL 73
|
....*
gi 489055622 470 HDYQP 474
Cdd:cd03709 74 IGYRE 78
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
71-203 |
2.12e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 43.44 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 71 VDTPG-----HAdFG----GEVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRpdgrheeVVNE 141
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL-------VKKE 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055622 142 vfDLFANLDATDEQLDF----PIlygSGRNGwmalspegpkdQGLAPLFDLVLKHVPapkvaEGPF 203
Cdd:COG1159 128 --ELLPLLAEYSELLDFaeivPI---SALKG-----------DNVDELLDEIAKLLP-----EGPP 172
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
210-289 |
4.46e-04 |
|
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: 39.19 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 210 LEADPFlGRIITGRIHSGSIKPNQAVKVLGQDGSVlengRISKILAFRGIERQAIDEAHAGDIVAIAGLsKGTVADTFCD 289
Cdd:cd04091 8 LEEGRF-GQLTYMRVYQGVLRKGDTIYNVRTGKKV----RVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFTD 81
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
71-203 |
6.34e-04 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 41.96 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 71 VDTPG-HADfggevERIL--SMVDGA----------IVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRpdgrhee 137
Cdd:PRK00089 58 VDTPGiHKP-----KRALnrAMNKAAwsslkdvdlvLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL------- 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 138 vVNEVFDLFANLDATDEQLDF----PIlygSgrngwmALspegpKDQGLAPLFDLVLKHVPapkvaEGPF 203
Cdd:PRK00089 126 -VKDKEELLPLLEELSELMDFaeivPI---S------AL-----KGDNVDELLDVIAKYLP-----EGPP 175
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
63-136 |
8.24e-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: 40.11 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 63 WKNTRINIVDTPGHADFGGE--------VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDRPDGR 134
Cdd:cd01894 42 WGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEE 121
|
..
gi 489055622 135 HE 136
Cdd:cd01894 122 EE 123
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
70-133 |
1.61e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.79 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055622 70 IVDTPGHADFGGEVERILSMVDGAIVLVDAAEGPMPQTKFVVgKALKVGLKP-IVAINKIDRPDG 133
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAI-NILRQYKTPfVVAANKIDLIPG 593
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
61-200 |
1.77e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.16 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 61 VVWKNTRINIVDTPG-----HADFGGE----VERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGlKP-IVAINKIDR 130
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILVVNKVDG 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055622 131 PDgrHEEVVNEVFDL-FANLdatdeqldFPIlygSGRNGwmalspegpkdQGLAPLFDLVLKHVPAPKVAE 200
Cdd:COG1160 124 PK--READAAEFYSLgLGEP--------IPI---SAEHG-----------RGVGDLLDAVLELLPEEEEEE 170
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
64-130 |
1.99e-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: 39.37 E-value: 1.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055622 64 KNTRINIVDTPG-HADFGG-------EVERILSMVDGAIVLVDAAEGPMPQTKFVVGKALKVGLKPIVAINKIDR 130
Cdd:cd04163 49 DDAQIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL 123
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
5-129 |
4.52e-03 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 39.99 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 5 NIAIIAHVDHGKTTLVDELLK-QSGSFREnqrvaermmdsndiEKERGITI-LAKATSVVWK------------------ 64
Cdd:PTZ00327 36 NIGTIGHVAHGKSTVVKALSGvKTVRFKR--------------EKVRNITIkLGYANAKIYKcpkcprptcyqsygsskp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055622 65 -NTR-------------INIVDTPGHaDF-------GGEVerilsmVDGAIVLVDAAEG-PMPQTKFVVGKALKVGLKPI 122
Cdd:PTZ00327 102 dNPPcpgcghkmtlkrhVSFVDCPGH-DIlmatmlnGAAV------MDAALLLIAANEScPQPQTSEHLAAVEIMKLKHI 174
|
....*...
gi 489055622 123 VAI-NKID 129
Cdd:PTZ00327 175 IILqNKID 182
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
397-474 |
7.61e-03 |
|
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: 197906 [Multi-domain] Cd Length: 85 Bit Score: 35.94 E-value: 7.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055622 397 LEPVEEVVIDVDEEYSGTVVQKMSERKAEMVELRpSGGNRVRLVFYAPTRGLIGYQSELLTDTRGTAIMNRLFHDYQP 474
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGME-QRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| |
