|
Name |
Accession |
Description |
Interval |
E-value |
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
31-572 |
0e+00 |
|
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: 654.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 31 KPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRARGAQVTDIVV 110
Cdd:COG0532 1 VPRPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-GGKITFLDTPGHEAFTAMRARGAQVTDIVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 111 LVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAE 190
Cdd:COG0532 80 LVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEWGGDTIFVPVSAKTGEGIDELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 191 ATIALAEILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMPV 270
Cdd:COG0532 160 MILLQAEVLELKANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTAYGRVRAMFDDRGKRVKEAGPSTPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 271 GIIGWRDLPSAGDEILEVESEPRAREVIEWRkseqkeekgkddlkimEEKRREHQEAHRKArekyGSLHwkersyiKFLE 350
Cdd:COG0532 240 EILGLSGVPQAGDEFVVVEDEKKAREIAEKR----------------QQKAREKKLARQKR----VSLE-------DLFS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 351 RKQQRPLKpkekverqsnVLPIIIKGDVDGSVEAI---LNLLDTydasHECELELVHFGLGDISENDVTFAETFDGVIYG 427
Cdd:COG0532 293 QIKEGEVK----------ELNLILKADVQGSVEALkdsLEKLST----DEVKVNIIHSGVGAITESDVNLAAASNAIIIG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 428 FNVEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSSRLPHTLEEYPIGEASILATFTVTegkkKIP-VAGCRVQKGQ 506
Cdd:COG0532 359 FNVRPDAKARKLAEREGVDIRYYSIIYDLIDDVKAAMEGMLEPEYKEEILGRAEVREVFKVS----KVGtIAGCYVTEGK 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720367942 507 LERHKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLDEEKvEFKPGDQVICYEENKVP 572
Cdd:COG0532 435 IKRNAKVRVLRDGVVIYEGELESLKRFKDDVKEVRAGYECGIGLKNFN-DIKEGDIIEAFEMEEVK 499
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
6-571 |
0e+00 |
|
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: 531.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 6 SKLKQERIRENKDAVRRPGTDPALLKPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT 85
Cdd:TIGR00487 59 VKVEVRVTLEETEAEEQDEDSGDLLVERPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHVENEDGKMIT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 86 FLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYDVVC 165
Cdd:TIGR00487 139 FLDTPGHEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 166 EEYGGDVQAVHVSALTGDNLMALAEATIALAEILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGK 245
Cdd:TIGR00487 219 EDWGGDTIFVPVSALTGDGIDELLDMILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVGA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 246 SWAKVRLIFDENGKILNEAYPSMPVGIIGWRDLPSAGDEILEVESEPRAREVIEWRKSEQKEEKGKDDLKImeekrrehq 325
Cdd:TIGR00487 299 AYGRVRAMIDENGKSVKEAGPSKPVEILGLSDVPAAGDEFIVFKDEKDARLVAEKRAGKLRQKALSRSVKV--------- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 326 eahrkarekygslhwkersyiKFLERKQQrpLKPKEKVErqsnvLPIIIKGDVDGSVEAILNLLDTYDAShECELELVHF 405
Cdd:TIGR00487 370 ---------------------TLDNLFEQ--IKEGELKE-----LNIILKADVQGSLEAIKNSLEKLNNE-EVKVKVIHS 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 406 GLGDISENDVTFAETFDGVIYGFNVEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSSRLPHTLEEYPIGEASILAT 485
Cdd:TIGR00487 421 GVGGITETDISLASASNAIIIGFNVRPDATAKNVAEAENVDIRYYSVIYKLIDEIRAAMKGMLDPEYEEEIIGQAEVRQV 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 486 FTVTegkKKIPVAGCRVQKGQLERHKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLDEEKvEFKPGDQVIC 565
Cdd:TIGR00487 501 FNVP---KIGNIAGCYVTEGVIKRGNPLRVIRDGVVIFEGEIDSLKRFKDDVKEVSNGYECGIGIKNYN-DIKEGDIIEA 576
|
....*.
gi 1720367942 566 YEENKV 571
Cdd:TIGR00487 577 FEVQEV 582
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
33-567 |
5.50e-148 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 444.28 E-value: 5.50e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 33 RSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLP---SGEKITFLDTPGHAAFSAMRARGAQVTDIV 109
Cdd:CHL00189 243 RPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGAYEVEFEykdENQKIVFLDTPGHEAFSSMRSRGANVTDIA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 110 VLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALA 189
Cdd:CHL00189 323 ILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKWGGDTPMIPISASQGTNIDKLL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 190 EATIALAEILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMP 269
Cdd:CHL00189 403 ETILLLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTSYAKIRGMINSLGNKINLATPSSV 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 270 VGIIGWRDLPSAGDEILEVESEPRAREVIEwrkseQKEEKGKDDLKimeeKRREHQEAHrkarekygslhwkerSYIKFL 349
Cdd:CHL00189 483 VEIWGLSSVPATGEHFQVFNSEKEAKLKII-----KNKENNKKDTT----KRITLSTTK---------------TINKKD 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 350 ERKQqrplkpkekverqsnvLPIIIKGDVDGSVEAILNLLDTYDAShECELELVHFGLGDISENDVTFAETFDGVIYGFN 429
Cdd:CHL00189 539 NKKQ----------------INLIIKTDTQGSIEAIINSISQIPQK-KVQLNILYASLGEVTETDVEFASTTNAEILAFN 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 430 VEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSSRLPHTLEEYPIGEASILATFTVTEGKkkipVAGCRVQKGQLER 509
Cdd:CHL00189 602 TNLAPGAKKAARKLNIIIKEYQVIYDLLEYIEALMEDLLDPEYKKVPIGEAEVKTVFPLAKRF----VAGCRVTEGKITK 677
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720367942 510 HKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLdEEKVEFKPGDQVICYE 567
Cdd:CHL00189 678 NALIKVIRENKLIYEGKITSLKRVKEDVEEAQEGNECGIFI-EEFQLWQSGDKIHAFE 734
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
35-199 |
1.55e-98 |
|
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: 296.69 E-value: 1.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 35 PVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVV 113
Cdd:cd01887 1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPIDvKIPGITFIDTPGHEAFTNMRARGASVTDIAILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 114 AADDGVMKQTVESIQHAKDAEVPIILAINKCDK---TDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAE 190
Cdd:cd01887 81 AADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSELGLVGEEWGGDVSIVPISAKTGEGIDDLLE 160
|
....*....
gi 1720367942 191 ATIALAEIL 199
Cdd:cd01887 161 AILLLAEVL 169
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
33-561 |
4.41e-59 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 206.95 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 33 RSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAF 95
Cdd:PRK04004 5 RQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAgplkkplpiklkipgllFIDTPGHEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 96 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKT---------------DADPEKVKKEL-- 158
Cdd:PRK04004 85 TNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIpgwkstedapflesiEKQSQRVQQELee 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 159 LAYDVVCE--EYGGD-------------VQAVHVSALTG----DNLMALAeatiALAEIL---ELKADPTGPVEGTVIES 216
Cdd:PRK04004 165 KLYELIGQlsELGFSadrfdrvkdftktVAIVPVSAKTGegipDLLMVLA----GLAQRYleeRLKIDVEGPGKGTVLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 217 FTDKGRGPVTTAIIQRGTLRKG-SILVAGKSWA---KVRLIFdengkilneaypsmpvgiigwrdLPSAGDEILEVESep 292
Cdd:PRK04004 241 KEERGLGTTIDVILYDGTLRKGdTIVVGGKDGPivtKVRALL-----------------------KPRPLDEMRDPED-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 293 rareviewrKSEQKEE-----------KGKDD------LKIMEEkrREHQEAHRKAREKYgslhwkersyikflerkqqr 355
Cdd:PRK04004 296 ---------KFKPVDEvvaaagvkisaPDLEDalagspLRVVRD--EDVEEVKEEVEEEI-------------------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 356 plkpkEKVERQSNVLPIIIKGDVDGSVEAILNLLDtydashECELELVHFGLGDISENDVTFAET------FDGVIYGFN 429
Cdd:PRK04004 345 -----EEIRIETDEEGVVVKADTLGSLEALVNELR------EEGIPIRKADVGDISKRDVIEASTvaekdpLYGVILAFN 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 430 VEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEelssrlpHTLEEYPIGEASILATFTVTeGKKKI----------P-VA 498
Cdd:PRK04004 414 VKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEK-------WVKEQKEAEKEKILEKIVRP-AKIRIlpgyvfrqsdPaIV 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720367942 499 GCRVQKGQLERhkKFKLIR-NGQVIwkGSLTSLKHHKDDISVIKTGMDCGLSLDEEKV--EFKPGD 561
Cdd:PRK04004 486 GVEVLGGTIKP--GVPLIKeDGKRV--GTIKQIQDQGENVKEAKAGMEVAISIDGPTVgrQIKEGD 547
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
33-552 |
9.43e-45 |
|
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: 167.30 E-value: 9.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 33 RSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGA--------------FLVSLPSGEKIT---FLDTPGHAAF 95
Cdd:TIGR00491 3 RQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAsevptdviekicgdLLKSFKIKLKIPgllFIDTPGHEAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 96 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA-----------------DPEKVKKEL 158
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGwkshegypflesinkqeQRVRQNLDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 159 LAYDVVCE--EYGGD-------------VQAVHVSALTGDNLMALAEATIALAE-ILE--LKADPTGPVEGTVIESFTDK 220
Cdd:TIGR00491 163 QVYNLVIQlaEQGFNaerfdrirdftktVAIIPVSAKTGEGIPELLAILAGLAQnYLEnkLKLAIEGPAKGTILEVKEEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 221 GRGPVTTAIIQRGTLRKGSILVAGKS----WAKVRLIFdengkilneaypsmpvgiigwrdLPSAGDEILEVESEPRARE 296
Cdd:TIGR00491 243 GLGYTIDAVIYDGILRKGDIIVLAGIddviVTRVRAIL-----------------------KPRPLQEMRLARKKFAQVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 297 VIEWRKSEQKEEKGKDDLKIMEEKRREHQEAHRKAREkygslhwkersyikflerkqqRPLKPKEKVERQSNVLPIIIKG 376
Cdd:TIGR00491 300 EVYAAAGVKVAAPNLDTVLAGSPIVVENNEEIEKYKE---------------------EIQKEVEEIKIYTDEEGIVVKA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 377 DVDGSVEAILNLL-DTYDASHECElelvhfgLGDISENDVTFAETFD------GVIYGFNVEAGSAIQQSAAQKGVKIKL 449
Cdd:TIGR00491 359 DTLGSLEALVNELrRRGIPIKKAD-------IGDVSKRDVVEAEIVKqeakeyGAIAAFNVKPLPGAEIEAEKYDIKLFS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 450 HKIIYHLIEDLQE----ELSSRLPHTLEEYpIGEASILATFTVTEGKKKIPVAGCRVQKGQLERhkKFKLIR-NGQVIwk 524
Cdd:TIGR00491 432 DNIIYQLMENFEKwiedIEESEKRKTLEAI-IKPGKIKIIPGYVFRRSDPAIVGVEVLGGIIRP--GYPLIKkDGRRV-- 506
|
570 580
....*....|....*....|....*...
gi 1720367942 525 GSLTSLKHHKDDISVIKTGMDCGLSLDE 552
Cdd:TIGR00491 507 GEVRQIQDNGKNVKRASAGMEVAIAIED 534
|
|
| IF2_mtIF2_II |
cd03702 |
Domain II of bacterial and mitochondrial Initiation Factor 2; This family represents domain II ... |
208-302 |
2.22e-41 |
|
Domain II of bacterial and mitochondrial Initiation Factor 2; This family represents domain II of bacterial Initiation Factor 2 (IF2) and its eukaryotic mitochondrial homolog mtIF2. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Bacterial IF-2 is structurally and functionally related to eukaryotic mitochondrial mtIF-2.
Pssm-ID: 293903 [Multi-domain] Cd Length: 96 Bit Score: 144.49 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 208 PVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMPVGIIGWRDLPSAGDEILE 287
Cdd:cd03702 1 LARGVVIESKLDKGRGPVATVLVQNGTLKVGDILVAGTTYGKVRAMIDDNGKRIKEAGPSTPVEILGLNGVPQAGDKFIV 80
|
90
....*....|....*
gi 1720367942 288 VESEPRAREVIEWRK 302
Cdd:cd03702 81 VDSEKEAREIAEKRQ 95
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
37-191 |
3.65e-39 |
|
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: 141.51 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKLRE--------TQVAA--------MEV---GGITQHIGAflVSLPSGE-KITFLDTPGHAAFS 96
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLLYytgaiskrGEVKGegeagldnLPEereRGITIKSAA--VSFETKDyLINLIDTPGHVDFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 97 AMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTD-ADPEKVKKELlaYDVVCEEYGGD---V 172
Cdd:pfam00009 84 KEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEV--SRELLEKYGEDgefV 161
|
170
....*....|....*....
gi 1720367942 173 QAVHVSALTGDNLMALAEA 191
Cdd:pfam00009 162 PVVPGSALKGEGVQTLLDA 180
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
48-551 |
3.68e-34 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 138.48 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 48 TTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAFSAMRARGAQVTDIVV 110
Cdd:PRK14845 475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICgpllkllkaeikipgllFIDTPGHEAFTSLRKRGGSLADLAV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 111 LVVAADDGVMKQTVESIQHAKDAEVPIILAINKCD-----------------KTDADPEKVKKELLAYDVVCEEYGGDVQ 173
Cdd:PRK14845 555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDlipgwnisedepfllnfNEQDQHALTELEIKLYELIGKLYELGFD 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 174 A---------------VHVSALTGDNLMALAEATIALAE-ILE--LKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTL 235
Cdd:PRK14845 635 AdrfdrvqdftrtvaiVPVSAKTGEGIPELLMMVAGLAQkYLEerLKLNVEGYAKGTILEVKEEKGLGTTIDAIIYDGTL 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 236 RKG-SILVAGKSWA---KVRLIF-----DEngkILNEAYPSMPVGIIgwrdLPSAGDEIleveSEPRAREVI---EWRKS 303
Cdd:PRK14845 715 RRGdTIVVGGPDDVivtKVRALLkpkplDE---IRDPRDKFDPVDEV----TAAAGVKI----AAPGLEEVLagsPIRIV 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 304 EQKEEkgkddlkimeekrrehqeahrkarekygslhwkersyikfLERKQQRPLKPKEKVERQSNVLPIIIKGDVDGSVE 383
Cdd:PRK14845 784 PTKEK----------------------------------------IEKAKEEVMKEVEEAKIETDKEGILIKADTLGSLE 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 384 AILNLLdtydasHECELELVHFGLGDISENDVTFA------ETFDGVIYGFNVEAGSAIQQSAAQKGVKIKLHKIIYHLI 457
Cdd:PRK14845 824 ALANEL------RKAGIPIKKAEVGDITKKDVIEAlsykqeNPLYGVILGFNVKVLPEAQEEAEKYGVKIFVDNIIYKLV 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 458 EDLQE---ELSSRLPHTLEEYPIGEASILATFTVTEGKKKIPVAGCRVQKGQLErhKKFKLIR-NGQVIwkGSLTSLKHH 533
Cdd:PRK14845 898 EDYTEwvkEEEEKKKRELFEKLIKPGIIRLLPDCIFRRSNPAIVGVEVLEGTLR--VGVTLIKeDGMKV--GTVRSIKDR 973
|
570
....*....|....*...
gi 1720367942 534 KDDISVIKTGMDCGLSLD 551
Cdd:PRK14845 974 GENVKEAKAGKAVAIAIE 991
|
|
| IF-2 |
pfam11987 |
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main ... |
360-461 |
2.00e-33 |
|
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main phylogenetic domains (Eukaryotes, Bacteria and Archaea). IF2 interacts with formylmethionine-tRNA, GTP, IF1, IF3 and both ribosomal subunits. Through these interactions, IF2 promotes the binding of the initiator tRNA to the A site in the smaller ribosomal subunit and catalyzes the hydrolysis of GTP following initiation-complex formation.
Pssm-ID: 463421 [Multi-domain] Cd Length: 116 Bit Score: 123.32 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 360 KEKVERQSNVLPIIIKGDVDGSVEAILNLLDTYDaSHECELELVHFGLGDISENDVTFAETFDGVIYGFNVEAGSAIQQS 439
Cdd:pfam11987 16 FSQIKEEVKELNLIIKADVQGSLEALKESLEKLS-NDEVKVNIIHSGVGAITESDVMLASASNAIIIGFNVRPDAKARKL 94
|
90 100
....*....|....*....|..
gi 1720367942 440 AAQKGVKIKLHKIIYHLIEDLQ 461
Cdd:pfam11987 95 AEKEGVDIRYYNIIYDLIDDVK 116
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
37-191 |
7.52e-31 |
|
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: 118.55 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKL---------------RETQVAAMEV-GGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRA 100
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLlyqtgaidrrgtrkeTFLDTLKEEReRGITIKTGVVEFEWP-KRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 101 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTD-ADPEKVKKE---LLAYDVVCEEYGGDVQAVH 176
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREikeLLKLIGFTFLKGKDVPIIP 160
|
170
....*....|....*
gi 1720367942 177 VSALTGDNLMALAEA 191
Cdd:cd00881 161 ISALTGEGIEELLDA 175
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
41-197 |
9.09e-27 |
|
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: 106.54 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 41 GHVDHGKTTLL--------DKLRETQVAamevgGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVV 110
Cdd:cd04171 6 GHIDHGKTTLIkaltgietDRLPEEKKR-----GITIDLGfAYL-DLPDGKRLGFIDVPGHEKFvKNMLA-GAGGIDAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 111 LVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDAD-PEKVKKELLAYdvvCEEYGG-DVQAVHVSALTGDNLMA 187
Cdd:cd04171 79 LVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVDEDrLELVEEEILEL---LAGTFLaDAPIFPVSSVTGEGIEE 155
|
170
....*....|
gi 1720367942 188 LAEATIALAE 197
Cdd:cd04171 156 LKNYLDELAE 165
|
|
| mtIF2_IVc |
cd03692 |
C2 subdomain of domain IV in mitochondrial translation initiation factor 2; This model ... |
478-565 |
2.52e-25 |
|
C2 subdomain of domain IV in mitochondrial translation initiation factor 2; This model represents the C2 subdomain of domain IV of mitochondrial translation initiation factor 2 (mtIF2) which adopts a beta-barrel fold displaying a high degree of structural similarity with domain II of the translation elongation factor EF-Tu. The C-terminal part of mtIF2 contains the entire fMet-tRNAfmet binding site of IF-2 and is resistant to proteolysis. This C-terminal portion consists of two domains, IF2 C1 and IF2 C2. IF2 C2 has been shown to contain all molecular determinants necessary and sufficient for the recognition and binding of fMet-tRNAfMet. Like IF2 from certain prokaryotes such as Thermus thermophilus, mtIF2lacks domain II which is thought to be involved in binding of E.coli IF-2 to 30S subunits.
Pssm-ID: 293893 [Multi-domain] Cd Length: 84 Bit Score: 99.49 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 478 GEASILATFTVTegkKKIPVAGCRVQKGQLERHKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLDEEKvEF 557
Cdd:cd03692 1 GEAEVRAVFKIS---KVGTIAGCYVTEGKIKRNAKVRVLRDGEVIYEGKISSLKRFKDDVKEVKKGYECGITLENFN-DI 76
|
....*...
gi 1720367942 558 KPGDQVIC 565
Cdd:cd03692 77 KEGDIIEA 84
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
35-190 |
5.53e-25 |
|
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: 101.29 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 35 PVVTVMGHVDHGKTTLLDKLRETQVAAME-VGGITQHIGAFLVSL-PSGEKITFLDTPGHAAFSAMR-------ARGAQV 105
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEyYPGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRrlyypqvERSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 106 TDIVVLVVAADDGVMKQTVEsIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAydvvcEEYGGDVqaVHVSALTGDNL 185
Cdd:TIGR00231 82 FDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDADLKTHVASEFA-----KLNGEPI--IPLSAETGKNI 153
|
....*
gi 1720367942 186 MALAE 190
Cdd:TIGR00231 154 DSAFK 158
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
41-251 |
5.38e-24 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 106.54 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 41 GHVDHGKTTLL--------DKLRETQVAamevgGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVV 110
Cdd:COG3276 7 GHIDHGKTTLVkaltgidtDRLKEEKKR-----GITIDLGfAYL-PLPDGRRLGFVDVPGHEKFiKNMLA-GAGGIDLVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 111 LVVAADDGVMKQTVE--------SIQHakdaevpIILAINKCDKtdADPEKVkkELLAYDvVCEEYGG----DVQAVHVS 178
Cdd:COG3276 80 LVVAADEGVMPQTREhlaildllGIKR-------GIVVLTKADL--VDEEWL--ELVEEE-IRELLAGtfleDAPIVPVS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720367942 179 ALTGDNLMALAEATIALAEILELKaDPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGS---ILVAGKSwAKVR 251
Cdd:COG3276 148 AVTGEGIDELRAALDALAAAVPAR-DADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDeleLLPSGKP-VRVR 221
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
37-238 |
5.00e-21 |
|
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: 96.99 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKL----------RETQVAAMEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 99
Cdd:TIGR01394 4 IAIIAHVDHGKTTLVDALlkqsgtfranEAVAERVMDSNdlererGIT--ILAKNTAIRyNGTKINIVDTPGHADFGGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 100 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHV 177
Cdd:TIGR01394 82 ERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVfdLFAELGADDEQLDFPIVYA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720367942 178 SALTGDNLMALAEATIALAEILEL--------KADPTGPVEG--TVIESFTDKGRgpVTTAIIQRGTLRKG 238
Cdd:TIGR01394 162 SGRAGWASLDLDDPSDNMAPLFDAivrhvpapKGDLDEPLQMlvTNLDYDEYLGR--IAIGRVHRGTVKKG 230
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
37-182 |
9.40e-21 |
|
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: 90.35 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKL-------RETQVAA---MEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 99
Cdd:cd01891 5 IAIIAHVDHGKTTLVDALlkqsgtfRENEEVGervMDSNdlererGIT--ILAKNTAITyKDTKINIIDTPGHADFGGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 100 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHV 177
Cdd:cd01891 83 ERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVfdLFLELNATDEQLDFPIVYA 162
|
....*
gi 1720367942 178 SALTG 182
Cdd:cd01891 163 SAKNG 167
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
37-182 |
1.35e-19 |
|
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: 87.04 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTL------------LDKLRETQVAamevgGITQHIG--AFLVSLPSGE-----------KITFLDTPG 91
Cdd:cd01889 3 VGLLGHVDSGKTSLakalseiastaaFDKNPQSQER-----GITLDLGfsSFEVDKPKHLednenpqienyQITLVDCPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 92 HAafSAMRA--RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCD-----KTDADPEKVKKELLayDVV 164
Cdd:cd01889 78 HA--SLIRTiiGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDlipeeERKRKIEKMKKRLQ--KTL 153
|
170
....*....|....*...
gi 1720367942 165 CEEYGGDVQAVHVSALTG 182
Cdd:cd01889 154 EKTRLKDSPIIPVSAKPG 171
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
36-242 |
2.01e-19 |
|
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: 91.86 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 36 VVTVMGHVDHGKTTLLDKLRETQVAAM---EVGGITQHIGAFLVSLPSgEKITFLDTPGHAAFSAMRARGAQVTDIVVLV 112
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAADRLpeeKKRGMTIDLGFAYFPLPD-YRLGFIDVPGHEKFISNAIAGGGGIDAALLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 113 VAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAEA 191
Cdd:TIGR00475 81 VDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTSAKTGQGIGELKKE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720367942 192 TIALAEILELKaDPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILV 242
Cdd:TIGR00475 161 LKNLLESLDIK-RIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLR 210
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
41-241 |
5.49e-19 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 90.50 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 41 GHVDHGKTTLL--------DKLRETQVAAMevggiTQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVVLV 112
Cdd:PRK10512 7 GHVDHGKTTLLqaitgvnaDRLPEEKKRGM-----TIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 113 VAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTD-ADPEKVKKELLAydvVCEEYGGDVQAVHV-SALTG------- 182
Cdd:PRK10512 82 VACDDGVMAQTREHLAILQLTGNPmLTVALTKADRVDeARIAEVRRQVKA---VLREYGFAEAKLFVtAATEGrgidalr 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720367942 183 DNLMALAEATIALAEILELKADptgpvegtviESFTDKGRGPVTTAIIQRGTLRKGSIL 241
Cdd:PRK10512 159 EHLLQLPEREHAAQHRFRLAID----------RAFTVKGAGLVVTGTALSGEVKVGDTL 207
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
42-193 |
2.58e-17 |
|
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: 79.89 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 42 HVDHGKTTLLDKLRE-----------TQVA-AMEVG---GITqhIGAFLVSLP----SGEK--ITFLDTPGHAAFSAMRA 100
Cdd:cd01890 8 HIDHGKSTLADRLLEltgtvseremkEQVLdSMDLErerGIT--IKAQAVRLFykakDGEEylLNLIDTPGHVDFSYEVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 101 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELlaydvvcEEY-GGDV-QAVHVS 178
Cdd:cd01890 86 RSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEI-------EDVlGLDAsEAILVS 158
|
170
....*....|....*
gi 1720367942 179 ALTGDNLMALAEATI 193
Cdd:cd01890 159 AKTGLGVEDLLEAIV 173
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
39-191 |
1.10e-16 |
|
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: 77.50 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 39 VMGHVDHGKTTLLDKLRETQVAAM-EVGGITQHIGAFLVSLPSG-EKITFLDTPGHAAFSAMRARG-----AQVTDIVVL 111
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVsDVPGTTRDPDVYVKELDKGkVKLVLVDTPGLDEFGGLGREElarllLRGADLILL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 112 VVAADDGVMKQTVE--SIQHAKDAEVPIILAINKCDKtdaDPEKVKKELLAYDVVCEEYGGDVqaVHVSALTGDNLMALA 189
Cdd:cd00882 82 VVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDL---LEEREVEELLRLEELAKILGVPV--FEVSAKTGEGVDELF 156
|
..
gi 1720367942 190 EA 191
Cdd:cd00882 157 EK 158
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
40-238 |
1.76e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 81.53 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 40 MGHVDHGKTTLLDKLreTQVAAmEVGGITQHIGAFLVSLPSgEK---ITF----------------LDTPGHAAFSAMRA 100
Cdd:PRK12736 18 IGHVDHGKTTLTAAI--TKVLA-ERGLNQAKDYDSIDAAPE-EKergITIntahveyetekrhyahVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 101 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELL-AYDvvceeYGGD- 171
Cdd:PRK12736 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLVD-DEELLElvemevRELLsEYD-----FPGDd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 172 VQAVHVSALtgdnlMALAEATIALAEILELKAD-----PTG----------PVEGTviesFTDKGRGPVTTAIIQRGTLR 236
Cdd:PRK12736 168 IPVIRGSAL-----KALEGDPKWEDAIMELMDAvdeyiPTPerdtdkpflmPVEDV----FTITGRGTVVTGRVERGTVK 238
|
..
gi 1720367942 237 KG 238
Cdd:PRK12736 239 VG 240
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
31-238 |
2.86e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 81.00 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 31 KPRSPVVTVmGHVDHGKTTLLDKLreTQVAAMEVG------------------GIT---QHIgaflvslpsgEKIT---- 85
Cdd:PRK00049 10 KPHVNVGTI-GHVDHGKTTLTAAI--TKVLAKKGGaeakaydqidkapeekarGITintAHV----------EYETekrh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 86 --FLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------K 156
Cdd:PRK00049 77 yaHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 157 ELLAydvvceEY---GGDVQAVHVSAltgdnLMALAEATIALAE--ILELKA-------DPTGPVEGTV---IES-FTDK 220
Cdd:PRK00049 156 ELLS------KYdfpGDDTPIIRGSA-----LKALEGDDDEEWEkkILELMDavdsyipTPERAIDKPFlmpIEDvFSIS 224
|
250
....*....|....*...
gi 1720367942 221 GRGPVTTAIIQRGTLRKG 238
Cdd:PRK00049 225 GRGTVVTGRVERGIIKVG 242
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
40-238 |
6.82e-16 |
|
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: 79.81 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 40 MGHVDHGKTTLLDKLreTQVAAMEVG------------------GIT---QHIgaflvslpsgEKIT------FLDTPGH 92
Cdd:COG0050 18 IGHVDHGKTTLTAAI--TKVLAKKGGakakaydqidkapeekerGITintSHV----------EYETekrhyaHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 93 AAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLaydvvc 165
Cdd:COG0050 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevRELL------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 166 EEY---GGDVQAVHVSAltgdnLMALAEATIALAE--ILELKA-------DPTG--------PVEGTviesFTDKGRGPV 225
Cdd:COG0050 159 SKYgfpGDDTPIIRGSA-----LKALEGDPDPEWEkkILELMDavdsyipEPERdtdkpflmPVEDV----FSITGRGTV 229
|
250
....*....|...
gi 1720367942 226 TTAIIQRGTLRKG 238
Cdd:COG0050 230 VTGRVERGIIKVG 242
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
37-146 |
2.53e-15 |
|
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: 75.00 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKL------------------RETQVAAMEVG-GITQHIGAFLVSLPSGEK----ITFLDTPGHA 93
Cdd:cd04167 3 VCIAGHLHHGKTSLLDMLieqthkrtpsvklgwkplRYTDTRKDEQErGISIKSNPISLVLEDSKGksylINIIDTPGHV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720367942 94 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDK 146
Cdd:cd04167 83 NFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
39-253 |
3.04e-15 |
|
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: 78.05 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 39 VMGHVDHGKTTLLDKLretqvaAMEVGGITQHI-----------G------AFLVSLPSGEK------------------ 83
Cdd:COG5256 12 VIGHVDHGKSTLVGRL------LYETGAIDEHIiekyeeeaekkGkesfkfAWVMDRLKEERergvtidlahkkfetdky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 84 -ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDADP---EKVKKEL 158
Cdd:COG5256 86 yFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAVNYSEkryEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 159 ------LAYDVvceeygGDVQAVHVSALTGDNLMALAEAT-----IALAEILELKADPTGPVEG----TVIESFTDKGRG 223
Cdd:COG5256 166 skllkmVGYKV------DKIPFIPVSAWKGDNVVKKSDNMpwyngPTLLEALDNLKEPEKPVDKplriPIQDVYSISGIG 239
|
250 260 270
....*....|....*....|....*....|...
gi 1720367942 224 PVTTAIIQRGTLRKGSILV---AGKSwAKVRLI 253
Cdd:COG5256 240 TVPVGRVETGVLKVGDKVVfmpAGVV-GEVKSI 271
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
31-238 |
7.09e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 77.17 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 31 KPRSPVVTVmGHVDHGKTTLLDKLreTQVAAmEVG-------------------GITqhIGAFLVSLPSGEK-ITFLDTP 90
Cdd:PLN03127 59 KPHVNVGTI-GHVDHGKTTLTAAI--TKVLA-EEGkakavafdeidkapeekarGIT--IATAHVEYETAKRhYAHVDCP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 91 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLAYdv 163
Cdd:PLN03127 133 GHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVVD-DEELLElvemelRELLSF-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 164 vcEEYGGD----VQAVHVSALTGDNLMALAEATIALAE-----ILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGT 234
Cdd:PLN03127 210 --YKFPGDeipiIRGSALSALQGTNDEIGKNAILKLMDavdeyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGT 287
|
....
gi 1720367942 235 LRKG 238
Cdd:PLN03127 288 IKVG 291
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
42-154 |
7.33e-15 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 77.75 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 42 HVDHGKTTLLDKL-------RETQVAA---MEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQ 104
Cdd:COG1217 14 HVDHGKTTLVDALlkqsgtfRENQEVAervMDSNdlererGIT--ILAKNTAVRyKGVKINIVDTPGHADFGGEVERVLS 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720367942 105 VTDIVVLVVAADDGVMKQT--VesIQHAKDAEVPIILAINKCDKTDADPEKV 154
Cdd:COG1217 92 MVDGVLLLVDAFEGPMPQTrfV--LKKALELGLKPIVVINKIDRPDARPDEV 141
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
37-238 |
7.90e-15 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 76.89 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKLretqvaAMEVGGITQHI-----------G------AFLVSLPSGEK---------------- 83
Cdd:PRK12317 9 LAVIGHVDHGKSTLVGRL------LYETGAIDEHIieelreeakekGkesfkfAWVMDRLKEERergvtidlahkkfetd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 84 ---ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD--GVMKQTVESIQHAKDAEVP-IILAINKCDKTDADPEK---V 154
Cdd:PRK12317 83 kyyFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINqLIVAINKMDAVNYDEKRyeeV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 155 KKEL------LAYDVvceeygGDVQAVHVSALTGDNLMALAEAT-----IALAEILELKADPTGPVEG----TVIESFTD 219
Cdd:PRK12317 163 KEEVskllkmVGYKP------DDIPFIPVSAFEGDNVVKKSENMpwyngPTLLEALDNLKPPEKPTDKplriPIQDVYSI 236
|
250
....*....|....*....
gi 1720367942 220 KGRGPVTTAIIQRGTLRKG 238
Cdd:PRK12317 237 SGVGTVPVGRVETGVLKVG 255
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
40-158 |
3.40e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 75.55 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 40 MGHVDHGKTTLLDK-LRETQV--AAMEVG---------------GITqhIGAFLVSLP-SGEKITFLDTPGHAAF----- 95
Cdd:PRK12740 1 VGHSGAGKTTLTEAiLFYTGAihRIGEVEdgtttmdfmpeererGIS--ITSAATTCEwKGHKINLIDTPGHVDFtgeve 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720367942 96 SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 158
Cdd:PRK12740 79 RALR-----VLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQL 136
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
39-199 |
6.62e-14 |
|
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: 69.58 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 39 VMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLPSGEKITFLDTPG-------HAAFSAMRARGAQVTDIVV 110
Cdd:cd00880 2 IFGRPNVGKSSLLNALlGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRADLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 111 LVVAADDGVMKQtVESIQHAKDAEVPIILAINKCDKTDADPEKVKkellaYDVVCEEYGGDVQAVHVSALTGDNLMALAE 190
Cdd:cd00880 82 LVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEEEL-----LRERKLELLPDLPVIAVSALPGEGIDELRK 155
|
....*....
gi 1720367942 191 atiALAEIL 199
Cdd:cd00880 156 ---KIAELL 161
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
40-201 |
8.67e-14 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 70.31 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 40 MGHVDHGKTTLLDKLreTQVAAMEVG------------------GITqhIGAFLVSLPSGEK-ITFLDTPGHAAF-SAMR 99
Cdd:cd01884 8 IGHVDHGKTTLTAAI--TKVLAKKGGakakkydeidkapeekarGIT--INTAHVEYETANRhYAHVDCPGHADYiKNMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 100 ARGAQVtDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLaydvvcEEYGGDV 172
Cdd:cd01884 84 TGAAQM-DGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMVD-DEELLElvemevRELL------SKYGFDG 155
|
170 180 190
....*....|....*....|....*....|.
gi 1720367942 173 QAVHVsaLTGDNLMAL--AEATIALAEILEL 201
Cdd:cd01884 156 DDTPI--VRGSALKALegDDPNKWVDKILEL 184
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
39-158 |
1.71e-13 |
|
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: 70.34 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 39 VMGHVDHGKTTLLDKLRETQVAAMEVG------------------GIT--QHIGAFLVslpSGEKITFLDTPGHAAFSAM 98
Cdd:cd04168 4 ILAHVDAGKTTLTESLLYTSGAIRELGsvdkgttrtdsmelerqrGITifSAVASFQW---EDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720367942 99 RARGAQVTDIVVLVVAADDGVMKQTvESIQHA-KDAEVPIILAINKCDKTDADPEKVKKEL 158
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQT-RILFRLlRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
39-158 |
3.80e-13 |
|
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: 72.39 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 39 VMGHVDHGKTTLL----------DKLRE-----TQVAAMEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 99
Cdd:COG0480 14 IVAHIDAGKTTLTerilfytgaiHRIGEvhdgnTVMDWMPEEqerGIT--ITSAATTCEwKGHKINIIDTPGHVDFTGEV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720367942 100 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 158
Cdd:COG0480 92 ERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQL 150
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
24-158 |
9.75e-13 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 70.86 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 24 GTDPALLKPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSL---PSGEKITFLDTPGHAAFSAMRA 100
Cdd:COG5180 389 GAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVPGdaeSVSGPAGLADQAGAAASTAMAD 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720367942 101 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 158
Cdd:COG5180 469 FVAPVTDATPVDVADVLGVRPDAILGGNVAPASGLDAETRIIEAEGAPATEDFVAAEL 526
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
37-260 |
1.82e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 70.12 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKL----------RETQVAAMEVGGITQHIGAFLVSLPSGEK-----ITFLDTPGHAAFSAMRAR 101
Cdd:PRK10218 8 IAIIAHVDHGKTTLVDKLlqqsgtfdsrAETQERVMDSNDLEKERGITILAKNTAIKwndyrINIVDTPGHADFGGEVER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 102 GAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHVSA 179
Cdd:PRK10218 88 VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVfdLFVNLDATDEQLDFPIVYASA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 180 LTG----------DNLMALAEATIALAEILELKADptGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAK 249
Cdd:PRK10218 168 LNGiagldhedmaEDMTPLYQAIVDHVPAPDVDLD--GPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGK 245
|
250
....*....|.
gi 1720367942 250 VRlifdeNGKI 260
Cdd:PRK10218 246 TR-----NAKV 251
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
31-241 |
1.47e-11 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 66.95 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 31 KPRSPVVTVmGHVDHGKTTLL---------------DKLRETQVAAMEVG-GITqhIGAFLVSLPSGEK-ITFLDTPGHA 93
Cdd:PLN03126 79 KPHVNIGTI-GHVDHGKTTLTaaltmalasmggsapKKYDEIDAAPEERArGIT--INTATVEYETENRhYAHVDCPGHA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 94 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLAydvvCE 166
Cdd:PLN03126 156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVD-DEELLElvelevRELLS----SY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 167 EYGGDvqavHVSALTGDNLMALaEATIA-----------LAEILEL--KADPTGPVEG---------TVIESFTDKGRGP 224
Cdd:PLN03126 231 EFPGD----DIPIISGSALLAL-EALMEnpnikrgdnkwVDKIYELmdAVDSYIPIPQrqtdlpfllAVEDVFSITGRGT 305
|
250
....*....|....*..
gi 1720367942 225 VTTAIIQRGTLRKGSIL 241
Cdd:PLN03126 306 VATGRVERGTVKVGETV 322
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
37-146 |
1.70e-11 |
|
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: 64.17 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLD---------------KLRETQVAAME-VGGITqhIGAFLVSL--------PSGEK--ITFLDTP 90
Cdd:cd01885 3 ICIIAHVDHGKTTLSDsllasagiiseklagKARYLDTREDEqERGIT--IKSSAISLyfeyeeekMDGNDylINLIDSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720367942 91 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDK 146
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| tufA |
CHL00071 |
elongation factor Tu |
41-238 |
1.85e-11 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 66.13 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 41 GHVDHGKTTLldklreTQVAAMEVGGITQHIGAFLVSLPSG--EK---ITF----------------LDTPGHAAFSAMR 99
Cdd:CHL00071 19 GHVDHGKTTL------TAAITMTLAAKGGAKAKKYDEIDSApeEKargITIntahveyetenrhyahVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 100 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPE-------KVKKELLAYDvvceeYGGD 171
Cdd:CHL00071 93 ITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVD-DEEllelvelEVRELLSKYD-----FPGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 172 vqavHVSALTGDNLMALaEATIALAE-----------ILEL--KAD---PTgPVEGT------VIES-FTDKGRGPVTTA 228
Cdd:CHL00071 167 ----DIPIVSGSALLAL-EALTENPKikrgenkwvdkIYNLmdAVDsyiPT-PERDTdkpflmAIEDvFSITGRGTVATG 240
|
250
....*....|
gi 1720367942 229 IIQRGTLRKG 238
Cdd:CHL00071 241 RIERGTVKVG 250
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
37-154 |
1.87e-11 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 66.90 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDK-LRET----QVAAMEVG-------------GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSA 97
Cdd:PRK13351 11 IGILAHIDAGKTTLTERiLFYTgkihKMGEVEDGttvtdwmpqeqerGIT--IESAATSCDWDNhRINLIDTPGHIDFTG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720367942 98 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKV 154
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKV 145
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
35-200 |
6.07e-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: 62.20 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 35 PVVTVmGHVDHGKTTLLDKL-------RETQVAAMEVGGITQHIG-----AFLV-SLP----------------SGEKIT 85
Cdd:cd04166 1 RFITC-GSVDDGKSTLIGRLlydsksiFEDQLAALERSKSSGTQGekldlALLVdGLQaereqgitidvayryfSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 86 FL--DTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT-----VES---IQHakdaevpIILAINKCDKTDADPEkvk 155
Cdd:cd04166 80 FIiaDTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTrrhsyIASllgIRH-------VVVAVNKMDLVDYDEE--- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720367942 156 kellAYDVVCEEYGG--------DVQAVHVSALTGDNLMALAEATI-----ALAEILE 200
Cdd:cd04166 150 ----VFEEIKADYLAfaaslgieDITFIPISALEGDNVVSRSENMPwykgpTLLEHLE 203
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
37-204 |
1.79e-10 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 59.99 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKLRETQVAAMEVG---GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSAMRA------RGAqvt 106
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLstnGVT--IDKKELKLDGLDvDLVIWDTPGQDEFRETRQfyarqlTGA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 107 DIVVLVVaadDGVMKQTVESI--------QHAKDAevPIILAINKCDKtdADPEKVKKELLAYDVVCEEYGGDVqaVHVS 178
Cdd:COG1100 81 SLYLFVV---DGTREETLQSLyelleslrRLGKKS--PIILVLNKIDL--YDEEEIEDEERLKEALSEDNIVEV--VATS 151
|
170 180
....*....|....*....|....*.
gi 1720367942 179 ALTGDNLMALAEatiALAEILELKAD 204
Cdd:COG1100 152 AKTGEGVEELFA---ALAEILRGEGD 174
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
37-185 |
2.78e-10 |
|
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: 61.07 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDK-LRETQVAAM----EVGG---------ITQHIGAFLVSLP---SGEKITFLDTPGHAAFSAmR 99
Cdd:cd04170 2 IALVGHSGSGKTTLAEAlLYATGAIDRlgrvEDGNtvsdydpeeKKRKMSIETSVAPlewNGHKINLIDTPGYADFVG-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 100 ARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYdvvceeYGGDVQAVHVS 178
Cdd:cd04170 81 TLSAlRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREA------FGRPVVPIQLP 154
|
....*..
gi 1720367942 179 ALTGDNL 185
Cdd:cd04170 155 IGEGDEF 161
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
29-203 |
4.37e-10 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 61.32 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 29 LLKPRSPVVTVMGHVDHGKTTLLDKLreTQVAAMEVGGI---TQHIGAFLVSLPSGEKITFLDTPG-------HAAFSAM 98
Cdd:COG3596 34 LVELPPPVIALVGKTGAGKSSLINAL--FGAEVAEVGVGrpcTREIQRYRLESDGLPGLVLLDTPGlgevnerDREYREL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 99 RARGAQVtDIVVLVVAADDGVMKQTVESIQ--HAKDAEVPIILAINKCDKTD-----------ADPEKVK--KELLAYdv 163
Cdd:COG3596 112 RELLPEA-DLILWVVKADDRALATDEEFLQalRAQYPDPPVLVVLTQVDRLEperewdppynwPSPPKEQniRRALEA-- 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720367942 164 VCEEYGGDVQAVH-VSALTGD---NLMALAEATI---------ALAEILELKA 203
Cdd:COG3596 189 IAEQLGVPIDRVIpVSAAEDRtgyGLEELVDALAealpeakrsRLARLLRAKA 241
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
41-270 |
5.06e-10 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 62.25 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 41 GHVDHGKTTLLDKLR-------ETQVAAME-----VGGITQHIG-AFLVSLPSGEK---IT--------------FL--D 88
Cdd:PRK05506 31 GSVDDGKSTLIGRLLydskmifEDQLAALErdskkVGTQGDEIDlALLVDGLAAEReqgITidvayryfatpkrkFIvaD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 89 TPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdaevpIILAINKCDKTDADPEKvkkella 160
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTrrhsfiasLLGIRH-------VVLAVNKMDLVDYDQEV------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 161 YDVVCEEYG--------GDVQAVHVSALTGDNLMALAEAT-----IALAEILElkadpTGPVEGTviESFTDKgRGPVTT 227
Cdd:PRK05506 177 FDEIVADYRafaaklglHDVTFIPISALKGDNVVTRSARMpwyegPSLLEHLE-----TVEIASD--RNLKDF-RFPVQY 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720367942 228 AI------------IQRGTLRKG---SILVAGKSwAKVRLIFDENGKiLNEAYPSMPV 270
Cdd:PRK05506 249 VNrpnldfrgfagtVASGVVRPGdevVVLPSGKT-SRVKRIVTPDGD-LDEAFAGQAV 304
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
84-195 |
6.82e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 60.39 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 84 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKtdAD 150
Cdd:COG1159 53 IVFVDTPGihkpkrklgrrmnKAAWSALED-----VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720367942 151 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGDNLMALAEATIAL 195
Cdd:COG1159 126 KEELLPLLAEY----SELLDFAEIVPISALKGDNVDELLDEIAKL 166
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
36-272 |
4.85e-09 |
|
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: 58.56 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 36 VVTVmGHVDHGKTTLL-------DKLRETQVAAME-----VGgiTQHIG-AFLV-SLPSgEK---IT------------- 85
Cdd:COG2895 20 FITC-GSVDDGKSTLIgrllydtKSIFEDQLAALErdskkRG--TQEIDlALLTdGLQA-EReqgITidvayryfstpkr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 86 -FL--DTPGHAAFSamR--ARGAQVTDIVVLVVAADDGVMKQT-----VES---IQHakdaevpIILAINKCDKTDADPE 152
Cdd:COG2895 96 kFIiaDTPGHEQYT--RnmVTGASTADLAILLIDARKGVLEQTrrhsyIASllgIRH-------VVVAVNKMDLVDYSEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 153 ---KVKKELLAYdvvCEEYG-GDVQAVHVSALTGDNLMALAEAT--------IALAEILELKADPTG-----PVEgTVIE 215
Cdd:COG2895 167 vfeEIVADYRAF---AAKLGlEDITFIPISALKGDNVVERSENMpwydgptlLEHLETVEVAEDRNDapfrfPVQ-YVNR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720367942 216 sFTDKGRGPVTTaiIQRGTLRKG---SILVAGKSwAKVRLI--FDENgkiLNEAYPSMPVGI 272
Cdd:COG2895 243 -PNLDFRGYAGT--IASGTVRVGdevVVLPSGKT-STVKSIvtFDGD---LEEAFAGQSVTL 297
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
37-143 |
4.88e-09 |
|
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: 54.16 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKL--RETQVAAMEvgGITQHIGAFLVSLpSGEKITFLDTPG-----HAAFSAMRA-RGAQVTDI 108
Cdd:pfam01926 2 VALVGRPNVGKSTLINALtgAKAIVSDYP--GTTRDPNEGRLEL-KGKQIILVDTPGliegaSEGEGLGRAfLAIIEADL 78
|
90 100 110
....*....|....*....|....*....|....*
gi 1720367942 109 VVLVVAADDGVMKQTVESIQHAKDAEVPIILAINK 143
Cdd:pfam01926 79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
40-158 |
5.50e-09 |
|
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: 57.50 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 40 MGHVDHGKTTL--LDKLRETqvaamevgGITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAAD 116
Cdd:cd01886 29 IGEVHGGGATMdwMEQERER--------GIT--IQSAATTCFwKDHRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAV 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720367942 117 DGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 158
Cdd:cd01886 99 AGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
41-322 |
6.29e-09 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 58.39 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 41 GHVDHGKTTLLDKL-------RETQVAAME-----VGGITQHIG-AFLVS-LP----------------SGEKITFL--D 88
Cdd:PRK05124 34 GSVDDGKSTLIGRLlhdtkqiYEDQLASLHndskrHGTQGEKLDlALLVDgLQaereqgitidvayryfSTEKRKFIiaD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 89 TPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdaevpIILAINKCDKTDADP---EKVKKE 157
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTrrhsfiatLLGIKH-------LVVAVNKMDLVDYSEevfERIRED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 158 LLAYdvvCEEYGG--DVQAVHVSALTGDNLMALAEAT-----IALAEILEL----KADPTGPVEGTVI------ESFtdk 220
Cdd:PRK05124 187 YLTF---AEQLPGnlDIRFVPLSALEGDNVVSQSESMpwysgPTLLEVLETvdiqRVVDAQPFRFPVQyvnrpnLDF--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 221 gRGPVTTaiIQRGTLRKGSILVA---GKSwAKVRLI--FDENgkiLNEAYPSMPVGIIGWRDLP-SAGDEILEVESEPRA 294
Cdd:PRK05124 261 -RGYAGT--LASGVVKVGDRVKVlpsGKE-SNVARIvtFDGD---LEEAFAGEAITLVLEDEIDiSRGDLLVAADEALQA 333
|
330 340 350
....*....|....*....|....*....|...
gi 1720367942 295 REVIE----WRkSEQKEEKGKD-DLKIMEEKRR 322
Cdd:PRK05124 334 VQHASadvvWM-AEQPLQPGQSyDIKIAGKKTR 365
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
84-196 |
1.37e-08 |
|
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: 54.39 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 84 ITFLDTPG-------------HAAFSAMRarGAqvtDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDaD 150
Cdd:cd04163 53 IIFVDTPGihkpkkklgermvKAAWSALK--DV---DLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVK-D 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720367942 151 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGDNLMALAEATIALA 196
Cdd:cd04163 127 KEDLLPLLEKL----KELHPFAEIFPISALKGENVDELLEYIVEYL 168
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
42-146 |
3.04e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 56.80 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 42 HVDHGKTTLLDKL--------RET--QVAAM---EVG---GITqhIGAFLVSLP---SGEK--ITFLDTPGHAAFSAMRA 100
Cdd:PRK07560 28 HIDHGKTTLSDNLlagagmisEELagEQLALdfdEEEqarGIT--IKAANVSMVheyEGKEylINLIDTPGHVDFGGDVT 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720367942 101 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDK 146
Cdd:PRK07560 106 RAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDR 151
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
84-208 |
6.87e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 54.28 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 84 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDaD 150
Cdd:PRK00089 55 IIFVDTPGihkpkralnramnKAAWSSLKD-----VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVK-D 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720367942 151 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGDNLMALAEatiALAEILelkadPTGP 208
Cdd:PRK00089 129 KEELLPLLEEL----SELMDFAEIVPISALKGDNVDELLD---VIAKYL-----PEGP 174
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
81-191 |
2.86e-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: 50.51 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 81 GEKITFLDTPG----------HAAFSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA 149
Cdd:cd01895 49 GQKYTLIDTAGirkkgkvtegIEKYSVLRTLKAiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEK 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720367942 150 DP---EKVKKEL------LAYdvvceeyggdVQAVHVSALTGDNLMALAEA 191
Cdd:cd01895 129 DEktmKEFEKELrrklpfLDY----------APIVFISALTGQGVDKLFDA 169
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
6-199 |
3.43e-07 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 50.92 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 6 SKLKQE-----RIRENKDAVRRpgtdpallKPRSPVVTVMGHVDHGKTTLLDKL--RETQVAAMevggitqhigafL--- 75
Cdd:cd01878 16 AKLRKElekvkKQRELQRARRK--------RSGVPTVALVGYTNAGKSTLFNALtgADVLAEDQ------------Lfat 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 76 -------VSLPSGEKITFLDTPG------H---AAFSAM--RARGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDAE 134
Cdd:cd01878 76 ldpttrrIKLPGGREVLLTDTVGfirdlpHqlvEAFRSTleEVAEA---DLLLHVVdASDPDREEQieTVEEVLKELGAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720367942 135 -VPIILAINKCDKtdADPEKVKKELLAydvvceeygGDVQAVHVSALTGDNLMALAEatiALAEIL 199
Cdd:cd01878 153 dIPIILVLNKIDL--LDDEELEERLRA---------GRPDAVFISAKTGEGLDLLKE---AIEELL 204
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
39-238 |
2.38e-06 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 50.24 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 39 VMGHVDHGKTTLLDKLreTQVAAM----EVG-GITQHIG----------------AFLVSlPSGE----------KITFL 87
Cdd:PRK04000 14 MVGHVDHGKTTLVQAL--TGVWTDrhseELKrGITIRLGyadatirkcpdceepeAYTTE-PKCPncgsetellrRVSFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 88 DTPGHAAFSAMRARGAQVTDIVVLVVAADDGV-MKQTVEsiqHAKDAEV----PIILAINKCDKTdaDPEKVK------K 156
Cdd:PRK04000 91 DAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKE---HLMALDIigikNIVIVQNKIDLV--SKERALenyeqiK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 157 ELLAyDVVCEeyggDVQAVHVSALTGDNLMALAEAtIAlAEILELKADPTGPVEGTVIESFT--------DKGRGPVTTA 228
Cdd:PRK04000 166 EFVK-GTVAE----NAPIIPVSALHKVNIDALIEA-IE-EEIPTPERDLDKPPRMYVARSFDvnkpgtppEKLKGGVIGG 238
|
250
....*....|
gi 1720367942 229 IIQRGTLRKG 238
Cdd:PRK04000 239 SLIQGVLKVG 248
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
81-191 |
3.06e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 49.64 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 81 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA 149
Cdd:COG1160 222 GKKYTLIDTAGirrkgkvDEGiekYSVLRTLRAiERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEK 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720367942 150 DP---EKVKKEL------LAYdvvceeyggdVQAVHVSALTG---DNLMALAEA 191
Cdd:COG1160 302 DRktrEELEKEIrrrlpfLDY----------APIVFISALTGqgvDKLLEAVDE 345
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
42-158 |
3.08e-06 |
|
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: 49.13 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 42 HVDHGKTTLLDKL---------------RETQVAA----MEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAM 98
Cdd:cd04169 10 HPDAGKTTLTEKLllfggaiqeagavkaRKSRKHAtsdwMEIEkqrGIS--VTSSVMQFEyKGCVINLLDTPGHEDFSED 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720367942 99 RARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADP----EKVKKEL 158
Cdd:cd04169 88 TYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPlellDEIENEL 151
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
76-200 |
7.86e-06 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 48.54 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 76 VSLPSGEKITFLDTPG------H---AAFSA--MRARGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDA-EVPIILA 140
Cdd:COG2262 241 LELPDGRPVLLTDTVGfirklpHqlvEAFRStlEEVREA---DLLLHVVdASDPDFEEQieTVNEVLEELGAdDKPIILV 317
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 141 INKCDKTDADPEKVKKEllaydvvceeygGDVQAVHVSALTGDNLMALAEatiALAEILE 200
Cdd:COG2262 318 FNKIDLLDDEELERLRA------------GYPDAVFISAKTGEGIDELLE---AIEERLP 362
|
|
| Ras_dva |
cd04147 |
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ... |
79-145 |
2.33e-05 |
|
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - dorsal-ventral anterior localization) subfamily consists of a set of proteins characterized only in Xenopus leavis, to date. In Xenopus Ras-dva expression is activated by the transcription factor Otx2 and begins during gastrulation throughout the anterior ectoderm. Ras-dva expression is inhibited in the anterior neural plate by factor Xanf1. Downregulation of Ras-dva results in head development abnormalities through the inhibition of several regulators of the anterior neural plate and folds patterning, including Otx2, BF-1, Xag2, Pax6, Slug, and Sox9. Downregulation of Ras-dva also interferes with the FGF-8a signaling within the anterior ectoderm. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.
Pssm-ID: 206714 [Multi-domain] Cd Length: 197 Bit Score: 45.60 E-value: 2.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720367942 79 PSGEKITF--LDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESI-----QHAKDAEVPIILAINKCD 145
Cdd:cd04147 42 VAGVKVTIdiLDTSGSYSFPAMRKLSIQNGDAFALVYSVDDPESFEEVKRLreeilEVKEDKFVPIVVVGNKID 115
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
107-195 |
7.30e-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: 43.19 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 107 DIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDktdadpeKVKKELLAYDvvCEEYG-GDVqaVHVSALTGDNL 185
Cdd:cd01894 78 DVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID-------NIKEEEEAAE--FYSLGfGEP--IPISAEHGRGI 146
|
90
....*....|
gi 1720367942 186 MALAEATIAL 195
Cdd:cd01894 147 GDLLDAILEL 156
|
|
| RalA_RalB |
cd04139 |
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ... |
76-185 |
1.16e-04 |
|
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206710 [Multi-domain] Cd Length: 163 Bit Score: 42.80 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 76 VSLPSGE-KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD----GVMKQTVESIQHAKDAE-VPIILAINKCDKTDa 149
Cdd:cd04139 41 VVLDGEEvQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDmesfTALAEFREQILRVKEDDnVPLLLVGNKCDLED- 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720367942 150 dpeKVKKELLAYDVVCEEYGgdVQAVHVSALTGDNL 185
Cdd:cd04139 120 ---KRQVSVEEAANLAEQWG--VNYVETSAKTRANV 150
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
35-159 |
1.37e-04 |
|
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.
Pssm-ID: 206691 [Multi-domain] Cd Length: 202 Bit Score: 43.46 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 35 PVVTVMGHVDHGKTTLLDKL-----RETQVAamevggITQHIGAFLVSLPSGEKITFLDTPGHAAFSAM-------RARG 102
Cdd:cd04105 1 PTVLLLGPSDSGKTALFTKLttgkvRSTVTS------IEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKlleylkaSLKA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720367942 103 aqvtdiVVLVV--AADDGVMKQTVE------SIQHAKDAEVPIILAINKCDKTDADPEKVKKELL 159
Cdd:cd04105 75 ------IVFVVdsATFQKNIRDVAEflydilTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELL 133
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
81-202 |
2.27e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.89 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 81 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA 149
Cdd:PRK00093 220 GQKYTLIDTAGirrkgkvTEGvekYSVIRTLKAiERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDE 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 150 DP-EKVKKEL------LAYdvvceeyggdVQAVHVSALTGDNLMALAEATIALAEILELK 202
Cdd:PRK00093 300 KTmEEFKKELrrrlpfLDY----------APIVFISALTGQGVDKLLEAIDEAYENANRR 349
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
66-185 |
5.80e-04 |
|
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: 40.96 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 66 GITQHIGAFLVslpsGEKITFLDTPG--HAAFS-AMRARGAQVTD----------IVVLVVAADDGVMKQTVESIQHAKD 132
Cdd:cd01876 33 GRTQLINFFNV----GDKFRLVDLPGygYAKVSkEVREKWGKLIEeylenrenlkGVVLLIDARHGPTPIDLEMLEFLEE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720367942 133 AEVPIILAINKCDKtdADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNL 185
Cdd:cd01876 109 LGIPFLIVLTKADK--LKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGI 159
|
|
| Sar1 |
cd00879 |
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ... |
46-175 |
9.30e-04 |
|
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.
Pssm-ID: 206645 [Multi-domain] Cd Length: 191 Bit Score: 40.72 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 46 GKTTLLDKLRETQVAAMEVggiTQHigaflvslPSGEKITF-------LDTPGHAAfsAMRARG---AQVTDIVVLVVAA 115
Cdd:cd00879 31 GKTTLLHMLKDDRLAQHVP---TLH--------PTSEELTIgnvkfttFDLGGHEQ--ARRVWKdyfPEVDGIVFLVDAA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720367942 116 DdgvmkqtVESIQHAKD-----------AEVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAV 175
Cdd:cd00879 98 D-------PERFQESKEeldsllndeelANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLKV 161
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
36-145 |
9.59e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 42.09 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 36 VVTVMGHVDHGKTTLLDKLRETQVAAME-VGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRARGA 103
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAVVEdTPGVTRD----RVSYDaewAGTDFKLVDTGGweadvegiDSAIASQAQIAV 352
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720367942 104 QVTDIVVLVVAADDGvMKQTVESI-QHAKDAEVPIILAINKCD 145
Cdd:PRK09518 353 SLADAVVFVVDGQVG-LTSTDERIvRMLRRAGKPVVLAVNKID 394
|
|
| Ras |
cd00876 |
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ... |
83-145 |
2.18e-03 |
|
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206642 [Multi-domain] Cd Length: 160 Bit Score: 39.05 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720367942 83 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAKDAE-VPIILAINKCD 145
Cdd:cd00876 48 TLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSResfeEIKNIREQILRVKDKEdVPIVLVGNKCD 115
|
|
| IF2_IF5B_II |
cd03701 |
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ... |
208-288 |
2.40e-03 |
|
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents domain II of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologue aeIF5B. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.
Pssm-ID: 293902 [Multi-domain] Cd Length: 96 Bit Score: 37.65 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 208 PVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKS----WAKVRLIFD----------ENGKILNEAYPSMPVGII 273
Cdd:cd03701 1 EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESkdviYTRIRALLDpdpleemesrKKGNKRKEVGAASGVKIL 80
|
90
....*....|....*.
gi 1720367942 274 GW-RDLPSAGDEILEV 288
Cdd:cd03701 81 GFgQELPHAGDPLEVV 96
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
107-197 |
2.73e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 38.63 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 107 DIVVLVVaadDGVMKQTVESIQ-HAKDAEVPIILAINKCDKTDADPEKVKKELLAydvvceeyggdvqAVHVSALTGDNL 185
Cdd:cd04164 84 DLVLLVV---DASEGLDEEDLEiLELPAKKPVIVVLNKSDLLSDAEGISELNGKP-------------IIAISAKTGEGI 147
|
90
....*....|..
gi 1720367942 186 MALAEATIALAE 197
Cdd:cd04164 148 DELKEALLELAG 159
|
|
| Rhes_like |
cd04143 |
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ... |
83-196 |
2.98e-03 |
|
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.
Pssm-ID: 133343 [Multi-domain] Cd Length: 247 Bit Score: 39.73 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 83 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAK---------DAEVPIILAINKCDKtdA 149
Cdd:cd04143 49 QLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNResfeEVCRLREQILETKsclknktkeNVKIPMVICGNKADR--D 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720367942 150 DPEKVKKellayDVVCEEYGGDVQAVH--VSALTGDNLMALAEATIALA 196
Cdd:cd04143 127 FPREVQR-----DEVEQLVGGDENCAYfeVSAKKNSNLDEMFRALFSLA 170
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
37-202 |
4.36e-03 |
|
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: 38.30 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 37 VTVMGHVDHGKTTLLDKLRETQVAAMEVG---GITQHIGaflVSLPSGekITFLDTPGhaaFSAMRARGAQVT------- 106
Cdd:cd09912 3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTpttAVITVLR---YGLLKG--VVLVDTPG---LNSTIEHHTEITesflpra 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 107 DIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDK-TDADPEKVKKELLAYDVVCEEYGGDVQAVHVSA-LTGD 183
Cdd:cd09912 75 DAVIFVLSADQPLTESEREFLKEILKWSGKkIFFVLNKIDLlSEEELEEVLEYSREELGVLELGGGEPRIFPVSAkEALE 154
|
170
....*....|....*....
gi 1720367942 184 NLMALAEATIALAEILELK 202
Cdd:cd09912 155 ARLQGDEELLEQSGFEELE 173
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
32-191 |
4.37e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.95 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 32 PRSpvVTVMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLpSGEKITFLDTPG----------HAAFSAMRA 100
Cdd:PRK03003 211 PRR--VALVGKPNVGKSSLLNKLaGEERSVVDDVAGTTVDPVDSLIEL-GGKTWRFVDTAGlrrrvkqasgHEYYASLRT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 101 RGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADpekvKKELLAYDVvceeyggDVQAVHV-- 177
Cdd:PRK03003 288 HAAiEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNKWDLVDED----RRYYLEREI-------DRELAQVpw 356
|
170 180
....*....|....*....|
gi 1720367942 178 ------SALTGDNLMALAEA 191
Cdd:PRK03003 357 aprvniSAKTGRAVDKLVPA 376
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
35-150 |
6.51e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.18 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367942 35 PVVTVMGHVDHGKTTLLDKL---RETQVAamEVGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRA 100
Cdd:PRK03003 39 PVVAVVGRPNVGKSTLVNRIlgrREAVVE--DVPGVTRD----RVSYDaewNGRRFTVVDTGGwepdakglQASVAEQAE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720367942 101 RGAQVTDIVVLVV-------AADDGVMKQTVESiqhakdaEVPIILAINKCD--KTDAD 150
Cdd:PRK03003 113 VAMRTADAVLFVVdatvgatATDEAVARVLRRS-------GKPVILAANKVDdeRGEAD 164
|
|
| |
