|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
1-615 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1178.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 1 MSIENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDKKtgiknrINIV 80
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVK------INIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 81 DTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQVFDLFDKLGA 160
Cdd:COG1217 75 DTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 161 TNEQLDFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIGIGRIQRGTLKK 240
Cdd:COG1217 155 TDEQLDFPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 241 NMQVAVIDREGKKRNGKVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDTPEALPALTVDEPTISMTFQV 320
Cdd:COG1217 235 GQQVALIKRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 321 NNSPFAGnKDlsgGKFLTSRQIKDRLDREKVHNVALKVEQLEDADKFLVSGRGELHLSVLIENMRREGYELAVSRPEVII 400
Cdd:COG1217 315 NDSPFAG-RE---GKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 401 KEIDGQMMEPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVF 480
Cdd:COG1217 391 KEIDGKKLEPIEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 481 DHYGPKeQGAIAKRINGVMIANAPGTTPAYSLGPLQERGKLFAAEGDNVYEGQLVGIHSKDNDLTVNAIKTKPLTNMRAS 560
Cdd:COG1217 471 DGYEPY-KGEIPGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRAS 549
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 692318981 561 GKDDAIQLTPAIKYSLEQALDFIEDDELVEITPKEIRLRKKFLTESDRKKASRGG 615
Cdd:COG1217 550 GSDEAIRLTPPRKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKK 604
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
6-610 |
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: 989.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 6 LRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDkktgikNRINIVDTPGH 85
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNG------TKINIVDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 86 ADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQVFDLFDKLGATNEQL 165
Cdd:TIGR01394 75 ADFGGEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 166 DFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVA 245
Cdd:TIGR01394 155 DFPIVYASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 246 VIDREGKKRNGKVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDTPEALPALTVDEPTISMTFQVNNSPF 325
Cdd:TIGR01394 235 LMKRDGTIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 326 AGnkdlSGGKFLTSRQIKDRLDREKVHNVALKVEQLEDADKFLVSGRGELHLSVLIENMRREGYELAVSRPEVIIKEIDG 405
Cdd:TIGR01394 315 AG----KEGKKVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 406 QMMEPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:TIGR01394 391 KKLEPIEELTIDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 486 kEQGAIAKRINGVMIANAPGTTPAYSLGPLQERGKLFAAEGDNVYEGQLVGIHSKDNDLTVNAIKTKPLTNMRASGKDDA 565
Cdd:TIGR01394 471 -WKGEIETRRNGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEA 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 692318981 566 IQLTPAIKYSLEQALDFIEDDELVEITPKEIRLRKKFLTESDRKK 610
Cdd:TIGR01394 550 VKLTPPRKLSLEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
3-615 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 839.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 3 IENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDKktgiknRINIVDT 82
Cdd:PRK10218 2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDY------RINIVDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 83 PGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQVFDLFDKLGATN 162
Cdd:PRK10218 76 PGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 163 EQLDFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIGIGRIQRGTLKKNM 242
Cdd:PRK10218 156 EQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 243 QVAVIDREGKKRNGKVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDTPEALPALTVDEPTISMTFQVNN 322
Cdd:PRK10218 236 QVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 323 SPFAGNKdlsgGKFLTSRQIKDRLDREKVHNVALKVEQLEDADKFLVSGRGELHLSVLIENMRREGYELAVSRPEVIIKE 402
Cdd:PRK10218 316 SPFCGKE----GKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 403 IDGQMMEPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDH 482
Cdd:PRK10218 392 IDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSH 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 483 YGPKEQGAIAKRINGVMIANAPGTTPAYSLGPLQERGKLFAAEGDNVYEGQLVGIHSKDNDLTVNAIKTKPLTNMRASGK 562
Cdd:PRK10218 472 YDDVRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGT 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 692318981 563 DDAIQLTPAIKYSLEQALDFIEDDELVEITPKEIRLRKKFLTESDRKKASRGG 615
Cdd:PRK10218 552 DEAVVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAP 604
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
5-204 |
2.71e-121 |
|
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: 356.90 E-value: 2.71e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 5 NLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDKKtgiknrINIVDTPG 84
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTK------INIIDTPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 85 HADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQVFDLFDKLGATNEQ 164
Cdd:cd01891 75 HADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 692318981 165 LDFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRP 204
Cdd:cd01891 155 LDFPIVYASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
4-202 |
1.11e-66 |
|
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: 215.85 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 4 ENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLA---ERVMDSNDQEKERGITILAKNTAITWEDKktgiknRINIV 80
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDY------LINLI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 81 DTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRP-GARPEWVIDQVFDLFDKLG 159
Cdd:pfam00009 75 DTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEVSRELLEKY 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 692318981 160 ATNEqLDFPIVYASGLNGYAgledtvrdgdMTPLYEAIMQHAP 202
Cdd:pfam00009 155 GEDG-EFVPVVPGSALKGEG----------VQTLLDALDEYLP 186
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-412 |
4.90e-62 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 218.58 E-value: 4.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 3 IENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDKktGIKNRINIVDT 82
Cdd:PRK07560 17 PEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMVHEYE--GKEYLINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 83 PGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDR--------P---GARPEWVIDQV 151
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPqemQQRLLKIIKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 152 FDLFD-----------KLGATNEQLDF-----------PIVYASGLNgYAGLEDTVRDGDM------TPLYEAIM----Q 199
Cdd:PRK07560 175 NKLIKgmapeefkekwKVDVEDGTVAFgsalynwaisvPMMQKTGIK-FKDIIDYYEKGKQkelaekAPLHEVVLdmvvK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 200 HAPRP-------------------------EVDPEGPFQMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVAVIDREGKKR 254
Cdd:PRK07560 254 HLPNPieaqkyripkiwkgdlnsevgkamlNCDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 255 ngkVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDTPEALPALT-VDEPTISMTFQVNNSpfagnKDLSg 333
Cdd:PRK07560 334 ---VQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVVSVEDMTPFESLKhISEPVVTVAIEAKNP-----KDLP- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 334 gKFL-TSRQikdrLDREkvhNVALKVEQLEDADKFLVSGRGELHLSVLIENMRRE-GYELAVSRPEVIIKEIDGQMMEPI 411
Cdd:PRK07560 405 -KLIeVLRQ----LAKE---DPTLVVKINEETGEHLLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGKSQVV 476
|
.
gi 692318981 412 E 412
Cdd:PRK07560 477 E 477
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
4-450 |
7.94e-62 |
|
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: 217.84 E-value: 7.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 4 ENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDKktGIKNRINIVDTP 83
Cdd:TIGR00490 17 KFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMVHEYE--GNEYLINLIDTP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDR------------------------ 139
Cdd:TIGR00490 95 GHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRlinelkltpqelqerfikiitevn 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 140 ---PGARPE-----WVIDqVFDLFDKLGAT--NEQLDFPIVYASGLN-----GYAGlEDTVRD-GDMTPLYEAIM----Q 199
Cdd:TIGR00490 175 kliKAMAPEefrdkWKVR-VEDGSVAFGSAyyNWAISVPSMKKTGIGfkdiyKYCK-EDKQKElAKKSPLHQVVLdmviR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 200 HAPRP-------------------------EVDPEGPFQMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVAVIDREGKKR 254
Cdd:TIGR00490 253 HLPSPieaqkyripviwkgdlnsevgkamlNCDPKGPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKAR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 255 ngkVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDTP-EALPALT-VDEPTISMTFQVNNSpfagnKDLS 332
Cdd:TIGR00490 333 ---IQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETICTTVENiTPFESIKhISEPVVTVAIEAKNT-----KDLP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 333 ggKFLtsrQIKDRLDREkvhNVALKVEQLEDADKFLVSGRGELHLSVLIENMRRE-GYELAVSRPEVIIKEIDGQMMEPI 411
Cdd:TIGR00490 405 --KLI---EVLRQVAKE---DPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRETVTGTSPVV 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 692318981 412 E--------QLVVDIEEIHQgGVMEKLgtRKGQLKNMESDGKGRVRL 450
Cdd:TIGR00490 477 EgkspnkhnRFYIVVEPLEE-SVIQAF--KEGKIVDMKMKKKERRRL 520
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
1-472 |
2.53e-56 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 200.25 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 1 MSIENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTvLAERVMDSNDQEKERGITILAKNTAITWEDKKtGIKNRINIV 80
Cdd:COG0481 1 MDQKNIRNFSIIAHIDHGKSTLADRLLELTGTLSERE-MKEQVLDSMDLERERGITIKAQAVRLNYKAKD-GETYQLNLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 81 DTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQVFDLFdKLGA 160
Cdd:COG0481 79 DTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDII-GIDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 161 TNeqldfpIVYASGLNGYaGLEDtvrdgdmtpLYEAIMQHAPRPEVDPEGPFQMRIsqLD--YNNFVGVIGIGRIQRGTL 238
Cdd:COG0481 158 SD------AILVSAKTGI-GIEE---------ILEAIVERIPPPKGDPDAPLQALI--FDswYDSYRGVVVYVRVFDGTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 239 KKNMQVAVIdregkkRNGKVLQV--LGFMGLERIEQDTAEAGD---IVA-ISGIQELTISDTICAPDTP--EALPALtvd 310
Cdd:COG0481 220 KKGDKIKMM------STGKEYEVdeVGVFTPKMTPVDELSAGEvgyIIAgIKDVRDARVGDTITLAKNPaaEPLPGF--- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 311 EPTISMTFQ----VNNSPFagnKDLsggkfltsrqiKDRLDREKVHNVALKVEQlEDADK--------FLvsgrGELHLS 378
Cdd:COG0481 291 KEVKPMVFAglypVDSDDY---EDL-----------RDALEKLQLNDASLTYEP-ETSAAlgfgfrcgFL----GLLHME 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 379 VLIENMRREgYELAV--SRPEVI--IKEIDGQMME-------PIEQLVVDIEE------IHQ-----GGVMEKLGTRKGQ 436
Cdd:COG0481 352 IIQERLERE-FDLDLitTAPSVVyeVTLTDGEVIEvdnpsdlPDPGKIEEIEEpivkatIITpseyvGAVMELCQEKRGV 430
|
490 500 510
....*....|....*....|....*....|....*..
gi 692318981 437 LKNMESDGKGRVRLEYSIP-ARGLIGFQNEFKTLTQG 472
Cdd:COG0481 431 QKNMEYLGENRVELTYELPlAEIVFDFFDRLKSITRG 467
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-398 |
3.97e-55 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 198.73 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 2 SIENLRNIAIVAHVDHGKTTLVDQLLKQSGTLS------ERTvlaeRVMDSNDQEKERGITIlakNTAIT---WEDKktg 72
Cdd:COG0480 5 PLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHrigevhDGN----TVMDWMPEEQERGITI---TSAATtceWKGH--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 73 iknRINIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGfKP-IVVVNKVDRPGARPEWVIDQ- 150
Cdd:COG0480 75 ---KINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYG-VPrIVFVNKMDREGADFDRVLEQl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 151 -----------------------VFDLF--------DKLGATNEQLDFP-----------------IV---------Yas 173
Cdd:COG0480 151 kerlganpvplqlpigaeddfkgVIDLVtmkayvydDELGAKYEEEEIPaelkeeaeeareelieaVAetddelmekY-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 174 gLNG--------YAGLEDTVRDGDMTP--------------LYEAIMQHAPRP-------------------EVDPEGPF 212
Cdd:COG0480 229 -LEGeelteeeiKAGLRKATLAGKIVPvlcgsafknkgvqpLLDAVVDYLPSPldvpaikgvdpdtgeeverKPDDDEPF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 213 QMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVAVIDREGKKRNGKVLQVlgfMGLERIEQDTAEAGDIVAISGIQELTIS 292
Cdd:COG0480 308 SALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRM---HGNKREEVDEAGAGDIVAVVKLKDTTTG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 293 DTICAPDTPEALPALTVDEPTISMTFQVnnspfagnkdlsggkfltsrqiKDRLDREKVHNV---------ALKVEQLED 363
Cdd:COG0480 385 DTLCDEDHPIVLEPIEFPEPVISVAIEP----------------------KTKADEDKLSTAlaklaeedpTFRVETDEE 442
|
490 500 510
....*....|....*....|....*....|....*.
gi 692318981 364 ADKFLVSGRGELHLSVLIENMRRE-GYELAVSRPEV 398
Cdd:COG0480 443 TGQTIISGMGELHLEIIVDRLKREfGVEVNVGKPQV 478
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
12-495 |
1.03e-54 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 197.27 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 12 VAHVDHGKTTLVDQLLKQSGTLSERTVLAE--RVMDSNDQEKERGITIlakNTAIT---WEDKKtgiknrINIVDTPGHA 86
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDgtTTMDFMPEERERGISI---TSAATtceWKGHK------INLIDTPGHV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 87 DFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGfKP-IVVVNKVDRPGARPEWVIDQvfdLFDKLGATNEQL 165
Cdd:PRK12740 72 DFTGEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYG-VPrIIFVNKMDRAGADFFRVLAQ---LQEKLGAPVVPL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 166 DFPI------------------VYASG--------------------------------------LNG--------YAGL 181
Cdd:PRK12740 148 QLPIgegddftgvvdllsmkayRYDEGgpseeieipaelldraeeareellealaefddelmekyLEGeelseeeiKAGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 182 EDTVRDGDMTP--------------LYEAIMQHAPRP-----------------EVDPEGPFQMRISQLDYNNFVGVIGI 230
Cdd:PRK12740 228 RKATLAGEIVPvfcgsalknkgvqrLLDAVVDYLPSPlevppvdgedgeegaelAPDPDGPLVALVFKTMDDPFVGKLSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 231 GRIQRGTLKKNMQVAVIDREGKKRNGKVLQvlgFMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDTPEALPALTVD 310
Cdd:PRK12740 308 VRVYSGTLKKGDTLYNSGTGKKERVGRLYR---MHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 311 EPTISMtfqvnnspfagnkdlsggkfltSRQIKDRLDREKVHNV---------ALKVEQLEDADKFLVSGRGELHLSVLI 381
Cdd:PRK12740 385 EPVISL----------------------AIEPKDKGDEEKLSEAlgklaeedpTLRVERDEETGQTILSGMGELHLDVAL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 382 ENMRRE-GYELAVSRPEVIIKE---------------------------------------------------------- 402
Cdd:PRK12740 443 ERLKREyGVEVETGPPQVPYREtirkkaeghgrhkkqsgghgqfgdvwleveplprgegfefvdkvvggavprqyipave 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 403 ------------------------IDGQM-----------------------------MEPIEQLVVDIEEIHQGGVMEK 429
Cdd:PRK12740 523 kgvrealekgvlagypvvdvkvtlTDGSYhsvdssemafkiaarlafrealpkakpvlLEPIMKVEVSVPEEFVGDVIGD 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 430 LGTRKGQLKNMESDGKG-RVRLEysIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGPKEqGAIAKRI 495
Cdd:PRK12740 603 LSSRRGRILGMESRGGGdVVRAE--VPLAEMFGYATDLRSLTQGRGSFSMEFSHYEEVP-GNVAEKV 666
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-409 |
3.57e-53 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 193.24 E-value: 3.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 1 MSIENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSER-TVlaER---VMDSNDQEKERGITILAKNTAITWEDkktgikNR 76
Cdd:PRK13351 3 MPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMgEV--EDgttVTDWMPQEQERGITIESAATSCDWDN------HR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 77 INIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGA-------------- 142
Cdd:PRK13351 75 INLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGAdlfkvledieerfg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 143 -RP-------------EWVIDQVF----------------------DLFDKLGATNEQL-----DF-PIVYASGLNG--- 177
Cdd:PRK13351 155 kRPlplqlpigsedgfEGVVDLITepelhfsegdggstveegpipeELLEEVEEAREKLiealaEFdDELLELYLEGeel 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 178 -----YAGLEDTVRDGDMTP--------------LYEAIMQHAPRP------------------EVDPEGPFQMRISQLD 220
Cdd:PRK13351 235 saeqlRAPLREGTRSGHLVPvlfgsalknigiepLLDAVVDYLPSPlevppprgskdngkpvkvDPDPEKPLLALVFKVQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 221 YNNFVGVIGIGRIQRGTLKKNMQVAVIDREGKKRNGKVLQVlgfMGLERIEQDTAEAGDIVAISGIQELTISDTICAPDT 300
Cdd:PRK13351 315 YDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRL---QGNKREEVDRAKAGDIVAVAGLKELETGDTLHDSAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 301 PEALPALTVDEPTISMTFqvnnSPfagnkdlsggkfltsrqiKDRLDREKVHNV---------ALKVEQLEDADKFLVSG 371
Cdd:PRK13351 392 PVLLELLTFPEPVVSLAV----EP------------------ERRGDEQKLAEAleklvwedpSLRVEEDEETGQTILSG 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 692318981 372 RGELHLSVLIENMRRE-GYELAVSRPEVIIKEIDGQMME 409
Cdd:PRK13351 450 MGELHLEVALERLRREfKLEVNTGKPQVAYRETIRKMAE 488
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
8-204 |
2.11e-52 |
|
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: 177.87 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITILAKNTAITWEDKktgiknRINIVDTPGHAD 87
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKR------RINFIDTPGHED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 88 FGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPG-ARPEWVIDQVFDLFDKLGATNE-QL 165
Cdd:cd00881 75 FSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTFLkGK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 692318981 166 DFPIVYASGLNGYagledtvrdgDMTPLYEAIMQHAPRP 204
Cdd:cd00881 155 DVPIIPISALTGE----------GIEELLDAIVEHLPPP 183
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
7-139 |
1.26e-43 |
|
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: 155.47 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 7 RNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITIlaKNTAITW-----EDKKTGIKNRINIVD 81
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAISLyfeyeEEKMDGNDYLINLID 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 692318981 82 TPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDR 139
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
312-394 |
5.13e-43 |
|
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios. It is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion.
Pssm-ID: 293920 [Multi-domain] Cd Length: 79 Bit Score: 148.61 E-value: 5.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 312 PTISMTFQVNNSPFAGNKdlsgGKFLTSRQIKDRLDREKVHNVALKVEQLEDADKFLVSGRGELHLSVLIENMRREGYEL 391
Cdd:cd16263 1 PTVSMTFGVNTSPFAGRE----GKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFEL 76
|
...
gi 692318981 392 AVS 394
Cdd:cd16263 77 QVS 79
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
212-305 |
3.08e-41 |
|
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: 144.25 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 212 FQMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVAVIDREGKKRNGKVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTI 291
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|....
gi 692318981 292 SDTICAPDTPEALP 305
Cdd:cd03691 81 GDTICDPEVPEPLP 94
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
7-204 |
3.80e-40 |
|
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: 144.60 E-value: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 7 RNIAIVAHVDHGKTTLVDQLLKQSGTLSERTvLAERVMDSNDQEKERGITILAKNTAITWEDKKtGIKNRINIVDTPGHA 86
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSERE-MKEQVLDSMDLERERGITIKAQAVRLFYKAKD-GEEYLLNLIDTPGHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 87 DFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQVFDLFDKLgaTNEqld 166
Cdd:cd01890 79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDVLGLD--ASE--- 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 692318981 167 fpIVYASGLNGYaGLEDtvrdgdmtpLYEAIMQHAPRP 204
Cdd:cd01890 154 --AILVSAKTGL-GVED---------LLEAIVERIPPP 179
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
409-487 |
4.12e-39 |
|
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: 138.02 E-value: 4.12e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692318981 409 EPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGPKE 487
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEPYK 79
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
8-151 |
1.18e-35 |
|
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: 133.90 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTvlaeRV------MDSNDQEKERGITILAKNTAITWEDKKtgiknrINIVD 81
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELG----SVdkgttrTDSMELERQRGITIFSAVASFQWEDTK------VNIID 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 82 TPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQV 151
Cdd:cd04168 71 TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
4-139 |
5.48e-32 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 132.09 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 4 ENLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITIlaKNTAI------TWEDKKTGIKNRI 77
Cdd:PTZ00416 17 DQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehDLEDGDDKQPFLI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 692318981 78 NIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDR 139
Cdd:PTZ00416 95 NLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
8-169 |
4.93e-30 |
|
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: 119.13 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAER--VMDSNDQEKERGITILAKNTAITWEDkktgikNRINIVDTPGH 85
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGgaTMDWMEQERERGITIQSAATTCFWKD------HRINIIDTPGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 86 ADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQvfdLFDKLGATNEQL 165
Cdd:cd01886 75 VDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQ---IREKLGANPVPL 151
|
....
gi 692318981 166 DFPI 169
Cdd:cd01886 152 QLPI 155
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
5-139 |
2.28e-28 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 120.98 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 5 NLRNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITIlaKNTAIT------------WEDKKTG 72
Cdd:PLN00116 18 NIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGISlyyemtdeslkdFKGERDG 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 73 IKNRINIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDR 139
Cdd:PLN00116 96 NEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
7-139 |
1.08e-26 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 108.12 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 7 RNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLA---ERVMDSNDQEKERGITIlaKNTAIT--WEDKKtGIKNRINIVD 81
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSVKLGwkpLRYTDTRKDEQERGISI--KSNPISlvLEDSK-GKSYLINIID 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 692318981 82 TPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDR 139
Cdd:cd04167 78 TPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-279 |
1.23e-25 |
|
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: 109.64 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTV-----LAER----------VMDSNDQEKERGITIlakntAITWEDKKTG 72
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGAIDEHIIekyeeEAEKkgkesfkfawVMDRLKEERERGVTI-----DLAHKKFETD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 73 iKNRINIVDTPGHADFggeverVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPG---A 142
Cdd:COG5256 84 -KYYFTIIDAPGHRDF------VKNMItgasqaDAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVNyseK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 143 RPEWVIDQVFDLFDKLGATNEqlDFPIVYASGLNGyaglEDTVRDGDMTP------LYEAI--MQHAPRPeVDPegPFQM 214
Cdd:COG5256 157 RYEEVKEEVSKLLKMVGYKVD--KIPFIPVSAWKG----DNVVKKSDNMPwyngptLLEALdnLKEPEKP-VDK--PLRI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692318981 215 RIsQLDYN-NFVGVIGIGRIQRGTLKKNMQVaVIDREGKKRNGKVLQvlgfMGLERIEQdtAEAGD 279
Cdd:COG5256 228 PI-QDVYSiSGIGTVPVGRVETGVLKVGDKV-VFMPAGVVGEVKSIE----MHHEELEQ--AEPGD 285
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
406-485 |
1.87e-23 |
|
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: 94.54 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 406 QMMEPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
8-178 |
2.13e-23 |
|
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: 99.98 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSER-TVLAE-RVMDSNDQEKERGITILAKNTAITWEDKKtgiknrINIVDTPGH 85
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVEDGnTVSDYDPEEKKRKMSIETSVAPLEWNGHK------INLIDTPGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 86 ADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQvfdLFDKLGATNEQL 165
Cdd:cd04170 75 ADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAA---LREAFGRPVVPI 151
|
170
....*....|...
gi 692318981 166 DFPIVYASGLNGY 178
Cdd:cd04170 152 QLPIGEGDEFTGV 164
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
409-485 |
5.23e-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: 92.93 E-value: 5.23e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 409 EPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEP 77
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
8-283 |
1.36e-22 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 100.40 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgTLSERTVLAERVMDSND---QEKERGITIlakNTA-ITWEDKKTGIKNriniVDTP 83
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAITK---VLAERGLNQAKDYDSIDaapEEKERGITI---NTAhVEYETEKRHYAH----VDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFggeverVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPGArpEWVID----QVF 152
Cdd:PRK12736 84 GHADY------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLARQVGVPYLVVfLNKVDLVDD--EELLElvemEVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 153 DLFDKLGATNEqlDFPIVYASG---LNGYAGLEDTVRDgdmtpLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIG 229
Cdd:PRK12736 156 ELLSEYDFPGD--DIPVIRGSAlkaLEGDPKWEDAIME-----LMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVV 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 230 IGRIQRGTLKKNMQVAVID-REGKKRNgkvlqvlgFMGLE--RIEQDTAEAGDIVAI 283
Cdd:PRK12736 229 TGRVERGTVKVGDEVEIVGiKETQKTV--------VTGVEmfRKLLDEGQAGDNVGV 277
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
7-158 |
1.29e-21 |
|
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: 94.97 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 7 RNIAIVAHVDHGKTTLVDQLLKQSGTLSER-TVLAER-----VMDSNDQEKERGITILAknTAITWEDKKTgiknRINIV 80
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAgAVKARKsrkhaTSDWMEIEKQRGISVTS--SVMQFEYKGC----VINLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 81 DTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRfvtqKAFA---MGFKPIV-VVNKVDRPGARPewvidqvFDLFD 156
Cdd:cd04169 77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTR----KLFEvcrLRGIPIItFINKLDREGRDP-------LELLD 145
|
..
gi 692318981 157 KL 158
Cdd:cd04169 146 EI 147
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
8-247 |
1.39e-21 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 97.97 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITIlakNTA-ITWEDKKTGIKNriniVDTPGHA 86
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITI---ATAhVEYETAKRHYAH----VDCPGHA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 87 DFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDrpgarpewVID--QVFDLFDKlgATNE 163
Cdd:PLN03127 136 DYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVD--------VVDdeELLELVEM--ELRE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 164 QLDF--------PIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIGIGRIQR 235
Cdd:PLN03127 206 LLSFykfpgdeiPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQ 285
|
250
....*....|..
gi 692318981 236 GTLKKNMQVAVI 247
Cdd:PLN03127 286 GTIKVGEEVEIV 297
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
8-283 |
1.89e-21 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 96.77 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgTLSERTVLAERVMDSND---QEKERGITIlakNTA-ITWEDKKTGIKNriniVDTP 83
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITT---VLAKEGGAAARAYDQIDnapEEKARGITI---NTAhVEYETETRHYAH----VDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPGARP--EWVIDQVFDLFDKLGA 160
Cdd:TIGR00485 84 GHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVRELLSQYDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 161 TNEqlDFPIVYASGL---NGYAGLEDTVRDgdmtpLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIGIGRIQRGT 237
Cdd:TIGR00485 164 PGD--DTPIIRGSALkalEGDAEWEAKILE-----LMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 692318981 238 LKKNMQVAVIdreGKKRNGKVLqvlgFMGLE--RIEQDTAEAGDIVAI 283
Cdd:TIGR00485 237 IKVGEEVEIV---GLKDTRKTT----VTGVEmfRKELDEGRAGDNVGL 277
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
8-177 |
5.69e-21 |
|
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: 91.78 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLA-ER--------------VMDSNDQEKERGITI---LAK-NTAitwed 68
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKyEKeakemgkesfkyawVLDKLKEERERGVTIdvgLAKfETE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 69 kktgiKNRINIVDTPGHADFggeverVLSMV------DTVLILVDAMDG-------PMPQTRFVTQKAFAMGFKP-IVVV 134
Cdd:cd01883 76 -----KYRFTIIDAPGHRDF------VKNMItgasqaDVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQlIVAV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 692318981 135 NKVDRPG-----ARPEWVIDQVFDLFDKLGATNEQLDF-PIvyaSGLNG 177
Cdd:cd01883 145 NKMDDVTvnwsqERYDEIKKKVSPFLKKVGYNPKDVPFiPI---SGFTG 190
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-319 |
5.75e-21 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 95.76 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAER---------------VMDSNDQEKERGITIlakntAITWEDKKTG 72
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELReeakekgkesfkfawVMDRLKEERERGVTI-----DLAHKKFETD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 73 iKNRINIVDTPGHADFggeverVLSMV------DTVLILVDAMD--GPMPQTRfvtQKAF---AMGFKP-IVVVNKVDRP 140
Cdd:PRK12317 83 -KYYFTIVDCPGHRDF------VKNMItgasqaDAAVLVVAADDagGVMPQTR---EHVFlarTLGINQlIVAINKMDAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 141 G---ARPEWVIDQVFDLFDKLGATNEqlDFPIVYASGLNGyaglEDTVRDGDMTP------LYEAI-MQHAPRPEVDPeg 210
Cdd:PRK12317 153 NydeKRYEEVKEEVSKLLKMVGYKPD--DIPFIPVSAFEG----DNVVKKSENMPwyngptLLEALdNLKPPEKPTDK-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 211 PFQMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVaVIDREGKKRNGKVLQvlgfMGLERIEQdtAEAGDIVAIS--GIQE 288
Cdd:PRK12317 225 PLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKV-VFMPAGVVGEVKSIE----MHHEELPQ--AEPGDNIGFNvrGVGK 297
|
330 340 350
....*....|....*....|....*....|...
gi 692318981 289 LTIS--DTICAPDTPealpaltvdePTISMTFQ 319
Cdd:PRK12317 298 KDIKrgDVCGHPDNP----------PTVAEEFT 320
|
|
| tufA |
CHL00071 |
elongation factor Tu |
8-287 |
6.48e-19 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 89.25 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqSGTLSERTVLAERV---MDSNDQEKERGITIlakNTA-ITWEDKKTGIKNriniVDTP 83
Cdd:CHL00071 14 NIGTIGHVDHGKTTLTAAI---TMTLAAKGGAKAKKydeIDSAPEEKARGITI---NTAhVEYETENRHYAH----VDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFggeverVLSM------VDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNK---VDRPGARpEWVIDQVFD 153
Cdd:CHL00071 84 GHADY------VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKedqVDDEELL-ELVELEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 154 LFDKLGATNEqlDFPIVYASGLngyAGLEDTVRDGDMTP-----------LYEAIMQHAPRPEVDPEGPFQMRISQLDYN 222
Cdd:CHL00071 157 LLSKYDFPGD--DIPIVSGSAL---LALEALTENPKIKRgenkwvdkiynLMDAVDSYIPTPERDTDKPFLMAIEDVFSI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692318981 223 NFVGVIGIGRIQRGTLKKNMQVAVIDReGKKRNGKVLqvlgfmGLERIEQ--DTAEAGDIVAIS--GIQ 287
Cdd:CHL00071 232 TGRGTVATGRIERGTVKVGDTVEIVGL-RETKTTTVT------GLEMFQKtlDEGLAGDNVGILlrGIQ 293
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
8-283 |
8.07e-19 |
|
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: 89.05 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgTLSERTVLAERVMDSND---QEKERGITIlakNTA-ITWEDKKTGIKNriniVDTP 83
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITK---VLAKKGGAKAKAYDQIDkapEEKERGITI---NTShVEYETEKRHYAH----VDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFggeverVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDrpGARPEWVID----QVF 152
Cdd:COG0050 84 GHADY------VKNMItgaaqmDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCD--MVDDEELLElvemEVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 153 DLFDKLGATNEqlDFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISqldyNNFV----GVI 228
Cdd:COG0050 156 ELLSKYGFPGD--DTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVE----DVFSitgrGTV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 692318981 229 GIGRIQRGTLKKNMQVAVID-REGKKrngkvlQVLgfMGLE--RIEQDTAEAGDIVAI 283
Cdd:COG0050 230 VTGRVERGIIKVGDEVEIVGiRDTQK------TVV--TGVEmfRKLLDEGEAGDNVGL 279
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
9-177 |
1.09e-18 |
|
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: 83.68 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 9 IAIVAHVDHGKTTLVDQLLKqsgtlsertvlaervmdSNDQEKE-RGIT--ILAknTAITWEDKktgiKNRINIVDTPGH 85
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK-----------------TNVAAGEaGGITqhIGA--YQVPIDVK----IPGITFIDTPGH 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 86 ADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEwVIDQVFDLfdkLGATNEQL 165
Cdd:cd01887 60 EAFTNMRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEA-DPERVKNE---LSELGLVG 135
|
170
....*....|....*..
gi 692318981 166 -----DFPIVYASGLNG 177
Cdd:cd01887 136 eewggDVSIVPISAKTG 152
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
8-283 |
2.98e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 87.20 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgTLSERTVLAERVMDSND---QEKERGITIlakNTA-ITWEDKKTGIKNriniVDTP 83
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITK---VLAKKGGGEAKAYDQIDnapEEKARGITI---NTShVEYETANRHYAH----VDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFggeverVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPGARP--EWVIDQVFDL 154
Cdd:PRK12735 84 GHADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEEllELVEMEVREL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 155 FDKLGATNEqlDFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQLdynnFV----GVIGI 230
Cdd:PRK12735 158 LSKYDFPGD--DTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDV----FSisgrGTVVT 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 692318981 231 GRIQRGTLKKNMQVAVID-REGKKRNgkvlqvlgFMGLE--RIEQDTAEAGDIVAI 283
Cdd:PRK12735 232 GRVERGIVKVGDEVEIVGiKETQKTT--------VTGVEmfRKLLDEGQAGDNVGV 279
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
8-283 |
5.32e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 86.40 E-value: 5.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgTLSERTVLAERVMDSND---QEKERGITIlakNTA-ITWEDKKTGIKNriniVDTP 83
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITK---VLAKKGGAEAKAYDQIDkapEEKARGITI---NTAhVEYETEKRHYAH----VDCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFggeverVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPgARPEW---VIDQVFD 153
Cdd:PRK00049 84 GHADY------VKNMItgaaqmDGAILVVSAADGPMPQTREHILLARQVGVPYIVVfLNKCDMV-DDEELlelVEMEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 154 LFDKLGATNEqlDFPIVYASGLNGYAGLEDTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQLdynnFV----GVIG 229
Cdd:PRK00049 157 LLSKYDFPGD--DTPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDV----FSisgrGTVV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 230 IGRIQRGTLKKNMQVAVID-REGKKRNgkvlqvlgFMGLE--RIEQDTAEAGDIVAI 283
Cdd:PRK00049 231 TGRVERGIIKVGEEVEIVGiRDTQKTT--------VTGVEmfRKLLDEGQAGDNVGA 279
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
8-291 |
6.84e-18 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 86.98 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITIlakNTA-ITWEDKKTGIKNriniVDTPGHA 86
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITI---NTAtVEYETENRHYAH----VDCPGHA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 87 DFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPGARP--EWVIDQVFDLFDKLGATNE 163
Cdd:PLN03126 156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVfLNKQDQVDDEEllELVELEVRELLSSYEFPGD 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 164 qlDFPIVYASGLNGYAGLED--TVRDGD------MTPLYEAIMQHAPRPEVDPEGPFQMRISQLDYNNFVGVIGIGRIQR 235
Cdd:PLN03126 236 --DIPIISGSALLALEALMEnpNIKRGDnkwvdkIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVER 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 236 GTLKKNMQVAVIDReGKKRNGKVlqvlgfMGLERIEQ--DTAEAGDIVAI--SGIQELTI 291
Cdd:PLN03126 314 GTVKVGETVDIVGL-RETRSTTV------TGVEMFQKilDEALAGDNVGLllRGIQKADI 366
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
7-160 |
1.45e-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: 80.11 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 7 RNIAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERvMDSNDQEKERGITIlakntaitwedkktgiknRINIVDTPGHA 86
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTR-NYVTTVIEEDGKTY------------------KFNLLDTAGQE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 87 DF-------GGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAfAMGFKPIVVVNKVDRPGARpewVIDQVFDLFDKLG 159
Cdd:TIGR00231 63 DYdairrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKIDLKDAD---LKTHVASEFAKLN 138
|
.
gi 692318981 160 A 160
Cdd:TIGR00231 139 G 139
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
14-303 |
1.79e-17 |
|
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: 86.12 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 14 HVDHGKTTLVDQLlkqSGTLSERtvLAErvmdsndqEKERGITI--------LAKNTaitwedkktgiknRINIVDTPGH 85
Cdd:COG3276 8 HIDHGKTTLVKAL---TGIDTDR--LKE--------EKKRGITIdlgfaylpLPDGR-------------RLGFVDVPGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 86 ADF--------GGevervlsmVDTVLILVDAMDGPMPQTRfvtqKAFA----MGFKP-IVVVNKVDRpgARPEW---VID 149
Cdd:COG3276 62 EKFiknmlagaGG--------IDLVLLVVAADEGVMPQTR----EHLAildlLGIKRgIVVLTKADL--VDEEWlelVEE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 150 QVFDLfdkLGATNeqL-DFPIVYASGLNGyAGLEDtvrdgdmtpLYEAIMQHAPR-PEVDPEGPFQMRISQLdynnF--- 224
Cdd:COG3276 128 EIREL---LAGTF--LeDAPIVPVSAVTG-EGIDE---------LRAALDALAAAvPARDADGPFRLPIDRV----Fsik 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 225 -VGVIGIGRIQRGTLKKNMQVAV--IDREGKKRNgkvLQVLGfmglerIEQDTAEAGDIVAI--SGIQELTIS--DTICA 297
Cdd:COG3276 189 gFGTVVTGTLLSGTVRVGDELELlpSGKPVRVRG---IQVHG------QPVEEAYAGQRVALnlAGVEKEEIErgDVLAA 259
|
....*.
gi 692318981 298 PDTPEA 303
Cdd:COG3276 260 PGALRP 265
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
7-295 |
8.84e-16 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 80.56 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 7 RNIAIVAHVDHGKTTLVDQLL------KQSGTLSERTvlAERVMDSN--DQEKERGITILAKNTAITWEDKktgiknRIN 78
Cdd:PRK00741 11 RTFAIISHPDAGKTTLTEKLLlfggaiQEAGTVKGRK--SGRHATSDwmEMEKQRGISVTSSVMQFPYRDC------LIN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 79 IVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRfvtqKAFA---MGFKPIVV-VNKVDRPGARPEWVIDQ---- 150
Cdd:PRK00741 83 LLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMEvcrLRDTPIFTfINKLDRDGREPLELLDEieev 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 151 --------------------VFDLFDK-------------------LGATNEQLDFPIvyasGLNGYAGL---------- 181
Cdd:PRK00741 159 lgiacapitwpigmgkrfkgVYDLYNDevelyqpgeghtiqeveiiKGLDNPELDELL----GEDLAEQLreelelvqga 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 182 -----EDTVRDGDMTPLY--------------EAIMQHAPRP--------EVDP-EGPF-------Q--M------RISq 218
Cdd:PRK00741 235 snefdLEAFLAGELTPVFfgsalnnfgvqeflDAFVEWAPAPqprqtderEVEPtEEKFsgfvfkiQanMdpkhrdRIA- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 219 ldynnFVgvigigRIQRGTLKKNMQVAVIdregkkRNGKVLQ---VLGFMGLERIEQDTAEAGDIVAI---SGIQeltIS 292
Cdd:PRK00741 314 -----FV------RVCSGKFEKGMKVRHV------RTGKDVRisnALTFMAQDREHVEEAYAGDIIGLhnhGTIQ---IG 373
|
...
gi 692318981 293 DTI 295
Cdd:PRK00741 374 DTF 376
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
8-183 |
1.06e-14 |
|
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: 73.00 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgTLSERTVLAERVMDSNDQ---EKERGITIlakNTA-ITWEDKktgiKNRINIVDTP 83
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITK---VLAKKGGAKAKKYDEIDKapeEKARGITI---NTAhVEYETA----NRHYAHVDCP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 84 GHADFggeverVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPgARPEW---VIDQVFD 153
Cdd:cd01884 74 GHADY------IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMV-DDEELlelVEMEVRE 146
|
170 180 190
....*....|....*....|....*....|
gi 692318981 154 LFDKLGATNEqlDFPIVYASGLNGYAGLED 183
Cdd:cd01884 147 LLSKYGFDGD--DTPIVRGSALKALEGDDP 174
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
14-183 |
1.86e-14 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 71.48 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 14 HVDHGKTTLVDQLLKQSGtlsertvlaervmDSNDQEKERGITIlakNTAITWEDKKTGIknRINIVDTPGHADFggeve 93
Cdd:cd04171 7 HIDHGKTTLIKALTGIET-------------DRLPEEKKRGITI---DLGFAYLDLPDGK--RLGFIDVPGHEKF----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 94 rVLSMV------DTVLILVDAMDGPMPQTRFVTQKAFAMGFKP-IVVVNKVDR-PGARPEWVIDQVFDLFdklgATNEQL 165
Cdd:cd04171 64 -VKNMLagaggiDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADLvDEDRLELVEEEILELL----AGTFLA 138
|
170
....*....|....*...
gi 692318981 166 DFPIVYASGLNGyAGLED 183
Cdd:cd04171 139 DAPIFPVSSVTG-EGIEE 155
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-244 |
6.38e-14 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 74.40 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSERTV------LAER---------VMDSNDQEKERGITIlakNTAItWedKKTG 72
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIekfekeAAEMgkgsfkyawVLDKLKAERERGITI---DIAL-W--KFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 73 IKNRINIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMP-------QTRFVTQKAFAMGFKPIVV-VNKVDRPG--- 141
Cdd:PTZ00141 83 PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVcINKMDDKTvny 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 142 --ARPEWVIDQVFDLFDKLGATNEQLDF-PIvyaSGLNGyaglEDTVRDGDMTPLY------EAIMQHAPrPEVDPEGPF 212
Cdd:PTZ00141 163 sqERYDEIKKEVSAYLKKVGYNPEKVPFiPI---SGWQG----DNMIEKSDNMPWYkgptllEALDTLEP-PKRPVDKPL 234
|
250 260 270
....*....|....*....|....*....|..
gi 692318981 213 QMRISQLDYNNFVGVIGIGRIQRGTLKKNMQV 244
Cdd:PTZ00141 235 RLPLQDVYKIGGIGTVPVGRVETGILKPGMVV 266
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
9-150 |
8.61e-14 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 74.42 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 9 IAIVAHVDHGKTTLVDQLLKQSGTLSERTvlaervmdsndqekerGITILAKNTAITWEDKKtgiknRINIVDTPGHADF 88
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSIRKTKVAQGEAG----------------GITQHIGAYHVENEDGK-----MITFLDTPGHEAF 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 692318981 89 GGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQ 150
Cdd:TIGR00487 149 TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQE 210
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
15-301 |
1.14e-13 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 73.18 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 15 VDHGKTTLVDQLLKQSGTLSERTVLA-ER----------------VMDSNDQEKERGITI-LAKNTAITweDKKTGIknr 76
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIYEDQLAAlERdskkhgtqggeidlalLVDGLQAEREQGITIdVAYRYFST--DKRKFI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 77 inIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPGARPEwVIDQVFDLF 155
Cdd:TIGR02034 84 --VADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMDLVDYDEE-VFENIKKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 156 DKLGATNEQLDFPIVYASGLNGyaglEDTVRDGDMTPLYEA--IMQHAPRPEVDP---EGPFQMRIS-----QLDYNNFV 225
Cdd:TIGR02034 161 LAFAEQLGFRDVTFIPLSALKG----DNVVSRSESMPWYSGptLLEILETVEVERdaqDLPLRFPVQyvnrpNLDFRGYA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692318981 226 GVIGIGRIQRGtlkknmQVAVIDREGkkRNGKVLQVLGFMGleriEQDTAEAGDIVAISGIQELTIS--DTICAPDTP 301
Cdd:TIGR02034 237 GTIASGSVHVG------DEVVVLPSG--RSSRVARIVTFDG----DLEQARAGQAVTLTLDDEIDISrgDLLAAADSA 302
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
8-139 |
1.59e-13 |
|
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: 73.37 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqSGTLSERtvLAErvmdsndqEKERGITILAKNTAITWEDKktgiknRINIVDTPGHAD 87
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---TGIAADR--LPE--------EKKRGMTIDLGFAYFPLPDY------RLGFIDVPGHEK 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 692318981 88 FGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKP-IVVVNKVDR 139
Cdd:TIGR00475 63 FISNAIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADR 115
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
9-264 |
1.82e-13 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 73.71 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 9 IAIVAHVDHGKTTLVDQLLKqsgtlsertvlaervmdSNDQEKERGiTILAKNTAITWEDKKTGIKNRINIVDTPGHADF 88
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAG-GITQKIGAYEVEFEYKDENQKIVFLDTPGHEAF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 89 GGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDRPGARPEWVIDQV--FDLF-DKLGAtneql 165
Cdd:CHL00189 309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLakYNLIpEKWGG----- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 166 DFPIVYASGLNGYagledtvrdgDMTPLYEAIMQHAPRPEV--DPEGPFQMRISQLDYNNFVGVIGIGRIQRGTLK---- 239
Cdd:CHL00189 384 DTPMIPISASQGT----------NIDKLLETILLLAEIEDLkaDPTQLAQGIILEAHLDKTKGPVATILVQNGTLHigdi 453
|
250 260 270
....*....|....*....|....*....|....*....
gi 692318981 240 ----------KNMqvavIDREGKKRN----GKVLQVLGF 264
Cdd:CHL00189 454 ivigtsyakiRGM----INSLGNKINlatpSSVVEIWGL 488
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
8-239 |
3.46e-13 |
|
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: 71.62 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqSGTLSertvlaervmDSNDQEKERGITI--------------LAKNTAITWEDK---- 69
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVWT----------DTHSEELKRGISIrlgyadaeiykcpeCDGPECYTTEPVcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 70 --KTGIKNRINIVDTPGHADFGGEVERVLSMVDTVLILVDAMDG-PMPQTRFVTQKAFAMGFKPIVVV-NKVDRpgARPE 145
Cdd:TIGR03680 73 gsETELLRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVqNKIDL--VSKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 146 WVIDQVFDL--FDKlGATNEqlDFPIVYASGLNGyagledtvrdGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQ----- 218
Cdd:TIGR03680 151 KALENYEEIkeFVK-GTVAE--NAPIIPVSALHN----------ANIDALLEAIEKFIPTPERDLDKPPLMYVARsfdvn 217
|
250 260
....*....|....*....|....*
gi 692318981 219 ---LDYNNFV-GVIGiGRIQRGTLK 239
Cdd:TIGR03680 218 kpgTPPEKLKgGVIG-GSLIQGKLK 241
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
8-138 |
8.09e-13 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 67.39 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqsgtlseRTVLAERVMDSNDQEKERGITI-------LAKNTAITWEDKKTGIKN-RINI 79
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL---------SEIASTAAFDKNPQSQERGITLdlgfssfEVDKPKHLEDNENPQIENyQITL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692318981 80 VDTPGHADF------GGEVervlsmVDTVLILVDAMDGPMPQTRF------VTQKafamgfKPIVVVNKVD 138
Cdd:cd01889 73 VDCPGHASLirtiigGAQI------IDLMLLVVDAKKGIQTQTAEclvigeLLCK------PLIVVLNKID 131
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
312-394 |
8.96e-13 |
|
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: 63.52 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 312 PTISMTFQVNNspfagnkdlsggkFLTSRQIKDRLDREKVHNVALKVEQLEDADKFLVSGRGELHLSVLIENMRRE-GYE 390
Cdd:cd16257 1 PVVFVTVEVKN-------------PLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVE 67
|
....
gi 692318981 391 LAVS 394
Cdd:cd16257 68 LVVS 71
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
14-150 |
1.11e-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: 70.43 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 14 HVDHGKTTLVDQLLKqsgtlsertvlaERVMdsndqEKE-RGIT--ILAknTAITWEDKKtgiknrINIVDTPGHADF-- 88
Cdd:COG0532 12 HVDHGKTSLLDAIRK------------TNVA-----AGEaGGITqhIGA--YQVETNGGK------ITFLDTPGHEAFta 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 89 ----GGEVervlsmVDTVLILVDAMDGPMPQTRFVTQKAFAMGFkPIVV-VNKVDRPGARPEWVIDQ 150
Cdd:COG0532 67 mrarGAQV------TDIVILVVAADDGVMPQTIEAINHAKAAGV-PIIVaINKIDKPGANPDRVKQE 126
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
10-178 |
1.34e-12 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 65.94 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 10 AIVAHVDHGKTTLVDQLLKQSGTLSERtvlaervmdsndqekERGITILAknTAITWEDKKTGIKnrINIVDTPGHADFG 89
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSD---------------VPGTTRDP--DVYVKELDKGKVK--LVLVDTPGLDEFG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 90 G-----EVERVLSMVDTVLILVDAMDGPMPQT-RFVTQKAFAMGFKPIVVV-NKVDRPGARPEWVIDQVFDLfdklgatN 162
Cdd:cd00882 62 GlgreeLARLLLRGADLILLVVDSTDRESEEDaKLLILRRLRKEGIPIILVgNKIDLLEEREVEELLRLEEL-------A 134
|
170
....*....|....*.
gi 692318981 163 EQLDFPIVYASGLNGY 178
Cdd:cd00882 135 KILGVPVFEVSAKTGE 150
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-244 |
6.88e-12 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 67.81 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTT---------------LVDQLLKQSGTLSERTVLAERVMDSNDQEKERGITIlakNTAItWEDKKTg 72
Cdd:PLN00043 9 NIVVIGHVDSGKSTttghliyklggidkrVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITI---DIAL-WKFETT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 73 iKNRINIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMP-------QTRFVTQKAFAMGFKPIV-VVNKVDR----- 139
Cdd:PLN00043 84 -KYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDAttpky 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 140 PGARPEWVIDQVFDLFDKLGATNEQLdfPIVYASGLNGYAGLE-DTVRDGDMTPLYEAIMQHAPRPEVDPEGPFQMRISQ 218
Cdd:PLN00043 163 SKARYDEIVKEVSSYLKKVGYNPDKI--PFVPISGFEGDNMIErSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQD 240
|
250 260
....*....|....*....|....*.
gi 692318981 219 LDYNNFVGVIGIGRIQRGTLKKNMQV 244
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPGMVV 266
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
15-301 |
9.85e-12 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 68.03 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 15 VDHGKTTLVDQLL------------------KQSGTLSERTVLAeRVMDSNDQEKERGITI-LAKNTAITweDKKTGIkn 75
Cdd:PRK05506 33 VDDGKSTLIGRLLydskmifedqlaalerdsKKVGTQGDEIDLA-LLVDGLAAEREQGITIdVAYRYFAT--PKRKFI-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 76 rinIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPGARPEwVIDQVFDL 154
Cdd:PRK05506 108 ---VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLaVNKMDLVDYDQE-VFDEIVAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 155 FDKLGAtneQLDFPIVYA---SGLNGyaglEDTVRDGDMTPLYE--AIMQH-------APRPEVDPEGPFQMRI-SQLDY 221
Cdd:PRK05506 184 YRAFAA---KLGLHDVTFipiSALKG----DNVVTRSARMPWYEgpSLLEHletveiaSDRNLKDFRFPVQYVNrPNLDF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 222 NNFVGVIGIGRIQRGTlkknmQVAVIDregKKRNGKVLQVLGFMGleriEQDTAEAGDIVAISGIQELTIS--DTICAPD 299
Cdd:PRK05506 257 RGFAGTVASGVVRPGD-----EVVVLP---SGKTSRVKRIVTPDG----DLDEAFAGQAVTLTLADEIDISrgDMLARAD 324
|
..
gi 692318981 300 TP 301
Cdd:PRK05506 325 NR 326
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
226-296 |
1.17e-11 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 60.36 E-value: 1.17e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692318981 226 GVIGIGRIQRGTLKKNMQVAVI--DREGKKRNGKVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTIC 296
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILpnGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
4-301 |
1.95e-10 |
|
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: 63.18 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 4 ENLRnIAIVAHVDHGKTTLVDQLLKQSGTLSE------RTVLAERVMDSND---------QEKERGITIlakNTA----I 64
Cdd:COG2895 16 DLLR-FITCGSVDDGKSTLIGRLLYDTKSIFEdqlaalERDSKKRGTQEIDlalltdglqAEREQGITI---DVAyryfS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 65 TweDKKTGIknrinIVDTPGHadfggeVERVLSMV------DTVLILVDAMDGPMPQTR---FVTQkafAMGFKPIVV-V 134
Cdd:COG2895 92 T--PKRKFI-----IADTPGH------EQYTRNMVtgastaDLAILLIDARKGVLEQTRrhsYIAS---LLGIRHVVVaV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 135 NKVDRPG---ARPEWVIDQVFDLFDKLGATNEQLdFPIvyaSGLNGyaglEDTVRDGDMTPLYE--AIMQH---APRPEV 206
Cdd:COG2895 156 NKMDLVDyseEVFEEIVADYRAFAAKLGLEDITF-IPI---SALKG----DNVVERSENMPWYDgpTLLEHletVEVAED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 207 DPEGPFQMRI-----SQLDYNNFVgvigiGRIQRGTLKKNMQVAVIdREGKKrnGKVLQVLGFMGleriEQDTAEAGDIV 281
Cdd:COG2895 228 RNDAPFRFPVqyvnrPNLDFRGYA-----GTIASGTVRVGDEVVVL-PSGKT--STVKSIVTFDG----DLEEAFAGQSV 295
|
330 340
....*....|....*....|..
gi 692318981 282 AISGIQELTIS--DTICAPDTP 301
Cdd:COG2895 296 TLTLEDEIDISrgDVIVAADAP 317
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
8-288 |
5.91e-10 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 61.87 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLkqSGTLSERTVLAERVMDSNDQEKERGIT---------------ILAKN-------TAIT 65
Cdd:COG5258 124 VVGVAGHVDHGKSTLVGTLV--TGKLDDGNGGTRSFLDVQPHEVERGLSadlsyavygfdddgpVRMKNplrktdrARVV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 66 WEDKKTgiknrINIVDTPGHadfggevERVLSM---------VDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNK 136
Cdd:COG5258 202 EESDKL-----VSFVDTVGH-------EPWLRTtirglvgqkLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 137 VDR-PGARPEWVIDQVFDLFDKLG------ATNEQLDF----------PIVYASGLNGyAGLEdtvrdgdmtpLYEAIMQ 199
Cdd:COG5258 270 IDKvDDERVEEVEREIENLLRIVGrtplevESRHDVDAaieeingrvvPILKTSAVTG-EGLD----------LLDELFE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 200 HAPRPEVDPEGPFQMRISQLdYN-NFVGVIGIGRIQRGTLKKNMQVAVidreGKKRNGKVLQV-LGFMGLERIEQDTAEA 277
Cdd:COG5258 339 RLPKRATDEDEPFLMYIDRI-YNvTGVGTVVSGTVKSGKVEAGDELLI----GPTKDGSFREVeVKSIEMHYHRVDKAEA 413
|
330
....*....|...
gi 692318981 278 GDIV--AISGIQE 288
Cdd:COG5258 414 GRIVgiALKGVEE 426
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
224-297 |
7.25e-10 |
|
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293905 [Multi-domain] Cd Length: 83 Bit Score: 55.61 E-value: 7.25e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692318981 224 FVGVIGIGRIQRGTLKKNMQVAVIDREGKKRNGKVLQVLGfmgLERIEQDTAEAGDIVAISGIQELTISDTICA 297
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHG---KKREEVEELGAGDIGAVVGLKDTRTGDTLCD 83
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
8-239 |
9.03e-10 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 61.02 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqSGTLSERtvlaervmdsNDQEKERGITI--------------LAKNTAITWEDK---- 69
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWTDR----------HSEELKRGITIrlgyadatirkcpdCEEPEAYTTEPKcpnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 70 --KTGIKNRINIVDTPGHadfggeveRVL--------SMVDTVLILVDA-MDGPMPQTR--FVTQKafAMGFKPIVVV-N 135
Cdd:PRK04000 78 gsETELLRRVSFVDAPGH--------ETLmatmlsgaALMDGAILVIAAnEPCPQPQTKehLMALD--IIGIKNIVIVqN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 136 KVdrpgarpewvidqvfDLFDKLGAT---NEQLDF---------PIVYASGLNGYagledtvrdgDMTPLYEAIMQHAPR 203
Cdd:PRK04000 148 KI---------------DLVSKERALenyEQIKEFvkgtvaenaPIIPVSALHKV----------NIDALIEAIEEEIPT 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 692318981 204 PEVDPEGPFQMRISQ-LDYN-------NFV-GVIGiGRIQRGTLK 239
Cdd:PRK04000 203 PERDLDKPPRMYVARsFDVNkpgtppeKLKgGVIG-GSLIQGVLK 246
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
8-138 |
1.16e-09 |
|
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: 58.35 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSGTLSE--------RTVLAER--------VMDSNDQEKERGITIlakNTAITW--EDK 69
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKSIFEdqlaalerSKSSGTQgekldlalLVDGLQAEREQGITI---DVAYRYfsTPK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 70 KTGIknrinIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVD 138
Cdd:cd04166 78 RKFI-----IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMD 142
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
8-138 |
4.21e-08 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 53.81 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqSGTLSERtvlaervmdsNDQEKERGITIlaK----NTAITWEDK-------------- 69
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVWTVR----------HKEELKRNITI--KlgyaNAKIYKCPNcgcprpydtpecec 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 70 -----KTGIKNRINIVDTPGHadfggeveRVL--------SMVDTVLILVDAMDG-PMPQTRfvtQKAFA---MGFKPIV 132
Cdd:cd01888 67 pgcggETKLVRHVSFVDCPGH--------EILmatmlsgaAVMDGALLLIAANEPcPQPQTS---EHLAAleiMGLKHII 135
|
....*..
gi 692318981 133 VV-NKVD 138
Cdd:cd01888 136 ILqNKID 142
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
212-296 |
9.59e-08 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 49.57 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 212 FQMRISQLDYNNFVGVIGIGRIQRGTLKKNMQVAVIdreGKKRNGKVLQVLGFMGleriEQDTAEAGDIVAIS--GIQEL 289
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRIL---PKGITGRVTSIERFHE----EVDEAKAGDIVGIGilGVKDI 73
|
....*..
gi 692318981 290 TISDTIC 296
Cdd:cd01342 74 LTGDTLT 80
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
8-239 |
1.31e-07 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 54.07 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLlkqSGTLSertvlaervmDSNDQEKERGITI--------------LAKNTAITWE------ 67
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWT----------DRHSEELKRGITIrlgyadatfykcpnCEPPEAYTTEpkcpnc 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 68 DKKTGIKNRINIVDTPGHAdfggevervlSMVDTVLILVDAMDG-----------PMPQTR--FVTQKafAMGFKPIVVV 134
Cdd:COG5257 74 GSETELLRRVSFVDAPGHE----------TLMATMLSGAALMDGailviaanepcPQPQTKehLMALD--IIGIKNIVIV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 135 -NKVD---RPGARPEWviDQVFDLFDKLGATNEqldfPIVYASGLNGYagledtvrdgDMTPLYEAIMQHAPRPEVDPEG 210
Cdd:COG5257 142 qNKIDlvsKERALENY--EQIKEFVKGTVAENA----PIIPVSAQHKV----------NIDALIEAIEEEIPTPERDLSK 205
|
250 260 270
....*....|....*....|....*....|....*...
gi 692318981 211 PFQMRISQ-LDYN-------NFVG-VIGiGRIQRGTLK 239
Cdd:COG5257 206 PPRMLVARsFDVNkpgtppkDLKGgVIG-GSLIQGVLK 242
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
409-485 |
2.21e-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: 48.68 E-value: 2.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 409 EPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGkGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRG-GWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
3-144 |
1.15e-06 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 51.72 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 3 IENLRN--IAIVAHVDHGKTTLVDqllKQSGTlsertvlaeRVmdsndQEKERG-IT--ILAknTAITW-------EDKK 70
Cdd:PRK04004 1 EKKLRQpiVVVLGHVDHGKTTLLD---KIRGT---------AV-----AAKEAGgITqhIGA--TEVPIdviekiaGPLK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 71 TGIKNRINI-----VDTPGHADF------GGevervlSMVDTVLILVDAMDGPMPQTRFVTQ--KAFAMGFkpIVVVNKV 137
Cdd:PRK04004 62 KPLPIKLKIpgllfIDTPGHEAFtnlrkrGG------ALADIAILVVDINEGFQPQTIEAINilKRRKTPF--VVAANKI 133
|
....*...
gi 692318981 138 DR-PGARP 144
Cdd:PRK04004 134 DRiPGWKS 141
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
226-298 |
1.82e-06 |
|
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: 46.44 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 226 GVIGIGRIQRGTLKKNMQVAVI------DREGKKRNGKVLQVLGFMGLERIEQDTAEAGDIVAISGI-QELTISDTICAP 298
Cdd:cd16268 17 GFVAFGRVFSGTVRRGQEVYILgpkyvpGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGLdDFLAKSGTTTSS 96
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
71-212 |
3.02e-06 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 49.22 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 71 TGIKNR----INIVDTPG-----HAdFG----GEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKV 137
Cdd:COG1159 43 RGIVTRedaqIVFVDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKI 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692318981 138 DRpgARPEwvidqvfDLFDKLGATNEQLDF-PIVYASGLNGYaGLEDtvrdgdmtpLYEAIMQHAprpevdPEGPF 212
Cdd:COG1159 122 DL--VKKE-------ELLPLLAEYSELLDFaEIVPISALKGD-NVDE---------LLDEIAKLL------PEGPP 172
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
408-485 |
4.49e-06 |
|
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: 45.19 E-value: 4.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692318981 408 MEPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGkGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:smart00838 2 LEPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRG-GAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
15-310 |
5.25e-06 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 49.14 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 15 VDHGKTTLVDQLL------------------KQSGTLSERTVLAERVmDSNDQEKERGITI-LAKNTAITweDKKTGIkn 75
Cdd:PRK05124 36 VDDGKSTLIGRLLhdtkqiyedqlaslhndsKRHGTQGEKLDLALLV-DGLQAEREQGITIdVAYRYFST--EKRKFI-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 76 rinIVDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVV-VNKVDRPG---ARPEWVIDQV 151
Cdd:PRK05124 111 ---IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVaVNKMDLVDyseEVFERIREDY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 152 FDLFDKLGAtneQLDFPIVYASGLNGyaglEDTVRDGDMTPLYEA-----IMQHAPRPEVDPEGPFQM---RISQ--LDY 221
Cdd:PRK05124 188 LTFAEQLPG---NLDIRFVPLSALEG----DNVVSQSESMPWYSGptlleVLETVDIQRVVDAQPFRFpvqYVNRpnLDF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 222 NNFVGVIGIGRIQRGtlkknmQVAVIDREGKKrnGKVLQVLGFMGleriEQDTAEAGDIVAISGIQELTIS--DTICAPD 299
Cdd:PRK05124 261 RGYAGTLASGVVKVG------DRVKVLPSGKE--SNVARIVTFDG----DLEEAFAGEAITLVLEDEIDISrgDLLVAAD 328
|
330
....*....|..
gi 692318981 300 -TPEALPALTVD 310
Cdd:PRK05124 329 eALQAVQHASAD 340
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
5-292 |
1.19e-05 |
|
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: 48.27 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 5 NLRN--IAIVAHVDHGKTTLVDQLLKQSGTLSERTVLAERVMDSndqekERGITILAKNTAITWedKKTGIKNRIN---I 79
Cdd:TIGR00491 1 RLRQpiVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAS-----EVPTDVIEKICGDLL--KSFKIKLKIPgllF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 80 VDTPGHADFGGEVERVLSMVDTVLILVDAMDGPMPQTRFVTQ--KAFAMGFkpIVVVNKVDRPgarPEWvidqvfdlfdk 157
Cdd:TIGR00491 74 IDTPGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNilRSRKTPF--VVAANKIDRI---PGW----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 158 lgatNEQLDFPIvyasgLNGYAGLEDTVRDGDMTPLYEAIMQHAprpEVDPEGPFQMRISqlDYNNFVGVIGI------- 230
Cdd:TIGR00491 138 ----KSHEGYPF-----LESINKQEQRVRQNLDKQVYNLVIQLA---EQGFNAERFDRIR--DFTKTVAIIPVsaktgeg 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692318981 231 ---------GRIQRgTLKKNMQVAVidrEGKKRnGKVLQV-----LGFMGLERIEQDTAEAGDIVAISGIQELTIS 292
Cdd:TIGR00491 204 ipellailaGLAQN-YLENKLKLAI---EGPAK-GTILEVkeeqgLGYTIDAVIYDGILRKGDIIVLAGIDDVIVT 274
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
9-197 |
1.55e-05 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 45.74 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 9 IAIVAHVDHGKTTLVDQLLkqsgtlsERTVLAERVMDSNdqekerGITIlaKNTAITWEDKKTgiknRINIVDTPGHADF 88
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLV-------GDIFSLEKYLSTN------GVTI--DKKELKLDGLDV----DLVIWDTPGQDEF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 89 ---GGEVERVLSMVDTVLILVDAmdgpmpqTRFVTQKAFAM---------GFKPIVVV-NKVDRpgaRPEWVIDQVFDLF 155
Cdd:COG1100 67 retRQFYARQLTGASLYLFVVDG-------TREETLQSLYElleslrrlgKKSPIILVlNKIDL---YDEEEIEDEERLK 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 692318981 156 DKLGATNEQldfPIVYASGLNGYagledtvrdgDMTPLYEAI 197
Cdd:COG1100 137 EALSEDNIV---EVVATSAKTGE----------GVEELFAAL 165
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
9-178 |
2.00e-05 |
|
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: 45.50 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 9 IAIVAHVDHGKTTLVDQLLKQsgtlsertvlaERVMDSNdqekERGITILAKNTAITWEDKKtgiknrINIVDTPG---- 84
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQK------YTLIDTAGirkk 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 85 -HADFGGE------VERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNK---VDRPGARPEWVIDQVFDL 154
Cdd:cd01895 64 gKVTEGIEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKwdlVEKDEKTMKEFEKELRRK 143
|
170 180
....*....|....*....|....*
gi 692318981 155 FDklgatneQLDF-PIVYASGLNGY 178
Cdd:cd01895 144 LP-------FLDYaPIVFISALTGQ 161
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
71-212 |
2.65e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 46.19 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 71 TGIKNR----INIVDTPG----HADFG----GEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVD 138
Cdd:PRK00089 45 RGIVTEddaqIIFVDTPGihkpKRALNramnKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKID 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692318981 139 RPGARPEwvidqvfdLFDKLGATNEQLDF-PIVYASGLNGYaGLEDtvrdgdmtpLYEAIMQHAprpevdPEGPF 212
Cdd:PRK00089 125 LVKDKEE--------LLPLLEELSELMDFaEIVPISALKGD-NVDE---------LLDVIAKYL------PEGPP 175
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
71-177 |
8.16e-05 |
|
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: 43.60 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 71 TGIKNR----INIVDTPG-HADFGG-------EVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVD 138
Cdd:cd04163 43 RGIYTDddaqIIFVDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKID 122
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 692318981 139 RPGARpewviDQVFDLFDKLgatNEQLDF-PIVYASGLNG 177
Cdd:cd04163 123 LVKDK-----EDLLPLLEKL---KELHPFaEIFPISALKG 154
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
409-485 |
1.26e-04 |
|
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.
Pssm-ID: 239682 [Multi-domain] Cd Length: 78 Bit Score: 40.68 E-value: 1.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 409 EPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGkGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFEDPQIKG-DEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRP 76
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
8-172 |
1.32e-04 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 42.92 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKQSgtlsertVLAERVmdsndqekergITILAKNTAITWedkktGIKNRINIVDTPG--- 84
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLGEE-------VLPTGV-----------TPTTAVITVLRY-----GLLKGVVLVDTPGlns 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 85 ----HADfggEVERVLSMVDTVLILVDAmDGPMPQT--RFVTQKAFAMGFKPIVVVNKVDRpgARPEWVIDQVFDLFDKL 158
Cdd:cd09912 59 tiehHTE---ITESFLPRADAVIFVLSA-DQPLTESerEFLKEILKWSGKKIFFVLNKIDL--LSEEELEEVLEYSREEL 132
|
170
....*....|....
gi 692318981 159 GATNEQLDFPIVYA 172
Cdd:cd09912 133 GVLELGGGEPRIFP 146
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
64-217 |
2.31e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 43.86 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 64 ITWEDKktgiknRINIVDTPG-----HADFGGE----VERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGfKP-IVV 133
Cdd:COG1160 45 AEWGGR------EFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPvILV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 134 VNKVDRPGARPEwvidqVFDLFdKLGatneqLD--FPIvyaSGLNGYaGLEDtvrdgdmtpLYEAIMQHAPRPEVDPEGP 211
Cdd:COG1160 118 VNKVDGPKREAD-----AAEFY-SLG-----LGepIPI---SAEHGR-GVGD---------LLDAVLELLPEEEEEEEED 173
|
....*.
gi 692318981 212 FQMRIS 217
Cdd:COG1160 174 DPIKIA 179
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
221-296 |
2.37e-04 |
|
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.
Pssm-ID: 293900 [Multi-domain] Cd Length: 86 Bit Score: 40.09 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 221 YNNFVGVIGIGRIQRGTLKKNMQVAVIdregkkRNGKVLQV--LGFMGLERIEQDTAEAGD---IVA-ISGIQELTISDT 294
Cdd:cd03699 10 YDPYRGVVVLVRVFDGTLKKGDKIRFM------ATGKEYEVleVGVFTPKMVPTDELSAGEvgyIIAgIKSVKDARVGDT 83
|
..
gi 692318981 295 IC 296
Cdd:cd03699 84 IT 85
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
92-174 |
3.16e-04 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 41.53 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 92 VERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKVDrpgARPEWVIDQVFDLFDKLGatneqldFPIVY 171
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVFESEG-------LPVVY 74
|
...
gi 692318981 172 ASG 174
Cdd:cd01859 75 VSA 77
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
409-472 |
4.31e-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: 39.40 E-value: 4.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692318981 409 EPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGKGRVRLEYSIPARGLI-GFQNEFKTLTQG 472
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIVyDFFDKLKSISKG 65
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
409-485 |
7.39e-04 |
|
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-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: 239764 [Multi-domain] Cd Length: 78 Bit Score: 38.46 E-value: 7.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692318981 409 EPIEQLVVDIEEIHQGGVMEKLGTRKGQLKNMESDGkGRVRLEYSIPARGLIGFQNEFKTLTQGSGLLFHVFDHYGP 485
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGE-DEFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRYAP 76
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
9-178 |
7.97e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.34 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 9 IAIVAHVDHGKTTLVDQLLKQsgtlsertvlaERVMDSNdqekERGITILAKNTAITWEDKKtgiknrINIVDTPG---- 84
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQK------YTLIDTAGirrk 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 85 ---HADfggeVE--------RVLSMVDTVLILVDAMDGpmpqtrFVTQKAFAMGF-----KPIV-VVNKVDrpgARPEWV 147
Cdd:PRK00093 235 gkvTEG----VEkysvirtlKAIERADVVLLVIDATEG------ITEQDLRIAGLaleagRALViVVNKWD---LVDEKT 301
|
170 180 190
....*....|....*....|....*....|...
gi 692318981 148 IDQVFDLFD-KLGatneQLDF-PIVYASGLNGY 178
Cdd:PRK00093 302 MEEFKKELRrRLP----FLDYaPIVFISALTGQ 330
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
8-136 |
8.39e-04 |
|
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: 39.52 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 8 NIAIVAHVDHGKTTLVDQLLKqsgtlseRTVLAERVMdsndqekerGITILAKNTAITWEDKKtgiknrINIVDTPG--- 84
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTG-------AKAIVSDYP---------GTTRDPNEGRLELKGKQ------IILVDTPGlie 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 692318981 85 --HADFG-GEVERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNK 136
Cdd:pfam01926 59 gaSEGEGlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
232-295 |
1.24e-03 |
|
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II 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: 293891 [Multi-domain] Cd Length: 86 Bit Score: 37.99 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692318981 232 RIQRGTLKKNMQVAVIDREGKkrnGKVLQVLGFMGLERIEQDTAEAGDIVAISGIQELTISDTI 295
Cdd:cd03690 24 RLYSGTLRLRDSVRVSGEEEK---IKITELRTFENGELVKVDRVYAGDIAILVGLKSLRVGDVL 84
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
343-387 |
1.25e-03 |
|
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.
Pssm-ID: 464188 [Multi-domain] Cd Length: 75 Bit Score: 37.85 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 692318981 343 KDRLDREKVHNV---------ALKVEQLEDADKFLVSGRGELHLSVLIENMRRE 387
Cdd:pfam14492 13 KTKGDEDKLSKAlnrlleedpTLRVERDEETGETILSGMGELHLEIVVDRLKRK 66
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
64-200 |
1.31e-03 |
|
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: 39.73 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 64 ITWEDKKtgiknrINIVDTPGHADFGGE--------VERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVN 135
Cdd:cd01894 40 AEWGGRE------FILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVN 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692318981 136 KVDrpGARPEWVIDQvfdlFDKLGATNeqldfpIVYASGLNGYaGLEDtvrdgdmtpLYEAIMQH 200
Cdd:cd01894 114 KID--NIKEEEEAAE----FYSLGFGE------PIPISAEHGR-GIGD---------LLDAILEL 156
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
64-217 |
1.82e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 41.19 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 64 ITWEDKKtgiknrINIVDTPG----HADFGGEV----ERVLSMVDTVLILVDAMDGPMPQTRFVTQKAFAMGfKP-IVVV 134
Cdd:PRK00093 44 AEWLGRE------FILIDTGGiepdDDGFEKQIreqaELAIEEADVILFVVDGRAGLTPADEEIAKILRKSN-KPvILVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 135 NKVDRPGARpewviDQVFDlFDKLGATNEqldFPIvyaSGLNGYaGLEDtvrdgdmtpLYEAIMQHAPRPEVDPEGPFQM 214
Cdd:PRK00093 117 NKVDGPDEE-----ADAYE-FYSLGLGEP---YPI---SAEHGR-GIGD---------LLDAILEELPEEEEEDEEDEPI 174
|
...
gi 692318981 215 RIS 217
Cdd:PRK00093 175 KIA 177
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
356-387 |
3.80e-03 |
|
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. 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 of the yeast homolog of mtEFG2, MEF2.
Pssm-ID: 293919 [Multi-domain] Cd Length: 76 Bit Score: 36.28 E-value: 3.80e-03
10 20 30
....*....|....*....|....*....|..
gi 692318981 356 LKVEQLEDADKFLVSGRGELHLSVLIENMRRE 387
Cdd:cd16262 34 LRVSRDEETGQTILSGMGELHLEIIVERLKRE 65
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
10-145 |
3.90e-03 |
|
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: 38.38 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318981 10 AIVAHVDHGKTTLVDQLLKQ-SGTLSER---TVLAERVmdsndqekergitilakntaiTWEDKKTGiknRINIVDTPGH 85
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQnVGIVSPIpgtTRDPVRK---------------------EWELLPLG---PVVLIDTPGL 56
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692318981 86 ADFGG-------EVERVLSMVDTVLILVDAmDGPMPQTRFVTQKAFAMGfKPIVVV-NKVDRPGARPE 145
Cdd:cd00880 57 DEEGGlgrerveEARQVADRADLVLLVVDS-DLTPVEEEAKLGLLRERG-KPVLLVlNKIDLVPESEE 122
|
|
| |
