|
Name |
Accession |
Description |
Interval |
E-value |
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
196-737 |
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: 662.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 196 KPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRARGAQVTDIVV 275
Cdd:COG0532 1 VPRPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-GGKITFLDTPGHEAFTAMRARGAQVTDIVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 276 LVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAE 355
Cdd:COG0532 80 LVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEWGGDTIFVPVSAKTGEGIDELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 356 ATIALAEILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMPV 435
Cdd:COG0532 160 MILLQAEVLELKANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTAYGRVRAMFDDRGKRVKEAGPSTPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 436 GIIGWRDLPSAGDEILEVESEPRAREVIEWRkseqkeekgkddlkimEEKRREHQEAHRKArekyGSLHwkersyiKFLE 515
Cdd:COG0532 240 EILGLSGVPQAGDEFVVVEDEKKAREIAEKR----------------QQKAREKKLARQKR----VSLE-------DLFS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 516 RKQQRPLKpkekverqsnVLPIIIKGDVDGSVEAI---LNLLDTydasHECELELVHFGLGDISENDVTFAETFDGVIYG 592
Cdd:COG0532 293 QIKEGEVK----------ELNLILKADVQGSVEALkdsLEKLST----DEVKVNIIHSGVGAITESDVNLAAASNAIIIG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 593 FNVEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSSRLPHTLEEYPIGEASILATFTVTegkkKIP-VAGCRVQKGQ 671
Cdd:COG0532 359 FNVRPDAKARKLAEREGVDIRYYSIIYDLIDDVKAAMEGMLEPEYKEEILGRAEVREVFKVS----KVGtIAGCYVTEGK 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530788299 672 LERHKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLDEEKvEFKPGDQVICYEENKVP 737
Cdd:COG0532 435 IKRNAKVRVLRDGVVIYEGELESLKRFKDDVKEVRAGYECGIGLKNFN-DIKEGDIIEAFEMEEVK 499
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
116-736 |
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: 546.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 116 MTVEDLASAMAKDIDCVYEALLNTAIDVdslEANSHLDEVWIKEVIKKAGmklkwSKLKQERIRENKDAVRRPGTDPALL 195
Cdd:TIGR00487 12 LTVSELANKMNIKVSDIIKKLMLLGVMV---TINQVLDKETAELVAEEFG-----VKVEVRVTLEETEAEEQDEDSGDLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 196 KPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVV 275
Cdd:TIGR00487 84 VERPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHVENEDGKMITFLDTPGHEAFTSMRARGAKVTDIVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 276 LVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAE 355
Cdd:TIGR00487 164 LVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIFVPVSALTGDGIDELLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 356 ATIALAEILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMPV 435
Cdd:TIGR00487 244 MILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVGAAYGRVRAMIDENGKSVKEAGPSKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 436 GIIGWRDLPSAGDEILEVESEPRAREVIEWRKSEQKEEKGKDDLKImeekrrehqeahrkarekygslhwkersyiKFLE 515
Cdd:TIGR00487 324 EILGLSDVPAAGDEFIVFKDEKDARLVAEKRAGKLRQKALSRSVKV------------------------------TLDN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 516 RKQQrpLKPKEKVErqsnvLPIIIKGDVDGSVEAILNLLDTYDAShECELELVHFGLGDISENDVTFAETFDGVIYGFNV 595
Cdd:TIGR00487 374 LFEQ--IKEGELKE-----LNIILKADVQGSLEAIKNSLEKLNNE-EVKVKVIHSGVGGITETDISLASASNAIIIGFNV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 596 EAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSSRLPHTLEEYPIGEASILATFTVTegkKKIPVAGCRVQKGQLERH 675
Cdd:TIGR00487 446 RPDATAKNVAEAENVDIRYYSVIYKLIDEIRAAMKGMLDPEYEEEIIGQAEVRQVFNVP---KIGNIAGCYVTEGVIKRG 522
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530788299 676 KKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLDEEKvEFKPGDQVICYEENKV 736
Cdd:TIGR00487 523 NPLRVIRDGVVIFEGEIDSLKRFKDDVKEVSNGYECGIGIKNYN-DIKEGDIIEAFEVQEV 582
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
90-732 |
8.74e-150 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 454.68 E-value: 8.74e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 90 TKKEKRPPRSQLS--PVKTKKEVEVWVGMTVEDLASAMakdidCVYEA-----LLNTAIdvdSLEANSHLDEVWIKEVIK 162
Cdd:CHL00189 138 KKKKVLSSKDELIkyDNNKPKSISIHSPLTIQELSTLL-----CIPETeiiksLFLKGI---SVTVNQIIDISIISQVAD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 163 KAGMKLKwsKLKQERIRENKDAVRRPGTDPALLKPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVS 242
Cdd:CHL00189 210 DFGINII--SEEKNNINEKTSNLDNTSAFTENSINRPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGAYEVE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 243 LP---SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKV 319
Cdd:CHL00189 288 FEykdENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 320 KKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAEATIALAEILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGT 399
Cdd:CHL00189 368 KQQLAKYNLIPEKWGGDTPMIPISASQGTNIDKLLETILLLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 400 LRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMPVGIIGWRDLPSAGDEILEVESEPRAREVIEwrkseQKEEKGKDDL 479
Cdd:CHL00189 448 LHIGDIIVIGTSYAKIRGMINSLGNKINLATPSSVVEIWGLSSVPATGEHFQVFNSEKEAKLKII-----KNKENNKKDT 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 480 KimeeKRREHQEAHrkarekygslhwkerSYIKFLERKQqrplkpkekverqsnvLPIIIKGDVDGSVEAILNLLDTYDA 559
Cdd:CHL00189 523 T----KRITLSTTK---------------TINKKDNKKQ----------------INLIIKTDTQGSIEAIINSISQIPQ 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 560 ShECELELVHFGLGDISENDVTFAETFDGVIYGFNVEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEELSSRLPHTLEE 639
Cdd:CHL00189 568 K-KVQLNILYASLGEVTETDVEFASTTNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLEYIEALMEDLLDPEYKK 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 640 YPIGEASILATFTVTEGKkkipVAGCRVQKGQLERHKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLdEEK 719
Cdd:CHL00189 647 VPIGEAEVKTVFPLAKRF----VAGCRVTEGKITKNALIKVIRENKLIYEGKITSLKRVKEDVEEAQEGNECGIFI-EEF 721
|
650
....*....|...
gi 530788299 720 VEFKPGDQVICYE 732
Cdd:CHL00189 722 QLWQSGDKIHAFE 734
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
200-364 |
3.96e-98 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 300.16 E-value: 3.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 200 PVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVV 278
Cdd:cd01887 1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPIDvKIPGITFIDTPGHEAFTNMRARGASVTDIAILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 279 AADDGVMKQTVESIQHAKDAEVPIILAINKCDK---TDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAE 355
Cdd:cd01887 81 AADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSELGLVGEEWGGDVSIVPISAKTGEGIDDLLE 160
|
....*....
gi 530788299 356 ATIALAEIL 364
Cdd:cd01887 161 AILLLAEVL 169
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
198-726 |
6.61e-60 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 212.73 E-value: 6.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 198 RSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAF 260
Cdd:PRK04004 5 RQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAgplkkplpiklkipgllFIDTPGHEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 261 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKT---------------DADPEKVKKEL-- 323
Cdd:PRK04004 85 TNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIpgwkstedapflesiEKQSQRVQQELee 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 324 LAYDVVCE--EYGGD-------------VQAVHVSALTG----DNLMALAeatiALAEIL---ELKADPTGPVEGTVIES 381
Cdd:PRK04004 165 KLYELIGQlsELGFSadrfdrvkdftktVAIVPVSAKTGegipDLLMVLA----GLAQRYleeRLKIDVEGPGKGTVLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 382 FTDKGRGPVTTAIIQRGTLRKG-SILVAGKSWA---KVRLIFdengkilneaypsmpvgiigwrdLPSAGDEILEVESep 457
Cdd:PRK04004 241 KEERGLGTTIDVILYDGTLRKGdTIVVGGKDGPivtKVRALL-----------------------KPRPLDEMRDPED-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 458 rareviewrKSEQKEE-----------KGKDD------LKIMEEkrREHQEAHRKAREKYgslhwkersyikflerkqqr 520
Cdd:PRK04004 296 ---------KFKPVDEvvaaagvkisaPDLEDalagspLRVVRD--EDVEEVKEEVEEEI-------------------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 521 plkpkEKVERQSNVLPIIIKGDVDGSVEAILNLLDtydashECELELVHFGLGDISENDVTFAET------FDGVIYGFN 594
Cdd:PRK04004 345 -----EEIRIETDEEGVVVKADTLGSLEALVNELR------EEGIPIRKADVGDISKRDVIEASTvaekdpLYGVILAFN 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 595 VEAGSAIQQSAAQKGVKIKLHKIIYHLIEDLQEelssrlpHTLEEYPIGEASILATFTVTeGKKKI----------P-VA 663
Cdd:PRK04004 414 VKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEK-------WVKEQKEAEKEKILEKIVRP-AKIRIlpgyvfrqsdPaIV 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530788299 664 GCRVQKGQLERhkKFKLIR-NGQVIwkGSLTSLKHHKDDISVIKTGMDCGLSLDEEKV--EFKPGD 726
Cdd:PRK04004 486 GVEVLGGTIKP--GVPLIKeDGKRV--GTIKQIQDQGENVKEAKAGMEVAISIDGPTVgrQIKEGD 547
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
198-717 |
1.66e-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: 171.92 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 198 RSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGA--------------FLVSLPSGEKIT---FLDTPGHAAF 260
Cdd:TIGR00491 3 RQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAsevptdviekicgdLLKSFKIKLKIPgllFIDTPGHEAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 261 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA-----------------DPEKVKKEL 323
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGwkshegypflesinkqeQRVRQNLDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 324 LAYDVVCE--EYGGD-------------VQAVHVSALTGDNLMALAEATIALAE-ILE--LKADPTGPVEGTVIESFTDK 385
Cdd:TIGR00491 163 QVYNLVIQlaEQGFNaerfdrirdftktVAIIPVSAKTGEGIPELLAILAGLAQnYLEnkLKLAIEGPAKGTILEVKEEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 386 GRGPVTTAIIQRGTLRKGSILVAGKS----WAKVRLIFdengkilneaypsmpvgiigwrdLPSAGDEILEVESEPRARE 461
Cdd:TIGR00491 243 GLGYTIDAVIYDGILRKGDIIVLAGIddviVTRVRAIL-----------------------KPRPLQEMRLARKKFAQVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 462 VIEWRKSEQKEEKGKDDLKIMEEKRREHQEAHRKAREkygslhwkersyikflerkqqRPLKPKEKVERQSNVLPIIIKG 541
Cdd:TIGR00491 300 EVYAAAGVKVAAPNLDTVLAGSPIVVENNEEIEKYKE---------------------EIQKEVEEIKIYTDEEGIVVKA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 542 DVDGSVEAILNLL-DTYDASHECElelvhfgLGDISENDVTFAETFD------GVIYGFNVEAGSAIQQSAAQKGVKIKL 614
Cdd:TIGR00491 359 DTLGSLEALVNELrRRGIPIKKAD-------IGDVSKRDVVEAEIVKqeakeyGAIAAFNVKPLPGAEIEAEKYDIKLFS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 615 HKIIYHLIEDLQE----ELSSRLPHTLEEYpIGEASILATFTVTEGKKKIPVAGCRVQKGQLERhkKFKLIR-NGQVIwk 689
Cdd:TIGR00491 432 DNIIYQLMENFEKwiedIEESEKRKTLEAI-IKPGKIKIIPGYVFRRSDPAIVGVEVLGGIIRP--GYPLIKkDGRRV-- 506
|
570 580
....*....|....*....|....*...
gi 530788299 690 GSLTSLKHHKDDISVIKTGMDCGLSLDE 717
Cdd:TIGR00491 507 GEVRQIQDNGKNVKRASAGMEVAIAIED 534
|
|
| IF2_mtIF2_II |
cd03702 |
Domain II of bacterial and mitochondrial Initiation Factor 2; This family represents domain II ... |
373-467 |
1.80e-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: 146.03 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 373 PVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAKVRLIFDENGKILNEAYPSMPVGIIGWRDLPSAGDEILE 452
Cdd:cd03702 1 LARGVVIESKLDKGRGPVATVLVQNGTLKVGDILVAGTTYGKVRAMIDDNGKRIKEAGPSTPVEILGLNGVPQAGDKFIV 80
|
90
....*....|....*
gi 530788299 453 VESEPRAREVIEWRK 467
Cdd:cd03702 81 VDSEKEAREIAEKRQ 95
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
202-356 |
3.05e-39 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 143.43 E-value: 3.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKLRE--------TQVAA--------MEV---GGITQHIGAflVSLPSGE-KITFLDTPGHAAFS 261
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLLYytgaiskrGEVKGegeagldnLPEereRGITIKSAA--VSFETKDyLINLIDTPGHVDFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 262 AMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTD-ADPEKVKKELlaYDVVCEEYGGD---V 337
Cdd:pfam00009 84 KEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgAELEEVVEEV--SRELLEKYGEDgefV 161
|
170
....*....|....*....
gi 530788299 338 QAVHVSALTGDNLMALAEA 356
Cdd:pfam00009 162 PVVPGSALKGEGVQTLLDA 180
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
213-716 |
7.83e-35 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 142.72 E-value: 7.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 213 TTLLDKLRETQVAAMEVGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAFSAMRARGAQVTDIVV 275
Cdd:PRK14845 475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICgpllkllkaeikipgllFIDTPGHEAFTSLRKRGGSLADLAV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 276 LVVAADDGVMKQTVESIQHAKDAEVPIILAINKCD-----------------KTDADPEKVKKELLAYDVVCE--EYGGD 336
Cdd:PRK14845 555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDlipgwnisedepfllnfNEQDQHALTELEIKLYELIGKlyELGFD 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 337 -------------VQAVHVSALTGDNLMALAEATIALAE-ILE--LKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGTL 400
Cdd:PRK14845 635 adrfdrvqdftrtVAIVPVSAKTGEGIPELLMMVAGLAQkYLEerLKLNVEGYAKGTILEVKEEKGLGTTIDAIIYDGTL 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 401 RKG-SILVAGKSWA---KVRLIF-----DEngkILNEAYPSMPVGIIgwrdLPSAGDEIleveSEPRAREVI---EWRKS 468
Cdd:PRK14845 715 RRGdTIVVGGPDDVivtKVRALLkpkplDE---IRDPRDKFDPVDEV----TAAAGVKI----AAPGLEEVLagsPIRIV 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 469 EQKEEkgkddlkimeekrrehqeahrkarekygslhwkersyikfLERKQQRPLKPKEKVERQSNVLPIIIKGDVDGSVE 548
Cdd:PRK14845 784 PTKEK----------------------------------------IEKAKEEVMKEVEEAKIETDKEGILIKADTLGSLE 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 549 AILNLLdtydasHECELELVHFGLGDISENDVTFA------ETFDGVIYGFNVEAGSAIQQSAAQKGVKIKLHKIIYHLI 622
Cdd:PRK14845 824 ALANEL------RKAGIPIKKAEVGDITKKDVIEAlsykqeNPLYGVILGFNVKVLPEAQEEAEKYGVKIFVDNIIYKLV 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 623 EDLQE---ELSSRLPHTLEEYPIGEASILATFTVTEGKKKIPVAGCRVQKGQLErhKKFKLIR-NGQVIwkGSLTSLKHH 698
Cdd:PRK14845 898 EDYTEwvkEEEEKKKRELFEKLIKPGIIRLLPDCIFRRSNPAIVGVEVLEGTLR--VGVTLIKeDGMKV--GTVRSIKDR 973
|
570
....*....|....*...
gi 530788299 699 KDDISVIKTGMDCGLSLD 716
Cdd:PRK14845 974 GENVKEAKAGKAVAIAIE 991
|
|
| IF-2 |
pfam11987 |
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main ... |
525-626 |
5.05e-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: 126.01 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 525 KEKVERQSNVLPIIIKGDVDGSVEAILNLLDTYDaSHECELELVHFGLGDISENDVTFAETFDGVIYGFNVEAGSAIQQS 604
Cdd:pfam11987 16 FSQIKEEVKELNLIIKADVQGSLEALKESLEKLS-NDEVKVNIIHSGVGAITESDVMLASASNAIIIGFNVRPDAKARKL 94
|
90 100
....*....|....*....|..
gi 530788299 605 AAQKGVKIKLHKIIYHLIEDLQ 626
Cdd:pfam11987 95 AEKEGVDIRYYNIIYDLIDDVK 116
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
202-356 |
2.53e-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: 120.86 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKL---------------RETQVAAMEV-GGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRA 265
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLlyqtgaidrrgtrkeTFLDTLKEEReRGITIKTGVVEFEWP-KRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 266 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTD-ADPEKVKKE---LLAYDVVCEEYGGDVQAVH 341
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGeEDFDEVLREikeLLKLIGFTFLKGKDVPIIP 160
|
170
....*....|....*
gi 530788299 342 VSALTGDNLMALAEA 356
Cdd:cd00881 161 ISALTGEGIEELLDA 175
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
206-362 |
4.36e-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: 108.08 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 206 GHVDHGKTTLL--------DKLRETQVAamevgGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVV 275
Cdd:cd04171 6 GHIDHGKTTLIkaltgietDRLPEEKKR-----GITIDLGfAYL-DLPDGKRLGFIDVPGHEKFvKNMLA-GAGGIDAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 276 LVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDAD-PEKVKKELLAYdvvCEEYGG-DVQAVHVSALTGDNLMA 352
Cdd:cd04171 79 LVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVDEDrLELVEEEILEL---LAGTFLaDAPIFPVSSVTGEGIEE 155
|
170
....*....|
gi 530788299 353 LAEATIALAE 362
Cdd:cd04171 156 LKNYLDELAE 165
|
|
| mtIF2_IVc |
cd03692 |
C2 subdomain of domain IV in mitochondrial translation initiation factor 2; This model ... |
643-730 |
5.69e-26 |
|
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: 101.80 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 643 GEASILATFTVTegkKKIPVAGCRVQKGQLERHKKFKLIRNGQVIWKGSLTSLKHHKDDISVIKTGMDCGLSLDEEKvEF 722
Cdd:cd03692 1 GEAEVRAVFKIS---KVGTIAGCYVTEGKIKRNAKVRVLRDGEVIYEGKISSLKRFKDDVKEVKKGYECGITLENFN-DI 76
|
....*...
gi 530788299 723 KPGDQVIC 730
Cdd:cd03692 77 KEGDIIEA 84
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
200-355 |
1.23e-25 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 103.61 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 200 PVVTVMGHVDHGKTTLLDKLRETQVAAME-VGGITQHIGAFLVSL-PSGEKITFLDTPGHAAFSAMR-------ARGAQV 270
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEyYPGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRrlyypqvERSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 271 TDIVVLVVAADDGVMKQTVEsIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAydvvcEEYGGDVqaVHVSALTGDNL 350
Cdd:TIGR00231 82 FDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDADLKTHVASEFA-----KLNGEPI--IPLSAETGKNI 153
|
....*
gi 530788299 351 MALAE 355
Cdd:TIGR00231 154 DSAFK 158
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
206-416 |
9.09e-24 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 106.54 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 206 GHVDHGKTTLL--------DKLRETQVAamevgGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVV 275
Cdd:COG3276 7 GHIDHGKTTLVkaltgidtDRLKEEKKR-----GITIDLGfAYL-PLPDGRRLGFVDVPGHEKFiKNMLA-GAGGIDLVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 276 LVVAADDGVMKQTVE--------SIQHakdaevpIILAINKCDKtdADPEKVkkELLAYDvVCEEYGG----DVQAVHVS 343
Cdd:COG3276 80 LVVAADEGVMPQTREhlaildllGIKR-------GIVVLTKADL--VDEEWL--ELVEEE-IRELLAGtfleDAPIVPVS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530788299 344 ALTGDNLMALAEATIALAEILELKaDPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGS---ILVAGKSwAKVR 416
Cdd:COG3276 148 AVTGEGIDELRAALDALAAAVPAR-DADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDeleLLPSGKP-VRVR 221
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
202-403 |
4.66e-21 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 97.76 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKL----------RETQVAAMEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 264
Cdd:TIGR01394 4 IAIIAHVDHGKTTLVDALlkqsgtfranEAVAERVMDSNdlererGIT--ILAKNTAIRyNGTKINIVDTPGHADFGGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 265 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHV 342
Cdd:TIGR01394 82 ERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVfdLFAELGADDEQLDFPIVYA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530788299 343 SALTGDNLMALAEATIALAEILEL--------KADPTGPVEG--TVIESFTDKGRgpVTTAIIQRGTLRKG 403
Cdd:TIGR01394 162 SGRAGWASLDLDDPSDNMAPLFDAivrhvpapKGDLDEPLQMlvTNLDYDEYLGR--IAIGRVHRGTVKKG 230
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
202-347 |
5.63e-21 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 91.50 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKL-------RETQVAA---MEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 264
Cdd:cd01891 5 IAIIAHVDHGKTTLVDALlkqsgtfRENEEVGervMDSNdlererGIT--ILAKNTAITyKDTKINIIDTPGHADFGGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 265 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHV 342
Cdd:cd01891 83 ERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVfdLFLELNATDEQLDFPIVYA 162
|
....*
gi 530788299 343 SALTG 347
Cdd:cd01891 163 SAKNG 167
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
202-347 |
6.44e-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: 88.19 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTL------------LDKLRETQVAamevgGITQHIG--AFLVSLPSGE-----------KITFLDTPG 256
Cdd:cd01889 3 VGLLGHVDSGKTSLakalseiastaaFDKNPQSQER-----GITLDLGfsSFEVDKPKHLednenpqienyQITLVDCPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 257 HAafSAMRA--RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCD-----KTDADPEKVKKELLayDVV 329
Cdd:cd01889 78 HA--SLIRTiiGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDlipeeERKRKIEKMKKRLQ--KTL 153
|
170
....*....|....*...
gi 530788299 330 CEEYGGDVQAVHVSALTG 347
Cdd:cd01889 154 EKTRLKDSPIIPVSAKPG 171
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
201-407 |
1.77e-19 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 93.01 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 201 VVTVMGHVDHGKTTLLDKLRETQVAAM---EVGGITQHIGAFLVSLPSgEKITFLDTPGHAAFSAMRARGAQVTDIVVLV 277
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALTGIAADRLpeeKKRGMTIDLGFAYFPLPD-YRLGFIDVPGHEKFISNAIAGGGGIDAALLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 278 VAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNLMALAEA 356
Cdd:TIGR00475 81 VDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTSAKTGQGIGELKKE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530788299 357 TIALAEILELKaDPTGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILV 407
Cdd:TIGR00475 161 LKNLLESLDIK-RIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLR 210
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
206-406 |
2.24e-18 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 89.34 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 206 GHVDHGKTTLL--------DKLRETQVAAMevggiTQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVVLV 277
Cdd:PRK10512 7 GHVDHGKTTLLqaitgvnaDRLPEEKKRGM-----TIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 278 VAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTD-ADPEKVKKELLAydvVCEEYGGDVQAVHV-SALTG------- 347
Cdd:PRK10512 82 VACDDGVMAQTREHLAILQLTGNPmLTVALTKADRVDeARIAEVRRQVKA---VLREYGFAEAKLFVtAATEGrgidalr 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530788299 348 DNLMALAEATIALAEILELKADptgpvegtviESFTDKGRGPVTTAIIQRGTLRKGSIL 406
Cdd:PRK10512 159 EHLLQLPEREHAAQHRFRLAID----------RAFTVKGAGLVVTGTALSGEVKVGDTL 207
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
207-358 |
1.56e-17 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 81.04 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 207 HVDHGKTTLLDKLRE-----------TQVA-AMEVG---GITqhIGAFLVSLP----SGEK--ITFLDTPGHAAFSAMRA 265
Cdd:cd01890 8 HIDHGKSTLADRLLEltgtvseremkEQVLdSMDLErerGIT--IKAQAVRLFykakDGEEylLNLIDTPGHVDFSYEVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 266 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELlaydvvcEEY-GGDV-QAVHVS 343
Cdd:cd01890 86 RSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEI-------EDVlGLDAsEAILVS 158
|
170
....*....|....*
gi 530788299 344 ALTGDNLMALAEATI 358
Cdd:cd01890 159 AKTGLGVEDLLEAIV 173
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
204-356 |
4.60e-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: 79.04 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 204 VMGHVDHGKTTLLDKLRETQVAAM-EVGGITQHIGAFLVSLPSG-EKITFLDTPGHAAFSAMRARG-----AQVTDIVVL 276
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVsDVPGTTRDPDVYVKELDKGkVKLVLVDTPGLDEFGGLGREElarllLRGADLILL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 277 VVAADDGVMKQTVE--SIQHAKDAEVPIILAINKCDKtdaDPEKVKKELLAYDVVCEEYGGDVqaVHVSALTGDNLMALA 354
Cdd:cd00882 82 VVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDL---LEEREVEELLRLEELAKILGVPV--FEVSAKTGEGVDELF 156
|
..
gi 530788299 355 EA 356
Cdd:cd00882 157 EK 158
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
205-403 |
6.56e-17 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 83.46 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 205 MGHVDHGKTTLLDKLreTQVAAmEVGGITQHIGAFLVSLPSgEK---ITF----------------LDTPGHAAFSAMRA 265
Cdd:PRK12736 18 IGHVDHGKTTLTAAI--TKVLA-ERGLNQAKDYDSIDAAPE-EKergITIntahveyetekrhyahVDCPGHADYVKNMI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 266 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELL-AYDvvceeYGGD- 336
Cdd:PRK12736 94 TGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLVD-DEELLElvemevRELLsEYD-----FPGDd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 337 VQAVHVSALtgdnlMALAEATIALAEILELKAD-----PTG----------PVEGTviesFTDKGRGPVTTAIIQRGTLR 401
Cdd:PRK12736 168 IPVIRGSAL-----KALEGDPKWEDAIMELMDAvdeyiPTPerdtdkpflmPVEDV----FTITGRGTVVTGRVERGTVK 238
|
..
gi 530788299 402 KG 403
Cdd:PRK12736 239 VG 240
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
196-403 |
1.11e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 82.93 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 196 KPRSPVVTVmGHVDHGKTTLLDKLreTQVAAMEVG------------------GIT---QHIgaflvslpsgEKIT---- 250
Cdd:PRK00049 10 KPHVNVGTI-GHVDHGKTTLTAAI--TKVLAKKGGaeakaydqidkapeekarGITintAHV----------EYETekrh 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 251 --FLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------K 321
Cdd:PRK00049 77 yaHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 322 ELLAydvvceEY---GGDVQAVHVSAltgdnLMALAEATIALAE--ILELKA-------DPTGPVEGTV---IES-FTDK 385
Cdd:PRK00049 156 ELLS------KYdfpGDDTPIIRGSA-----LKALEGDDDEEWEkkILELMDavdsyipTPERAIDKPFlmpIEDvFSIS 224
|
250
....*....|....*...
gi 530788299 386 GRGPVTTAIIQRGTLRKG 403
Cdd:PRK00049 225 GRGTVVTGRVERGIIKVG 242
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
205-403 |
2.93e-16 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 81.35 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 205 MGHVDHGKTTLLDKLreTQVAAMEVG------------------GIT---QHIgaflvslpsgEKIT------FLDTPGH 257
Cdd:COG0050 18 IGHVDHGKTTLTAAI--TKVLAKKGGakakaydqidkapeekerGITintSHV----------EYETekrhyaHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 258 AAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLaydvvc 330
Cdd:COG0050 86 ADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevRELL------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 331 EEY---GGDVQAVHVSAltgdnLMALAEATIALAE--ILELKA-------DPTG--------PVEGTviesFTDKGRGPV 390
Cdd:COG0050 159 SKYgfpGDDTPIIRGSA-----LKALEGDPDPEWEkkILELMDavdsyipEPERdtdkpflmPVEDV----FSITGRGTV 229
|
250
....*....|...
gi 530788299 391 TTAIIQRGTLRKG 403
Cdd:COG0050 230 VTGRVERGIIKVG 242
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
204-418 |
1.39e-15 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 79.59 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 204 VMGHVDHGKTTLLDKLretqvaAMEVGGITQHI-----------G------AFLVSLPSGEK------------------ 248
Cdd:COG5256 12 VIGHVDHGKSTLVGRL------LYETGAIDEHIiekyeeeaekkGkesfkfAWVMDRLKEERergvtidlahkkfetdky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 249 -ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDADP---EKVKKEL 323
Cdd:COG5256 86 yFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAVNYSEkryEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 324 ------LAYDVvceeygGDVQAVHVSALTGDNLMALAEAT-----IALAEILELKADPTGPVEG----TVIESFTDKGRG 388
Cdd:COG5256 166 skllkmVGYKV------DKIPFIPVSAWKGDNVVKKSDNMpwyngPTLLEALDNLKEPEKPVDKplriPIQDVYSISGIG 239
|
250 260 270
....*....|....*....|....*....|...
gi 530788299 389 PVTTAIIQRGTLRKGSILV---AGKSwAKVRLI 418
Cdd:COG5256 240 TVPVGRVETGVLKVGDKVVfmpAGVV-GEVKSI 271
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
202-311 |
2.85e-15 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 75.38 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKL------------------RETQVAAMEVG-GITQHIGAFLVSLPSGEK----ITFLDTPGHA 258
Cdd:cd04167 3 VCIAGHLHHGKTSLLDMLieqthkrtpsvklgwkplRYTDTRKDEQErGISIKSNPISLVLEDSKGksylINIIDTPGHV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 530788299 259 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDK 311
Cdd:cd04167 83 NFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
202-403 |
3.40e-15 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 78.43 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKLretqvaAMEVGGITQHI-----------G------AFLVSLPSGEK---------------- 248
Cdd:PRK12317 9 LAVIGHVDHGKSTLVGRL------LYETGAIDEHIieelreeakekGkesfkfAWVMDRLKEERergvtidlahkkfetd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 249 ---ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD--GVMKQTVESIQHAKDAEVP-IILAINKCDKTDADPEK---V 319
Cdd:PRK12317 83 kyyFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINqLIVAINKMDAVNYDEKRyeeV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 320 KKEL------LAYDVvceeygGDVQAVHVSALTGDNLMALAEAT-----IALAEILELKADPTGPVEG----TVIESFTD 384
Cdd:PRK12317 163 KEEVskllkmVGYKP------DDIPFIPVSAFEGDNVVKKSENMpwyngPTLLEALDNLKPPEKPTDKplriPIQDVYSI 236
|
250
....*....|....*....
gi 530788299 385 KGRGPVTTAIIQRGTLRKG 403
Cdd:PRK12317 237 SGVGTVPVGRVETGVLKVG 255
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
196-403 |
5.38e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 77.94 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 196 KPRSPVVTVmGHVDHGKTTLLDKLreTQVAAmEVG-------------------GITqhIGAFLVSLPSGEK-ITFLDTP 255
Cdd:PLN03127 59 KPHVNVGTI-GHVDHGKTTLTAAI--TKVLA-EEGkakavafdeidkapeekarGIT--IATAHVEYETAKRhYAHVDCP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 256 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLAYdv 328
Cdd:PLN03127 133 GHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVVD-DEELLElvemelRELLSF-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 329 vcEEYGGD----VQAVHVSALTGDNLMALAEATIALAE-----ILELKADPTGPVEGTVIESFTDKGRGPVTTAIIQRGT 399
Cdd:PLN03127 210 --YKFPGDeipiIRGSALSALQGTNDEIGKNAILKLMDavdeyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGT 287
|
....
gi 530788299 400 LRKG 403
Cdd:PLN03127 288 IKVG 291
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
207-319 |
7.08e-15 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 78.14 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 207 HVDHGKTTLLDKL-------RETQVAA---MEVG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQ 269
Cdd:COG1217 14 HVDHGKTTLVDALlkqsgtfRENQEVAervMDSNdlererGIT--ILAKNTAVRyKGVKINIVDTPGHADFGGEVERVLS 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 530788299 270 VTDIVVLVVAADDGVMKQT--VesIQHAKDAEVPIILAINKCDKTDADPEKV 319
Cdd:COG1217 92 MVDGVLLLVDAFEGPMPQTrfV--LKKALELGLKPIVVINKIDRPDARPDEV 141
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
205-323 |
2.78e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 76.70 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 205 MGHVDHGKTTLLDK-LRETQV--AAMEVG---------------GITqhIGAFLVSLP-SGEKITFLDTPGHAAF----- 260
Cdd:PRK12740 1 VGHSGAGKTTLTEAiLFYTGAihRIGEVEdgtttmdfmpeererGIS--ITSAATTCEwKGHKINLIDTPGHVDFtgeve 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530788299 261 SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 323
Cdd:PRK12740 79 RALR-----VLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQL 136
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
204-364 |
4.07e-14 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 70.74 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 204 VMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLPSGEKITFLDTPG-------HAAFSAMRARGAQVTDIVV 275
Cdd:cd00880 2 IFGRPNVGKSSLLNALlGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRADLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 276 LVVAADDGVMKQtVESIQHAKDAEVPIILAINKCDKTDADPEKVKkellaYDVVCEEYGGDVQAVHVSALTGDNLMALAE 355
Cdd:cd00880 82 LVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEEEEL-----LRERKLELLPDLPVIAVSALPGEGIDELRK 155
|
....*....
gi 530788299 356 atiALAEIL 364
Cdd:cd00880 156 ---KIAELL 161
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
205-366 |
4.55e-14 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 71.46 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 205 MGHVDHGKTTLLDKLreTQVAAMEVG------------------GITqhIGAFLVSLPSGEK-ITFLDTPGHAAF-SAMR 264
Cdd:cd01884 8 IGHVDHGKTTLTAAI--TKVLAKKGGakakkydeidkapeekarGIT--INTAHVEYETANRhYAHVDCPGHADYiKNMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 265 ARGAQVtDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLaydvvcEEYGGDV 337
Cdd:cd01884 84 TGAAQM-DGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMVD-DEELLElvemevRELL------SKYGFDG 155
|
170 180 190
....*....|....*....|....*....|.
gi 530788299 338 QAVHVsaLTGDNLMAL--AEATIALAEILEL 366
Cdd:cd01884 156 DDTPI--VRGSALKALegDDPNKWVDKILEL 184
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
204-323 |
1.10e-13 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 71.11 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 204 VMGHVDHGKTTLLDKLRETQVAAMEVG------------------GIT--QHIGAFLVslpSGEKITFLDTPGHAAFSAM 263
Cdd:cd04168 4 ILAHVDAGKTTLTESLLYTSGAIRELGsvdkgttrtdsmelerqrGITifSAVASFQW---EDTKVNIIDTPGHMDFIAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530788299 264 RARGAQVTDIVVLVVAADDGVMKQTvESIQHA-KDAEVPIILAINKCDKTDADPEKVKKEL 323
Cdd:cd04168 81 VERSLSVLDGAILVISAVEGVQAQT-RILFRLlRKLNIPTIIFVNKIDRAGADLEKVYQEI 140
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
204-323 |
2.93e-13 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 73.16 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 204 VMGHVDHGKTTLL----------DKLRE-----TQVAAMEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAF---- 260
Cdd:COG0480 14 IVAHIDAGKTTLTerilfytgaiHRIGEvhdgnTVMDWMPEEqerGIT--ITSAATTCEwKGHKINIIDTPGHVDFtgev 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530788299 261 -SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 323
Cdd:COG0480 92 eRSLR-----VLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQL 150
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
189-323 |
1.50e-12 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 70.86 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 189 GTDPALLKPRSPVVTVMGHVDHGKTTLLDKLRETQVAAMEVGGITQHIGAFLVSL---PSGEKITFLDTPGHAAFSAMRA 265
Cdd:COG5180 389 GAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVPGdaeSVSGPAGLADQAGAAASTAMAD 468
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530788299 266 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 323
Cdd:COG5180 469 FVAPVTDATPVDVADVLGVRPDAILGGNVAPASGLDAETRIIEAEGAPATEDFVAAEL 526
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
202-425 |
1.85e-12 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 70.51 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKL----------RETQVAAMEVGGITQHIGAFLVSLPSGEK-----ITFLDTPGHAAFSAMRAR 266
Cdd:PRK10218 8 IAIIAHVDHGKTTLVDKLlqqsgtfdsrAETQERVMDSNDLEKERGITILAKNTAIKwndyrINIVDTPGHADFGGEVER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 267 GAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL--LAYDVVCEEYGGDVQAVHVSA 344
Cdd:PRK10218 88 VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVfdLFVNLDATDEQLDFPIVYASA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 345 LTG----------DNLMALAEATIALAEILELKADptGPVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKSWAK 414
Cdd:PRK10218 168 LNGiagldhedmaEDMTPLYQAIVDHVPAPDVDLD--GPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGK 245
|
250
....*....|.
gi 530788299 415 VRlifdeNGKI 425
Cdd:PRK10218 246 TR-----NAKV 251
|
|
| tufA |
CHL00071 |
elongation factor Tu |
206-403 |
6.07e-12 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 68.06 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 206 GHVDHGKTTLldklreTQVAAMEVGGITQHIGAFLVSLPSG--EK---ITF----------------LDTPGHAAFSAMR 264
Cdd:CHL00071 19 GHVDHGKTTL------TAAITMTLAAKGGAKAKKYDEIDSApeEKargITIntahveyetenrhyahVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 265 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPE-------KVKKELLAYDvvceeYGGD 336
Cdd:CHL00071 93 ITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVD-DEEllelvelEVRELLSKYD-----FPGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 337 vqavHVSALTGDNLMALaEATIALAE-----------ILEL--KAD---PTgPVEGT------VIES-FTDKGRGPVTTA 393
Cdd:CHL00071 167 ----DIPIVSGSALLAL-EALTENPKikrgenkwvdkIYNLmdAVDsyiPT-PERDTdkpflmAIEDvFSITGRGTVATG 240
|
250
....*....|
gi 530788299 394 IIQRGTLRKG 403
Cdd:CHL00071 241 RIERGTVKVG 250
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
137-416 |
8.84e-12 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 68.42 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 137 LNTAIDVDSL---EANSHLDEVWIKEViKKAGMklkwskLKQERIRENKDAvrrpgtdpallKPRSPVVTVMGHVDHGKT 213
Cdd:COG5258 75 FSESMDVLSLlaeEIGAKIEDVETWEV-GDGGL------VGVVTIREGKEK-----------DPEHIVVGVAGHVDHGKS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 214 TL--------LD----KLR---ETQVAAMEVG---GITQHIGAF------------------LVSLPSGEKITFLDTPGH 257
Cdd:COG5258 137 TLvgtlvtgkLDdgngGTRsflDVQPHEVERGlsaDLSYAVYGFdddgpvrmknplrktdraRVVEESDKLVSFVDTVGH 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 258 AAFSAMRARG--AQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKtdADPEKVK------KELL----- 324
Cdd:COG5258 217 EPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDK--VDDERVEevereiENLLrivgr 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 325 ----------AYDVVCEEYGGDVQAVHVSALTGDNLMALAEatiaLAEIL-ELKADPTGPVEGTVIESFTDKGRGPVTTA 393
Cdd:COG5258 295 tplevesrhdVDAAIEEINGRVVPILKTSAVTGEGLDLLDE----LFERLpKRATDEDEPFLMYIDRIYNVTGVGTVVSG 370
|
330 340
....*....|....*....|....*..
gi 530788299 394 IIQRGTLRKGSILVAGK----SWAKVR 416
Cdd:COG5258 371 TVKSGKVEAGDELLIGPtkdgSFREVE 397
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
196-406 |
9.35e-12 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 68.10 E-value: 9.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 196 KPRSPVVTVmGHVDHGKTTLL---------------DKLRETQVAAMEVG-GITqhIGAFLVSLPSGEK-ITFLDTPGHA 258
Cdd:PLN03126 79 KPHVNIGTI-GHVDHGKTTLTaaltmalasmggsapKKYDEIDAAPEERArGIT--INTATVEYETENRhYAHVDCPGHA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 259 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDKTDaDPEKVK------KELLAydvvCE 331
Cdd:PLN03126 156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVD-DEELLElvelevRELLS----SY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 332 EYGGDvqavHVSALTGDNLMALaEATIA-----------LAEILEL--KADPTGPVEG---------TVIESFTDKGRGP 389
Cdd:PLN03126 231 EFPGD----DIPIISGSALLAL-EALMEnpnikrgdnkwVDKIYELmdAVDSYIPIPQrqtdlpfllAVEDVFSITGRGT 305
|
250
....*....|....*..
gi 530788299 390 VTTAIIQRGTLRKGSIL 406
Cdd:PLN03126 306 VATGRVERGTVKVGETV 322
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
202-319 |
1.71e-11 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 67.67 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDK-LRET----QVAAMEVG-------------GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSA 262
Cdd:PRK13351 11 IGILAHIDAGKTTLTERiLFYTgkihKMGEVEDGttvtdwmpqeqerGIT--IESAATSCDWDNhRINLIDTPGHIDFTG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 530788299 263 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKV 319
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKV 145
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
202-311 |
2.08e-11 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 64.17 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLD---------------KLRETQVAAME-VGGITqhIGAFLVSL--------PSGEK--ITFLDTP 255
Cdd:cd01885 3 ICIIAHVDHGKTTLSDsllasagiiseklagKARYLDTREDEqERGIT--IKSSAISLyfeyeeekMDGNDylINLIDSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530788299 256 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDK 311
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
200-365 |
5.18e-11 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 62.97 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 200 PVVTVmGHVDHGKTTLLDKL-------RETQVAAMEVGGITQHIG-----AFLV-SLP----------------SGEKIT 250
Cdd:cd04166 1 RFITC-GSVDDGKSTLIGRLlydsksiFEDQLAALERSKSSGTQGekldlALLVdGLQaereqgitidvayryfSTPKRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 251 FL--DTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT-----VES---IQHakdaevpIILAINKCDKTDADPEkvk 320
Cdd:cd04166 80 FIiaDTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTrrhsyIASllgIRH-------VVVAVNKMDLVDYDEE--- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530788299 321 kellAYDVVCEEYGG--------DVQAVHVSALTGDNLMALAEATI-----ALAEILE 365
Cdd:cd04166 150 ----VFEEIKADYLAfaaslgieDITFIPISALEGDNVVSRSENMPwykgpTLLEHLE 203
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
202-369 |
9.02e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 61.54 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKLRETQVAAMEVG---GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSAMRA------RGAqvt 271
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLstnGVT--IDKKELKLDGLDvDLVIWDTPGQDEFRETRQfyarqlTGA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 272 DIVVLVVaadDGVMKQTVESI--------QHAKDAevPIILAINKCDKtdADPEKVKKELLAYDVVCEEYGGDVqaVHVS 343
Cdd:COG1100 81 SLYLFVV---DGTREETLQSLyelleslrRLGKKS--PIILVLNKIDL--YDEEEIEDEERLKEALSEDNIVEV--VATS 151
|
170 180
....*....|....*....|....*.
gi 530788299 344 ALTGDNLMALAEatiALAEILELKAD 369
Cdd:COG1100 152 AKTGEGVEELFA---ALAEILRGEGD 174
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
202-350 |
1.84e-10 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 62.23 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDK-LRETQVAAM----EVGG---------ITQHIGAFLVSLP---SGEKITFLDTPGHAAFSAmR 264
Cdd:cd04170 2 IALVGHSGSGKTTLAEAlLYATGAIDRlgrvEDGNtvsdydpeeKKRKMSIETSVAPlewNGHKINLIDTPGYADFVG-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 265 ARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKELLAYdvvceeYGGDVQAVHVS 343
Cdd:cd04170 81 TLSAlRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREA------FGRPVVPIQLP 154
|
....*..
gi 530788299 344 ALTGDNL 350
Cdd:cd04170 155 IGEGDEF 161
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
249-360 |
5.62e-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: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 249 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKtdAD 315
Cdd:COG1159 53 IVFVDTPGihkpkrklgrrmnKAAWSALED-----VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530788299 316 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGDNLMALAEATIAL 360
Cdd:COG1159 126 KEELLPLLAEY----SELLDFAEIVPISALKGDNVDELLDEIAKL 166
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
206-435 |
6.93e-10 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 62.25 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 206 GHVDHGKTTLLDKLR-------ETQVAAME-----VGGITQHIG-AFLVSLPSGEK---IT--------------FL--D 253
Cdd:PRK05506 31 GSVDDGKSTLIGRLLydskmifEDQLAALErdskkVGTQGDEIDlALLVDGLAAEReqgITidvayryfatpkrkFIvaD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 254 TPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdaevpIILAINKCDKTDADPEKvkkella 325
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTrrhsfiasLLGIRH-------VVLAVNKMDLVDYDQEV------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 326 YDVVCEEYG--------GDVQAVHVSALTGDNLMALAEAT-----IALAEILElkadpTGPVEGTviESFTDKgRGPVTT 392
Cdd:PRK05506 177 FDEIVADYRafaaklglHDVTFIPISALKGDNVVTRSARMpwyegPSLLEHLE-----TVEIASD--RNLKDF-RFPVQY 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530788299 393 AI------------IQRGTLRKG---SILVAGKSwAKVRLIFDENGKiLNEAYPSMPV 435
Cdd:PRK05506 249 VNrpnldfrgfagtVASGVVRPGdevVVLPSGKT-SRVKRIVTPDGD-LDEAFAGQAV 304
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
194-368 |
7.59e-10 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 60.94 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 194 LLKPRSPVVTVMGHVDHGKTTLLDKLreTQVAAMEVGGI---TQHIGAFLVSLPSGEKITFLDTPG-------HAAFSAM 263
Cdd:COG3596 34 LVELPPPVIALVGKTGAGKSSLINAL--FGAEVAEVGVGrpcTREIQRYRLESDGLPGLVLLDTPGlgevnerDREYREL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 264 RARGAQVtDIVVLVVAADDGVMKQTVESIQ--HAKDAEVPIILAINKCDKTD-----------ADPEKVK--KELLAYdv 328
Cdd:COG3596 112 RELLPEA-DLILWVVKADDRALATDEEFLQalRAQYPDPPVLVVLTQVDRLEperewdppynwPSPPKEQniRRALEA-- 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530788299 329 VCEEYGGDVQAVH-VSALTGD---NLMALAEATI---------ALAEILELKA 368
Cdd:COG3596 189 IAEQLGVPIDRVIpVSAAEDRtgyGLEELVDALAealpeakrsRLARLLRAKA 241
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
202-308 |
3.32e-09 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 54.93 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKL--RETQVAAMEvgGITQHIGAFLVSLpSGEKITFLDTPG-----HAAFSAMRA-RGAQVTDI 273
Cdd:pfam01926 2 VALVGRPNVGKSTLINALtgAKAIVSDYP--GTTRDPNEGRLEL-KGKQIILVDTPGliegaSEGEGLGRAfLAIIEADL 78
|
90 100 110
....*....|....*....|....*....|....*
gi 530788299 274 VVLVVAADDGVMKQTVESIQHAKDAEVPIILAINK 308
Cdd:pfam01926 79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
201-437 |
3.75e-09 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 59.72 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 201 VVTVmGHVDHGKTTLL-------DKLRETQVAAME-----VGgiTQHIG-AFLV-SLPSgEK---IT------------- 250
Cdd:COG2895 20 FITC-GSVDDGKSTLIgrllydtKSIFEDQLAALErdskkRG--TQEIDlALLTdGLQA-EReqgITidvayryfstpkr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 251 -FL--DTPGHAAFSamR--ARGAQVTDIVVLVVAADDGVMKQT-----VES---IQHakdaevpIILAINKCDKTDADPE 317
Cdd:COG2895 96 kFIiaDTPGHEQYT--RnmVTGASTADLAILLIDARKGVLEQTrrhsyIASllgIRH-------VVVAVNKMDLVDYSEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 318 ---KVKKELLAYdvvCEEYG-GDVQAVHVSALTGDNLMALAEAT--------IALAEILELKADPTG-----PVEgTVIE 380
Cdd:COG2895 167 vfeEIVADYRAF---AAKLGlEDITFIPISALKGDNVVERSENMpwydgptlLEHLETVEVAEDRNDapfrfPVQ-YVNR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530788299 381 sFTDKGRGPVTTaiIQRGTLRKG---SILVAGKSwAKVRLI--FDENgkiLNEAYPSMPVGI 437
Cdd:COG2895 243 -PNLDFRGYAGT--IASGTVRVGdevVVLPSGKT-STVKSIvtFDGD---LEEAFAGQSVTL 297
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
205-323 |
5.04e-09 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 57.89 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 205 MGHVDHGKTTL--LDKLRETqvaamevgGITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAAD 281
Cdd:cd01886 29 IGEVHGGGATMdwMEQERER--------GIT--IQSAATTCFwKDHRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAV 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530788299 282 DGVMKQTVESIQHAKDAEVPIILAINKCDKTDADPEKVKKEL 323
Cdd:cd01886 99 AGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
206-487 |
5.30e-09 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 59.16 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 206 GHVDHGKTTLLDKL-------RETQVAAME-----VGGITQHIG-AFLVS-LP----------------SGEKITFL--D 253
Cdd:PRK05124 34 GSVDDGKSTLIGRLlhdtkqiYEDQLASLHndskrHGTQGEKLDlALLVDgLQaereqgitidvayryfSTEKRKFIiaD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 254 TPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdaevpIILAINKCDKTDADP---EKVKKE 322
Cdd:PRK05124 114 TPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTrrhsfiatLLGIKH-------LVVAVNKMDLVDYSEevfERIRED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 323 LLAYdvvCEEYGG--DVQAVHVSALTGDNLMALAEAT-----IALAEILEL----KADPTGPVEGTVI------ESFtdk 385
Cdd:PRK05124 187 YLTF---AEQLPGnlDIRFVPLSALEGDNVVSQSESMpwysgPTLLEVLETvdiqRVVDAQPFRFPVQyvnrpnLDF--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 386 gRGPVTTaiIQRGTLRKGSILVA---GKSwAKVRLI--FDENgkiLNEAYPSMPVGIIGWRDLP-SAGDEILEVESEPRA 459
Cdd:PRK05124 261 -RGYAGT--LASGVVKVGDRVKVlpsGKE-SNVARIvtFDGD---LEEAFAGEAITLVLEDEIDiSRGDLLVAADEALQA 333
|
330 340 350
....*....|....*....|....*....|...
gi 530788299 460 REVIE----WRkSEQKEEKGKD-DLKIMEEKRR 487
Cdd:PRK05124 334 VQHASadvvWM-AEQPLQPGQSyDIKIAGKKTR 365
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
249-361 |
1.16e-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: 55.16 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 249 ITFLDTPG-------------HAAFSAMRarGAqvtDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDaD 315
Cdd:cd04163 53 IIFVDTPGihkpkkklgermvKAAWSALK--DV---DLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVK-D 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530788299 316 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGDNLMALAEATIALA 361
Cdd:cd04163 127 KEDLLPLLEKL----KELHPFAEIFPISALKGENVDELLEYIVEYL 168
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
207-311 |
2.53e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 57.57 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 207 HVDHGKTTLLDKL--------RET--QVAAM---EVG---GITqhIGAFLVSLP---SGEK--ITFLDTPGHAAFSAMRA 265
Cdd:PRK07560 28 HIDHGKTTLSDNLlagagmisEELagEQLALdfdEEEqarGIT--IKAANVSMVheyEGKEylINLIDTPGHVDFGGDVT 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530788299 266 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDK 311
Cdd:PRK07560 106 RAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDR 151
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
249-373 |
4.88e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 55.05 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 249 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDaD 315
Cdd:PRK00089 55 IIFVDTPGihkpkralnramnKAAWSSLKD-----VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVK-D 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530788299 316 PEKVKKELLAYdvvcEEYGGDVQAVHVSALTGDNLMALAEatiALAEILelkadPTGP 373
Cdd:PRK00089 129 KEELLPLLEEL----SELMDFAEIVPISALKGDNVDELLD---VIAKYL-----PEGP 174
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
211-356 |
2.11e-07 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 51.28 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 211 GKTTLLDKL-RETQVAAMEVGGITQ-------HIGaflvslpsGEKITFLDTPG----------HAAFSAMRARGA-QVT 271
Cdd:cd01895 14 GKSSLLNALlGEERVIVSDIAGTTRdsidvpfEYD--------GQKYTLIDTAGirkkgkvtegIEKYSVLRTLKAiERA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 272 DIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADP---EKVKKEL------LAYdvvceeyggdVQAVHV 342
Cdd:cd01895 86 DVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEktmKEFEKELrrklpfLDY----------APIVFI 155
|
170
....*....|....
gi 530788299 343 SALTGDNLMALAEA 356
Cdd:cd01895 156 SALTGQGVDKLFDA 169
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
171-364 |
3.00e-07 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 51.69 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 171 SKLKQE-----RIRENKDAVRRpgtdpallKPRSPVVTVMGHVDHGKTTLLDKL--RETQVAAMevggitqhigafL--- 240
Cdd:cd01878 16 AKLRKElekvkKQRELQRARRK--------RSGVPTVALVGYTNAGKSTLFNALtgADVLAEDQ------------Lfat 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 241 -------VSLPSGEKITFLDTPG------H---AAFSAM--RARGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDAE 299
Cdd:cd01878 76 ldpttrrIKLPGGREVLLTDTVGfirdlpHqlvEAFRSTleEVAEA---DLLLHVVdASDPDREEQieTVEEVLKELGAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530788299 300 -VPIILAINKCDKtdADPEKVKKELLAydvvceeygGDVQAVHVSALTGDNLMALAEatiALAEIL 364
Cdd:cd01878 153 dIPIILVLNKIDL--LDDEELEERLRA---------GRPDAVFISAKTGEGLDLLKE---AIEELL 204
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
204-403 |
1.34e-06 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 51.39 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 204 VMGHVDHGKTTLLDKLreTQVAAM----EVG-GITQHIG----------------AFLVSlPSGE----------KITFL 252
Cdd:PRK04000 14 MVGHVDHGKTTLVQAL--TGVWTDrhseELKrGITIRLGyadatirkcpdceepeAYTTE-PKCPncgsetellrRVSFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 253 DTPGHAAFSAMRARGAQVTDIVVLVVAADDGV-MKQTVEsiqHAKDAEV----PIILAINKCDKTdaDPEKVK------K 321
Cdd:PRK04000 91 DAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKE---HLMALDIigikNIVIVQNKIDLV--SKERALenyeqiK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 322 ELLAyDVVCEeyggDVQAVHVSALTGDNLMALAEAtIAlAEILELKADPTGPVEGTVIESFT--------DKGRGPVTTA 393
Cdd:PRK04000 166 EFVK-GTVAE----NAPIIPVSALHKVNIDALIEA-IE-EEIPTPERDLDKPPRMYVARSFDvnkpgtppEKLKGGVIGG 238
|
250
....*....|
gi 530788299 394 IIQRGTLRKG 403
Cdd:PRK04000 239 SLIQGVLKVG 248
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
246-356 |
2.67e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 50.41 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 246 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA 314
Cdd:COG1160 222 GKKYTLIDTAGirrkgkvDEGiekYSVLRTLRAiERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEK 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530788299 315 DP---EKVKKEL------LAYdvvceeyggdVQAVHVSALTG---DNLMALAEA 356
Cdd:COG1160 302 DRktrEELEKEIrrrlpfLDY----------APIVFISALTGqgvDKLLEAVDE 345
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
207-323 |
2.70e-06 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 49.52 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 207 HVDHGKTTLLDKL---------------RETQVAA----MEVG---GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAM 263
Cdd:cd04169 10 HPDAGKTTLTEKLllfggaiqeagavkaRKSRKHAtsdwMEIEkqrGIS--VTSSVMQFEyKGCVINLLDTPGHEDFSED 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530788299 264 RARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADP----EKVKKEL 323
Cdd:cd04169 88 TYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPlellDEIENEL 151
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
241-365 |
8.68e-06 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 48.93 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 241 VSLPSGEKITFLDTPG------H---AAFsamRA-----RGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDA-EVPI 302
Cdd:COG2262 241 LELPDGRPVLLTDTVGfirklpHqlvEAF---RStleevREA---DLLLHVVdASDPDFEEQieTVNEVLEELGAdDKPI 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530788299 303 ILAINKCDKTDADPEKVKKEllaydvvceeygGDVQAVHVSALTGDNLMALAEatiALAEILE 365
Cdd:COG2262 315 ILVFNKIDLLDDEELERLRA------------GYPDAVFISAKTGEGIDELLE---AIEERLP 362
|
|
| Ras_dva |
cd04147 |
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ... |
244-310 |
2.92e-05 |
|
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - dorsal-ventral anterior localization) subfamily consists of a set of proteins characterized only in Xenopus leavis, to date. In Xenopus Ras-dva expression is activated by the transcription factor Otx2 and begins during gastrulation throughout the anterior ectoderm. Ras-dva expression is inhibited in the anterior neural plate by factor Xanf1. Downregulation of Ras-dva results in head development abnormalities through the inhibition of several regulators of the anterior neural plate and folds patterning, including Otx2, BF-1, Xag2, Pax6, Slug, and Sox9. Downregulation of Ras-dva also interferes with the FGF-8a signaling within the anterior ectoderm. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.
Pssm-ID: 206714 [Multi-domain] Cd Length: 197 Bit Score: 45.60 E-value: 2.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530788299 244 PSGEKITF--LDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESI-----QHAKDAEVPIILAINKCD 310
Cdd:cd04147 42 VAGVKVTIdiLDTSGSYSFPAMRKLSIQNGDAFALVYSVDDPESFEEVKRLreeilEVKEDKFVPIVVVGNKID 115
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
272-360 |
6.54e-05 |
|
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206681 [Multi-domain] Cd Length: 157 Bit Score: 43.96 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 272 DIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDktdadpeKVKKELLAYDvvCEEYG-GDVqaVHVSALTGDNL 350
Cdd:cd01894 78 DVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID-------NIKEEEEAAE--FYSLGfGEP--IPISAEHGRGI 146
|
90
....*....|
gi 530788299 351 MALAEATIAL 360
Cdd:cd01894 147 GDLLDAILEL 156
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
200-324 |
9.84e-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: 44.23 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 200 PVVTVMGHVDHGKTTLLDKL-----RETQVAamevggITQHIGAFLVSLPSGEKITFLDTPGHAAFSAM-------RARG 267
Cdd:cd04105 1 PTVLLLGPSDSGKTALFTKLttgkvRSTVTS------IEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKlleylkaSLKA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530788299 268 aqvtdiVVLVV--AADDGVMKQTVE------SIQHAKDAEVPIILAINKCDKTDADPEKVKKELL 324
Cdd:cd04105 75 ------IVFVVdsATFQKNIRDVAEflydilTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELL 133
|
|
| RalA_RalB |
cd04139 |
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ... |
241-350 |
1.03e-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: 43.57 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 241 VSLPSGE-KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD----GVMKQTVESIQHAKDAE-VPIILAINKCDKTDa 314
Cdd:cd04139 41 VVLDGEEvQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDmesfTALAEFREQILRVKEDDnVPLLLVGNKCDLED- 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 530788299 315 dpeKVKKELLAYDVVCEEYGgdVQAVHVSALTGDNL 350
Cdd:cd04139 120 ---KRQVSVEEAANLAEQWG--VNYVETSAKTRANV 150
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
246-367 |
2.13e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 44.27 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 246 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDA 314
Cdd:PRK00093 220 GQKYTLIDTAGirrkgkvTEGvekYSVIRTLKAiERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDE 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 315 DP-EKVKKEL------LAYdvvceeyggdVQAVHVSALTGDNLMALAEATIALAEILELK 367
Cdd:PRK00093 300 KTmEEFKKELrrrlpfLDY----------APIVFISALTGQGVDKLLEAIDEAYENANRR 349
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
231-350 |
6.73e-04 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 40.96 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 231 GITQHIGAFLVslpsGEKITFLDTPG--HAAFS-AMRARGAQVTD----------IVVLVVAADDGVMKQTVESIQHAKD 297
Cdd:cd01876 33 GRTQLINFFNV----GDKFRLVDLPGygYAKVSkEVREKWGKLIEeylenrenlkGVVLLIDARHGPTPIDLEMLEFLEE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 530788299 298 AEVPIILAINKCDKtdADPEKVKKELLAYDVVCEEYGGDVQAVHVSALTGDNL 350
Cdd:cd01876 109 LGIPFLIVLTKADK--LKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGI 159
|
|
| Sar1 |
cd00879 |
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ... |
211-340 |
1.22e-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: 40.72 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 211 GKTTLLDKLRETQVAAMEVggiTQHigaflvslPSGEKITF-------LDTPGHAAfsAMRARG---AQVTDIVVLVVAA 280
Cdd:cd00879 31 GKTTLLHMLKDDRLAQHVP---TLH--------PTSEELTIgnvkfttFDLGGHEQ--ARRVWKdyfPEVDGIVFLVDAA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530788299 281 DdgvmkqtVESIQHAKD-----------AEVPIILAINKCDKTDADPEKVKKELLAYDVVCEEYGGDVQAV 340
Cdd:cd00879 98 D-------PERFQESKEeldsllndeelANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLKV 161
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
201-310 |
1.25e-03 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 42.09 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 201 VVTVMGHVDHGKTTLLDKLRETQVAAME-VGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRARGA 268
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAVVEdTPGVTRD----RVSYDaewAGTDFKLVDTGGweadvegiDSAIASQAQIAV 352
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530788299 269 QVTDIVVLVVAADDGvMKQTVESI-QHAKDAEVPIILAINKCD 310
Cdd:PRK09518 353 SLADAVVFVVDGQVG-LTSTDERIvRMLRRAGKPVVLAVNKID 394
|
|
| IF2_IF5B_II |
cd03701 |
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ... |
373-453 |
1.54e-03 |
|
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents domain II of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologue aeIF5B. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.
Pssm-ID: 293902 [Multi-domain] Cd Length: 96 Bit Score: 38.42 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 373 PVEGTVIESFTDKGRGPVTTAIIQRGTLRKGSILVAGKS----WAKVRLIFD----------ENGKILNEAYPSMPVGII 438
Cdd:cd03701 1 EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESkdviYTRIRALLDpdpleemesrKKGNKRKEVGAASGVKIL 80
|
90
....*....|....*.
gi 530788299 439 GW-RDLPSAGDEILEV 453
Cdd:cd03701 81 GFgQELPHAGDPLEVV 96
|
|
| Ras |
cd00876 |
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ... |
248-310 |
1.83e-03 |
|
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206642 [Multi-domain] Cd Length: 160 Bit Score: 39.82 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530788299 248 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAKDAE-VPIILAINKCD 310
Cdd:cd00876 48 TLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSResfeEIKNIREQILRVKDKEdVPIVLVGNKCD 115
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
272-362 |
2.27e-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: 39.40 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 272 DIVVLVVaadDGVMKQTVESIQ-HAKDAEVPIILAINKCDKTDADPEKVKKELLAydvvceeyggdvqAVHVSALTGDNL 350
Cdd:cd04164 84 DLVLLVV---DASEGLDEEDLEiLELPAKKPVIVVLNKSDLLSDAEGISELNGKP-------------IIAISAKTGEGI 147
|
90
....*....|..
gi 530788299 351 MALAEATIALAE 362
Cdd:cd04164 148 DELKEALLELAG 159
|
|
| Rhes_like |
cd04143 |
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ... |
248-361 |
3.83e-03 |
|
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.
Pssm-ID: 133343 [Multi-domain] Cd Length: 247 Bit Score: 39.73 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 248 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAK---------DAEVPIILAINKCDKtdA 314
Cdd:cd04143 49 QLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNResfeEVCRLREQILETKsclknktkeNVKIPMVICGNKADR--D 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530788299 315 DPEKVKKellayDVVCEEYGGDVQAVH--VSALTGDNLMALAEATIALA 361
Cdd:cd04143 127 FPREVQR-----DEVEQLVGGDENCAYfeVSAKKNSNLDEMFRALFSLA 170
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
202-367 |
3.84e-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: 39.07 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 202 VTVMGHVDHGKTTLLDKLRETQVAAMEVG---GITQHIGaflVSLPSGekITFLDTPGhaaFSAMRARGAQVT------- 271
Cdd:cd09912 3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTpttAVITVLR---YGLLKG--VVLVDTPG---LNSTIEHHTEITesflpra 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 272 DIVVLVVAADDGVMKQTVESIQHAKDAEVP-IILAINKCDK-TDADPEKVKKELLAYDVVCEEYGGDVQAVHVSA-LTGD 348
Cdd:cd09912 75 DAVIFVLSADQPLTESEREFLKEILKWSGKkIFFVLNKIDLlSEEELEEVLEYSREELGVLELGGGEPRIFPVSAkEALE 154
|
170
....*....|....*....
gi 530788299 349 NLMALAEATIALAEILELK 367
Cdd:cd09912 155 ARLQGDEELLEQSGFEELE 173
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
197-356 |
6.12e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.95 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 197 PRSpvVTVMGHVDHGKTTLLDKL-RETQVAAMEVGGITQHIGAFLVSLpSGEKITFLDTPG----------HAAFSAMRA 265
Cdd:PRK03003 211 PRR--VALVGKPNVGKSSLLNKLaGEERSVVDDVAGTTVDPVDSLIEL-GGKTWRFVDTAGlrrrvkqasgHEYYASLRT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 266 RGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAEVPIILAINKCDKTDADpekvKKELLAYDVvceeyggDVQAVHV-- 342
Cdd:PRK03003 288 HAAiEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNKWDLVDED----RRYYLEREI-------DRELAQVpw 356
|
170 180
....*....|....*....|
gi 530788299 343 ------SALTGDNLMALAEA 356
Cdd:PRK03003 357 aprvniSAKTGRAVDKLVPA 376
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
200-315 |
9.25e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 39.18 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530788299 200 PVVTVMGHVDHGKTTLLDKL---RETQVAamEVGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRA 265
Cdd:PRK03003 39 PVVAVVGRPNVGKSTLVNRIlgrREAVVE--DVPGVTRD----RVSYDaewNGRRFTVVDTGGwepdakglQASVAEQAE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530788299 266 RGAQVTDIVVLVV-------AADDGVMKQTVESiqhakdaEVPIILAINKCD--KTDAD 315
Cdd:PRK03003 113 VAMRTADAVLFVVdatvgatATDEAVARVLRRS-------GKPVILAANKVDdeRGEAD 164
|
|
| |
