|
Name |
Accession |
Description |
Interval |
E-value |
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
3-609 |
0e+00 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 1180.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 3 NKREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHA 82
Cdd:COG1217 1 MMREDIRNIAIIAHVDHGKTTLVDALLKQSGTFRENQEVAERVMDSNDLERERGITILAKNTAVRYKGVKINIVDTPGHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 83 DFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLE 162
Cdd:COG1217 81 DFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVFDLFIELGATDEQLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 163 FPVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSL 242
Cdd:COG1217 161 FPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 243 IKLDGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVTPHDHQEALPVLRIDEPTLEMTFKVNNSPFA 322
Cdd:COG1217 241 IKRDGKVEKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDINIGDTICDPENPEALPPIKIDEPTLSMTFSVNDSPFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 323 GREGDFVTARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRREGYELQVSKPQVIIKEIDGVMCEP 402
Cdd:COG1217 321 GREGKFVTSRQIRERLEKELETNVALRVEETDSPDAFKVSGRGELHLSILIETMRREGYELQVSRPEVIFKEIDGKKLEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 403 FERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRPrIKAQ 482
Cdd:COG1217 401 IEELTIDVPEEYSGAVIEKLGQRKGEMTNMEPDGGGRVRLEFLIPSRGLIGFRTEFLTDTRGTGIMNHVFDGYEP-YKGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 483 IGGRRNGALISMDQGSASTYAILGLEDRGVNFMEPGTEVYEGMIVGEHNRENDLTVNITKTKHQTNVRSATKDQTQTMNR 562
Cdd:COG1217 480 IPGRRNGSLISMETGKATAYALFNLQERGTLFIGPGTEVYEGMIVGEHSRDNDLVVNVCKEKKLTNMRASGSDEAIRLTP 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1799428405 563 PRILTLEEALQFINDDELVEVTPESIRLRKKILNKNVREKEAKRIKQ 609
Cdd:COG1217 560 PRKMSLEQALEFIEDDELVEVTPKSIRLRKKILDENERKRAAKKKKK 606
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
8-602 |
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: 1009.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 8 VRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGE 87
Cdd:TIGR01394 1 IRNIAIIAHVDHGKTTLVDALLKQSGTFRANEAVAERVMDSNDLERERGITILAKNTAIRYNGTKINIVDTPGHADFGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 88 VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLEFPVVY 167
Cdd:TIGR01394 81 VERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVFDLFAELGADDEQLDFPIVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 168 ASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIKLDG 247
Cdd:TIGR01394 161 ASGRAGWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 248 TVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVTPHDHQEALPVLRIDEPTLEMTFKVNNSPFAGREGD 327
Cdd:TIGR01394 241 TIENGRISKLLGFEGLERVEIDEAGAGDIVAVAGLEDINIGETIADPEVPEALPTITVDEPTLSMTFSVNDSPLAGKEGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 328 FVTARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRREGYELQVSKPQVIIKEIDGVMCEPFERVQ 407
Cdd:TIGR01394 321 KVTSRHIRDRLMRELETNVALRVEDTESADKFEVSGRGELHLSILIETMRREGFELQVGRPQVIYKEIDGKKLEPIEELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 408 CEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRPrIKAQIGGRR 487
Cdd:TIGR01394 401 IDVPEEHVGAVIEKLGKRKGEMVDMEPSGNGRTRLEFKIPSRGLIGFRTEFLTDTRGTGIMNHVFDEYEP-WKGEIETRR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 488 NGALISMDQGSASTYAILGLEDRGVNFMEPGTEVYEGMIVGEHNRENDLTVNITKTKHQTNVRSATKDQTQTMNRPRILT 567
Cdd:TIGR01394 480 NGSLVSMEDGTATAYALWNLQERGVMFVSPGTEVYEGMIIGEHSRENDLDVNPCKAKKLTNVRSSGKDEAVKLTPPRKLS 559
|
570 580 590
....*....|....*....|....*....|....*
gi 1799428405 568 LEEALQFINDDELVEVTPESIRLRKKILNKNVREK 602
Cdd:TIGR01394 560 LEQALEYIEDDELVEVTPKSIRLRKRVLDPNERKR 594
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
6-609 |
0e+00 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 666.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 6 EDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFG 85
Cdd:PRK10218 3 EKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 86 GEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLEFPV 165
Cdd:PRK10218 83 GEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 166 VYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIKL 245
Cdd:PRK10218 163 VYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 246 DGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVTPHDHQEALPVLRIDEPTLEMTFKVNNSPFAGRE 325
Cdd:PRK10218 243 EGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 326 GDFVTARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRREGYELQVSKPQVIIKEIDGVMCEPFER 405
Cdd:PRK10218 323 GKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYEN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 406 VQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRPRIKAQIGG 485
Cdd:PRK10218 403 VTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVGQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 486 RRNGALISMDQGSASTYAILGLEDRGVNFMEPGTEVYEGMIVGEHNRENDLTVNITKTKHQTNVRSATKDQTQTMNRPRI 565
Cdd:PRK10218 483 RQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIR 562
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1799428405 566 LTLEEALQFINDDELVEVTPESIRLRKKILNKNVREKEAKRIKQ 609
Cdd:PRK10218 563 MTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKD 606
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
7-200 |
2.35e-134 |
|
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: 390.42 E-value: 2.35e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 7 DVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGG 86
Cdd:cd01891 1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRENEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 EVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLEFPVV 166
Cdd:cd01891 81 EVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVFDLFLELNATDEQLDFPIV 160
|
170 180 190
....*....|....*....|....*....|....
gi 1799428405 167 YASAVNGTASLDPEKQDDNLQSLYETIIDYVPAP 200
Cdd:cd01891 161 YASAKNGWASLNLDDPSEDLDPLFETIIEHVPAP 194
|
|
| lepA |
TIGR01393 |
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ... |
8-477 |
2.40e-72 |
|
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]
Pssm-ID: 130460 [Multi-domain] Cd Length: 595 Bit Score: 243.77 E-value: 2.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 8 VRNIAIIAHVDHGKTTLVDELLKQSGIFRENEhVDERAMDSNDIERERGITILAKNTAVDYK-----GTRINILDTPGHA 82
Cdd:TIGR01393 3 IRNFSIIAHIDHGKSTLADRLLEYTGAISERE-MREQVLDSMDLERERGITIKAQAVRLNYKakdgeTYVLNLIDTPGHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 83 DFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLfIELEANDeqle 162
Cdd:TIGR01393 82 DFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKKEIEEV-IGLDASE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 163 fpVVYASAVNGTasldpekqddNLQSLYETIIDYVPAPIDNSDEPLQfqvALL-D--YNDYVGRIGIGRVFRGKMRVGDN 239
Cdd:TIGR01393 157 --AILASAKTGI----------GIEEILEAIVKRVPPPKGDPDAPLK---ALIfDshYDNYRGVVALVRVFEGTIKPGDK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 240 vslIKLDGTVKNFRVTKIfGYFGLKRLEIEEAQAGD---LIA-VSGMEDINVGETVTPHDHQ--EALPVLRideptlemt 313
Cdd:TIGR01393 222 ---IRFMSTGKEYEVDEV-GVFTPKLTKTDELSAGEvgyIIAgIKDVSDVRVGDTITHVKNPakEPLPGFK--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 314 fKVNNSPFAG----REGDFVTARQIQERLnqQLeTDVSLkvsnTDSPDTWVVAGR-------GELHLSILIENMRREgYE 382
Cdd:TIGR01393 289 -EVKPMVFAGlypiDTEDYEDLRDALEKL--KL-NDASL----TYEPESSPALGFgfrcgflGLLHMEIIQERLERE-FN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 383 LQV--SKPQVIIK---------------------EIDGVMcEPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGL 439
Cdd:TIGR01393 360 LDLitTAPSVIYRvyltngevievdnpsdlpdpgKIEHVE-EPYVKATIITPTEYLGPIMTLCQEKRGVQTNMEYLDPNR 438
|
490 500 510
....*....|....*....|....*....|....*....
gi 1799428405 440 TRLIFNVP-ARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:TIGR01393 439 VELIYEMPlAEIVYDFFDKLKSISRGYASFDYELIGYRP 477
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
6-199 |
9.94e-71 |
|
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: 226.25 E-value: 9.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 6 EDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVD---ERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHA 82
Cdd:pfam00009 1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKgegEAGLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 83 DFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPS-ARPEGVVDEVLDLFIELEANDEqL 161
Cdd:pfam00009 81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEVSRELLEKYGEDG-E 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1799428405 162 EFPVVYASAVNGtasldpekqdDNLQSLYETIIDYVPA 199
Cdd:pfam00009 160 FVPVVPGSALKG----------EGVQTLLDALDEYLPS 187
|
|
| LepA |
COG0481 |
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ... |
4-477 |
1.32e-68 |
|
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440249 [Multi-domain] Cd Length: 598 Bit Score: 233.76 E-value: 1.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 4 KREDVRNIAIIAHVDHGKTTLVDELLKQSGIfrenehVDERAM-----DSNDIERERGITILAKNTAVDYKGT-----RI 73
Cdd:COG0481 2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGT------LSEREMkeqvlDSMDLERERGITIKAQAVRLNYKAKdgetyQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 74 NILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLfIE 153
Cdd:COG0481 76 NLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKIDLPSADPERVKQEIEDI-IG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 154 LEANDeqlefpVVYASAVNGTasldpekqddNLQSLYETIIDYVPAPIDNSDEPLQfqvALL-D--YNDYVGRIGIGRVF 230
Cdd:COG0481 155 IDASD------AILVSAKTGI----------GIEEILEAIVERIPPPKGDPDAPLQ---ALIfDswYDSYRGVVVYVRVF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 231 RGKMRVGDNvslIKLDGTVKNFRVTKIfGYFGLKRLEIEEAQAGD---LIAvsGM---EDINVGETVTPHDH--QEALPv 302
Cdd:COG0481 216 DGTLKKGDK---IKMMSTGKEYEVDEV-GVFTPKMTPVDELSAGEvgyIIA--GIkdvRDARVGDTITLAKNpaAEPLP- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 303 lrideptlemTFK-VNNSPFAG----REGDFVTARQIQERLnqQLeTDVSLkvsnTDSPDTWVVAG---R----GELHLS 370
Cdd:COG0481 289 ----------GFKeVKPMVFAGlypvDSDDYEDLRDALEKL--QL-NDASL----TYEPETSAALGfgfRcgflGLLHME 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 371 ILIENMRRE--------------------GYELQVSKPQVI-----IKEIDgvmcEPFERVQCEVPQENAGAVIESLGAR 425
Cdd:COG0481 352 IIQERLEREfdldlittapsvvyevtltdGEVIEVDNPSDLpdpgkIEEIE----EPIVKATIITPSEYVGAVMELCQEK 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1799428405 426 KGEMVDMTTTDNGLTRLIFNVPARGMIgytTEFM----SMTRGYGIINHTFEEFRP 477
Cdd:COG0481 428 RGVQKNMEYLGENRVELTYELPLAEIV---FDFFdrlkSITRGYASLDYEFIGYRE 480
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
1-477 |
1.09e-58 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 208.65 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 1 MTNKREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERA--MDSNDIERERGITILAKNTAVDYKGTRINILDT 78
Cdd:PRK13351 1 AEMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTtvTDWMPQEQERGITIESAATSCDWDNHRINLIDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 79 PGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKID---------------KPSARP--- 140
Cdd:PRK13351 81 PGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDrvgadlfkvledieeRFGKRPlpl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 141 ----------EGVVD-----------------------------------------------EVLDLFIELEA-NDEQLE 162
Cdd:PRK13351 161 qlpigsedgfEGVVDlitepelhfsegdggstveegpipeelleeveearekliealaefddELLELYLEGEElSAEQLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 163 ------------FPVVYASAvngtasldpeKQDDNLQSLYETIIDYVPAPID------------------NSDEPLQFQV 212
Cdd:PRK13351 241 aplregtrsghlVPVLFGSA----------LKNIGIEPLLDAVVDYLPSPLEvppprgskdngkpvkvdpDPEKPLLALV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 213 ALLDYNDYVGRIGIGRVFRGKMRVGDNVslikLDGTVKN-FRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETV 291
Cdd:PRK13351 311 FKVQYDPYAGKLTYLRVYSGTLRAGSQL----YNGTGGKrEKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 292 TPHDHQEALPVLRIDEPTLEMTFKvnnspfAGREGDfvtaRQ-IQERLNQQLETDVSLKVS-NTDSPDTwVVAGRGELHL 369
Cdd:PRK13351 387 HDSADPVLLELLTFPEPVVSLAVE------PERRGD----EQkLAEALEKLVWEDPSLRVEeDEETGQT-ILSGMGELHL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 370 SILIENMRRE-GYELQVSKPQVIIKE------------------------------------------------------ 394
Cdd:PRK13351 456 EVALERLRREfKLEVNTGKPQVAYREtirkmaegvyrhkkqfggkgqfgevhlrveplergagfifvskvvggaipeeli 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 395 ----------------------------IDG-----------------------------VMCEPFERVQCEVPQENAGA 417
Cdd:PRK13351 536 pavekgirealasgplagypvtdlrvtvLDGkyhpvdssesafkaaarkafleafrkanpVLLEPIMELEITVPTEHVGD 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 418 VIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:PRK13351 616 VLGDLSQRRGRIEGTEPRGDGEVLVKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDP 675
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
1-390 |
3.67e-58 |
|
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: 207.21 E-value: 3.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 1 MTNKR-EDVRNIAIIAHVDHGKTTLVDELLKQSG-IFRENEhVDERA--MDSNDIERERGITILAKNTAVDYKGTRINIL 76
Cdd:COG0480 1 MAEYPlEKIRNIGIVAHIDAGKTTLTERILFYTGaIHRIGE-VHDGNtvMDWMPEEQERGITITSAATTCEWKGHKINII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 77 DTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDE---------- 146
Cdd:COG0480 80 DTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQlkerlganpv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 147 --------------VLDLF-----------------------------------IEL--EANDEQLE------------- 162
Cdd:COG0480 160 plqlpigaeddfkgVIDLVtmkayvyddelgakyeeeeipaelkeeaeeareelIEAvaETDDELMEkylegeelteeei 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 163 -------------FPVVYASAVNGTAsldpekqddnLQSLYETIIDYVPAPID-------------------NSDEPLqf 210
Cdd:COG0480 240 kaglrkatlagkiVPVLCGSAFKNKG----------VQPLLDAVVDYLPSPLDvpaikgvdpdtgeeverkpDDDEPF-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 211 qVALL--DYND-YVGRIGIGRVFRGKMRVGDNV--SlikldGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDI 285
Cdd:COG0480 308 -SALVfkTMTDpFVGKLSFFRVYSGTLKSGSTVynS-----TKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 286 NVGETVTPHDHQEALPVLRIDEPTLEMTFKVNNspfagrEGDfvtarqiQERLNQQL----ETDVSLKVS-NTDSPDTwV 360
Cdd:COG0480 382 TTGDTLCDEDHPIVLEPIEFPEPVISVAIEPKT------KAD-------EDKLSTALaklaEEDPTFRVEtDEETGQT-I 447
|
490 500 510
....*....|....*....|....*....|.
gi 1799428405 361 VAGRGELHLSILIENMRRE-GYELQVSKPQV 390
Cdd:COG0480 448 ISGMGELHLEIIVDRLKREfGVEVNVGKPQV 478
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
3-404 |
4.23e-57 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 205.10 E-value: 4.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 3 NKREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAV--DYKGTR--INILDT 78
Cdd:PRK07560 15 KNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISEELAGEQLALDFDEEEQARGITIKAANVSMvhEYEGKEylINLIDT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 79 PGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDK--------PS---ARPEGVVDEV 147
Cdd:PRK07560 95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRlikelkltPQemqQRLLKIIKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 148 LDLfIELEANDE-----QLEF---PVVYASAVNGTASLDPEKQ--------------DDNLQSL------YETIID---- 195
Cdd:PRK07560 175 NKL-IKGMAPEEfkekwKVDVedgTVAFGSALYNWAISVPMMQktgikfkdiidyyeKGKQKELaekaplHEVVLDmvvk 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 196 YVPAPID-------------------------NSDEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIkldGTVK 250
Cdd:PRK07560 254 HLPNPIEaqkyripkiwkgdlnsevgkamlncDPNGPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLV---GAKK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 251 NFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVTphDHQEALPVLRID---EPTLEMTfkvnnspfagregd 327
Cdd:PRK07560 331 KNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVV--SVEDMTPFESLKhisEPVVTVA-------------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 328 fVTARQIQ------ERLNQQLETDVSLKVS-NTDSPDTwVVAGRGELHLSILIENMRRE-GYELQVSKPQVIIKEIDGVM 399
Cdd:PRK07560 395 -IEAKNPKdlpkliEVLRQLAKEDPTLVVKiNEETGEH-LLSGMGELHLEVITYRIKRDyGIEVVTSEPIVVYRETVRGK 472
|
....*
gi 1799428405 400 CEPFE 404
Cdd:PRK07560 473 SQVVE 477
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
4-394 |
1.09e-55 |
|
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: 200.89 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 4 KREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAV--DYKGTR--INILDTP 79
Cdd:TIGR00490 15 KPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvhEYEGNEylINLIDTP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 80 GHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDE 159
Cdd:TIGR00490 95 GHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQERFIKIITEVN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 160 QL-------EFP-----------VVYASAVNGTASLDP------------------EKQDDNLQS--LYETIIDYV---- 197
Cdd:TIGR00490 175 KLikamapeEFRdkwkvrvedgsVAFGSAYYNWAISVPsmkktgigfkdiykyckeDKQKELAKKspLHQVVLDMVirhl 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 198 PAPID--------------NSDE-----------PLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIklDGTVKNf 252
Cdd:TIGR00490 255 PSPIEaqkyripviwkgdlNSEVgkamlncdpkgPLALMITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIV--DRKAKA- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 253 RVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETV-TPHDHQEALPVLR-IDEPTLEMTFKVNNSPfagregdfvT 330
Cdd:TIGR00490 332 RIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETIcTTVENITPFESIKhISEPVVTVAIEAKNTK---------D 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799428405 331 ARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRRE-GYELQVSKPQVIIKE 394
Cdd:TIGR00490 403 LPKLIEVLRQVAKEDPTVHVEINEETGEHLISGMGELHLEIIVEKIREDyGLDVETSPPIVVYRE 467
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
14-477 |
4.32e-53 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 192.65 E-value: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 14 IAHVDHGKTTLVDELLKQSG-IFRENEhVDERA--MDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGEVER 90
Cdd:PRK12740 1 VGHSGAGKTTLTEAILFYTGaIHRIGE-VEDGTttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 91 IMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDE------------------------ 146
Cdd:PRK12740 80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQlqeklgapvvplqlpigegddftg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 147 VLDLF---------------------------------IE--LEANDEQLE--------------------------FPV 165
Cdd:PRK12740 160 VVDLLsmkayrydeggpseeieipaelldraeeareelLEalAEFDDELMEkylegeelseeeikaglrkatlageiVPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 166 VYASAVNGTAsldpekqddnLQSLYETIIDYVPAPID-----------------NSDEPLQFQVALLDYNDYVGRIGIGR 228
Cdd:PRK12740 240 FCGSALKNKG----------VQRLLDAVVDYLPSPLEvppvdgedgeegaelapDPDGPLVALVFKTMDDPFVGKLSLVR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 229 VFRGKMRVGDNVsliKLDGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVTPHDHQEALPVLRIDEP 308
Cdd:PRK12740 310 VYSGTLKKGDTL---YNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKGDPILLEPMEFPEP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 309 TLEMTFKvnnspfAGREGDfvtarqiQERLNQQL----ETDVSLKVS-NTDSPDTwVVAGRGELHLSILIENMRRE-GYE 382
Cdd:PRK12740 387 VISLAIE------PKDKGD-------EEKLSEALgklaEEDPTLRVErDEETGQT-ILSGMGELHLDVALERLKREyGVE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 383 LQVSKPQVIIKE-------------------------------------------------------------------- 394
Cdd:PRK12740 453 VETGPPQVPYREtirkkaeghgrhkkqsgghgqfgdvwleveplprgegfefvdkvvggavprqyipavekgvrealekg 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 395 --------------IDG-----------------------------VMCEPFERVQCEVPQENAGAVIESLGARKGEMVD 431
Cdd:PRK12740 533 vlagypvvdvkvtlTDGsyhsvdssemafkiaarlafrealpkakpVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGRILG 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1799428405 432 MTTTDNGlTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:PRK12740 613 MESRGGG-DVVRAEVPLAEMFGYATDLRSLTQGRGSFSMEFSHYEE 657
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
10-200 |
1.15e-50 |
|
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: 173.25 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGEVE 89
Cdd:cd00881 1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 90 RIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPS-ARPEGVVDEVLDLFIELEAN-DEQLEFPVVY 167
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREIKELLKLIGFTfLKGKDVPIIP 160
|
170 180 190
....*....|....*....|....*....|...
gi 1799428405 168 ASAVNGtasldpekqdDNLQSLYETIIDYVPAP 200
Cdd:cd00881 161 ISALTG----------EGIEELLDAIVEHLPPP 183
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
9-200 |
2.46e-47 |
|
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: 163.86 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 9 RNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVdERAMDSNDIERERGITILAKNTAVDYK---GTR--INILDTPGHAD 83
Cdd:cd01890 1 RNFSIIAHIDHGKSTLADRLLELTGTVSEREMK-EQVLDSMDLERERGITIKAQAVRLFYKakdGEEylLNLIDTPGHVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 84 FGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLfIELEANDeqlef 163
Cdd:cd01890 80 FSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIEDV-LGLDASE----- 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1799428405 164 pVVYASAVNGTasldpekqddNLQSLYETIIDYVPAP 200
Cdd:cd01890 154 -AILVSAKTGL----------GVEDLLEAIVERIPPP 179
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
9-200 |
1.54e-46 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 163.17 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 9 RNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlaKNTAV-----------DYKGTRINILD 77
Cdd:cd01885 1 RNICIIAHVDHGKTTLSDSLLASAGIISEKLAGKARYLDTREDEQERGITI--KSSAIslyfeyeeekmDGNDYLINLID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 78 TPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDK--------PS---ARPEGVVDE 146
Cdd:cd01885 79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRlilelklsPEeayQRLLRIVED 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799428405 147 V---LDLFIELEANDEQLEFP-----VVYASAVNGTA-SLdpeKQDDNLQSLYETIIDYVPAP 200
Cdd:cd01885 159 VnaiIETYAPEEFKQEKWKFSpqkgnVAFGSALDGWGfTI---IKFADIYAVLEMVVKHLPSP 218
|
|
| BipA_III |
cd16263 |
Domain III of GTP-binding protein BipA (TypA); BipA (also called TypA) is a highly conserved ... |
308-386 |
2.36e-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: 149.77 E-value: 2.36e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799428405 308 PTLEMTFKVNNSPFAGREGDFVTARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRREGYELQVS 386
Cdd:cd16263 1 PTVSMTFGVNTSPFAGREGKFVTSRKIRDRLEKELETNVALRVEETESPDSFIVSGRGELHLSILIETMRREGFELQVS 79
|
|
| BipA_TypA_II |
cd03691 |
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ... |
208-301 |
9.39e-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: 143.10 E-value: 9.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 208 LQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIKLDGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINV 287
Cdd:cd03691 1 FQMLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITI 80
|
90
....*....|....
gi 1799428405 288 GETVTPHDHQEALP 301
Cdd:cd03691 81 GDTICDPEVPEPLP 94
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
10-150 |
7.12e-39 |
|
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: 143.15 E-value: 7.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERA--MDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGE 87
Cdd:cd04168 1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTtrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 88 VERIMKMVDGVVLVVDAYEGTMPQTRfVLKKALEQ-NLKPVVVVNKIDKPSARPEGVVDEVLDL 150
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQTR-ILFRLLRKlNIPTIIFVNKIDRAGADLEKVYQEIKEK 143
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
10-147 |
4.11e-36 |
|
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: 136.47 E-value: 4.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERA--MDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGE 87
Cdd:cd01886 1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGatMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 88 VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEV 147
Cdd:cd01886 81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
3-135 |
5.82e-36 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 144.42 E-value: 5.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 3 NKREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlaKNTAV--------DYKGTR-- 72
Cdd:PTZ00416 14 DNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIISSKNAGDARFTDTRADEQERGITI--KSTGIslyyehdlEDGDDKqp 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799428405 73 --INILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDK 135
Cdd:PTZ00416 92 flINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
|
|
| BipA_TypA_C |
cd03710 |
BipA_TypA_C: a C-terminal portion of BipA or TypA having homology to the C terminal domains of ... |
401-477 |
1.33e-34 |
|
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: 125.69 E-value: 1.33e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:cd03710 1 EPIEELTIDVPEEYSGAVIEKLGKRKGEMVDMEPDGNGRTRLEFKIPSRGLIGFRSEFLTDTRGTGIMNHVFDGYEP 77
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
3-161 |
2.71e-32 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 132.93 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 3 NKREDVRNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlaKNTAV------------DYKG 70
Cdd:PLN00116 14 DKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRMTDTRADEAERGITI--KSTGIslyyemtdeslkDFKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 71 TR------INILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKpsarpegvv 144
Cdd:PLN00116 92 ERdgneylINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR--------- 162
|
170
....*....|....*..
gi 1799428405 145 devldLFIELEANDEQL 161
Cdd:PLN00116 163 -----CFLELQVDGEEA 174
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
9-135 |
4.72e-30 |
|
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: 117.75 E-value: 4.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 9 RNIAIIAHVDHGKTTLVDELLKQS---GIFRENEHVDERAMDSNDIERERGITI-------LAKNTavDYKGTRINILDT 78
Cdd:cd04167 1 RNVCIAGHLHHGKTSLLDMLIEQThkrTPSVKLGWKPLRYTDTRKDEQERGISIksnpislVLEDS--KGKSYLINIIDT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1799428405 79 PGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDK 135
Cdd:cd04167 79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
10-299 |
2.55e-27 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 114.27 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlakNTA-VDYK-GTR-INILDTPGHADFgg 86
Cdd:PRK12736 14 NIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITI---NTAhVEYEtEKRhYAHVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 everIMKMV------DGVVLVVDAYEGTMPQTR--FVLKKALEQNlKPVVVVNKIDKPSArpegvvDEVLDLfIELEAND 158
Cdd:PRK12736 89 ----VKNMItgaaqmDGAILVVAATDGPMPQTRehILLARQVGVP-YLVVFLNKVDLVDD------EELLEL-VEMEVRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 159 --EQLEF-----PVVYAS---AVNGtaslDPEKQdDNLQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDYVGR--IGI 226
Cdd:PRK12736 157 llSEYDFpgddiPVIRGSalkALEG----DPKWE-DAIMELMDAVDEYIPTPERDTDKP--FLMPVEDVFTITGRgtVVT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 227 GRVFRGKMRVGDNVSLIKLDGTVKNFrVTKI--FgyfglkRLEIEEAQAGDLIAV----SGMEDINVGE------TVTPH 294
Cdd:PRK12736 230 GRVERGTVKVGDEVEIVGIKETQKTV-VTGVemF------RKLLDEGQAGDNVGVllrgVDRDEVERGQvlakpgSIKPH 302
|
....*
gi 1799428405 295 DHQEA 299
Cdd:PRK12736 303 TKFKA 307
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
10-151 |
2.38e-26 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 108.45 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDE--RAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGE 87
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDgnTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 88 VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLF 151
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAF 144
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
9-147 |
5.07e-26 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 107.68 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 9 RNIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAM------DSNDIERERGITILAKNTAVDYKGTRINILDTPGHA 82
Cdd:cd04169 3 RTFAIISHPDAGKTTLTEKLLLFGGAIQEAGAVKARKSrkhatsDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799428405 83 DFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEV 147
Cdd:cd04169 83 DFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEI 147
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
10-299 |
1.50e-25 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 109.12 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlakNTA-VDYKGTRINI--LDTPGHADFgg 86
Cdd:PRK00049 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITI---NTAhVEYETEKRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 everIMKMV------DGVVLVVDAYEGTMPQTRfvlkkalEQNL--------KPVVVVNKIDkpsarpegVVD--EVLDL 150
Cdd:PRK00049 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTR-------EHILlarqvgvpYIVVFLNKCD--------MVDdeELLEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 151 fIELEAND--EQLEF-----PVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDYVGR 223
Cdd:PRK00049 150 -VEMEVREllSKYDFpgddtPIIRGSALKALEGDDDEEWEKKILELMDAVDSYIPTPERAIDKP--FLMPIEDVFSISGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 224 --IGIGRVFRGKMRVGDNVSLIKLDGTVKNFrVTKI--FgyfglkRLEIEEAQAGDLIAV----SGMEDINVGE------ 289
Cdd:PRK00049 227 gtVVTGRVERGIIKVGEEVEIVGIRDTQKTT-VTGVemF------RKLLDEGQAGDNVGAllrgIKREDVERGQvlakpg 299
|
330
....*....|
gi 1799428405 290 TVTPHDHQEA 299
Cdd:PRK00049 300 SITPHTKFEA 309
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
10-327 |
5.05e-25 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 108.37 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKqsgIFRENEHVDERAMDSNDI---ERERGITIlakNTA-VDYKGTRINI--LDTPGHAD 83
Cdd:PLN03127 63 NVGTIGHVDHGKTTLTAAITK---VLAEEGKAKAVAFDEIDKapeEKARGITI---ATAhVEYETAKRHYahVDCPGHAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 84 FGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVV-VNKIDkpsarpegVVD--EVLDLfIELEANdEQ 160
Cdd:PLN03127 137 YVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVD--------VVDdeELLEL-VEMELR-EL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 161 LEF--------PVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDYVGR--IGIGRVF 230
Cdd:PLN03127 207 LSFykfpgdeiPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKP--FLMPIEDVFSIQGRgtVATGRVE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 231 RGKMRVGDNVSLIKLD--GTVKnfrvTKIFGYFGLKRLeIEEAQAGDLIA--VSGM--EDINVGE------TVTPHDHQE 298
Cdd:PLN03127 285 QGTIKVGEEVEIVGLRpgGPLK----TTVTGVEMFKKI-LDQGQAGDNVGllLRGLkrEDVQRGQvickpgSIKTYKKFE 359
|
330 340 350
....*....|....*....|....*....|.
gi 1799428405 299 A-LPVLRIDEPTLEMTFKVNNSP-FAGREGD 327
Cdd:PLN03127 360 AeIYVLTKDEGGRHTPFFSNYRPqFYLRTAD 390
|
|
| EFG_C |
pfam00679 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
398-477 |
5.91e-25 |
|
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
Pssm-ID: 425814 [Multi-domain] Cd Length: 88 Bit Score: 98.77 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 398 VMCEPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:pfam00679 1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGGRVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQP 80
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
10-307 |
8.08e-25 |
|
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: 106.79 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKqsgIFRENEHVDERAMDSNDI---ERERGITIlakNTA-VDYKGTRINI--LDTPGHAD 83
Cdd:TIGR00485 14 NVGTIGHVDHGKTTLTAAITT---VLAKEGGAAARAYDQIDNapeEKARGITI---NTAhVEYETETRHYahVDCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 84 FGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVV-VNKIDKpsarpegVVDEVLDLFIELEAND--EQ 160
Cdd:TIGR00485 88 YVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDM-------VDDEELLELVEMEVREllSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 161 LEF-----PVVYASAVNgtaSLDPEKQ-DDNLQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDYVGR--IGIGRVFRG 232
Cdd:TIGR00485 161 YDFpgddtPIIRGSALK---ALEGDAEwEAKILELMDAVDEYIPTPEREIDKP--FLLPIEDVFSITGRgtVVTGRVERG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 233 KMRVGDNVSLIKLDGTVKNfRVTKIFGYfglkRLEIEEAQAGDLIAV----SGMEDINVGE------TVTPHDHQEA-LP 301
Cdd:TIGR00485 236 IIKVGEEVEIVGLKDTRKT-TVTGVEMF----RKELDEGRAGDNVGLllrgIKREEIERGMvlakpgSIKPHTKFEAeVY 310
|
....*.
gi 1799428405 302 VLRIDE 307
Cdd:TIGR00485 311 VLSKEE 316
|
|
| tufA |
CHL00071 |
elongation factor Tu |
10-299 |
2.03e-24 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 105.81 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTL---VDELLKQSGifrenehvDERAMDSNDI-----ERERGITIlakNTA-VDYKGTRINI--LDT 78
Cdd:CHL00071 14 NIGTIGHVDHGKTTLtaaITMTLAAKG--------GAKAKKYDEIdsapeEKARGITI---NTAhVEYETENRHYahVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 79 PGHADFggeverIMKM------VDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVV-VNKIDKpsarpegVVDEVLDLF 151
Cdd:CHL00071 83 PGHADY------VKNMitgaaqMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQ-------VDDEELLEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 152 IELEAND--EQLEFPVVYASAVNGTA--SLDPEKQDDNLQ-----------SLYETIIDYVPAPIDNSDEPlqFQVALLD 216
Cdd:CHL00071 150 VELEVREllSKYDFPGDDIPIVSGSAllALEALTENPKIKrgenkwvdkiyNLMDAVDSYIPTPERDTDKP--FLMAIED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 217 YNDYVGR--IGIGRVFRGKMRVGDNVSLIKLDGTvknfRVTKIFGyfglkrLE-----IEEAQAGDLIAVS--GM--EDI 285
Cdd:CHL00071 228 VFSITGRgtVATGRIERGTVKVGDTVEIVGLRET----KTTTVTG------LEmfqktLDEGLAGDNVGILlrGIqkEDI 297
|
330 340
....*....|....*....|
gi 1799428405 286 NVG------ETVTPHDHQEA 299
Cdd:CHL00071 298 ERGmvlakpGTITPHTKFEA 317
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
10-307 |
5.99e-24 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 105.47 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDEL---LKQSGIFRENEHvDEraMDSNDIERERGITIlakNTA-VDYKGTRINI--LDTPGHAD 83
Cdd:PLN03126 83 NIGTIGHVDHGKTTLTAALtmaLASMGGSAPKKY-DE--IDAAPEERARGITI---NTAtVEYETENRHYahVDCPGHAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 84 FGGEVERIMKMVDGVVLVVDAYEGTMPQTR---FVLKKALEQNLkpVVVVNKIDKpsarpegVVDEVLDLFIELEAND-- 158
Cdd:PLN03126 157 YVKNMITGAAQMDGAILVVSGADGPMPQTKehiLLAKQVGVPNM--VVFLNKQDQ-------VDDEELLELVELEVREll 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 159 EQLEFPVVYASAVNGTASLDPE--------KQDDN-----LQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDYVGR-- 223
Cdd:PLN03126 228 SSYEFPGDDIPIISGSALLALEalmenpniKRGDNkwvdkIYELMDAVDSYIPIPQRQTDLP--FLLAVEDVFSITGRgt 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 224 IGIGRVFRGKMRVGDNVSLIKLDGTvknfRVTKIFGYFGLKRLeIEEAQAGDLIAV--SGME--DINVGE------TVTP 293
Cdd:PLN03126 306 VATGRVERGTVKVGETVDIVGLRET----RSTTVTGVEMFQKI-LDEALAGDNVGLllRGIQkaDIQRGMvlakpgSITP 380
|
330
....*....|....*
gi 1799428405 294 HDHQEALP-VLRIDE 307
Cdd:PLN03126 381 HTKFEAIVyVLKKEE 395
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
10-299 |
6.91e-24 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 104.15 E-value: 6.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlakNTA-VDYKGTRINI--LDTPGHADFgg 86
Cdd:PRK12735 14 NVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITI---NTShVEYETANRHYahVDCPGHADY-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 everIMKMV------DGVVLVVDAYEGTMPQTR--FVLKKaleQNLKPVVVV--NKIDkpsarpegVVD--EVLDLfIEL 154
Cdd:PRK12735 89 ----VKNMItgaaqmDGAILVVSAADGPMPQTRehILLAR---QVGVPYIVVflNKCD--------MVDdeELLEL-VEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 155 EAND--EQLEF-----PVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDYVGR--IG 225
Cdd:PRK12735 153 EVREllSKYDFpgddtPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKP--FLMPIEDVFSISGRgtVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 226 IGRVFRGKMRVGDNVSLIKLDGTVKNFrVTKI--FgyfglkRLEIEEAQAGDLIAV----SGMEDINVGE------TVTP 293
Cdd:PRK12735 231 TGRVERGIVKVGDEVEIVGIKETQKTT-VTGVemF------RKLLDEGQAGDNVGVllrgTKREDVERGQvlakpgSIKP 303
|
....*.
gi 1799428405 294 HDHQEA 299
Cdd:PRK12735 304 HTKFEA 309
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
10-299 |
1.16e-23 |
|
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: 103.31 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlakNTA-VDYK-GTR----InilDTPGHAD 83
Cdd:COG0050 14 NIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITI---NTShVEYEtEKRhyahV---DCPGHAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 84 FggeverIMKMV------DGVVLVVDAYEGTMPQTRfvlkkalEQNL--------KPVVVVNKIDkpsarpegVVD--EV 147
Cdd:COG0050 88 Y------VKNMItgaaqmDGAILVVSATDGPMPQTR-------EHILlarqvgvpYIVVFLNKCD--------MVDdeEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 148 LDLfIELEAND--EQLEF-----PVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAPIDNSDEPlqFQVALLDYNDY 220
Cdd:COG0050 147 LEL-VEMEVREllSKYGFpgddtPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKP--FLMPVEDVFSI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 221 VGR--IGIGRVFRGKMRVGDNVSLIKLDGTVKNFrVTKI--FgyfglkRLEIEEAQAGDLIAV----SGMEDINVGE--- 289
Cdd:COG0050 224 TGRgtVVTGRVERGIIKVGDEVEIVGIRDTQKTV-VTGVemF------RKLLDEGEAGDNVGLllrgIKREDVERGQvla 296
|
330
....*....|...
gi 1799428405 290 ---TVTPHDHQEA 299
Cdd:COG0050 297 kpgSITPHTKFEA 309
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
10-295 |
2.16e-23 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 103.08 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFREN--EHVDERA-------------MDSNDIERERGITILAKNTAVDYKGTRIN 74
Cdd:PRK12317 8 NLAVIGHVDHGKSTLVGRLLYETGAIDEHiiEELREEAkekgkesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 75 ILDTPGHADFggeverIMKMV------DGVVLVVDAYE--GTMPQTR--FVLKKALEQNlKPVVVVNKIDKPS---ARPE 141
Cdd:PRK12317 88 IVDCPGHRDF------VKNMItgasqaDAAVLVVAADDagGVMPQTRehVFLARTLGIN-QLIVAINKMDAVNydeKRYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 142 GVVDEVLDLFIELEANDEQLEF-PVvyaSAVNGTaslDPEKQDDNL-----QSLYETiIDYVPAPIDNSDEPLQFQVAll 215
Cdd:PRK12317 161 EVKEEVSKLLKMVGYKPDDIPFiPV---SAFEGD---NVVKKSENMpwyngPTLLEA-LDNLKPPEKPTDKPLRIPIQ-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 216 dyNDY----VGRIGIGRVFRGKMRVGDNVSLIKLD--GTVKNFRvtkifgyfgLKRLEIEEAQAGDLI--AVSGME--DI 285
Cdd:PRK12317 232 --DVYsisgVGTVPVGRVETGVLKVGDKVVFMPAGvvGEVKSIE---------MHHEELPQAEPGDNIgfNVRGVGkkDI 300
|
330
....*....|
gi 1799428405 286 NVGETVTPHD 295
Cdd:PRK12317 301 KRGDVCGHPD 310
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
11-174 |
2.19e-23 |
|
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: 97.16 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKqsgifrenehvderamdSNDIERE-RGIT--ILAKNTAVDYKGTRINILDTPGHADFGGE 87
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK-----------------TNVAAGEaGGITqhIGAYQVPIDVKIPGITFIDTPGHEAFTNM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 88 VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSAR---PEGVVDEVLDLFIELEANDEQLefP 164
Cdd:cd01887 66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTeadPERVKNELSELGLVGEEWGGDV--S 143
|
170
....*....|
gi 1799428405 165 VVYASAVNGT 174
Cdd:cd01887 144 IVPISAKTGE 153
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
10-295 |
3.45e-23 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 102.32 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSG-----IFRENEHVDERA----------MDSNDIERERGITILAKNTAVDYKGTRIN 74
Cdd:COG5256 9 NLVVIGHVDHGKSTLVGRLLYETGaidehIIEKYEEEAEKKgkesfkfawvMDRLKEERERGVTIDLAHKKFETDKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 75 ILDTPGHADFggeverIMKMV------DGVVLVVDAYEGTMPQTR--FVLKKALEQNlKPVVVVNKIDKPS---ARPEGV 143
Cdd:COG5256 89 IIDAPGHRDF------VKNMItgasqaDAAILVVSAKDGVMGQTRehAFLARTLGIN-QLIVAVNKMDAVNyseKRYEEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 144 VDEVLDLFIELEANDEqlEFPVVYASAVNGTaslDPEKQDDNL-----QSLYETiIDYVPAPIDNSDEPLQFQVAllD-Y 217
Cdd:COG5256 162 KEEVSKLLKMVGYKVD--KIPFIPVSAWKGD---NVVKKSDNMpwyngPTLLEA-LDNLKEPEKPVDKPLRIPIQ--DvY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 218 N-DYVGRIGIGRVFRGKMRVGDNVSLI--KLDGTVKNFRvtkifgyfgLKRLEIEEAQAGDLI--AVSGME--DINVGET 290
Cdd:COG5256 234 SiSGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKSIE---------MHHEELEQAEPGDNIgfNVRGVEknDIKRGDV 304
|
....*
gi 1799428405 291 VTPHD 295
Cdd:COG5256 305 AGHPD 309
|
|
| Elongation_Factor_C |
cd01514 |
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ... |
401-477 |
1.87e-22 |
|
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: 91.39 E-value: 1.87e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:cd01514 1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPRGTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEP 77
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
10-200 |
9.57e-22 |
|
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: 93.42 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIERERGITIlakNTA-VDYKGTRINI--LDTPGHADFgg 86
Cdd:cd01884 4 NVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITI---NTAhVEYETANRHYahVDCPGHADY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 everIMKMV------DGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVV-VNKIDKpsarpegVVD-EVLDLfIELEAND 158
Cdd:cd01884 79 ----IKNMItgaaqmDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADM-------VDDeELLEL-VEMEVRE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1799428405 159 --EQLEF-----PVVYASAVNGTASLDPEKQDDNLQSLYETIIDYVPAP 200
Cdd:cd01884 147 llSKYGFdgddtPIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
10-174 |
3.58e-19 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 86.39 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIfrenehVDER---------------------AMDSNDIERERGITILAKNTAVDY 68
Cdd:cd01883 1 NLVVIGHVDAGKSTLTGHLLYKLGG------VDKRtiekyekeakemgkesfkyawVLDKLKEERERGVTIDVGLAKFET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 69 KGTRINILDTPGHADFggeverIMKMVDGV------VLVVDAYEG-------TMPQTR--FVLKKALEQNlKPVVVVNKI 133
Cdd:cd01883 75 EKYRFTIIDAPGHRDF------VKNMITGAsqadvaVLVVSARKGefeagfeKGGQTRehALLARTLGVK-QLIVAVNKM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1799428405 134 DKPS-----ARPEGVVDEVLDLFIELEANDEQLEF-PVvyaSAVNGT 174
Cdd:cd01883 148 DDVTvnwsqERYDEIKKKVSPFLKKVGYNPKDVPFiPI---SGFTGD 191
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
2-147 |
1.58e-18 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 89.04 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 2 TNKRedvRNIAIIAHVDHGKTTLVDELLKQSGIFRE---------NEHVDERAMDsndIERERGITIlakNTAV---DYK 69
Cdd:PRK00741 7 VAKR---RTFAIISHPDAGKTTLTEKLLLFGGAIQEagtvkgrksGRHATSDWME---MEKQRGISV---TSSVmqfPYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 70 GTRINILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRfvlkKALE----QNLKPVVVVNKIDKPSARPEGVVD 145
Cdd:PRK00741 78 DCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTR----KLMEvcrlRDTPIFTFINKLDRDGREPLELLD 153
|
..
gi 1799428405 146 EV 147
Cdd:PRK00741 154 EI 155
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
9-160 |
2.24e-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: 79.72 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 9 RNIAIIAHVDHGKTTLVDELLK--------QSGIFRenehvderaMDSNDIERERGITIlakntavdykgtRINILDTPG 80
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGnkgsiteyYPGTTR---------NYVTTVIEEDGKTY------------KFNLLDTAG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 81 HADF-------GGEVERIMKMVDGVVLVVDAYEGTMPQTRfVLKKALEQNLKPVVVVNKIDKPSAR-PEGVVDEVLDL-- 150
Cdd:TIGR00231 61 QEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEKQTK-EIIHHADSGVPIILVGNKIDLKDADlKTHVASEFAKLng 139
|
170
....*....|..
gi 1799428405 151 --FIELEANDEQ 160
Cdd:TIGR00231 140 epIIPLSAETGK 151
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
10-283 |
5.01e-17 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 84.54 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELlkqSGIfrenehvderAMDSNDIERERGITILAKNTAVDYKGTRINILDTPGHADFGGEVE 89
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL---TGI----------AADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 90 RIMKMVDGVVLVVDAYEGTMPQTRFVLKKA-LEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLEFPVVYA 168
Cdd:TIGR00475 69 AGGGGIDAALLVVDADEGVMTQTGEHLAVLdLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTSA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 169 SAVNGTASLDPEkqddnLQSLYETIidyvpaPIDNSDEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNvslIKLDGT 248
Cdd:TIGR00475 149 KTGQGIGELKKE-----LKNLLESL------DIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDN---LRLLPI 214
|
250 260 270
....*....|....*....|....*....|....*
gi 1799428405 249 VKNFRVTKIFGYfglkRLEIEEAQAGDLIAVSGME 283
Cdd:TIGR00475 215 NHEVRVKAIQAQ----NQDVEIAYAGQRIALNLMD 245
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
11-174 |
5.57e-17 |
|
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: 84.43 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKqsgifrenehVDERAMDSNDIERERGITILAKNtavdyKGTRINILDTPGHADFGGEVER 90
Cdd:TIGR00487 90 VTIMGHVDHGKTSLLDSIRK----------TKVAQGEAGGITQHIGAYHVENE-----DGKMITFLDTPGHEAFTSMRAR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 91 IMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLFIELEANDEQLEFpvVYASA 170
Cdd:TIGR00487 155 GAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIF--VPVSA 232
|
....
gi 1799428405 171 VNGT 174
Cdd:TIGR00487 233 LTGD 236
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
11-143 |
9.73e-17 |
|
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: 83.14 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKqsgifrenehvderamdSNDIERE-RGIT--ILAknTAVDYKGTRINILDTPGHADF--- 84
Cdd:COG0532 7 VTVMGHVDHGKTSLLDAIRK-----------------TNVAAGEaGGITqhIGA--YQVETNGGKITFLDTPGHEAFtam 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799428405 85 ---GGEVERImkmvdgVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGV 143
Cdd:COG0532 68 rarGAQVTDI------VILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRV 123
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
16-173 |
2.76e-16 |
|
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: 76.88 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 16 HVDHGKTTLVDELlkqSGIfrENEHVDEramdsndiERERGITI-LAKNTAVDYKGTRINILDTPGHADFggeverIMKM 94
Cdd:cd04171 7 HIDHGKTTLIKAL---TGI--ETDRLPE--------EKKRGITIdLGFAYLDLPDGKRLGFIDVPGHEKF------VKNM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 95 V------DGVVLVVDAYEGTMPQTR---FVLKkaLEQNLKPVVVVNKIDK-PSARPEGVVDEVLDLFieleANDEQLEFP 164
Cdd:cd04171 68 LagaggiDAVLLVVAADEGIMPQTRehlEILE--LLGIKKGLVVLTKADLvDEDRLELVEEEILELL----AGTFLADAP 141
|
....*....
gi 1799428405 165 VVYASAVNG 173
Cdd:cd04171 142 IFPVSSVTG 150
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
11-194 |
1.30e-15 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 80.26 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKqsgifrenehvderamdSNDIERERG-IT--ILAKNTAVDYKGTRINI--LDTPGHADFG 85
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRK-----------------TQIAQKEAGgITqkIGAYEVEFEYKDENQKIvfLDTPGHEAFS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 86 GEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPEGVVDEVLDLfiELEANDEQLEFPV 165
Cdd:CHL00189 310 SMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKY--NLIPEKWGGDTPM 387
|
170 180
....*....|....*....|....*....
gi 1799428405 166 VYASAVNGTasldpekqddNLQSLYETII 194
Cdd:CHL00189 388 IPISASQGT----------NIDKLLETIL 406
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
10-279 |
1.51e-15 |
|
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: 78.94 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELlkqSGIFrenehvderaMDSNDIERERGITI-LAKNTAVDYK------------------- 69
Cdd:TIGR03680 6 NIGMVGHVDHGKTTLTKAL---TGVW----------TDTHSEELKRGISIrLGYADAEIYKcpecdgpecyttepvcpnc 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 70 GT------RINILDTPGHadfggevERIM-------KMVDGVVLVVDAYEG-TMPQTRFVLkKALE-QNLKPVVVV-NKI 133
Cdd:TIGR03680 73 GSetellrRVSFVDAPGH-------ETLMatmlsgaALMDGALLVIAANEPcPQPQTKEHL-MALEiIGIKNIVIVqNKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 134 DkpsarpegVVDEvldlfiE--LEANDEQLEF---------PVVYASAVNGTasldpekqddNLQSLYETIIDYVPAPID 202
Cdd:TIGR03680 145 D--------LVSK------EkaLENYEEIKEFvkgtvaenaPIIPVSALHNA----------NIDALLEAIEKFIPTPER 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 203 NSDEPLQFQVAL--------LDYNDYVGRIGIGRVFRGKMRVGDNVSL-----IKLDGTVKNFRV-TKIFG-YFGLKrlE 267
Cdd:TIGR03680 201 DLDKPPLMYVARsfdvnkpgTPPEKLKGGVIGGSLIQGKLKVGDEIEIrpgikVEKGGKTKWEPIyTEITSlRAGGY--K 278
|
330
....*....|..
gi 1799428405 268 IEEAQAGDLIAV 279
Cdd:TIGR03680 279 VEEARPGGLVGV 290
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
13-306 |
2.12e-14 |
|
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: 76.49 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 13 IIA---HVDHGKTTLVDELlkqSGIfrENEHVDEramdsndiERERGITI--------LAKntavdykGTRINILDTPGH 81
Cdd:COG3276 2 IIGtagHIDHGKTTLVKAL---TGI--DTDRLKE--------EKKRGITIdlgfaylpLPD-------GRRLGFVDVPGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 82 ADF--------GGeverimkmVDGVVLVVDAYEGTMPQTR--------FVLKKAleqnlkpVVVVNKIDK-PSARPEGVV 144
Cdd:COG3276 62 EKFiknmlagaGG--------IDLVLLVVAADEGVMPQTRehlaildlLGIKRG-------IVVLTKADLvDEEWLELVE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 145 DEVLDLFIE--LEandeqlEFPVVYASAVNGtASLdpekqdDNLQSLYETIIDYVPA---------PIDNSdeplqFQVA 213
Cdd:COG3276 127 EEIRELLAGtfLE------DAPIVPVSAVTG-EGI------DELRAALDALAAAVPArdadgpfrlPIDRV-----FSIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 214 lldyndyvgriGIGRV-----FRGKMRVGDNVSL--IKLDGTVKNFRVtkifgyFGLKRleiEEAQAGDLIAV--SGM-- 282
Cdd:COG3276 189 -----------GFGTVvtgtlLSGTVRVGDELELlpSGKPVRVRGIQV------HGQPV---EEAYAGQRVALnlAGVek 248
|
330 340
....*....|....*....|....
gi 1799428405 283 EDINVGETVTPHDHqeALPVLRID 306
Cdd:COG3276 249 EEIERGDVLAAPGA--LRPTDRID 270
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
12-195 |
2.14e-14 |
|
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: 70.95 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 12 AIIAHVDHGKTTLVDELLKQSGIFRENEHVDERAMDSNDIErergitilakntaVDYKGTRINILDTPGHADFGG----- 86
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKE-------------LDKGKVKLVLVDTPGLDEFGGlgree 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 EVERIMKMVDGVVLVVDA--YEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSARPegvVDEVLDLFIELEANDEqlefP 164
Cdd:cd00882 68 LARLLLRGADLILLVVDStdRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEERE---VEELLRLEELAKILGV----P 140
|
170 180 190
....*....|....*....|....*....|.
gi 1799428405 165 VVYASAVNGTasldpekqddNLQSLYETIID 195
Cdd:cd00882 141 VFEVSAKTGE----------GVDELFEKLIE 161
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
10-297 |
4.49e-13 |
|
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: 71.27 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSG-IF-------------RENEHVD-ERAMDSNDIERERGITIlakntAVDYK----G 70
Cdd:COG2895 19 RFITCGSVDDGKSTLIGRLLYDTKsIFedqlaalerdskkRGTQEIDlALLTDGLQAEREQGITI-----DVAYRyfstP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 71 TR--InILDTPGHadfggeVERIMKMVDG------VVLVVDAYEGTMPQTR---FVLkkaleqNL----KPVVVVNKIDK 135
Cdd:COG2895 94 KRkfI-IADTPGH------EQYTRNMVTGastadlAILLIDARKGVLEQTRrhsYIA------SLlgirHVVVAVNKMDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 136 ---PSARPEGVVDEVLDLFieleandEQLEFPVVYA---SAVNGtasldpekqdDNLQSL------YE--TIIDY---VP 198
Cdd:COG2895 161 vdySEEVFEEIVADYRAFA-------AKLGLEDITFipiSALKG----------DNVVERsenmpwYDgpTLLEHletVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 199 APIDNSDEPLQFQVAL-----LDYNDYVGRIGIGRVfrgkmRVGDNVslikldgTV----KNFRVTKIFGYFGlkrlEIE 269
Cdd:COG2895 224 VAEDRNDAPFRFPVQYvnrpnLDFRGYAGTIASGTV-----RVGDEV-------VVlpsgKTSTVKSIVTFDG----DLE 287
|
330 340 350
....*....|....*....|....*....|
gi 1799428405 270 EAQAGDLIAVSGMEDINV--GETVTPHDHQ 297
Cdd:COG2895 288 EAFAGQSVTLTLEDEIDIsrGDVIVAADAP 317
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
10-240 |
3.76e-12 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 68.62 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELL-KQSGI-FRENEHVDERA-------------MDSNDIERERGITI---LAKNTAVDYKGT 71
Cdd:PTZ00141 9 NLVVIGHVDSGKSTTTGHLIyKCGGIdKRTIEKFEKEAaemgkgsfkyawvLDKLKAERERGITIdiaLWKFETPKYYFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 72 rinILDTPGHADFggeverIMKMVDGV------VLVVDA----YEGTMP---QTRFVLKKALEQNLKPVVV-VNKIDKPS 137
Cdd:PTZ00141 89 ---IIDAPGHRDF------IKNMITGTsqadvaILVVAStageFEAGISkdgQTREHALLAFTLGVKQMIVcINKMDDKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 138 -----ARPEGVVDEVLDLFIELEANDEqlEFPVVYASAVNGTASLDPEkqdDNL-----QSLYETiIDYVPAPIDNSDEP 207
Cdd:PTZ00141 160 vnysqERYDEIKKEVSAYLKKVGYNPE--KVPFIPISGWQGDNMIEKS---DNMpwykgPTLLEA-LDTLEPPKRPVDKP 233
|
250 260 270
....*....|....*....|....*....|...
gi 1799428405 208 LQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNV 240
Cdd:PTZ00141 234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVV 266
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
10-134 |
5.60e-12 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 65.08 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELlkqsgifreNEHVDERAMDSNDIERERGITI--------------LAKNTAVDYKGTRINI 75
Cdd:cd01889 2 NVGLLGHVDSGKTSLAKAL---------SEIASTAAFDKNPQSQERGITLdlgfssfevdkpkhLEDNENPQIENYQITL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799428405 76 LDTPGHADF-----GGEverimKMVDGVVLVVDAYEGTMPQTR--FVLKKALeqNLKPVVVVNKID 134
Cdd:cd01889 73 VDCPGHASLirtiiGGA-----QIIDLMLLVVDAKKGIQTQTAecLVIGELL--CKPLIVVLNKID 131
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
10-173 |
1.24e-11 |
|
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: 64.13 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSG-IF-------RENEHVDERA--------MDSNDIERERGITIlakNTAVDYKGT-- 71
Cdd:cd04166 1 RFITCGSVDDGKSTLIGRLLYDSKsIFedqlaalERSKSSGTQGekldlallVDGLQAEREQGITI---DVAYRYFSTpk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 72 -RINILDTPGHADFggeverIMKMVDG------VVLVVDAYEGTMPQTR---FVLkkALEQNLKPVVVVNKID---KPSA 138
Cdd:cd04166 78 rKFIIADTPGHEQY------TRNMVTGastadlAILLVDARKGVLEQTRrhsYIA--SLLGIRHVVVAVNKMDlvdYDEE 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1799428405 139 RPEGVVDEVLDLFIELEANDEQlefpVVYASAVNG 173
Cdd:cd04166 150 VFEEIKADYLAFAASLGIEDIT----FIPISALEG 180
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
10-279 |
3.72e-11 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 65.26 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELlkqSGIF--RENEhvderamdsndiERERGITI-LAKNTAVDYK----------------- 69
Cdd:PRK04000 11 NIGMVGHVDHGKTTLVQAL---TGVWtdRHSE------------ELKRGITIrLGYADATIRKcpdceepeayttepkcp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 70 --GT------RINILDTPGHadfggevERIM-------KMVDGVVLVVDAYEGT-MPQTRFVLkKALE----QNLkpVVV 129
Cdd:PRK04000 76 ncGSetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPCpQPQTKEHL-MALDiigiKNI--VIV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 130 VNKIDkpsarpegVVDEvlDLFIEleaNDEQL-EF---------PVVYASAVNGTasldpekqddNLQSLYETIIDYVPA 199
Cdd:PRK04000 146 QNKID--------LVSK--ERALE---NYEQIkEFvkgtvaenaPIIPVSALHKV----------NIDALIEAIEEEIPT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 200 PIDNSDEPLQFQVAL-LDYN-------DYVGRIGIGRVFRGKMRVGDNVSL---IKLDGTVKNFRV---TKIFG-YFGlk 264
Cdd:PRK04000 203 PERDLDKPPRMYVARsFDVNkpgtppeKLKGGVIGGSLIQGVLKVGDEIEIrpgIKVEEGGKTKWEpitTKIVSlRAG-- 280
|
330
....*....|....*
gi 1799428405 265 RLEIEEAQAGDLIAV 279
Cdd:PRK04000 281 GEKVEEARPGGLVGV 295
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
17-288 |
4.16e-10 |
|
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: 62.00 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 17 VDHGKTTLVDELLKQSGIFRENE----HVDERA-------------MDSNDIERERGITIlakNTAVDYKGT--RINIL- 76
Cdd:TIGR02034 9 VDDGKSTLIGRLLHDTKQIYEDQlaalERDSKKhgtqggeidlallVDGLQAEREQGITI---DVAYRYFSTdkRKFIVa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 77 DTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVV-VNKIDKPSARpEGVVDEVLDLFIELE 155
Cdd:TIGR02034 86 DTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLaVNKMDLVDYD-EEVFENIKKDYLAFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 156 ANDEQLEFPVVYASAVNGTASLDPEKQDDNLQ--SLYEtIIDYVPAPIDNSDEPLQFQVAL-----LDYNDYVGRIGIGR 228
Cdd:TIGR02034 165 EQLGFRDVTFIPLSALKGDNVVSRSESMPWYSgpTLLE-ILETVEVERDAQDLPLRFPVQYvnrpnLDFRGYAGTIASGS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 229 VfrgkmRVGDNVSLIKldgTVKNFRVTKIFGYFGlkrlEIEEAQAGDLIAVSGMEDINVG 288
Cdd:TIGR02034 244 V-----HVGDEVVVLP---SGRSSRVARIVTFDG----DLEQARAGQAVTLTLDDEIDIS 291
|
|
| EFG_III-like |
cd16257 |
Domain III of Elongation factor G (EF-G) and related proteins; Bacterial Elongation factor G ... |
308-386 |
5.33e-10 |
|
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: 55.82 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 308 PTLEMTFKVNNspfagregdFVTARQIQERLNQQLETDVSLKVSNTDSPDTWVVAGRGELHLSILIENMRRE-GYELQVS 386
Cdd:cd16257 1 PVVFVTVEVKN---------PLDQEKLLEGLERLSEEDPALQVYREESTGEFILSGLGELHLEIIVARLEREyGVELVVS 71
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
222-292 |
5.73e-10 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 55.73 E-value: 5.73e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799428405 222 GRIGIGRVFRGKMRVGDNVSLIKLD--GTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVT 292
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGtgKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| EFG_mtEFG_II |
cd04088 |
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ... |
220-292 |
7.17e-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: 7.17e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 220 YVGRIGIGRVFRGKMRVGDNVslikLDGTV-KNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINVGETVT 292
Cdd:cd04088 13 FVGKLTFFRVYSGTLKSGSTV----YNSTKgKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLC 82
|
|
| EFG_mtEFG_C |
cd03713 |
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ... |
401-477 |
7.28e-09 |
|
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: 52.53 E-value: 7.28e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDMtTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:cd03713 1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGT-ESRGGWKVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEE 76
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
20-197 |
8.26e-09 |
|
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: 54.94 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 20 GKTTLVDELLKQ-SGIfrenehVDERAMDSNDIERERGITIlakntavdyKGTRINILDTPGHADFGGE-VERIMKM--- 94
Cdd:cd00880 9 GKSSLLNALLGQnVGI------VSPIPGTTRDPVRKEWELL---------PLGPVVLIDTPGLDEEGGLgRERVEEArqv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 95 ---VDGVVLVVDayeGTMPQTRFVLKKA-LEQNLKPVVVV-NKIDKPSARPEgvvdEVLDLFIELEANDEQlefPVVYAS 169
Cdd:cd00880 74 adrADLVLLVVD---SDLTPVEEEAKLGlLRERGKPVLLVlNKIDLVPESEE----EELLRERKLELLPDL---PVIAVS 143
|
170 180
....*....|....*....|....*...
gi 1799428405 170 AVNGTasldpekqddNLQSLYETIIDYV 197
Cdd:cd00880 144 ALPGE----------GIDELRKKIAELL 161
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
11-135 |
9.13e-09 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 58.29 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKQSGIFRE----NEHVDERAMDSNDIERERGitILAKNTAVDYKGTRINILDTPGHADFGG 86
Cdd:TIGR00491 7 VVVLGHVDHGKTTLLDKIRGTAVVKKEaggiTQHIGASEVPTDVIEKICG--DLLKSFKIKLKIPGLLFIDTPGHEAFTN 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1799428405 87 EVERIMKMVDGVVLVVDAYEGTMPQTRFVLkKALEQNLKP-VVVVNKIDK 135
Cdd:TIGR00491 85 LRKRGGALADIAILVVDINEGFKPQTLEAL-NILRSRKTPfVVAANKIDR 133
|
|
| mtEFG1_C |
cd04097 |
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ... |
401-466 |
9.61e-09 |
|
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: 52.32 E-value: 9.61e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDmTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYG 466
Cdd:cd04097 1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVD-TDTGEDEFTLEAEVPLNDMFGYSTELRSMTQGKG 65
|
|
| EFG_C |
smart00838 |
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ... |
401-477 |
1.08e-08 |
|
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: 52.51 E-value: 1.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTdNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:smart00838 3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQR-GGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
11-135 |
1.60e-08 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 57.50 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKQSGIFRE----NEHVDERAMDSNDIERERGitilaknTAVDYKGTRINI-----LDTPGH 81
Cdd:PRK04004 9 VVVLGHVDHGKTTLLDKIRGTAVAAKEaggiTQHIGATEVPIDVIEKIAG-------PLKKPLPIKLKIpgllfIDTPGH 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799428405 82 ADF------GGEVerimkmVDGVVLVVDAYEGTMPQTRFVLkKALEQNLKP-VVVVNKIDK 135
Cdd:PRK04004 82 EAFtnlrkrGGAL------ADIAILVVDINEGFQPQTIEAI-NILKRRKTPfVVAANKIDR 135
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
10-237 |
2.53e-08 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 56.64 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSG---------IFRENEHVDERA------MDSNDIERERGITI---LAKNTAVDYKGT 71
Cdd:PLN00043 9 NIVVIGHVDSGKSTTTGHLIYKLGgidkrvierFEKEAAEMNKRSfkyawvLDKLKAERERGITIdiaLWKFETTKYYCT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 72 rinILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMP-------QTRFVLKKALEQNLKPVV-VVNKIDKPS-----A 138
Cdd:PLN00043 89 ---VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMIcCCNKMDATTpkyskA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 139 RPEGVVDEVLDLFIELEANDEQLEFPVVYA----SAVNGTASLDPEKQDDNLQSLyetiiDYVPAPIDNSDEPLQFQVAL 214
Cdd:PLN00043 166 RYDEIVKEVSSYLKKVGYNPDKIPFVPISGfegdNMIERSTNLDWYKGPTLLEAL-----DQINEPKRPSDKPLRLPLQD 240
|
250 260
....*....|....*....|...
gi 1799428405 215 LDYNDYVGRIGIGRVFRGKMRVG 237
Cdd:PLN00043 241 VYKIGGIGTVPVGRVETGVIKPG 263
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
10-279 |
4.01e-08 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 56.00 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELlkqSGIF--RENEhvderamdsndiERERGITI-LAKNTAVDYK----------------- 69
Cdd:COG5257 7 NIGVVGHVDHGKTTLVQAL---TGVWtdRHSE------------ELKRGITIrLGYADATFYKcpnceppeayttepkcp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 70 --GT------RINILDTPGHadfggevERIM-------KMVDGVVLVVDAYEGT-MPQTRFVLkKALE----QNLkpVVV 129
Cdd:COG5257 72 ncGSetellrRVSFVDAPGH-------ETLMatmlsgaALMDGAILVIAANEPCpQPQTKEHL-MALDiigiKNI--VIV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 130 VNKIDkpsarpegVVDEVldlfiELEANDEQL-EF---------PVVYASAvngtasldpeKQDDNLQSLYETIIDYVPA 199
Cdd:COG5257 142 QNKID--------LVSKE-----RALENYEQIkEFvkgtvaenaPIIPVSA----------QHKVNIDALIEAIEEEIPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 200 PI-DNSDEPLQFQVALLDYN-------DYVGRIGIGRVFRGKMRVGDNVSL-----IKLDGTVKNFR-VTKIFG-YFGlk 264
Cdd:COG5257 199 PErDLSKPPRMLVARSFDVNkpgtppkDLKGGVIGGSLIQGVLKVGDEIEIrpgikVEKGGKTKYEPiTTTVVSlRAG-- 276
|
330
....*....|....*
gi 1799428405 265 RLEIEEAQAGDLIAV 279
Cdd:COG5257 277 GEEVEEAKPGGLVAV 291
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
10-134 |
4.42e-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: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELlkqSGIFrenehvderaMDSNDIERERGITI-LAKNTAVDYKGT----------------- 71
Cdd:cd01888 2 NIGTIGHVAHGKTTLVKAL---SGVW----------TVRHKEELKRNITIkLGYANAKIYKCPncgcprpydtpececpg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 72 ---------RINILDTPGHadfggevERIM-------KMVDGVVLVVDAYEGT-MPQTRFVLkKALE-QNLKPVVVV-NK 132
Cdd:cd01888 69 cggetklvrHVSFVDCPGH-------EILMatmlsgaAVMDGALLLIAANEPCpQPQTSEHL-AALEiMGLKHIIILqNK 140
|
..
gi 1799428405 133 ID 134
Cdd:cd01888 141 ID 142
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
10-132 |
5.56e-08 |
|
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: 51.47 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKQSGIfrenehVDERAmdsndiererGITILAKNTAVDYKGTRINILDTPG-----HADF 84
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAI------VSDYP----------GTTRDPNEGRLELKGKQIILVDTPGliegaSEGE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1799428405 85 G-GEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNK 132
Cdd:pfam01926 65 GlGRAFLAIIEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
76-213 |
6.91e-08 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 54.22 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 76 LDTPG-----HAdFG----GEVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPSArpegvvDE 146
Cdd:COG1159 56 VDTPGihkpkRK-LGrrmnKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKK------EE 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 147 VLDLFIELEandEQLEF-PVVYASAVNGtasldpekqdDNLQSLYETIIDYVPA-----PIDN-SDEPLQFQVA 213
Cdd:COG1159 129 LLPLLAEYS---ELLDFaEIVPISALKG----------DNVDELLDEIAKLLPEgppyyPEDQiTDRPERFLAA 189
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
7-174 |
1.46e-07 |
|
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: 51.66 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 7 DVRNIAIIAHVDHGKTTLVDELLKQsgifrenehvdERAMDSNdierERGITILAKNTAVDYKGTRINILDTPG-----H 81
Cdd:cd01895 1 DPIKIAIIGRPNVGKSSLLNALLGE-----------ERVIVSD----IAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 82 ADFGGE------VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKpsarpegvVDEVLDLFIELE 155
Cdd:cd01895 66 VTEGIEkysvlrTLKAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDL--------VEKDEKTMKEFE 137
|
170 180
....*....|....*....|....
gi 1799428405 156 AN-DEQLEF----PVVYASAVNGT 174
Cdd:cd01895 138 KElRRKLPFldyaPIVFISALTGQ 161
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
208-292 |
2.38e-07 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 48.41 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 208 LQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNvslIKLDGTVKNFRVTKIFgyfgLKRLEIEEAQAGDLIAVS--GMEDI 285
Cdd:cd01342 1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDE---IRILPKGITGRVTSIE----RFHEEVDEAKAGDIVGIGilGVKDI 73
|
....*..
gi 1799428405 286 NVGETVT 292
Cdd:cd01342 74 LTGDTLT 80
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
11-289 |
3.83e-07 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 53.13 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELlkqSGIfrENEHVDEramdsndiERERGITIlakNTAVDY----KGTRINILDTPGHADF-- 84
Cdd:PRK10512 3 IATAGHVDHGKTTLLQAI---TGV--NADRLPE--------EKKRGMTI---DLGYAYwpqpDGRVLGFIDVPGHEKFls 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 85 ------GGeverimkmVDGVVLVVDAYEGTMPQTR---FVLKkaLEQNLKPVVVVNKIDK-PSARPEGVVDEVLDLFIEL 154
Cdd:PRK10512 67 nmlagvGG--------IDHALLVVACDDGVMAQTRehlAILQ--LTGNPMLTVALTKADRvDEARIAEVRRQVKAVLREY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 155 EANDEQLeFPVVYASAVnGTASLdpekqDDNLQSLYETiidyvpapidnsDEPLQ--FQVALldynDYV------GRIGI 226
Cdd:PRK10512 137 GFAEAKL-FVTAATEGR-GIDAL-----REHLLQLPER------------EHAAQhrFRLAI----DRAftvkgaGLVVT 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 227 GRVFRGKMRVGDNVSLIKLDgtvKNFRVTkifgyfGL--KRLEIEEAQAGDLIA--VSG---MEDINVGE 289
Cdd:PRK10512 194 GTALSGEVKVGDTLWLTGVN---KPMRVR------GLhaQNQPTEQAQAGQRIAlnIAGdaeKEQINRGD 254
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
76-196 |
1.09e-06 |
|
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: 49.00 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 76 LDTPG-HADFGG-------EVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKaLEQNLKPVV-VVNKIDKPSARpegvvDE 146
Cdd:cd04163 56 VDTPGiHKPKKKlgermvkAAWSALKDVDLVLFVVDASEWIGEGDEFILEL-LKKSKTPVIlVLNKIDLVKDK-----ED 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1799428405 147 VLDLFIELEANDEQLEfpVVYASAVNGtasldpekqdDNLQSLYETIIDY 196
Cdd:cd04163 130 LLPLLEKLKELHPFAE--IFPISALKG----------ENVDELLEYIVEY 167
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
17-288 |
2.06e-06 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 50.70 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 17 VDHGKTTLVDELLKQSG-IF-----------RENEHVDERA-----MDSNDIERERGITIlakNTAVDYKGT---RINIL 76
Cdd:PRK05506 33 VDDGKSTLIGRLLYDSKmIFedqlaalerdsKKVGTQGDEIdlallVDGLAAEREQGITI---DVAYRYFATpkrKFIVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 77 DTPGHADFggeverIMKMVDG------VVLVVDAYEGTMPQTR---FVLKKALEQNLkpVVVVNKID---KPSARPEGVV 144
Cdd:PRK05506 110 DTPGHEQY------TRNMVTGastadlAIILVDARKGVLTQTRrhsFIASLLGIRHV--VLAVNKMDlvdYDQEVFDEIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 145 DEVLDLFIELEANDeqleFPVVYASAVNGtasldpekqdDNL------------QSLYEtIIDYVPAPIDNSDEPLQFQV 212
Cdd:PRK05506 182 ADYRAFAAKLGLHD----VTFIPISALKG----------DNVvtrsarmpwyegPSLLE-HLETVEIASDRNLKDFRFPV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 213 AL-----LDYNDYVGRIGIGRVfrgkmRVGDNVSLIKldgTVKNFRVTKIFGYFGlkrlEIEEAQAGDLIAVSGMEDINV 287
Cdd:PRK05506 247 QYvnrpnLDFRGFAGTVASGVV-----RPGDEVVVLP---SGKTSRVKRIVTPDG----DLDEAFAGQAVTLTLADEIDI 314
|
.
gi 1799428405 288 G 288
Cdd:PRK05506 315 S 315
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
95-213 |
2.18e-06 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 49.66 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 95 VDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKpsarpegvVDEVLDLFIELEANDEQLEF-PVVYASAVNG 173
Cdd:PRK00089 85 VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL--------VKDKEELLPLLEELSELMDFaEIVPISALKG 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1799428405 174 tasldpekqdDNLQSLYETIIDYVPA-----PIDN-SDEPLQFQVA 213
Cdd:PRK00089 157 ----------DNVDELLDVIAKYLPEgppyyPEDQiTDRPERFLAA 192
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
10-194 |
2.49e-06 |
|
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: 48.31 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 10 NIAIIAHVDHGKTTLVDELLKqsgifrenehvdERAMDSndiererGITIL-AKNTAVDY---KGtrINILDTPG----- 80
Cdd:cd09912 2 LLAVVGEFSAGKSTLLNALLG------------EEVLPT-------GVTPTtAVITVLRYgllKG--VVLVDTPGlnsti 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 81 --HADfggEVERIMKMVDGVVLVVDAyEGTMPQT-RFVLKKALEQNLKPVV-VVNKIDKpsARPEGVVDEVLDLFIELEA 156
Cdd:cd09912 61 ehHTE---ITESFLPRADAVIFVLSA-DQPLTESeREFLKEILKWSGKKIFfVLNKIDL--LSEEELEEVLEYSREELGV 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1799428405 157 NDEQLEFPVVYasAVNGTASLDPEKQDDNLQSLYETII 194
Cdd:cd09912 135 LELGGGEPRIF--PVSAKEALEARLQGDEELLEQSGFE 170
|
|
| Tet_C |
cd03711 |
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ... |
401-477 |
2.69e-06 |
|
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: 45.31 E-value: 2.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDmTTTDNGLTRLIFNVPARGMIGYTTEFMSMTRGYGIINHTFEEFRP 477
Cdd:cd03711 1 EPYLRFELEVPQDALGRAMSDLAKMGATFED-PQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRP 76
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
11-195 |
4.26e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 49.28 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 11 IAIIAHVDHGKTTLVDELLKQsgifrenehvdERAMDSNdierERGITILAKNTAVDYKGTRINILDTPG-------HAD 83
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGE-----------ERVIVSD----IAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 84 fggeVE--------RIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDkpsarpeGVVDEVLDLFI-EL 154
Cdd:PRK00093 241 ----VEkysvirtlKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWD-------LVDEKTMEEFKkEL 309
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1799428405 155 EANDEQLEF-PVVYASAVNGTasldpekqddNLQSLYETIID 195
Cdd:PRK00093 310 RRRLPFLDYaPIVFISALTGQ----------GVDKLLEAIDE 341
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
66-174 |
4.69e-06 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 46.80 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 66 VDYKGTRINILDtpghadFGGEvERIMKM-------VDGVVLVVDAYEGT-MPQTRFVLKKAL-EQNLK--PVVVV-NKI 133
Cdd:cd00878 38 VEYKNVKFTVWD------VGGQ-DKIRPLwkhyyenTDGLIFVVDSSDRErIEEAKNELHKLLnEEELKgaPLLILaNKQ 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799428405 134 DKPSARPEGVVDEVLDLFieleaNDEQLEFPVVYASAVNGT 174
Cdd:cd00878 111 DLPGALTESELIELLGLE-----SIKGRRWHIQPCSAVTGD 146
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
3-137 |
9.72e-06 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 48.64 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 3 NKREDVRNIAIIAHVDHGKTTLVDELLKQsgifreNEHVDEramDSNDIERERgITILAkntavDYKGTRINILDTPG-- 80
Cdd:PRK09518 270 AGPKAVGVVAIVGRPNVGKSTLVNRILGR------REAVVE---DTPGVTRDR-VSYDA-----EWAGTDFKLVDTGGwe 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 81 ------HADFGGEVERIMKMVDGVVLVVDAYEGtMPQTRFVLKKALEQNLKPV-VVVNKIDKPS 137
Cdd:PRK09518 335 advegiDSAIASQAQIAVSLADAVVFVVDGQVG-LTSTDERIVRMLRRAGKPVvLAVNKIDDQA 397
|
|
| EFG_III |
cd16262 |
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ... |
334-389 |
2.22e-05 |
|
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: 42.83 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1799428405 334 IQERLNQQLETDVSLKVS-NTDSPDTwVVAGRGELHLSILIENMRRE-GYELQVSKPQ 389
Cdd:cd16262 20 LSKALARLAEEDPTLRVSrDEETGQT-ILSGMGELHLEIIVERLKREyGVEVEVGKPQ 76
|
|
| EF4_II |
cd03699 |
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ... |
217-292 |
2.36e-05 |
|
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: 43.18 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 217 YNDYVGRIGIGRVFRGKMRVGDNvslIKLDGTVKNFRVTKIfGYFGLKRLEIEEAQAGDL-IAVSGM---EDINVGETVT 292
Cdd:cd03699 10 YDPYRGVVVLVRVFDGTLKKGDK---IRFMATGKEYEVLEV-GVFTPKMVPTDELSAGEVgYIIAGIksvKDARVGDTIT 85
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
20-178 |
2.60e-05 |
|
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441830 [Multi-domain] Cd Length: 189 Bit Score: 45.20 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 20 GKTTLVDELlkqSGIFREneHVDERAMDSNdIERERGITIlakntAVDY------KGTRINILDTPGHADFGGEVERIMK 93
Cdd:COG2229 24 GKTTFVRSI---SEIEPL--STEGRLTDAS-LETKTTTTV-----AFDFgrltlgDGLRLHLFGTPGQVRFDFMWDILLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 94 MVDGVVLVVDAYEGTMPQTRFVLkKALEQNLK--PVVV-VNKIDKPSARPEGVVDEVLDLfieleandeQLEFPVVYASA 170
Cdd:COG2229 93 GADGVVFLADSRRLEDSFNAESL-DFFEERLEklPFVVaVNKRDLPDALSLEELREALDL---------GPDVPVVEADA 162
|
....*...
gi 1799428405 171 VNGTASLD 178
Cdd:COG2229 163 RDGESVKE 170
|
|
| lepA_C |
cd03709 |
lepA_C: This family represents the C-terminal region of LepA, a GTP-binding protein localized ... |
401-477 |
3.09e-05 |
|
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: 42.48 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 401 EPFERVQCEVPQENAGAVIESLGARKGEMVDMTTTDNGLTRLIFNVPARGMIgytTEFM----SMTRGYGIINHTFEEFR 476
Cdd:cd03709 1 EPFVKATIITPSEYLGAIMELCQERRGVQKDMEYLDANRVMLTYELPLAEIV---YDFFdklkSISKGYASLDYELIGYR 77
|
.
gi 1799428405 477 P 477
Cdd:cd03709 78 E 78
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
66-141 |
4.09e-05 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 43.96 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 66 VDYKGTRINILDTPGHADFGGE--------VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDKPS 137
Cdd:cd01894 40 AEWGGREFILIDTGGIEPDDEGiskeireqAEIAIEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIK 119
|
....
gi 1799428405 138 ARPE 141
Cdd:cd01894 120 EEEE 123
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
66-223 |
6.13e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 45.79 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 66 VDYKGTRINILDTPG-----HADFGGE----VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNlKPV-VVVNKIDK 135
Cdd:COG1160 45 AEWGGREFTLIDTGGiepddDDGLEAEireqAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSG-KPViLVVNKVDG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 136 PSARpegvvDEVLDLFieleandeQLEFPVVYA-SAVNGTasldpekqddNLQSLYETIIDYVPAPIDNSDEPLQFQVAL 214
Cdd:COG1160 124 PKRE-----ADAAEFY--------SLGLGEPIPiSAEHGR----------GVGDLLDAVLELLPEEEEEEEEDDPIKIAI 180
|
....*....
gi 1799428405 215 ldyndyVGR 223
Cdd:COG1160 181 ------VGR 183
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
17-277 |
1.97e-04 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 44.13 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 17 VDHGKTTLVDELLKQSGIFRENE----HVDERAM-------------DSNDIERERGITIlakNTAVDYKGT---RINIL 76
Cdd:PRK05124 36 VDDGKSTLIGRLLHDTKQIYEDQlaslHNDSKRHgtqgekldlallvDGLQAEREQGITI---DVAYRYFSTekrKFIIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 77 DTPGHADFggevERIM----KMVDGVVLVVDAYEGTMPQTR---FVlkkALEQNLKPVVV-VNKID---KPSARPEGVVD 145
Cdd:PRK05124 113 DTPGHEQY----TRNMatgaSTCDLAILLIDARKGVLDQTRrhsFI---ATLLGIKHLVVaVNKMDlvdYSEEVFERIRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 146 EVLDlFIELEANDEQLEFpvVYASA------VNGTASLdPEKQDDNLQSLYETIidyvpaPIDNSDE--PLQFQVAL--- 214
Cdd:PRK05124 186 DYLT-FAEQLPGNLDIRF--VPLSAlegdnvVSQSESM-PWYSGPTLLEVLETV------DIQRVVDaqPFRFPVQYvnr 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799428405 215 --LDYNDYVGRIGIGRVfrgkmRVGDNVSLIKlDGTVKNfrVTKIFGYFGlkrlEIEEAQAGDLI 277
Cdd:PRK05124 256 pnLDFRGYAGTLASGVV-----KVGDRVKVLP-SGKESN--VARIVTFDG----DLEEAFAGEAI 308
|
|
| EF2_II |
cd16268 |
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ... |
224-293 |
2.01e-04 |
|
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: 40.66 E-value: 2.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1799428405 224 IGIGRVFRGKMRVGDNVSLI------KLDGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMEDINV--GETVTP 293
Cdd:cd16268 19 VAFGRVFSGTVRRGQEVYILgpkyvpGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGLVGLDDFLAksGTTTSS 96
|
|
| EFG_III |
pfam14492 |
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ... |
334-385 |
2.36e-04 |
|
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: 39.77 E-value: 2.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 334 IQERLNQQLETDVSLKVSNtdSPDT--WVVAGRGELHLSILIENMRREgYELQV 385
Cdd:pfam14492 21 LSKALNRLLEEDPTLRVER--DEETgeTILSGMGELHLEIVVDRLKRK-YGVEV 71
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
66-223 |
5.73e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.73 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 66 VDYKGTRINILDTPGHADFGGEVERIMK--------MVDGVVLVVDAYEGTMPQTRFVLKKALEQNlKPVV-VVNKIDKP 136
Cdd:PRK00093 44 AEWLGREFILIDTGGIEPDDDGFEKQIReqaelaieEADVILFVVDGRAGLTPADEEIAKILRKSN-KPVIlVVNKVDGP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 137 SARpEGVVDevldlFIELEANDeqlefpVVYASAVNGTasldpekqddNLQSLYETIIDYVPAPIDNSDEPLQFQVALld 216
Cdd:PRK00093 123 DEE-ADAYE-----FYSLGLGE------PYPISAEHGR----------GIGDLLDAILEELPEEEEEDEEDEPIKIAI-- 178
|
....*..
gi 1799428405 217 yndyVGR 223
Cdd:PRK00093 179 ----IGR 181
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
56-199 |
1.22e-03 |
|
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 39.75 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 56 GITILAKNTAVDYKGTRINILDTPGHADFGG--EVERIMKMV------DGVVLVVDAyegtmpqtrfvlkKALEQNL--- 124
Cdd:cd01879 29 GVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPysEDEKVARDFllgeepDLIVNVVDA-------------TNLERNLylt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 125 -------KPVVVV-NKIDKpsARPEGVVdevldlfIELEANDEQLEFPVVYASAVNGTasldpekqddNLQSLYETIIDY 196
Cdd:cd01879 96 lqllelgLPVVVAlNMIDE--AEKRGIK-------IDLDKLSELLGVPVVPTSARKGE----------GIDELLDAIAKL 156
|
...
gi 1799428405 197 VPA 199
Cdd:cd01879 157 AES 159
|
|
| mtEFG1_II_like |
cd04091 |
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ... |
228-292 |
1.37e-03 |
|
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.
Pssm-ID: 293908 [Multi-domain] Cd Length: 81 Bit Score: 38.04 E-value: 1.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799428405 228 RVFRGKMRVGDnvsLIKLDGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGmEDINVGETVT 292
Cdd:cd04091 20 RVYQGVLRKGD---TIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFG-IDCASGDTFT 80
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
66-208 |
1.98e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 40.81 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 66 VDYKGTRINILDTPGHADFGGEVERI--------MKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLkpVVVVNKIDKPS 137
Cdd:COG0486 256 INIGGIPVRLIDTAGLRETEDEVEKIgierareaIEEADLVLLLLDASEPLTEEDEEILEKLKDKPV--IVVLNKIDLPS 333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799428405 138 ARPEGVvdevldlfieleanDEQLEFPVVYASAVNGtasldpekqdDNLQSLYETIIDYVPAPIDNSDEPL 208
Cdd:COG0486 334 EADGEL--------------KSLPGEPVIAISAKTG----------EGIDELKEAILELVGEGALEGEGVL 380
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
88-170 |
2.10e-03 |
|
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: 39.22 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 88 VERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKIDkpsARPEGVVDEVLDLFieleandEQLEFPVVY 167
Cdd:cd01859 5 VRRIIKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKAD---LVPREVLEKWKEVF-------ESEGLPVVY 74
|
...
gi 1799428405 168 ASA 170
Cdd:cd01859 75 VSA 77
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
70-174 |
3.35e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 38.65 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 70 GTRINILDTPGhadFGG------EVERIMKMVD----------GVVLVVDAYEGTMPQTRFVLKKALEQNLKPVVVVNKI 133
Cdd:cd01876 44 GDKFRLVDLPG---YGYakvskeVREKWGKLIEeylenrenlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKA 120
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1799428405 134 DKpsaRPEGVVDEVLDLFIELEANDEQLEfPVVYASAVNGT 174
Cdd:cd01876 121 DK---LKKSELAKVLKKIKEELNLFNILP-PVILFSSKKGT 157
|
|
| Arl9_Arfrp2_like |
cd04162 |
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ... |
65-189 |
4.80e-03 |
|
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.
Pssm-ID: 133362 [Multi-domain] Cd Length: 164 Bit Score: 38.20 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 65 AVDYKGTRINILDTPGHADFGGEVERIMKMVDGVVLVVD-AYEGTMPQTRFVLKKALEQN--LKPVVVVNKIDKPSARPE 141
Cdd:cd04162 38 AIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDsADSERLPLARQELHQLLQHPpdLPLVVLANKQDLPAARSV 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1799428405 142 GVVDEVLdlfiELEANDEQLEFPVVYASAVNGTASLDPEKQDDNLQSL 189
Cdd:cd04162 118 QEIHKEL----ELEPIARGRRWILQGTSLDDDGSPSRMEAVKDLLSQL 161
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
70-198 |
5.35e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.36 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 70 GTRINILDTPGHADFGG------EVERIMKMVDGVVLVVDAYEGTMPQTRFVLKKALEQNLKP--VVVVNKIDKpsARPE 141
Cdd:COG3596 87 LPGLVLLDTPGLGEVNErdreyrELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPDPpvLVVLTQVDR--LEPE 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799428405 142 GVVDEVLDLFIE---------LEANDEQLEFPVVYASAVngtaSLDPEKQDDNLQSLYETIIDYVP 198
Cdd:COG3596 165 REWDPPYNWPSPpkeqnirraLEAIAEQLGVPIDRVIPV----SAAEDRTGYGLEELVDALAEALP 226
|
|
| Tet_II |
cd03690 |
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ... |
205-291 |
6.71e-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: 36.06 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 205 DEPLQFQVALLDYNDYVGRIGIGRVFRGKMRVGDNVSLIkldGTVKNFRVTKIFGYFGLKRLEIEEAQAGDLIAVSGMED 284
Cdd:cd03690 1 ESELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVS---GEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKS 77
|
....*..
gi 1799428405 285 INVGETV 291
Cdd:cd03690 78 LRVGDVL 84
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
75-135 |
7.42e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 39.48 E-value: 7.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799428405 75 ILDTPGHADFGGEVERIMKMVDGVVLVVDAYEGTMPQTrFVLKKALEQNLKP-VVVVNKIDK 135
Cdd:PRK14845 530 FIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQT-IEAINILRQYKTPfVVAANKIDL 590
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
75-132 |
9.25e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 36.25 E-value: 9.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799428405 75 ILDTPGHADFGGEVERIM-----KMVDGVVLVVDAYEGTMPQTRFVL--KKALEQNLKP-VVVVNK 132
Cdd:cd01983 42 LIDGGGGLETGLLLGTIVallalKKADEVIVVVDPELGSLLEAVKLLlaLLLLGIGIRPdGIVLNK 107
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
66-208 |
9.96e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 38.62 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799428405 66 VDYKGTRINILDTPG---HADfggEVERI--------MKMVDGVVLVVDAYEGTMPQTRFVLKKaLEQNLKPVVVVNKId 134
Cdd:pfam12631 137 INIGGIPLRLIDTAGireTDD---EVEKIgierareaIEEADLVLLVLDASRPLDEEDLEILEL-LKDKKPIIVVLNKS- 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799428405 135 kpsarpegvvdevlDLFIELEANDEQLEFPVVYASAVNGTasldpekqddNLQSLYETIIDYVPAPIDNSDEPL 208
Cdd:pfam12631 212 --------------DLLGEIDELEELKGKPVLAISAKTGE----------GLDELEEAIKELFLAGEIASDGPI 261
|
|
| |
