|
Name |
Accession |
Description |
Interval |
E-value |
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
177-718 |
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: 668.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRARGAQVTDIVV 256
Cdd:COG0532 1 VPRPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-GGKITFLDTPGHEAFTAMRARGAQVTDIVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 257 LVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNLMALAE 336
Cdd:COG0532 80 LVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEWGGDTIFVPVSAKTGEGIDELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 337 ATIALAEMLELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILVAGKSWAKVRLMFDENGKTVNEAYPSMPV 416
Cdd:COG0532 160 MILLQAEVLELKANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTAYGRVRAMFDDRGKRVKEAGPSTPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 417 GIIGWRDLPSAGDEILEVQSEPRAREVVDWRKSEQKEEKGKDDLKI-MEEKRKEHQEAhrkarekygslhwkqrsyikyl 495
Cdd:COG0532 240 EILGLSGVPQAGDEFVVVEDEKKAREIAEKRQQKAREKKLARQKRVsLEDLFSQIKEG---------------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 496 ERKEqrplkpkekverdsnvLPIIIKGDVDGSVEAI---LNLLDTydasHECELELVHFGLGDISENDVTFAETFDGVIY 572
Cdd:COG0532 298 EVKE----------------LNLILKADVQGSVEALkdsLEKLST----DEVKVNIIHSGVGAITESDVNLAAASNAIII 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 573 GFNVDAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSNRLPYKVEEYPIGEASILATFTITegkkKVP-VAGCRVQKG 651
Cdd:COG0532 358 GFNVRPDAKARKLAEREGVDIRYYSIIYDLIDDVKAAMEGMLEPEYKEEILGRAEVREVFKVS----KVGtIAGCYVTEG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958676470 652 QLERQKKFKLIRNGQVIWKGSLTSLKHHKDDVLVIKTGVDCGLSLDEENvEFKVGDQVICYEENKVP 718
Cdd:COG0532 434 KIKRNAKVRVLRDGVVIYEGELESLKRFKDDVKEVRAGYECGIGLKNFN-DIKEGDIIEAFEMEEVK 499
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
97-717 |
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: 553.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 97 MTVEELARAMAKDTDCVYEALLNTAIdidSLEANSHLDEVWIKEVIKKAGmklkwSKLKLERIRENKDAVRRPGADPALL 176
Cdd:TIGR00487 12 LTVSELANKMNIKVSDIIKKLMLLGV---MVTINQVLDKETAELVAEEFG-----VKVEVRVTLEETEAEEQDEDSGDLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVV 256
Cdd:TIGR00487 84 VERPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHVENEDGKMITFLDTPGHEAFTSMRARGAKVTDIVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 257 LVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNLMALAE 336
Cdd:TIGR00487 164 LVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIFVPVSALTGDGIDELLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 337 ATIALAEMLELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILVAGKSWAKVRLMFDENGKTVNEAYPSMPV 416
Cdd:TIGR00487 244 MILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVGAAYGRVRAMIDENGKSVKEAGPSKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 417 GIIGWRDLPSAGDEILEVQSEPRAREVVDWRKSEQKEEKGKDDLKIMEEKRKEHqeahrkarekygslhwkqrsyIKYLE 496
Cdd:TIGR00487 324 EILGLSDVPAAGDEFIVFKDEKDARLVAEKRAGKLRQKALSRSVKVTLDNLFEQ---------------------IKEGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 497 RKEqrplkpkekverdsnvLPIIIKGDVDGSVEAILNLLDTYDAShECELELVHFGLGDISENDVTFAETFDGVIYGFNV 576
Cdd:TIGR00487 383 LKE----------------LNIILKADVQGSLEAIKNSLEKLNNE-EVKVKVIHSGVGGITETDISLASASNAIIIGFNV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 577 DAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSNRLPYKVEEYPIGEASILATFTITegkKKVPVAGCRVQKGQLERQ 656
Cdd:TIGR00487 446 RPDATAKNVAEAENVDIRYYSVIYKLIDEIRAAMKGMLDPEYEEEIIGQAEVRQVFNVP---KIGNIAGCYVTEGVIKRG 522
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958676470 657 KKFKLIRNGQVIWKGSLTSLKHHKDDVLVIKTGVDCGLSLDEENvEFKVGDQVICYEENKV 717
Cdd:TIGR00487 523 NPLRVIRDGVVIFEGEIDSLKRFKDDVKEVSNGYECGIGIKNYN-DIKEGDIIEAFEVQEV 582
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
71-713 |
1.11e-153 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 463.92 E-value: 1.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 71 TKKEKRPPRSQLS--PIKTKKEVEVWVGMTVEELARAMA-KDTDCVYEALLNTAididSLEANSHLDEVWIKEVIKKAGM 147
Cdd:CHL00189 138 KKKKVLSSKDELIkyDNNKPKSISIHSPLTIQELSTLLCiPETEIIKSLFLKGI----SVTVNQIIDISIISQVADDFGI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 148 KL----------KWSKLKlERIRENKDAVRRPgadpallkprsPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHI 217
Cdd:CHL00189 214 NIiseeknnineKTSNLD-NTSAFTENSINRP-----------PIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 218 GAFLVSLP---SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTD 294
Cdd:CHL00189 282 GAYEVEFEykdENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKAN 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 295 ADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNLMALAEATIALAEMLELKADPTGPVEGTVIESFTDKGRGPVTTA 374
Cdd:CHL00189 362 ANTERIKQQLAKYNLIPEKWGGDTPMIPISASQGTNIDKLLETILLLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATI 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 375 IIQRGTLKKGSILVAGKSWAKVRLMFDENGKTVNEAYPSMPVGIIGWRDLPSAGDEILEVQSEPRAREvvdwrKSEQKEE 454
Cdd:CHL00189 442 LVQNGTLHIGDIIVIGTSYAKIRGMINSLGNKINLATPSSVVEIWGLSSVPATGEHFQVFNSEKEAKL-----KIIKNKE 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 455 KGKDDLKimeeKRKEHQEAHrkarekygslhwkqrSYIKYLERKEqrplkpkekverdsnvLPIIIKGDVDGSVEAILNL 534
Cdd:CHL00189 517 NNKKDTT----KRITLSTTK---------------TINKKDNKKQ----------------INLIIKTDTQGSIEAIINS 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 535 LDTYDAShECELELVHFGLGDISENDVTFAETFDGVIYGFNVDAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSNRL 614
Cdd:CHL00189 562 ISQIPQK-KVQLNILYASLGEVTETDVEFASTTNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLEYIEALMEDLL 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 615 PYKVEEYPIGEASILATFTITEGKkkvpVAGCRVQKGQLERQKKFKLIRNGQVIWKGSLTSLKHHKDDVLVIKTGVDCGL 694
Cdd:CHL00189 641 DPEYKKVPIGEAEVKTVFPLAKRF----VAGCRVTEGKITKNALIKVIRENKLIYEGKITSLKRVKEDVEEAQEGNECGI 716
|
650
....*....|....*....
gi 1958676470 695 SLdEENVEFKVGDQVICYE 713
Cdd:CHL00189 717 FI-EEFQLWQSGDKIHAFE 734
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
181-345 |
7.93e-99 |
|
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: 301.70 E-value: 7.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 181 PVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVV 259
Cdd:cd01887 1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPIDvKIPGITFIDTPGHEAFTNMRARGASVTDIAILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 260 AADDGVMKQTVESIQHAKDAGVPIILAINKCDK---TDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNLMALAE 336
Cdd:cd01887 81 AADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSELGLVGEEWGGDVSIVPISAKTGEGIDDLLE 160
|
....*....
gi 1958676470 337 ATIALAEML 345
Cdd:cd01887 161 AILLLAEVL 169
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
179-689 |
4.08e-57 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 204.64 E-value: 4.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 179 RSPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAF 241
Cdd:PRK04004 5 RQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAgplkkplpiklkipgllFIDTPGHEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 242 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKT---------------DADPEKVKKEL-- 304
Cdd:PRK04004 85 TNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIpgwkstedapflesiEKQSQRVQQELee 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 305 LAYDVVCE--EYGGD-------------VQAVHVSALTGKN----LMALAeatiALAEML---ELKADPTGPVEGTVIES 362
Cdd:PRK04004 165 KLYELIGQlsELGFSadrfdrvkdftktVAIVPVSAKTGEGipdlLMVLA----GLAQRYleeRLKIDVEGPGKGTVLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 363 FTDKGRGPVTTAIIQRGTLKKG-SILVAGKSWA---KVRLMF-----------DENGKTVNEAYPSMPVGIIGwRDLPS- 426
Cdd:PRK04004 241 KEERGLGTTIDVILYDGTLRKGdTIVVGGKDGPivtKVRALLkprpldemrdpEDKFKPVDEVVAAAGVKISA-PDLEDa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 427 -AGDEILEVQSEPRArevvdwrkseqkeekgkddlKIMEEKRKEHQEAhrkarekygslhwkqrsyikylerkeqrplkp 505
Cdd:PRK04004 320 lAGSPLRVVRDEDVE--------------------EVKEEVEEEIEEI-------------------------------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 506 keKVERDSNvlPIIIKGDVDGSVEAILNLLDtydashECELELVHFGLGDISENDVTFAET------FDGVIYGFNVDAG 579
Cdd:PRK04004 348 --RIETDEE--GVVVKADTLGSLEALVNELR------EEGIPIRKADVGDISKRDVIEASTvaekdpLYGVILAFNVKVL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 580 SAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSNRlpYKVEEYPIGEASIL-ATFTITEG----KKKVPVAGCRVQKGQLE 654
Cdd:PRK04004 418 PDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQ--KEAEKEKILEKIVRpAKIRILPGyvfrQSDPAIVGVEVLGGTIK 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958676470 655 RqkKFKLIR-NGQVIwkGSLTSLKHHKDDVLVIKTG 689
Cdd:PRK04004 496 P--GVPLIKeDGKRV--GTIKQIQDQGENVKEAKAG 527
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
179-698 |
1.28e-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: 172.31 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 179 RSPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGA--------------FLVSLPSGEKIT---FLDTPGHAAF 241
Cdd:TIGR00491 3 RQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAsevptdviekicgdLLKSFKIKLKIPgllFIDTPGHEAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 242 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDA-----------------DPEKVKKEL 304
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGwkshegypflesinkqeQRVRQNLDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 305 LAYDVVCE--EYGGD-------------VQAVHVSALTGKNLMALAEATIALAEML---ELKADPTGPVEGTVIESFTDK 366
Cdd:TIGR00491 163 QVYNLVIQlaEQGFNaerfdrirdftktVAIIPVSAKTGEGIPELLAILAGLAQNYlenKLKLAIEGPAKGTILEVKEEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 367 GRGPVTTAIIQRGTLKKGSILVAGKS----WAKVRLMFdengktvneaypsmpvgiigwrdLPSAGDEILEVQSEPRARE 442
Cdd:TIGR00491 243 GLGYTIDAVIYDGILRKGDIIVLAGIddviVTRVRAIL-----------------------KPRPLQEMRLARKKFAQVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 443 VVDWRKSEQKEEKGKDDLKIMEEKRKEHQEAHRKAREkygslhwkqrsyikylerkeqRPLKPKEKVERDSNVLPIIIKG 522
Cdd:TIGR00491 300 EVYAAAGVKVAAPNLDTVLAGSPIVVENNEEIEKYKE---------------------EIQKEVEEIKIYTDEEGIVVKA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 523 DVDGSVEAILNLL-DTYDASHECElelvhfgLGDISENDVTFAETFD------GVIYGFNVDAGSAIQQSAAQKGVKIKL 595
Cdd:TIGR00491 359 DTLGSLEALVNELrRRGIPIKKAD-------IGDVSKRDVVEAEIVKqeakeyGAIAAFNVKPLPGAEIEAEKYDIKLFS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 596 HKIIYHLIEDLQ---EELSNRLPYKVEEYPIGEASILATFTITEGKKKVPVAGCRVQKGQLERqkKFKLIR-NGQVIwkG 671
Cdd:TIGR00491 432 DNIIYQLMENFEkwiEDIEESEKRKTLEAIIKPGKIKIIPGYVFRRSDPAIVGVEVLGGIIRP--GYPLIKkDGRRV--G 507
|
570 580
....*....|....*....|....*..
gi 1958676470 672 SLTSLKHHKDDVLVIKTGVDCGLSLDE 698
Cdd:TIGR00491 508 EVRQIQDNGKNVKRASAGMEVAIAIED 534
|
|
| IF2_mtIF2_II |
cd03702 |
Domain II of bacterial and mitochondrial Initiation Factor 2; This family represents domain II ... |
354-448 |
1.47e-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: 146.42 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 354 PVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILVAGKSWAKVRLMFDENGKTVNEAYPSMPVGIIGWRDLPSAGDEILE 433
Cdd:cd03702 1 LARGVVIESKLDKGRGPVATVLVQNGTLKVGDILVAGTTYGKVRAMIDDNGKRIKEAGPSTPVEILGLNGVPQAGDKFIV 80
|
90
....*....|....*
gi 1958676470 434 VQSEPRAREVVDWRK 448
Cdd:cd03702 81 VDSEKEAREIAEKRQ 95
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
183-337 |
2.19e-40 |
|
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: 146.52 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKLRE--------TQVAA--------MEV---GGITQHIGAflVSLPSGE-KITFLDTPGHAAFS 242
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLLYytgaiskrGEVKGegeagldnLPEereRGITIKSAA--VSFETKDyLINLIDTPGHVDFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 243 AMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTD-ADPEKVKKELlaYDVVCEEYGGD---V 318
Cdd:pfam00009 84 KEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEV--SRELLEKYGEDgefV 161
|
170
....*....|....*....
gi 1958676470 319 QAVHVSALTGKNLMALAEA 337
Cdd:pfam00009 162 PVVPGSALKGEGVQTLLDA 180
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
194-697 |
4.59e-35 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 143.10 E-value: 4.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 194 TTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAFSAMRARGAQVTDIVV 256
Cdd:PRK14845 475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICgpllkllkaeikipgllFIDTPGHEAFTSLRKRGGSLADLAV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 257 LVVAADDGVMKQTVESIQHAKDAGVPIILAINKCD-----------------KTDADPEKVKKELLAYDVVCE--EYGGD 317
Cdd:PRK14845 555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDlipgwnisedepfllnfNEQDQHALTELEIKLYELIGKlyELGFD 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 318 -------------VQAVHVSALTGKNLMALAEATIALAE-MLE--LKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTL 381
Cdd:PRK14845 635 adrfdrvqdftrtVAIVPVSAKTGEGIPELLMMVAGLAQkYLEerLKLNVEGYAKGTILEVKEEKGLGTTIDAIIYDGTL 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 382 KKG-SILVAGKSWA---KVRL---------MFDENGK--TVNEAYPSMPVGIigwrdlpsAGDEILEVQSEPRAREVvdw 446
Cdd:PRK14845 715 RRGdTIVVGGPDDVivtKVRAllkpkpldeIRDPRDKfdPVDEVTAAAGVKI--------AAPGLEEVLAGSPIRIV--- 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 447 rKSEQKEEKGKddlkimEEKRKEHQEAhrkarekygslhwkqrsyikylerkeqrplkpkeKVERDSnvLPIIIKGDVDG 526
Cdd:PRK14845 784 -PTKEKIEKAK------EEVMKEVEEA----------------------------------KIETDK--EGILIKADTLG 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 527 SVEAILNLLdtydasHECELELVHFGLGDISENDVTFA------ETFDGVIYGFNVDAGSAIQQSAAQKGVKIKLHKIIY 600
Cdd:PRK14845 821 SLEALANEL------RKAGIPIKKAEVGDITKKDVIEAlsykqeNPLYGVILGFNVKVLPEAQEEAEKYGVKIFVDNIIY 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 601 HLIEDLQE---ELSNRLPYKVEEYPIGEASILATFTITEGKKKVPVAGCRVQKGQLerQKKFKLIR-NGQVIwkGSLTSL 676
Cdd:PRK14845 895 KLVEDYTEwvkEEEEKKKRELFEKLIKPGIIRLLPDCIFRRSNPAIVGVEVLEGTL--RVGVTLIKeDGMKV--GTVRSI 970
|
570 580
....*....|....*....|.
gi 1958676470 677 KHHKDDVLVIKTGVDCGLSLD 697
Cdd:PRK14845 971 KDRGENVKEAKAGKAVAIAIE 991
|
|
| IF-2 |
pfam11987 |
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main ... |
506-607 |
2.53e-34 |
|
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: 126.79 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 506 KEKVERDSNVLPIIIKGDVDGSVEAILNLLDTYDaSHECELELVHFGLGDISENDVTFAETFDGVIYGFNVDAGSAIQQS 585
Cdd:pfam11987 16 FSQIKEEVKELNLIIKADVQGSLEALKESLEKLS-NDEVKVNIIHSGVGAITESDVMLASASNAIIIGFNVRPDAKARKL 94
|
90 100
....*....|....*....|..
gi 1958676470 586 AAQKGVKIKLHKIIYHLIEDLQ 607
Cdd:pfam11987 95 AEKEGVDIRYYNIIYDLIDDVK 116
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
183-337 |
2.52e-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: 120.48 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL---------------RETQVAAMEV-GGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRA 246
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLlyqtgaidrrgtrkeTFLDTLKEEReRGITIKTGVVEFEWP-KRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 247 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTD-ADPEKVKKE---LLAYDVVCEEYGGDVQAVH 322
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREikeLLKLIGFTFLKGKDVPIIP 160
|
170
....*....|....*
gi 1958676470 323 VSALTGKNLMALAEA 337
Cdd:cd00881 161 ISALTGEGIEELLDA 175
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
187-343 |
2.10e-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: 108.85 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVDHGKTTLL--------DKLRETQVAamevgGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVV 256
Cdd:cd04171 6 GHIDHGKTTLIkaltgietDRLPEEKKR-----GITIDLGfAYL-DLPDGKRLGFIDVPGHEKFvKNMLA-GAGGIDAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 257 LVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDAD-PEKVKKELLAYdvvCEEYGG-DVQAVHVSALTGKNLMA 333
Cdd:cd04171 79 LVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVDEDrLELVEEEILEL---LAGTFLaDAPIFPVSSVTGEGIEE 155
|
170
....*....|
gi 1958676470 334 LAEATIALAE 343
Cdd:cd04171 156 LKNYLDELAE 165
|
|
| mtIF2_IVc |
cd03692 |
C2 subdomain of domain IV in mitochondrial translation initiation factor 2; This model ... |
624-711 |
8.98e-27 |
|
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: 104.11 E-value: 8.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 624 GEASILATFTITegkKKVPVAGCRVQKGQLERQKKFKLIRNGQVIWKGSLTSLKHHKDDVLVIKTGVDCGLSLDEENvEF 703
Cdd:cd03692 1 GEAEVRAVFKIS---KVGTIAGCYVTEGKIKRNAKVRVLRDGEVIYEGKISSLKRFKDDVKEVKKGYECGITLENFN-DI 76
|
....*...
gi 1958676470 704 KVGDQVIC 711
Cdd:cd03692 77 KEGDIIEA 84
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
181-336 |
1.84e-26 |
|
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: 105.92 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 181 PVVTIMGHVDHGKTTLLDKLRETQVAAME-VGGITQHIGAFLVSL-PSGEKITFLDTPGHAAFSAMR-------ARGAQV 251
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEyYPGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRrlyypqvERSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 252 TDIVVLVVAADDGVMKQTVEsIQHAKDAGVPIILAINKCDKTDADPEKVKKELLAydvvcEEYGGDVqaVHVSALTGKNL 331
Cdd:TIGR00231 82 FDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDADLKTHVASEFA-----KLNGEPI--IPLSAETGKNI 153
|
....*
gi 1958676470 332 MALAE 336
Cdd:TIGR00231 154 DSAFK 158
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
187-418 |
1.12e-25 |
|
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: 112.70 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVDHGKTTLL--------DKLRETQVAamevgGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVV 256
Cdd:COG3276 7 GHIDHGKTTLVkaltgidtDRLKEEKKR-----GITIDLGfAYL-PLPDGRRLGFVDVPGHEKFiKNMLA-GAGGIDLVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 257 LVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKtdADPEKVkkELLAYDvVCEEYGG----DVQAVHVSALTGKNL 331
Cdd:COG3276 80 LVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADL--VDEEWL--ELVEEE-IRELLAGtfleDAPIVPVSAVTGEGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 332 MALAEATIALAEMLELKaDPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLKKGS---ILVAGKSwAKVRlmfdeN----G 404
Cdd:COG3276 155 DELRAALDALAAAVPAR-DADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDeleLLPSGKP-VRVR-----GiqvhG 227
|
250
....*....|....
gi 1958676470 405 KTVNEAYPSMPVGI 418
Cdd:COG3276 228 QPVEEAYAGQRVAL 241
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
183-408 |
1.37e-23 |
|
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: 105.85 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL----------RETQVAAMEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:TIGR01394 4 IAIIAHVDHGKTTLVDALlkqsgtfranEAVAERVMDSNdlererGIT--ILAKNTAIRyNGTKINIVDTPGHADFGGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 246 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHV 323
Cdd:TIGR01394 82 ERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVfdLFAELGADDEQLDFPIVYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 324 SALTGKNLMALAEATIALAEMLEL--------KADPTGPVEG--TVIESFTDKGRgpVTTAIIQRGTLKKGSilvagksw 393
Cdd:TIGR01394 162 SGRAGWASLDLDDPSDNMAPLFDAivrhvpapKGDLDEPLQMlvTNLDYDEYLGR--IAIGRVHRGTVKKGQ-------- 231
|
250
....*....|....*
gi 1958676470 394 aKVRLMfDENGKTVN 408
Cdd:TIGR01394 232 -QVALM-KRDGTIEN 244
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
183-328 |
1.44e-22 |
|
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: 95.74 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL-------RETQVAA---MEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:cd01891 5 IAIIAHVDHGKTTLVDALlkqsgtfRENEEVGervMDSNdlererGIT--ILAKNTAITyKDTKINIIDTPGHADFGGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 246 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHV 323
Cdd:cd01891 83 ERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVfdLFLELNATDEQLDFPIVYA 162
|
....*
gi 1958676470 324 SALTG 328
Cdd:cd01891 163 SAKNG 167
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
182-388 |
4.61e-21 |
|
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: 97.64 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 182 VVTIMGHVDHGKTTLLDKLRETQVAAM---EVGGITQHIGAFLVSLPSgEKITFLDTPGHAAFSAMRARGAQVTDIVVLV 258
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAADRLpeeKKRGMTIDLGFAYFPLPD-YRLGFIDVPGHEKFISNAIAGGGGIDAALLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 259 VAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNLMALAEA 337
Cdd:TIGR00475 81 VDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTSAKTGQGIGELKKE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958676470 338 TIALAEMLELKaDPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILV 388
Cdd:TIGR00475 161 LKNLLESLDIK-RIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLR 210
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
183-328 |
1.79e-20 |
|
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: 89.73 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTL------------LDKLRETQVAamevgGITQHIG--AFLVSLPSGE-----------KITFLDTPG 237
Cdd:cd01889 3 VGLLGHVDSGKTSLakalseiastaaFDKNPQSQER-----GITLDLGfsSFEVDKPKHLednenpqienyQITLVDCPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 238 HAafSAMRA--RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCD-----KTDADPEKVKKELLayDVV 310
Cdd:cd01889 78 HA--SLIRTiiGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDlipeeERKRKIEKMKKRLQ--KTL 153
|
170
....*....|....*...
gi 1958676470 311 CEEYGGDVQAVHVSALTG 328
Cdd:cd01889 154 EKTRLKDSPIIPVSAKPG 171
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
187-387 |
1.96e-19 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 92.81 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVDHGKTTLL--------DKLRETQVAAMevggiTQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVVLV 258
Cdd:PRK10512 7 GHVDHGKTTLLqaitgvnaDRLPEEKKRGM-----TIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 259 VAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTD-ADPEKVKKELLAydvVCEEYGGDVQAVHV-SALTGK------ 329
Cdd:PRK10512 82 VACDDGVMAQTREHLAILQLTGNPmLTVALTKADRVDeARIAEVRRQVKA---VLREYGFAEAKLFVtAATEGRgidalr 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958676470 330 -NLMALAEATIALAEMLELKADptgpvegtviESFTDKGRGPVTTAIIQRGTLKKGSIL 387
Cdd:PRK10512 159 eHLLQLPEREHAAQHRFRLAID----------RAFTVKGAGLVVTGTALSGEVKVGDTL 207
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
185-339 |
5.03e-19 |
|
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: 85.28 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTLLDKLRE-----------TQVA-AMEVG---GITqhIGAFLVSLP----SGEK--ITFLDTPGHAAFSA 243
Cdd:cd01890 5 IIAHIDHGKSTLADRLLEltgtvseremkEQVLdSMDLErerGIT--IKAQAVRLFykakDGEEylLNLIDTPGHVDFSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 244 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKELlaydvvcEEY-GGDV-QAV 321
Cdd:cd01890 83 EVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEI-------EDVlGLDAsEAI 155
|
170
....*....|....*...
gi 1958676470 322 HVSALTGKNLMALAEATI 339
Cdd:cd01890 156 LVSAKTGLGVEDLLEAIV 173
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
177-384 |
1.61e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 88.32 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLLDKLreTQVAAMEVG------------------GIT---QHIgaflvslpsgEKIT---- 231
Cdd:PRK00049 10 KPHVNVGTI-GHVDHGKTTLTAAI--TKVLAKKGGaeakaydqidkapeekarGITintAHV----------EYETekrh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 232 --FLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPEKVK------K 302
Cdd:PRK00049 77 yaHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 303 ELLAydvvceEY---GGDVQAVHVSAltgknLMAL--------AEATIALAEML-ELKADPTGPVEGTV---IES-FTDK 366
Cdd:PRK00049 156 ELLS------KYdfpGDDTPIIRGSA-----LKALegdddeewEKKILELMDAVdSYIPTPERAIDKPFlmpIEDvFSIS 224
|
250
....*....|....*...
gi 1958676470 367 GRGPVTTAIIQRGTLKKG 384
Cdd:PRK00049 225 GRGTVVTGRVERGIIKVG 242
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
177-384 |
2.15e-18 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 88.08 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLLDKLreTQVAAmEVGGITQHIGAFLVSLPSgEK---ITF----------------LDTPG 237
Cdd:PRK12736 10 KPHVNIGTI-GHVDHGKTTLTAAI--TKVLA-ERGLNQAKDYDSIDAAPE-EKergITIntahveyetekrhyahVDCPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 238 HAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPEKVK------KELL-AYDv 309
Cdd:PRK12736 85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLVD-DEELLElvemevRELLsEYD- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 310 vceeYGGD-VQAVHVSALTG--------KNLMALAEATIALAEMLELKADPT--GPVEGTviesFTDKGRGPVTTAIIQR 378
Cdd:PRK12736 163 ----FPGDdIPVIRGSALKAlegdpkweDAIMELMDAVDEYIPTPERDTDKPflMPVEDV----FTITGRGTVVTGRVER 234
|
....*.
gi 1958676470 379 GTLKKG 384
Cdd:PRK12736 235 GTVKVG 240
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
177-384 |
1.49e-17 |
|
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: 85.20 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLLDKLreTQVAAMEVG------------------GIT---QHIgaflvslpsgEKIT---- 231
Cdd:COG0050 10 KPHVNIGTI-GHVDHGKTTLTAAI--TKVLAKKGGakakaydqidkapeekerGITintSHV----------EYETekrh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 232 --FLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPEKVK------K 302
Cdd:COG0050 77 yaHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 303 ELLaydvvcEEY---GGDVQAVHVSAltgknLMALAEATIALAE--MLELKA-------DPTG--------PVEGTvies 362
Cdd:COG0050 156 ELL------SKYgfpGDDTPIIRGSA-----LKALEGDPDPEWEkkILELMDavdsyipEPERdtdkpflmPVEDV---- 220
|
250 260
....*....|....*....|..
gi 1958676470 363 FTDKGRGPVTTAIIQRGTLKKG 384
Cdd:COG0050 221 FSITGRGTVVTGRVERGIIKVG 242
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
177-384 |
1.61e-17 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 85.65 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLLDKLreTQVAAmEVG-------------------GITqhIGAFLVSLPSGEK-ITFLDTP 236
Cdd:PLN03127 59 KPHVNVGTI-GHVDHGKTTLTAAI--TKVLA-EEGkakavafdeidkapeekarGIT--IATAHVEYETAKRhYAHVDCP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 237 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPEKVK------KELLAYdv 309
Cdd:PLN03127 133 GHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVVD-DEELLElvemelRELLSF-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 310 vcEEYGGD----VQAVHVSALTGKNLMALAEATIALAEML-ELKADPT----GPVEGTVIESFTDKGRGPVTTAIIQRGT 380
Cdd:PLN03127 210 --YKFPGDeipiIRGSALSALQGTNDEIGKNAILKLMDAVdEYIPEPVrvldKPFLMPIEDVFSIQGRGTVATGRVEQGT 287
|
....
gi 1958676470 381 LKKG 384
Cdd:PLN03127 288 IKVG 291
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
185-337 |
2.63e-17 |
|
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: 79.81 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTLLDKLRETQVAAM-EVGGITQHIGAFLVSLPSG-EKITFLDTPGHAAFSAMRARG-----AQVTDIVVL 257
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVsDVPGTTRDPDVYVKELDKGkVKLVLVDTPGLDEFGGLGREElarllLRGADLILL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 258 VVAADDGVMKQTVE--SIQHAKDAGVPIILAINKCDKtdaDPEKVKKELLAYDVVCEEYGGDVqaVHVSALTGKNLMALA 335
Cdd:cd00882 82 VVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDL---LEEREVEELLRLEELAKILGVPV--FEVSAKTGEGVDELF 156
|
..
gi 1958676470 336 EA 337
Cdd:cd00882 157 EK 158
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
177-388 |
8.62e-17 |
|
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: 83.44 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLLDKLretqvaAMEVGGITQHI-----------G------AFLVSLPSGEK---------- 229
Cdd:COG5256 5 KPHLNLVVI-GHVDHGKSTLVGRL------LYETGAIDEHIiekyeeeaekkGkesfkfAWVMDRLKEERergvtidlah 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 230 ---------ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDADP-- 297
Cdd:COG5256 78 kkfetdkyyFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAVNYSEkr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 298 -EKVKKEL------LAYDVvceeygGDVQAVHVSALTGKNLMALAEAT--------IALAEMLELKADPTG-PVEGTVIE 361
Cdd:COG5256 158 yEEVKEEVskllkmVGYKV------DKIPFIPVSAWKGDNVVKKSDNMpwyngptlLEALDNLKEPEKPVDkPLRIPIQD 231
|
250 260
....*....|....*....|....*..
gi 1958676470 362 SFTDKGRGPVTTAIIQRGTLKKGSILV 388
Cdd:COG5256 232 VYSISGIGTVPVGRVETGVLKVGDKVV 258
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
183-300 |
1.37e-16 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 83.53 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL-------RETQVAA---MEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:COG1217 9 IAIIAHVDHGKTTLVDALlkqsgtfRENQEVAervMDSNdlererGIT--ILAKNTAVRyKGVKINIVDTPGHADFGGEV 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958676470 246 ARGAQVTDIVVLVVAADDGVMKQT--VesIQHAKDAGVPIILAINKCDKTDADPEKV 300
Cdd:COG1217 87 ERVLSMVDGVLLLVDAFEGPMPQTrfV--LKKALELGLKPIVVINKIDRPDARPDEV 141
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
183-292 |
7.63e-16 |
|
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: 76.92 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL------------------RETQVAAMEVG-GITQHIGAFLVSLPSGEK----ITFLDTPGHA 239
Cdd:cd04167 3 VCIAGHLHHGKTSLLDMLieqthkrtpsvklgwkplRYTDTRKDEQErGISIKSNPISLVLEDSKGksylINIIDTPGHV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958676470 240 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDK 292
Cdd:cd04167 83 NFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
177-384 |
1.23e-15 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 79.97 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLLDKLretqvaAMEVGGITQHI-----------G------AFLVSLPSGEK---------- 229
Cdd:PRK12317 4 KPHLNLAVI-GHVDHGKSTLVGRL------LYETGAIDEHIieelreeakekGkesfkfAWVMDRLKEERergvtidlah 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 230 ---------ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD--GVMKQTVESIQHAKDAGVP-IILAINKCDKTDADP 297
Cdd:PRK12317 77 kkfetdkyyFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINqLIVAINKMDAVNYDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 298 EK---VKKEL------LAYDVvceeygGDVQAVHVSALTGKNLMALAEAT-----IALAEMLELKADPTGPVEG----TV 359
Cdd:PRK12317 157 KRyeeVKEEVskllkmVGYKP------DDIPFIPVSAFEGDNVVKKSENMpwyngPTLLEALDNLKPPEKPTDKplriPI 230
|
250 260
....*....|....*....|....*
gi 1958676470 360 IESFTDKGRGPVTTAIIQRGTLKKG 384
Cdd:PRK12317 231 QDVYSISGVGTVPVGRVETGVLKVG 255
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
185-345 |
5.76e-15 |
|
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: 73.05 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLPSGEKITFLDTPG-------HAAFSAMRARGAQVTDIVV 256
Cdd:cd00880 2 IFGRPNVGKSSLLNALlGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRADLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 257 LVVAADDGVMKQtVESIQHAKDAGVPIILAINKCDKTDADPEKVKkellaYDVVCEEYGGDVQAVHVSALTGKNLMALAE 336
Cdd:cd00880 82 LVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEEEL-----LRERKLELLPDLPVIAVSALPGEGIDELRK 155
|
....*....
gi 1958676470 337 atiALAEML 345
Cdd:cd00880 156 ---KIAELL 161
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
184-334 |
6.11e-15 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 73.77 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 184 TImGHVDHGKTTLLDKLreTQVAAMEVG------------------GITqhIGAFLVSLPSGEK-ITFLDTPGHAAF-SA 243
Cdd:cd01884 7 TI-GHVDHGKTTLTAAI--TKVLAKKGGakakkydeidkapeekarGIT--INTAHVEYETANRhYAHVDCPGHADYiKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 244 MRARGAQVtDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPEKVK------KELLaydvvcEEYGG 316
Cdd:cd01884 82 MITGAAQM-DGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMVD-DEELLElvemevRELL------SKYGF 153
|
170
....*....|....*...
gi 1958676470 317 DVQAVHVsaLTGKNLMAL 334
Cdd:cd01884 154 DGDDTPI--VRGSALKAL 169
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
186-304 |
1.08e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.86 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 186 MGHVDHGKTTLLDK-LRETQV--AAMEVG---------------GITqhIGAFLVSLP-SGEKITFLDTPGHAAF----- 241
Cdd:PRK12740 1 VGHSGAGKTTLTEAiLFYTGAihRIGEVEdgtttmdfmpeererGIS--ITSAATTCEwKGHKINLIDTPGHVDFtgeve 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958676470 242 SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL 304
Cdd:PRK12740 79 RALR-----VLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQL 136
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
185-304 |
1.36e-14 |
|
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: 73.81 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTLLDKLRETQVAAMEVG------------------GIT--QHIGAFLVslpSGEKITFLDTPGHAAFSAM 244
Cdd:cd04168 4 ILAHVDAGKTTLTESLLYTSGAIRELGsvdkgttrtdsmelerqrGITifSAVASFQW---EDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958676470 245 RARGAQVTDIVVLVVAADDGVMKQTvESIQHA-KDAGVPIILAINKCDKTDADPEKVKKEL 304
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQT-RILFRLlRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
185-304 |
2.36e-14 |
|
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: 76.62 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTLL----------DKLRE-----TQVAAMEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAF---- 241
Cdd:COG0480 14 IVAHIDAGKTTLTerilfytgaiHRIGEvhdgnTVMDWMPEEqerGIT--ITSAATTCEwKGHKINIIDTPGHVDFtgev 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958676470 242 -SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL 304
Cdd:COG0480 92 eRSLR-----VLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQL 150
|
|
| tufA |
CHL00071 |
elongation factor Tu |
177-384 |
5.58e-14 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 74.61 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLldklreTQVAAMEVGGITQHIGAFLVSLPSG--EK---ITF----------------LDT 235
Cdd:CHL00071 10 KPHVNIGTI-GHVDHGKTTL------TAAITMTLAAKGGAKAKKYDEIDSApeEKargITIntahveyetenrhyahVDC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 236 PGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPE-------KVKKELLAY 307
Cdd:CHL00071 83 PGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVD-DEEllelvelEVRELLSKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 308 DvvceeYGGDvqavHVSALTGKNLMALaEATIALAEM-----------LEL--KAD---PTgPVEGT------VIES-FT 364
Cdd:CHL00071 162 D-----FPGD----DIPIVSGSALLAL-EALTENPKIkrgenkwvdkiYNLmdAVDsyiPT-PERDTdkpflmAIEDvFS 230
|
250 260
....*....|....*....|
gi 1958676470 365 DKGRGPVTTAIIQRGTLKKG 384
Cdd:CHL00071 231 ITGRGTVATGRIERGTVKVG 250
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
183-431 |
7.73e-14 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 75.13 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL----------RETQVAAMEVGGITQHIGAFLVSLPSGEK-----ITFLDTPGHAAFSAMRAR 247
Cdd:PRK10218 8 IAIIAHVDHGKTTLVDKLlqqsgtfdsrAETQERVMDSNDLEKERGITILAKNTAIKwndyrINIVDTPGHADFGGEVER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 248 GAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHVSA 325
Cdd:PRK10218 88 VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVfdLFVNLDATDEQLDFPIVYASA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 326 LTG----------KNLMALAEATIALAEMLELKADptGPVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILVAGKSWAK 395
Cdd:PRK10218 168 LNGiagldhedmaEDMTPLYQAIVDHVPAPDVDLD--GPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGK 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958676470 396 VRlmfdeNGKtVNEAYPSMPVGIIGwRDLPSAGDEI 431
Cdd:PRK10218 246 TR-----NAK-VGKVLGHLGLERIE-TDLAEAGDIV 274
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
170-304 |
9.22e-14 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 74.71 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 170 GADPALLKPRSPVVTIMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSL---PSGEKITFLDTPGHAAFSAMRA 246
Cdd:COG5180 389 GAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVPGdaeSVSGPAGLADQAGAAASTAMAD 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958676470 247 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL 304
Cdd:COG5180 469 FVAPVTDATPVDVADVLGVRPDAILGGNVAPASGLDAETRIIEAEGAPATEDFVAAEL 526
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
177-387 |
4.82e-13 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 71.96 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 177 KPRSPVVTImGHVDHGKTTLL---------------DKLRETQVAAMEVG-GITqhIGAFLVSLPSGEK-ITFLDTPGHA 239
Cdd:PLN03126 79 KPHVNIGTI-GHVDHGKTTLTaaltmalasmggsapKKYDEIDAAPEERArGIT--INTATVEYETENRhYAHVDCPGHA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 240 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDKTDaDPEKVK------KELLAydvvCE 312
Cdd:PLN03126 156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVD-DEELLElvelevRELLS----SY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 313 EYGGDvqavHVSALTGKNLMALaEATIA-----------LAEMLEL--KADPTGPVEG---------TVIESFTDKGRGP 370
Cdd:PLN03126 231 EFPGD----DIPIISGSALLAL-EALMEnpnikrgdnkwVDKIYELmdAVDSYIPIPQrqtdlpfllAVEDVFSITGRGT 305
|
250
....*....|....*..
gi 1958676470 371 VTTAIIQRGTLKKGSIL 387
Cdd:PLN03126 306 VATGRVERGTVKVGETV 322
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
183-300 |
1.51e-12 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 71.14 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDK-LRET----QVAAMEVG-------------GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSA 243
Cdd:PRK13351 11 IGILAHIDAGKTTLTERiLFYTgkihKMGEVEDGttvtdwmpqeqerGIT--IESAATSCDWDNhRINLIDTPGHIDFTG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958676470 244 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKV 300
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKV 145
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
183-292 |
5.29e-12 |
|
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: 65.72 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLD---------------KLRETQVAAME-VGGITqhIGAFLVSL--------PSGEK--ITFLDTP 236
Cdd:cd01885 3 ICIIAHVDHGKTTLSDsllasagiiseklagKARYLDTREDEqERGIT--IKSSAISLyfeyeeekMDGNDylINLIDSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958676470 237 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDK 292
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
155-355 |
5.47e-11 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 64.40 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 155 KLERIRENKDAVRRPGADPALLKPRSPVVTIMGHVDHGKTTLLDKLreTQVAAMEVGGI---TQHIGAFLVSLPSGEKIT 231
Cdd:COG3596 14 ALKRLPQVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINAL--FGAEVAEVGVGrpcTREIQRYRLESDGLPGLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 232 FLDTPG-------HAAFSAMRARGAQVtDIVVLVVAADDGVMKQTVESIQ--HAKDAGVPIILAINKCDKTdadpekvkk 302
Cdd:COG3596 92 LLDTPGlgevnerDREYRELRELLPEA-DLILWVVKADDRALATDEEFLQalRAQYPDPPVLVVLTQVDRL--------- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958676470 303 ellaydvvceeYGGDVQAVHVSALTGKNLMALAEATIALAEMLELKADPTGPV 355
Cdd:COG3596 162 -----------EPEREWDPPYNWPSPPKEQNIRRALEAIAEQLGVPIDRVIPV 203
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
183-304 |
7.28e-11 |
|
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: 63.38 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDK-LRETQVAAM----EVGG---------ITQHIGAFLVSLP---SGEKITFLDTPGHAAFSAmR 245
Cdd:cd04170 2 IALVGHSGSGKTTLAEAlLYATGAIDRlgrvEDGNtvsdydpeeKKRKMSIETSVAPlewNGHKINLIDTPGYADFVG-E 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 246 ARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL 304
Cdd:cd04170 81 TLSAlRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAAL 140
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
183-346 |
1.38e-10 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 60.77 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKLRETQVAAMEVG---GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSAMRA------RGAqvt 252
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLstnGVT--IDKKELKLDGLDvDLVIWDTPGQDEFRETRQfyarqlTGA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 253 DIVVLVVaadDGVMKQTVESI----QHAKDAG--VPIILAINKCDKtdADPEKVKKELLAYDVVCEEYGGDVqaVHVSAL 326
Cdd:COG1100 81 SLYLFVV---DGTREETLQSLyellESLRRLGkkSPIILVLNKIDL--YDEEEIEDEERLKEALSEDNIVEV--VATSAK 153
|
170 180
....*....|....*....|....
gi 1958676470 327 TGKNLM----ALAEATIALAEMLE 346
Cdd:COG1100 154 TGEGVEelfaALAEILRGEGDSLD 177
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
187-338 |
3.71e-10 |
|
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: 60.28 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVDHGKTTLLDKL-------RETQVAAMEVGGITQHIG-----AFLV-SLP----------------SGEKITFL--DT 235
Cdd:cd04166 6 GSVDDGKSTLIGRLlydsksiFEDQLAALERSKSSGTQGekldlALLVdGLQaereqgitidvayryfSTPKRKFIiaDT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 236 PGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVesiQHAKDA---GVP-IILAINKCDKTDADPEkvkkellAYDVVC 311
Cdd:cd04166 86 PGHEQYTRNMVTGASTADLAILLVDARKGVLEQTR---RHSYIAsllGIRhVVVAVNKMDLVDYDEE-------VFEEIK 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1958676470 312 EEYGG--------DVQAVHVSALTGKNLMALAEAT 338
Cdd:cd04166 156 ADYLAfaaslgieDITFIPISALEGDNVVSRSENM 190
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
183-337 |
4.08e-10 |
|
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: 59.37 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL-RETQVAAMEVGGITQ-------HIGaflvslpsGEKITFLDTPG----------HAAFSAM 244
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALlGEERVIVSDIAGTTRdsidvpfEYD--------GQKYTLIDTAGirkkgkvtegIEKYSVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 245 RARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADP---EKVKKEL------LAYdvvceey 314
Cdd:cd01895 77 RTLKAiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEktmKEFEKELrrklpfLDY------- 149
|
170 180
....*....|....*....|...
gi 1958676470 315 ggdVQAVHVSALTGKNLMALAEA 337
Cdd:cd01895 150 ---APIVFISALTGQGVDKLFDA 169
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
185-304 |
4.69e-10 |
|
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: 60.97 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTL----------LDKLRE-----TQVAAMEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:cd01886 4 IIAHIDAGKTTTterilyytgrIHKIGEvhgggATMDWMEQErerGIT--IQSAATTCFwKDHRINIIDTPGHVDFTIEV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958676470 246 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKEL 304
Cdd:cd01886 82 ERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
230-354 |
5.00e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 61.16 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 230 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKtdAD 296
Cdd:COG1159 53 IVFVDTPGihkpkrklgrrmnKAAWSALED-----VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VK 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958676470 297 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGKNLMALAEatiALAEMLelkadPTGP 354
Cdd:COG1159 126 KEELLPLLAEY----SELLDFAEIVPISALKGDNVDELLD---EIAKLL-----PEGP 171
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
183-289 |
1.01e-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: 56.47 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL--RETQVAAMEvgGITQHIGAFLVSLpSGEKITFLDTPG-----HAAFSAMRA-RGAQVTDI 254
Cdd:pfam01926 2 VALVGRPNVGKSTLINALtgAKAIVSDYP--GTTRDPNEGRLEL-KGKQIILVDTPGliegaSEGEGLGRAfLAIIEADL 78
|
90 100 110
....*....|....*....|....*....|....*
gi 1958676470 255 VVLVVAADDGVMKQTVESIQHAKDAGVPIILAINK 289
Cdd:pfam01926 79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
155-292 |
2.44e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 60.65 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 155 KLERIRENKDAVRRPGadpallkprspvvtIMGHVDHGKTTLLDKL--------RET--QVAAM---EVG---GITqhIG 218
Cdd:PRK07560 9 KILELMKNPEQIRNIG--------------IIAHIDHGKTTLSDNLlagagmisEELagEQLALdfdEEEqarGIT--IK 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958676470 219 AFLVSLP---SGEK--ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDK 292
Cdd:PRK07560 73 AANVSMVheyEGKEylINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDR 151
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
227-343 |
1.36e-08 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 57.73 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 227 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDA 295
Cdd:COG1160 222 GKKYTLIDTAGirrkgkvDEGiekYSVLRTLRAiERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEK 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958676470 296 DP---EKVKKEL------LAYdvvceeyggdVQAVHVSALTGKNLMALAEATIALAE 343
Cdd:COG1160 302 DRktrEELEKEIrrrlpfLDY----------APIVFISALTGQGVDKLLEAVDEVYE 348
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
230-342 |
1.72e-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: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 230 ITFLDTPG-------------HAAFSAMRarGAqvtDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDaD 296
Cdd:cd04163 53 IIFVDTPGihkpkkklgermvKAAWSALK--DV---DLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVK-D 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958676470 297 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGKNLMALAEATIALA 342
Cdd:cd04163 127 KEDLLPLLEKL----KELHPFAEIFPISALKGENVDELLEYIVEYL 168
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
230-354 |
3.06e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 55.82 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 230 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDaD 296
Cdd:PRK00089 55 IIFVDTPGihkpkralnramnKAAWSSLKD-----VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVK-D 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958676470 297 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGKNLMALAEatiALAEMLelkadPTGP 354
Cdd:PRK00089 129 KEELLPLLEEL----SELMDFAEIVPISALKGDNVDELLD---VIAKYL-----PEGP 174
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
187-338 |
5.51e-08 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 56.09 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVDHGKTTLLDKLR-------ETQVAAME-----VGGITQHIG-AFLVSLPSGEK---IT--------------FL--D 234
Cdd:PRK05506 31 GSVDDGKSTLIGRLLydskmifEDQLAALErdskkVGTQGDEIDlALLVDGLAAEReqgITidvayryfatpkrkFIvaD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 235 TPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdagvpIILAINKCDKTDADPEKvkkella 306
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTrrhsfiasLLGIRH-------VVLAVNKMDLVDYDQEV------- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958676470 307 YDVVCEEYG--------GDVQAVHVSALTGKNLMALAEAT 338
Cdd:PRK05506 177 FDEIVADYRafaaklglHDVTFIPISALKGDNVVTRSARM 216
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
155-337 |
8.29e-08 |
|
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: 53.23 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 155 KLERIRENKDAVRRpgadpallKPRSPVVTIMGHVDHGKTTLLDKL--RETQVAAMevggitqhigafL----------V 222
Cdd:cd01878 24 KVKKQRELQRARRK--------RSGVPTVALVGYTNAGKSTLFNALtgADVLAEDQ------------LfatldpttrrI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 223 SLPSGEKITFLDTPG------H---AAFSAM--RARGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDA-GVPIILAI 287
Cdd:cd01878 84 KLPGGREVLLTDTVGfirdlpHqlvEAFRSTleEVAEA---DLLLHVVdASDPDREEQieTVEEVLKELGAdDIPIILVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958676470 288 NKCDKtdADPEKVKKELLAydvvceeygGDVQAVHVSALTGKNLMALAEA 337
Cdd:cd01878 161 NKIDL--LDDEELEERLRA---------GRPDAVFISAKTGEGLDLLKEA 199
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
187-347 |
1.47e-07 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 54.53 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVDHGKTTLLDKL-------RETQVAAME-----VGGITQHIG-AFLVS-LP----------------SGEKITFL--D 234
Cdd:PRK05124 34 GSVDDGKSTLIGRLlhdtkqiYEDQLASLHndskrHGTQGEKLDlALLVDgLQaereqgitidvayryfSTEKRKFIiaD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 235 TPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdagvpIILAINKCDKTDADP---EKVKKE 303
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTrrhsfiatLLGIKH-------LVVAVNKMDLVDYSEevfERIRED 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958676470 304 LLAYdvvCEEYGG--DVQAVHVSALTGKNLMALAEAT-----IALAEMLEL 347
Cdd:PRK05124 187 YLTF---AEQLPGnlDIRFVPLSALEGDNVVSQSESMpwysgPTLLEVLET 234
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
185-304 |
1.85e-07 |
|
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: 52.98 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 185 IMGHVDHGKTTLLDKL---------------RETQVAA----MEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAF 241
Cdd:cd04169 7 IISHPDAGKTTLTEKLllfggaiqeagavkaRKSRKHAtsdwMEIEkqrGIS--VTSSVMQFEyKGCVINLLDTPGHEDF 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958676470 242 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADP----EKVKKEL 304
Cdd:cd04169 85 SEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPlellDEIENEL 151
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
181-418 |
1.15e-06 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 51.39 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 181 PVVTI--MGHVDHGKTTLLDKLreTQVAAM----EVG-GITQHIG----------------AFLVSlPSGE--------- 228
Cdd:PRK04000 8 PEVNIgmVGHVDHGKTTLVQAL--TGVWTDrhseELKrGITIRLGyadatirkcpdceepeAYTTE-PKCPncgsetell 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 229 -KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGV-MKQTVESIQHAKDAGVP-IILAINKCDKTdaDPEKVK---- 301
Cdd:PRK04000 85 rRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKnIVIVQNKIDLV--SKERALenye 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 302 --KELLAyDVVCEeyggDVQAVHVSALTGKNLMALAEatiALAEMLEL-KADPTGPVEGTVIESFT--------DKGRGP 370
Cdd:PRK04000 163 qiKEFVK-GTVAE----NAPIIPVSALHKVNIDALIE---AIEEEIPTpERDLDKPPRMYVARSFDvnkpgtppEKLKGG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958676470 371 VTTAIIQRGTLKKGS---------ILVAGKS-W----AKVR-LMFdeNGKTVNEAYPSMPVGI 418
Cdd:PRK04000 235 VIGGSLIQGVLKVGDeieirpgikVEEGGKTkWepitTKIVsLRA--GGEKVEEARPGGLVGV 295
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
183-339 |
3.22e-06 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 50.56 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLpSGEKITFLDTPG----------HAAFSAMRARGA-Q 250
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLtHEERAVVNDLAGTTRDPVDEIVEI-DGEDWLFIDTAGikrrqhkltgAEYYSSLRTQAAiE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 251 VTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADpekvKKELLAYDVVCE-EYGGDVQAVHVSALTGK 329
Cdd:PRK09518 532 RSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWDLMDEF----RRQRLERLWKTEfDRVTWARRVNLSAKTGW 607
|
170
....*....|
gi 1958676470 330 NLMALAEATI 339
Cdd:PRK09518 608 HTNRLAPAMQ 617
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
227-343 |
3.78e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 50.05 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 227 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQtVESI-QHAKDAGVPIILAINKCDKTD 294
Cdd:PRK00093 220 GQKYTLIDTAGirrkgkvTEGvekYSVIRTLKAiERADVVLLVIDATEGITEQ-DLRIaGLALEAGRALVIVVNKWDLVD 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958676470 295 ADP-EKVKKEL------LAYdvvceeyggdVQAVHVSALTGKNLMALAEATIALAE 343
Cdd:PRK00093 299 EKTmEEFKKELrrrlpfLDY----------APIVFISALTGQGVDKLLEAIDEAYE 344
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
222-346 |
1.05e-05 |
|
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: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 222 VSLPSGEKITFLDTPG------H---AAFsamRA-----RGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDAG-VPI 283
Cdd:COG2262 241 LELPDGRPVLLTDTVGfirklpHqlvEAF---RStleevREA---DLLLHVVdASDPDFEEQieTVNEVLEELGADdKPI 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958676470 284 ILAINKCDKTDADPEKVKKEllaydvvceeygGDVQAVHVSALTGKNLMALAEatiALAEMLE 346
Cdd:COG2262 315 ILVFNKIDLLDDEELERLRA------------GYPDAVFISAKTGEGIDELLE---AIEERLP 362
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
181-305 |
1.35e-05 |
|
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: 46.55 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 181 PVVTIMGHVDHGKTTLLDKL-----RETQVAamevggITQHIGAFLVSLPSGEKITFLDTPGHAAFSAM-------RARG 248
Cdd:cd04105 1 PTVLLLGPSDSGKTALFTKLttgkvRSTVTS------IEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKlleylkaSLKA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958676470 249 aqvtdiVVLVV--AADDGVMKQTVE------SIQHAKDAGVPIILAINKCDKTDADPEKVKKELL 305
Cdd:cd04105 75 ------IVFVVdsATFQKNIRDVAEflydilTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELL 133
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
253-341 |
2.45e-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: 45.12 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 253 DIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDktdadpeKVKKELLAYDvvCEEYG-GDVqaVHVSALTGKNL 331
Cdd:cd01894 78 DVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID-------NIKEEEEAAE--FYSLGfGEP--IPISAEHGRGI 146
|
90
....*....|
gi 1958676470 332 MALAEATIAL 341
Cdd:cd01894 147 GDLLDAILEL 156
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
178-337 |
4.76e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 46.50 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 178 PRSpvVTIMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLpSGEKITFLDTPG----------HAAFSAMRA 246
Cdd:PRK03003 211 PRR--VALVGKPNVGKSSLLNKLaGEERSVVDDVAGTTVDPVDSLIEL-GGKTWRFVDTAGlrrrvkqasgHEYYASLRT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 247 RGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADpekvKKELLAYDVvceeyggDVQAVHV-- 323
Cdd:PRK03003 288 HAAiEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNKWDLVDED----RRYYLEREI-------DRELAQVpw 356
|
170 180
....*....|....*....|
gi 1958676470 324 ------SALTGKNLMALAEA 337
Cdd:PRK03003 357 aprvniSAKTGRAVDKLVPA 376
|
|
| Ras_dva |
cd04147 |
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ... |
225-291 |
1.05e-04 |
|
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: 44.06 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958676470 225 PSGEKITF--LDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESI-----QHAKDAGVPIILAINKCD 291
Cdd:cd04147 42 VAGVKVTIdiLDTSGSYSFPAMRKLSIQNGDAFALVYSVDDPESFEEVKRLreeilEVKEDKFVPIVVVGNKID 115
|
|
| IF2_IF5B_II |
cd03701 |
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ... |
354-434 |
1.14e-04 |
|
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: 41.50 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 354 PVEGTVIESFTDKGRGPVTTAIIQRGTLKKGSILVAGKS----WAKVRLMFD----------ENGKTVNEAYPSMPVGII 419
Cdd:cd03701 1 EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESkdviYTRIRALLDpdpleemesrKKGNKRKEVGAASGVKIL 80
|
90
....*....|....*.
gi 1958676470 420 GW-RDLPSAGDEILEV 434
Cdd:cd03701 81 GFgQELPHAGDPLEVV 96
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
253-342 |
1.74e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.54 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 253 DIVVLVVAADDG-----------VMkqtvesiqhAKDAGVPIILAINKCDKtdADPEKVKKELLAYdvvcEEYGGDVqaV 321
Cdd:cd01854 4 DQVLIVFSLKEPffnlrlldrylVA---------AEASGIEPVIVLNKADL--VDDEELEELLEIY----EKLGYPV--L 66
|
90 100
....*....|....*....|....*
gi 1958676470 322 HVSALTGKNLMALAEA----TIALA 342
Cdd:cd01854 67 AVSAKTGEGLDELRELlkgkTSVLV 91
|
|
| RalA_RalB |
cd04139 |
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ... |
222-331 |
2.42e-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: 42.41 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 222 VSLPSGE-KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD----GVMKQTVESI-QHAKDAGVPIILAINKCDKTDa 295
Cdd:cd04139 41 VVLDGEEvQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDmesfTALAEFREQIlRVKEDDNVPLLLVGNKCDLED- 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958676470 296 dpeKVKKELLAYDVVCEEYGgdVQAVHVSALTGKNL 331
Cdd:cd04139 120 ---KRQVSVEEAANLAEQWG--VNYVETSAKTRANV 150
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
212-331 |
2.60e-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: 42.11 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 212 GITQHIGAFLVslpsGEKITFLDTPG--HAAFS-AMRARGAQVTD----------IVVLVVAADDGVMKQTVESIQHAKD 278
Cdd:cd01876 33 GRTQLINFFNV----GDKFRLVDLPGygYAKVSkEVREKWGKLIEeylenrenlkGVVLLIDARHGPTPIDLEMLEFLEE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958676470 279 AGVPIILAINKCDKtdADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGKNL 331
Cdd:cd01876 109 LGIPFLIVLTKADK--LKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGI 159
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
182-291 |
3.76e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 44.01 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 182 VVTIMGHVDHGKTTLLDKLRETQVAAME-VGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRARGA 249
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAVVEdTPGVTRD----RVSYDaewAGTDFKLVDTGGweadvegiDSAIASQAQIAV 352
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958676470 250 QVTDIVVLVVAADDGvMKQTVESI-QHAKDAGVPIILAINKCD 291
Cdd:PRK09518 353 SLADAVVFVVDGQVG-LTSTDERIvRMLRRAGKPVVLAVNKID 394
|
|
| Sar1 |
cd00879 |
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ... |
192-321 |
2.92e-03 |
|
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: 39.57 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 192 GKTTLLDKLRETQVAAMEVggiTQHigaflvslPSGEKITF-------LDTPGHAAfsAMRARG---AQVTDIVVLVVAA 261
Cdd:cd00879 31 GKTTLLHMLKDDRLAQHVP---TLH--------PTSEELTIgnvkfttFDLGGHEQ--ARRVWKdyfPEVDGIVFLVDAA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958676470 262 DdgvmkqtVESIQHAKD-----------AGVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAV 321
Cdd:cd00879 98 D-------PERFQESKEeldsllndeelANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLKV 161
|
|
| ARLTS1 |
cd04156 |
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ... |
183-344 |
3.60e-03 |
|
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.
Pssm-ID: 133356 [Multi-domain] Cd Length: 160 Bit Score: 38.94 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKLRetqvaamevggitqhIGAFLVSLPS-GEKITFLDTPGHAAFSAMRARGAQV---------- 251
Cdd:cd04156 2 VLLLGLDSAGKSTLLYKLK---------------HAELVTTIPTvGFNVEMLQLEKHLSLTVWDVGGQEKmrtvwkcyle 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 252 -TDIVVLVVAADDG-----VMKQTVESIQHAKDAGVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAvhVSA 325
Cdd:cd04156 67 nTDGLVYVVDSSDEarldeSQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSDRDWYVQP--CSA 144
|
170
....*....|....*....
gi 1958676470 326 LTGKnlmALAEATIALAEM 344
Cdd:cd04156 145 VTGE---GLAEAFRKLASF 160
|
|
| Ras |
pfam00071 |
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ... |
187-330 |
5.54e-03 |
|
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.
Pssm-ID: 425451 [Multi-domain] Cd Length: 162 Bit Score: 38.26 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 187 GHVdhGKTTLL-----DKLRETQVAAMEVGGITQHIGAFlvslpsGEKITF--LDTPGHAAFSAMRA---RGAQVTDIVV 256
Cdd:pfam00071 8 GGV--GKSSLLirftqNKFPEEYIPTIGVDFYTKTIEVD------GKTVKLqiWDTAGQERFRALRPlyyRGADGFLLVY 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958676470 257 LVVAAD--DGVMKQtVESIQHAKDAGVPIILAINKCDKtdADPEKVKKE---LLAydvvcEEYGgdVQAVHVSALTGKN 330
Cdd:pfam00071 80 DITSRDsfENVKKW-VEEILRHADENVPIVLVGNKCDL--EDQRVVSTEegeALA-----KELG--LPFMETSAKTNEN 148
|
|
| Ras |
cd00876 |
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ... |
229-291 |
6.00e-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: 38.28 E-value: 6.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958676470 229 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAKDAG-VPIILAINKCD 291
Cdd:cd00876 48 TLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSResfeEIKNIREQILRVKDKEdVPIVLVGNKCD 115
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
181-296 |
6.03e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.95 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 181 PVVTIMGHVDHGKTTLLDKL---RETQVAamEVGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRA 246
Cdd:PRK03003 39 PVVAVVGRPNVGKSTLVNRIlgrREAVVE--DVPGVTRD----RVSYDaewNGRRFTVVDTGGwepdakglQASVAEQAE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958676470 247 RGAQVTDIVVLVV-------AADDGVMKQTVESiqhakdaGVPIILAINKCD--KTDAD 296
Cdd:PRK03003 113 VAMRTADAVLFVVdatvgatATDEAVARVLRRS-------GKPVILAANKVDdeRGEAD 164
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
183-347 |
9.18e-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: 37.91 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 183 VTIMGHVDHGKTTLLDKLRETQVAAMEVG---GITQHIGaflVSLPSGekITFLDTPGhaaFSAMRARGAQVT------- 252
Cdd:cd09912 3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTpttAVITVLR---YGLLKG--VVLVDTPG---LNSTIEHHTEITesflpra 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 253 DIVVLVVAADDGVMKQTVESIQHAKDAGVP-IILAINKCDK-TDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALtgKN 330
Cdd:cd09912 75 DAVIFVLSADQPLTESEREFLKEILKWSGKkIFFVLNKIDLlSEEELEEVLEYSREELGVLELGGGEPRIFPVSAK--EA 152
|
170
....*....|....*..
gi 1958676470 331 LMALAEATIALAEMLEL 347
Cdd:cd09912 153 LEARLQGDEELLEQSGF 169
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
253-343 |
9.51e-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: 37.47 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 253 DIVVLVVaadDGVMKQTVESIQ-HAKDAGVPIILAINKCDKTDADPEKVKKELLAydvvceeyggdvqAVHVSALTGKNL 331
Cdd:cd04164 84 DLVLLVV---DASEGLDEEDLEiLELPAKKPVIVVLNKSDLLSDAEGISELNGKP-------------IIAISAKTGEGI 147
|
90
....*....|..
gi 1958676470 332 MALAEATIALAE 343
Cdd:cd04164 148 DELKEALLELAG 159
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
253-355 |
9.95e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 38.88 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676470 253 DIVVLVVAADDGVMKQTVESIQHAKDAGVPIILAINKCDKTDADPEkvkkellAYDvvCEEYG-GDVQAvhVSALTGKNL 331
Cdd:PRK00093 82 DVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEAD-------AYE--FYSLGlGEPYP--ISAEHGRGI 150
|
90 100
....*....|....*....|....
gi 1958676470 332 MALAEATIALAEMLELKADPTGPV 355
Cdd:PRK00093 151 GDLLDAILEELPEEEEEDEEDEPI 174
|
|
| |
