|
Name |
Accession |
Description |
Interval |
E-value |
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
178-720 |
0e+00 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 654.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 178 PRSPVVTIMGHVDHGKTTLLDKFRKTQVAAVETGGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRARGAQVTDIVVL 257
Cdd:COG0532 2 PRPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-GGKITFLDTPGHEAFTAMRARGAQVTDIVIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 258 VVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKELLAYDVVCEDYGGDVQAVPVSALTGDNLMALAEA 337
Cdd:COG0532 81 VVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEWGGDTIFVPVSAKTGEGIDELLEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 338 TVALAEMLELKADPNGPVEGTVIESFTDKGRGLVTTAIIQRGTLRKGSVLVAGKCWAKVRLMFDENGKTIDEAYPSMPVG 417
Cdd:COG0532 161 ILLQAEVLELKANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTAYGRVRAMFDDRGKRVKEAGPSTPVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 418 ITGWRDLPSAGEEILEVESEPRAREVVDWRkyeqeqekgqedlkiiEEKRKEHKEAHQKarekyghllwkKRSILRFLER 497
Cdd:COG0532 241 ILGLSGVPQAGDEFVVVEDEKKAREIAEKR----------------QQKAREKKLARQK-----------RVSLEDLFSQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 498 keqipLKPKEKRErdsnvLSVIIKGDVDGSVEAI---LNIIDTydasHECELELVHFGVGDVSANDVNLAETFDGVIYGF 574
Cdd:COG0532 294 -----IKEGEVKE-----LNLILKADVQGSVEALkdsLEKLST----DEVKVNIIHSGVGAITESDVNLAAASNAIIIGF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 575 NVNAGNVIQQSAAKKGVKIKLHKIIYRLVEDLQEELSSRLPCAVEEHPVGEASILATFSVTegkkKVP-VAGCRVQKGQL 653
Cdd:COG0532 360 NVRPDAKARKLAEREGVDIRYYSIIYDLIDDVKAAMEGMLEPEYKEEILGRAEVREVFKVS----KVGtIAGCYVTEGKI 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53729339 654 EKQKKFKLTRNGHVIWKGSLTSLKHHKDDISIVKTGMDCGLSLDEDNmEFQVGDRIVCYEEKQIQAK 720
Cdd:COG0532 436 KRNAKVRVLRDGVVIYEGELESLKRFKDDVKEVRAGYECGIGLKNFN-DIKEGDIIEAFEMEEVKRT 501
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
97-718 |
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: 535.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 97 MTIEELARAMEKNTDYVYEALLNTDIdidSLEADSHLDEVWIKEVITKAGmklkwSKLKQDKVRKNKDAVRRPQADPALL 176
Cdd:TIGR00487 12 LTVSELANKMNIKVSDIIKKLMLLGV---MVTINQVLDKETAELVAEEFG-----VKVEVRVTLEETEAEEQDEDSGDLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 177 TPRSPVVTIMGHVDHGKTTLLDKFRKTQVAAVETGGITQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVV 256
Cdd:TIGR00487 84 VERPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHVENEDGKMITFLDTPGHEAFTSMRARGAKVTDIVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 257 LVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKELLAYDVVCEDYGGDVQAVPVSALTGDNLMALAE 336
Cdd:TIGR00487 164 LVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIFVPVSALTGDGIDELLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 337 ATVALAEMLELKADPNGPVEGTVIESFTDKGRGLVTTAIIQRGTLRKGSVLVAGKCWAKVRLMFDENGKTIDEAYPSMPV 416
Cdd:TIGR00487 244 MILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVGAAYGRVRAMIDENGKSVKEAGPSKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 417 GITGWRDLPSAGEEILEVESEPRAREVVDWRKYEQEQEKGQEDLKiieekrkehkeahqkarekyghllwkkrsiLRFLE 496
Cdd:TIGR00487 324 EILGLSDVPAAGDEFIVFKDEKDARLVAEKRAGKLRQKALSRSVK------------------------------VTLDN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 497 RKEQIplkpkekRERDSNVLSVIIKGDVDGSVEAILNIIDTYDAShECELELVHFGVGDVSANDVNLAETFDGVIYGFNV 576
Cdd:TIGR00487 374 LFEQI-------KEGELKELNIILKADVQGSLEAIKNSLEKLNNE-EVKVKVIHSGVGGITETDISLASASNAIIIGFNV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 577 NAGNVIQQSAAKKGVKIKLHKIIYRLVEDLQEELSSRLPCAVEEHPVGEASILATFSVTegkKKVPVAGCRVQKGQLEKQ 656
Cdd:TIGR00487 446 RPDATAKNVAEAENVDIRYYSVIYKLIDEIRAAMKGMLDPEYEEEIIGQAEVRQVFNVP---KIGNIAGCYVTEGVIKRG 522
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53729339 657 KKFKLTRNGHVIWKGSLTSLKHHKDDISIVKTGMDCGLSLDEDNmEFQVGDRIVCYEEKQIQ 718
Cdd:TIGR00487 523 NPLRVIRDGVVIFEGEIDSLKRFKDDVKEVSNGYECGIGIKNYN-DIKEGDIIEAFEVQEVK 583
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
71-720 |
9.63e-150 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 453.91 E-value: 9.63e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 71 TKKEEGPWKSQLSSTKSKKVVEVWIG--MTIEELARAMEKNTDYVYEALLNTDIdidSLEADSHLDEVWIKEVITKAGMK 148
Cdd:CHL00189 138 KKKKVLSSKDELIKYDNNKPKSISIHspLTIQELSTLLCIPETEIIKSLFLKGI---SVTVNQIIDISIISQVADDFGIN 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 149 LKwSKLKQDKVRKNKDaVRRPQADPALLTPRSPVVTIMGHVDHGKTTLLDKFRKTQVAAVETGGITQHIGAFLVSLP--- 225
Cdd:CHL00189 215 II-SEEKNNINEKTSN-LDNTSAFTENSINRPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGAYEVEFEykd 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 226 SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKELL 305
Cdd:CHL00189 293 ENQKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 306 AYDVVCEDYGGDVQAVPVSALTGDNLMALAEATVALAEMLELKADPNGPVEGTVIESFTDKGRGLVTTAIIQRGTLRKGS 385
Cdd:CHL00189 373 KYNLIPEKWGGDTPMIPISASQGTNIDKLLETILLLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 386 VLVAGKCWAKVRLMFDENGKTIDEAYPSMPVGITGWRDLPSAGEEILEVESEPRAREvvdwrKYEQEQEKGQEDLKIiee 465
Cdd:CHL00189 453 IIVIGTSYAKIRGMINSLGNKINLATPSSVVEIWGLSSVPATGEHFQVFNSEKEAKL-----KIIKNKENNKKDTTK--- 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 466 krkehkeahqkarekyghllwkkrsilRFLERKEQIPLKPKEKRErdsnvLSVIIKGDVDGSVEAILNIIDTYDAShECE 545
Cdd:CHL00189 525 ---------------------------RITLSTTKTINKKDNKKQ-----INLIIKTDTQGSIEAIINSISQIPQK-KVQ 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 546 LELVHFGVGDVSANDVNLAETFDGVIYGFNVNAGNVIQQSAAKKGVKIKLHKIIYRLVEDLQEELSSRLPCAVEEHPVGE 625
Cdd:CHL00189 572 LNILYASLGEVTETDVEFASTTNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLEYIEALMEDLLDPEYKKVPIGE 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 626 ASILATFSVTEGKkkvpVAGCRVQKGQLEKQKKFKLTRNGHVIWKGSLTSLKHHKDDISIVKTGMDCGLSLdEDNMEFQV 705
Cdd:CHL00189 652 AEVKTVFPLAKRF----VAGCRVTEGKITKNALIKVIRENKLIYEGKITSLKRVKEDVEEAQEGNECGIFI-EEFQLWQS 726
|
650
....*....|....*
gi 53729339 706 GDRIVCYEEKQIQAK 720
Cdd:CHL00189 727 GDKIHAFELIPKKKS 741
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
181-345 |
5.46e-97 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 296.69 E-value: 5.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 181 PVVTIMGHVDHGKTTLLDKFRKTQVAAVETGGITQHIGAFLVSLP-SGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVV 259
Cdd:cd01887 1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPIDvKIPGITFIDTPGHEAFTNMRARGASVTDIAILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 260 AADDGVMKQTVESIQHAKDAQVPIILAVNKCDK---AEADPEKVKKELLAYDVVCEDYGGDVQAVPVSALTGDNLMALAE 336
Cdd:cd01887 81 AADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSELGLVGEEWGGDVSIVPISAKTGEGIDDLLE 160
|
....*....
gi 53729339 337 ATVALAEML 345
Cdd:cd01887 161 AILLLAEVL 169
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
179-697 |
2.41e-59 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 210.81 E-value: 2.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 179 RSPVVTIMGHVDHGKTTLLDKFRKTQVAAVETGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAF 241
Cdd:PRK04004 5 RQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAgplkkplpiklkipgllFIDTPGHEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 242 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA---------------EADPEKVKKEL-- 304
Cdd:PRK04004 85 TNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIpgwkstedapflesiEKQSQRVQQELee 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 305 LAYDVVCE---------------DYGGDVQAVPVSALTG----DNLMALAeatvALAEML---ELKADPNGPVEGTVIES 362
Cdd:PRK04004 165 KLYELIGQlselgfsadrfdrvkDFTKTVAIVPVSAKTGegipDLLMVLA----GLAQRYleeRLKIDVEGPGKGTVLEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 363 FTDKGRGLVTTAIIQRGTLRKGSVLVAGkcwakvrlmfdengkTIDEAYpsmpvgITGWRDL--PSAGEEILEVESepra 440
Cdd:PRK04004 241 KEERGLGTTIDVILYDGTLRKGDTIVVG---------------GKDGPI------VTKVRALlkPRPLDEMRDPED---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 441 revvdwrKYEQ-EQEKGQEDLKIIEEK----------RKEHKEAHQKAREkyghllwkkrsilrflERKEQIplkpkEKR 509
Cdd:PRK04004 296 -------KFKPvDEVVAAAGVKISAPDledalagsplRVVRDEDVEEVKE----------------EVEEEI-----EEI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 510 ERDSNVLSVIIKGDVDGSVEAILNIIDtydashECELELVHFGVGDVSANDVNLAET------FDGVIYGFNVNAGNVIQ 583
Cdd:PRK04004 348 RIETDEEGVVVKADTLGSLEALVNELR------EEGIPIRKADVGDISKRDVIEASTvaekdpLYGVILAFNVKVLPDAE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 584 QSAAKKGVKIKLHKIIYRLVEDLQEelssrlpcAVEEhpVGEASILATFS--VTEGK-----------KKVPVAGCRVQK 650
Cdd:PRK04004 422 EEAEKSDVKIFTGDVIYQLIEDYEK--------WVKE--QKEAEKEKILEkiVRPAKirilpgyvfrqSDPAIVGVEVLG 491
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 53729339 651 GQLekQKKFKLTR-NGHVIwkGSLTSLKHHKDDISIVKTGMDCGLSLD 697
Cdd:PRK04004 492 GTI--KPGVPLIKeDGKRV--GTIKQIQDQGENVKEAKAGMEVAISID 535
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
179-608 |
1.03e-49 |
|
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: 183.86 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 179 RSPVVTIMGHVDHGKTTLLDKFRKTQVAAVETGGITQHIGA--------------FLVSLPSGEKIT---FLDTPGHAAF 241
Cdd:TIGR00491 3 RQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGAsevptdviekicgdLLKSFKIKLKIPgllFIDTPGHEAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 242 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDK-----------------AEADPEKVKKEL 304
Cdd:TIGR00491 83 TNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRipgwkshegypflesinKQEQRVRQNLDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 305 LAYDVVCE---------------DYGGDVQAVPVSALTGDNLMALAEATVALAEML---ELKADPNGPVEGTVIESFTDK 366
Cdd:TIGR00491 163 QVYNLVIQlaeqgfnaerfdrirDFTKTVAIIPVSAKTGEGIPELLAILAGLAQNYlenKLKLAIEGPAKGTILEVKEEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 367 GRGLVTTAIIQRGTLRKGSVLVAGkcwakvrlmfdengkTIDEaypsmpVGITGWRDL--PSAGEEILEVESEPRAREVV 444
Cdd:TIGR00491 243 GLGYTIDAVIYDGILRKGDIIVLA---------------GIDD------VIVTRVRAIlkPRPLQEMRLARKKFAQVDEV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 445 DWRKYEQEQEKGQEDLKIIEEKRKEHKEAHQKAREkyghllwkkrsilRFLERKEQIPLKPKEKrerdsnvlSVIIKGDV 524
Cdd:TIGR00491 302 YAAAGVKVAAPNLDTVLAGSPIVVENNEEIEKYKE-------------EIQKEVEEIKIYTDEE--------GIVVKADT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 525 DGSVEAILNII-DTYDASHECElelvhfgVGDVSANDVNLAETFD------GVIYGFNVNAGNVIQQSAAKKGVKIKLHK 597
Cdd:TIGR00491 361 LGSLEALVNELrRRGIPIKKAD-------IGDVSKRDVVEAEIVKqeakeyGAIAAFNVKPLPGAEIEAEKYDIKLFSDN 433
|
490
....*....|.
gi 53729339 598 IIYRLVEDLQE 608
Cdd:TIGR00491 434 IIYQLMENFEK 444
|
|
| IF2_mtIF2_II |
cd03702 |
Domain II of bacterial and mitochondrial Initiation Factor 2; This family represents domain II ... |
354-448 |
4.25e-40 |
|
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: 142.18 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 354 PVEGTVIESFTDKGRGLVTTAIIQRGTLRKGSVLVAGKCWAKVRLMFDENGKTIDEAYPSMPVGITGWRDLPSAGEEILE 433
Cdd:cd03702 1 LARGVVIESKLDKGRGPVATVLVQNGTLKVGDILVAGTTYGKVRAMIDDNGKRIKEAGPSTPVEILGLNGVPQAGDKFIV 80
|
90
....*....|....*
gi 53729339 434 VESEPRAREVVDWRK 448
Cdd:cd03702 81 VDSEKEAREIAEKRQ 95
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
183-337 |
7.65e-39 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 142.28 E-value: 7.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDK------------FRKTQVAAV-------ETGGITQHIGAflVSLPSGE-KITFLDTPGHAAFS 242
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRllyytgaiskrgEVKGEGEAGldnlpeeRERGITIKSAA--VSFETKDyLINLIDTPGHVDFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 243 AMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA-EADPEKVKKELlaYDVVCEDYGGD---V 318
Cdd:pfam00009 84 KEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVdGAELEEVVEEV--SRELLEKYGEDgefV 161
|
170
....*....|....*....
gi 53729339 319 QAVPVSALTGDNLMALAEA 337
Cdd:pfam00009 162 PVVPGSALKGEGVQTLLDA 180
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
194-608 |
1.18e-36 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 148.11 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 194 TTLLDKFRKTQVAAVETGGITQHIGAFLVSLPSGEKIT-----------------FLDTPGHAAFSAMRARGAQVTDIVV 256
Cdd:PRK14845 475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICgpllkllkaeikipgllFIDTPGHEAFTSLRKRGGSLADLAV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 257 LVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDK------AEADP---------EKVKKELLA--------------- 306
Cdd:PRK14845 555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLipgwniSEDEPfllnfneqdQHALTELEIklyeligklyelgfd 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 307 ---YDVVcEDYGGDVQAVPVSALTGDNLMALAEATVALAE-MLE--LKADPNGPVEGTVIESFTDKGRGLVTTAIIQRGT 380
Cdd:PRK14845 635 adrFDRV-QDFTRTVAIVPVSAKTGEGIPELLMMVAGLAQkYLEerLKLNVEGYAKGTILEVKEEKGLGTTIDAIIYDGT 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 381 LRKGSVLVAGkcwakvrlmfdengkTIDEAYpsmpvgITGWRDL--PSAGEEIleveSEPRAR-----EVVDWRKYEQEQ 453
Cdd:PRK14845 714 LRRGDTIVVG---------------GPDDVI------VTKVRALlkPKPLDEI----RDPRDKfdpvdEVTAAAGVKIAA 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 454 EKGQEDLKIIEEKRKEHKEAHQKAREkyghllwkkrsilRFLERKEQIPLKPKEKrerdsnvlSVIIKGDVDGSVEAILN 533
Cdd:PRK14845 769 PGLEEVLAGSPIRIVPTKEKIEKAKE-------------EVMKEVEEAKIETDKE--------GILIKADTLGSLEALAN 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 534 IIdtydasHECELELVHFGVGDVSANDVNLA------ETFDGVIYGFNVNAGNVIQQSAAKKGVKIKLHKIIYRLVEDLQ 607
Cdd:PRK14845 828 EL------RKAGIPIKKAEVGDITKKDVIEAlsykqeNPLYGVILGFNVKVLPEAQEEAEKYGVKIFVDNIIYKLVEDYT 901
|
.
gi 53729339 608 E 608
Cdd:PRK14845 902 E 902
|
|
| IF-2 |
pfam11987 |
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main ... |
506-607 |
1.50e-33 |
|
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main phylogenetic domains (Eukaryotes, Bacteria and Archaea). IF2 interacts with formylmethionine-tRNA, GTP, IF1, IF3 and both ribosomal subunits. Through these interactions, IF2 promotes the binding of the initiator tRNA to the A site in the smaller ribosomal subunit and catalyzes the hydrolysis of GTP following initiation-complex formation.
Pssm-ID: 463421 [Multi-domain] Cd Length: 116 Bit Score: 124.47 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 506 KEKRERDSNVLSVIIKGDVDGSVEAILNIIDTYDaSHECELELVHFGVGDVSANDVNLAETFDGVIYGFNVNAGNVIQQS 585
Cdd:pfam11987 16 FSQIKEEVKELNLIIKADVQGSLEALKESLEKLS-NDEVKVNIIHSGVGAITESDVMLASASNAIIIGFNVRPDAKARKL 94
|
90 100
....*....|....*....|..
gi 53729339 586 AAKKGVKIKLHKIIYRLVEDLQ 607
Cdd:pfam11987 95 AEKEGVDIRYYNIIYDLIDDVK 116
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
183-343 |
1.58e-32 |
|
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: 123.94 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLD---------------KFRKTQVAAVE-TGGITQHIGAFLVSLPsGEKITFLDTPGHAAFSAMRA 246
Cdd:cd00881 2 VGVIGHVDHGKTTLTGsllyqtgaidrrgtrKETFLDTLKEErERGITIKTGVVEFEWP-KRRINFIDTPGHEDFSKETV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 247 RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA-EADPEKVKKE---LLAYDVVCEDYGGDVQAVP 322
Cdd:cd00881 81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVgEEDFDEVLREikeLLKLIGFTFLKGKDVPIIP 160
|
170 180
....*....|....*....|.
gi 53729339 323 VSALTGDNLMALAEATVALAE 343
Cdd:cd00881 161 ISALTGEGIEELLDAIVEHLP 181
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
181-336 |
1.85e-27 |
|
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: 109.00 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 181 PVVTIMGHVDHGKTTLLDKFRKTQVAAVETG-GITQHIGAFLVSL-PSGEKITFLDTPGHAAFSAMR-------ARGAQV 251
Cdd:TIGR00231 2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYpGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRrlyypqvERSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 252 TDIVVLVVAADDGVMKQTVEsIQHAKDAQVPIILAVNKCDKAEADPEKVKKELLAydvvcEDYGGDVqaVPVSALTGDNL 331
Cdd:TIGR00231 82 FDIVILVLDVEEILEKQTKE-IIHHADSGVPIILVGNKIDLKDADLKTHVASEFA-----KLNGEPI--IPLSAETGKNI 153
|
....*
gi 53729339 332 MALAE 336
Cdd:TIGR00231 154 DSAFK 158
|
|
| mtIF2_IVc |
cd03692 |
C2 subdomain of domain IV in mitochondrial translation initiation factor 2; This model ... |
624-711 |
1.71e-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: 103.34 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 624 GEASILATFSVTegkKKVPVAGCRVQKGQLEKQKKFKLTRNGHVIWKGSLTSLKHHKDDISIVKTGMDCGLSLDEDNmEF 703
Cdd:cd03692 1 GEAEVRAVFKIS---KVGTIAGCYVTEGKIKRNAKVRVLRDGEVIYEGKISSLKRFKDDVKEVKKGYECGITLENFN-DI 76
|
....*...
gi 53729339 704 QVGDRIVC 711
Cdd:cd03692 77 KEGDIIEA 84
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
187-343 |
6.18e-25 |
|
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: 101.91 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 187 GHVDHGKTTL---LDKFRKTQVAAVETGGITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVTDIVVLVVAA 261
Cdd:cd04171 6 GHIDHGKTTLikaLTGIETDRLPEEKKRGITIDLGfAYL-DLPDGKRLGFIDVPGHEKFvKNMLA-GAGGIDAVLLVVAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 262 DDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEAD-PEKVKKELLAYdvvCEDYGG-DVQAVPVSALTGDNLMALAEAT 338
Cdd:cd04171 84 DEGIMPQTREHLEILELLGIKkGLVVLTKADLVDEDrLELVEEEILEL---LAGTFLaDAPIFPVSSVTGEGIEELKNYL 160
|
....*
gi 53729339 339 VALAE 343
Cdd:cd04171 161 DELAE 165
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
187-386 |
3.52e-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: 107.69 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 187 GHVDHGKTTLldkfrktqVAAVeTG------------GITQHIG-AFLvSLPSGEKITFLDTPGHAAF-SAMRArGAQVT 252
Cdd:COG3276 7 GHIDHGKTTL--------VKAL-TGidtdrlkeekkrGITIDLGfAYL-PLPDGRRLGFVDVPGHEKFiKNMLA-GAGGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 253 DIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEADP-EKVK---KELLAyDVVCEdyggDVQAVPVSALT 327
Cdd:COG3276 76 DLVLLVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADLVDEEWlELVEeeiRELLA-GTFLE----DAPIVPVSAVT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 53729339 328 GDNLMALAEATVALAEMLELKaDPNGPVEGTVIESFTDKGRGLVTTaiiqrGTLRKGSV 386
Cdd:COG3276 151 GEGIDELRAALDALAAAVPAR-DADGPFRLPIDRVFSIKGFGTVVT-----GTLLSGTV 203
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
183-328 |
2.28e-20 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 89.35 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTL------------LDKFRKTQvaaveTGGITQHIG--AFLVSLPSGE-----------KITFLDTPG 237
Cdd:cd01889 3 VGLLGHVDSGKTSLakalseiastaaFDKNPQSQ-----ERGITLDLGfsSFEVDKPKHLednenpqienyQITLVDCPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 238 HAafSAMRA--RGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCD-----KAEADPEKVKKELLayDVV 310
Cdd:cd01889 78 HA--SLIRTiiGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDlipeeERKRKIEKMKKRLQ--KTL 153
|
170
....*....|....*...
gi 53729339 311 CEDYGGDVQAVPVSALTG 328
Cdd:cd01889 154 EKTRLKDSPIIPVSAKPG 171
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
183-384 |
2.41e-20 |
|
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: 95.45 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDK-------FR-KTQVA--AVETG------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:TIGR01394 4 IAIIAHVDHGKTTLVDAllkqsgtFRaNEAVAerVMDSNdlererGIT--ILAKNTAIRyNGTKINIVDTPGHADFGGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 246 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL--LAYDVVCEDYGGDVQAVPV 323
Cdd:TIGR01394 82 ERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEVfdLFAELGADDEQLDFPIVYA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53729339 324 SALTGDNLMALAEATVALAEMLEL--------KADPNGPVEG--TVIESFTDKGRglVTTAIIQRGTLRKG 384
Cdd:TIGR01394 162 SGRAGWASLDLDDPSDNMAPLFDAivrhvpapKGDLDEPLQMlvTNLDYDEYLGR--IAIGRVHRGTVKKG 230
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
182-393 |
8.86e-20 |
|
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: 93.78 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 182 VVTIMGHVDHGKTTLLDKFrkTQVAAV-----ETGGITQHIGAFLVSLPSgEKITFLDTPGHAAFSAMRARGAQVTDIVV 256
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKAL--TGIAADrlpeeKKRGMTIDLGFAYFPLPD-YRLGFIDVPGHEKFISNAIAGGGGIDAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 257 LVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKA-EADPEKVKKELLAydvVCEDYGGDVQA--VPVSALTGDNLM 332
Cdd:TIGR00475 79 LVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVnEEEIKRTEMFMKQ---ILNSYIFLKNAkiFKTSAKTGQGIG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53729339 333 ALAEATVALAEMLELKaDPNGPVEGTVIESFTDKGRGLVTTaiiqrGTLRKGSVLVAGKCW 393
Cdd:TIGR00475 156 ELKKELKNLLESLDIK-RIQKPLRMAIDRAFKVKGAGTVVT-----GTAFSGEVKVGDNLR 210
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
187-393 |
2.36e-19 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 92.42 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 187 GHVDHGKTTLLDKFrkTQVAAV-----ETGGITQHIGAFLVSLPSGEKITFLDTPGHAAFSAMRARGAQVTDIVVLVVAA 261
Cdd:PRK10512 7 GHVDHGKTTLLQAI--TGVNADrlpeeKKRGMTIDLGYAYWPQPDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALLVVAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 262 DDGVMKQTVESIQHAKDAQVP-IILAVNKCDK-AEADPEKVKKELLAydvVCEDYG-GDVQAVPVSALTG-------DNL 331
Cdd:PRK10512 85 DDGVMAQTREHLAILQLTGNPmLTVALTKADRvDEARIAEVRRQVKA---VLREYGfAEAKLFVTAATEGrgidalrEHL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53729339 332 MALAEATVALAEMLELKADpngpvegtviESFTDKGRGLVTTaiiqrGTLRKGSVLVAGKCW 393
Cdd:PRK10512 162 LQLPEREHAAQHRFRLAID----------RAFTVKGAGLVVT-----GTALSGEVKVGDTLW 208
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
183-328 |
2.97e-19 |
|
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: 86.49 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDK-------FRKTQVAAVET---------GGITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:cd01891 5 IAIIAHVDHGKTTLVDAllkqsgtFRENEEVGERVmdsndlereRGIT--ILAKNTAITyKDTKINIIDTPGHADFGGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 246 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL--LAYDVVCEDYGGDVQAVPV 323
Cdd:cd01891 83 ERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEVfdLFLELNATDEQLDFPIVYA 162
|
....*
gi 53729339 324 SALTG 328
Cdd:cd01891 163 SAKNG 167
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
185-388 |
1.21e-17 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 86.14 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKFrktqvaAVETGGITQHI-----------G------AFLVSLPSGEK------------------ 229
Cdd:COG5256 12 VIGHVDHGKSTLVGRL------LYETGAIDEHIiekyeeeaekkGkesfkfAWVMDRLKEERergvtidlahkkfetdky 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 230 -ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEADP---EKVKKEL 304
Cdd:COG5256 86 yFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAVNYSEkryEEVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 305 ------LAYDVvcedygGDVQAVPVSALTGDNLMALAEAT-----VALAEMLELKADPNGPVEG----TVIESFTDKGRG 369
Cdd:COG5256 166 skllkmVGYKV------DKIPFIPVSAWKGDNVVKKSDNMpwyngPTLLEALDNLKEPEKPVDKplriPIQDVYSISGIG 239
|
250
....*....|....*....
gi 53729339 370 LVTTAIIQRGTLRKGSVLV 388
Cdd:COG5256 240 TVPVGRVETGVLKVGDKVV 258
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
185-337 |
1.61e-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: 80.19 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKFRKTQVAAV-ETGGITQHIGAFLVSLPSG-EKITFLDTPGHAAFSAMRARG-----AQVTDIVVL 257
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVsDVPGTTRDPDVYVKELDKGkVKLVLVDTPGLDEFGGLGREElarllLRGADLILL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 258 VVAADDGVMKQTVE--SIQHAKDAQVPIILAVNKCDKaeaDPEKVKKELLAYDVVCEDYGGDVqaVPVSALTGDNLMALA 335
Cdd:cd00882 82 VVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDL---LEEREVEELLRLEELAKILGVPV--FEVSAKTGEGVDELF 156
|
..
gi 53729339 336 EA 337
Cdd:cd00882 157 EK 158
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
185-339 |
3.30e-17 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 79.89 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKF-----------RKTQV---AAVETG-GITqhIGAFLVSLP----SGEK--ITFLDTPGHAAFSA 243
Cdd:cd01890 5 IIAHIDHGKSTLADRLleltgtvsereMKEQVldsMDLERErGIT--IKAQAVRLFykakDGEEylLNLIDTPGHVDFSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 244 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKELLaydvvcEDYGGDV-QAVP 322
Cdd:cd01890 83 EVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIE------DVLGLDAsEAIL 156
|
170
....*....|....*..
gi 53729339 323 VSALTGDNLMALAEATV 339
Cdd:cd01890 157 VSAKTGLGVEDLLEAIV 173
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
183-388 |
2.06e-16 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 82.28 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTL---------------LDKFRKtqvAAVETG-------------------GITqhIGAFLVSLPSGE 228
Cdd:PRK12317 9 LAVIGHVDHGKSTLvgrllyetgaidehiIEELRE---EAKEKGkesfkfawvmdrlkeererGVT--IDLAHKKFETDK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 229 K-ITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADD--GVMKQTVESIQHAKDAQVP-IILAVNKCDKAEADPEK---VK 301
Cdd:PRK12317 84 YyFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINqLIVAINKMDAVNYDEKRyeeVK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 302 KEL------LAYDVvcedygGDVQAVPVSALTGDNLMALAEAT-----VALAEMLELKADPNGPVEG----TVIESFTDK 366
Cdd:PRK12317 164 EEVskllkmVGYKP------DDIPFIPVSAFEGDNVVKKSENMpwyngPTLLEALDNLKPPEKPTDKplriPIQDVYSIS 237
|
250 260
....*....|....*....|..
gi 53729339 367 GRGLVTTAIIQRGTLRKGSVLV 388
Cdd:PRK12317 238 GVGTVPVGRVETGVLKVGDKVV 259
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
181-384 |
2.06e-16 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 81.91 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 181 PVVTI--MGHVDHGKTTLldkfrktqvaaveTGGITQHIGAFLVSLPSG---------EK---ITF-------------- 232
Cdd:PRK12736 11 PHVNIgtIGHVDHGKTTL-------------TAAITKVLAERGLNQAKDydsidaapeEKergITIntahveyetekrhy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 233 --LDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPEKVK------KE 303
Cdd:PRK12736 78 ahVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLVD-DEELLElvemevRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 304 LL-AYDvvcedYGGDvqAVPV------SALTGD-----NLMALAEATVALAEMLELKADPN--GPVEGTviesFTDKGRG 369
Cdd:PRK12736 157 LLsEYD-----FPGD--DIPVirgsalKALEGDpkwedAIMELMDAVDEYIPTPERDTDKPflMPVEDV----FTITGRG 225
|
250
....*....|....*
gi 53729339 370 LVTTAIIQRGTLRKG 384
Cdd:PRK12736 226 TVVTGRVERGTVKVG 240
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
178-384 |
6.74e-15 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 77.56 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 178 PRSPVVTImGHVDHGKTTL-------LDKFRKTQVAAVE---------TGGITqhIGAFLVSLPSGEK-ITFLDTPGHAA 240
Cdd:PLN03127 60 PHVNVGTI-GHVDHGKTTLtaaitkvLAEEGKAKAVAFDeidkapeekARGIT--IATAHVEYETAKRhYAHVDCPGHAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 241 FSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPEKVK------KELLAYdvvcED 313
Cdd:PLN03127 137 YVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVVD-DEELLElvemelRELLSF----YK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 314 YGGD----VQAVPVSALTGDNLMALAEATVALAEML-ELKADP----NGPVEGTVIESFTDKGRGLVTTAIIQRGTLRKG 384
Cdd:PLN03127 212 FPGDeipiIRGSALSALQGTNDEIGKNAILKLMDAVdEYIPEPvrvlDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVG 291
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
186-304 |
1.05e-14 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 77.86 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 186 MGHVDHGKTTLLDKF-----RKTQVAAVETG-------------GITqhIGAFLVSLP-SGEKITFLDTPGHAAF----- 241
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfytgAIHRIGEVEDGtttmdfmpeererGIS--ITSAATTCEwKGHKINLIDTPGHVDFtgeve 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53729339 242 SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL 304
Cdd:PRK12740 79 RALR-----VLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQL 136
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
186-384 |
1.17e-14 |
|
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: 76.34 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 186 MGHVDHGKTTLldkfrktqvaaveTGGITQhigaFLVSLPSGEKITF--------------------------------L 233
Cdd:COG0050 18 IGHVDHGKTTL-------------TAAITK----VLAKKGGAKAKAYdqidkapeekergitintshveyetekrhyahV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 234 DTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPEKVK------KELL- 305
Cdd:COG0050 81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevRELLs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 306 AYdvvceDYGGD-VQAVPVS---ALTGDNLMALAEATVALAEML-----ELKADPNGP----VEGTviesFTDKGRGLVT 372
Cdd:COG0050 160 KY-----GFPGDdTPIIRGSalkALEGDPDPEWEKKILELMDAVdsyipEPERDTDKPflmpVEDV----FSITGRGTVV 230
|
250
....*....|..
gi 53729339 373 TAIIQRGTLRKG 384
Cdd:COG0050 231 TGRVERGIIKVG 242
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
185-345 |
1.58e-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: 71.89 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKFRKTQVAAV-ETGGITQHIGAFLVSLPSGEKITFLDTPG-------HAAFSAMRARGAQVTDIVV 256
Cdd:cd00880 2 IFGRPNVGKSSLLNALLGQNVGIVsPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRADLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 257 LVVAADDGVMKQtVESIQHAKDAQVPIILAVNKCDKAEADPEkvkKELLAYDVVCEDYGGDVqaVPVSALTGDNLMALAE 336
Cdd:cd00880 82 LVVDSDLTPVEE-EAKLGLLRERGKPVLLVLNKIDLVPESEE---EELLRERKLELLPDLPV--IAVSALPGEGIDELRK 155
|
....*....
gi 53729339 337 atvALAEML 345
Cdd:cd00880 156 ---KIAELL 161
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
183-292 |
2.83e-14 |
|
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: 72.30 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF------------------RKTQVAAVETG-GITQHIGAFLVSLPSGEK----ITFLDTPGHA 239
Cdd:cd04167 3 VCIAGHLHHGKTSLLDMLieqthkrtpsvklgwkplRYTDTRKDEQErGISIKSNPISLVLEDSKGksylINIIDTPGHV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 53729339 240 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDK 292
Cdd:cd04167 83 NFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
184-384 |
3.47e-14 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 75.23 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 184 TImGHVDHGKTTLL--------DKFRKTQVA------AVETG--GIT---QHIgaflvslpsgEKIT------FLDTPGH 238
Cdd:PRK00049 17 TI-GHVDHGKTTLTaaitkvlaKKGGAEAKAydqidkAPEEKarGITintAHV----------EYETekrhyaHVDCPGH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 239 AAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPEKVK------KELLA-YDVV 310
Cdd:PRK00049 86 ADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELLElvemevRELLSkYDFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 311 cedyGGDVQAVPVSAltgdnLMALAEATVALAE--MLELKA-------DPNGPVEGTV---IES-FTDKGRGLVTTAIIQ 377
Cdd:PRK00049 165 ----GDDTPIIRGSA-----LKALEGDDDEEWEkkILELMDavdsyipTPERAIDKPFlmpIEDvFSISGRGTVVTGRVE 235
|
....*..
gi 53729339 378 RGTLRKG 384
Cdd:PRK00049 236 RGIIKVG 242
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
185-304 |
5.35e-14 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 75.47 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKF-----RKTQVAAVETG-------------GITqhIGAFLVSLP-SGEKITFLDTPGHAAF---- 241
Cdd:COG0480 14 IVAHIDAGKTTLTERIlfytgAIHRIGEVHDGntvmdwmpeeqerGIT--ITSAATTCEwKGHKINIIDTPGHVDFtgev 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53729339 242 -SAMRargaqVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL 304
Cdd:COG0480 92 eRSLR-----VLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQL 150
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
183-420 |
9.14e-14 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 74.67 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDK-------FRKTQVAAvETG----------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAM 244
Cdd:COG1217 9 IAIIAHVDHGKTTLVDAllkqsgtFRENQEVA-ERVmdsndlererGIT--ILAKNTAVRyKGVKINIVDTPGHADFGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 245 RARGAQVTDIVVLVVAADDGVMKQT--VesIQHAKDAQVPIILAVNKCDKAEADPEKVKKEllAYDVVCEDYGGDVQA-V 321
Cdd:COG1217 86 VERVLSMVDGVLLLVDAFEGPMPQTrfV--LKKALELGLKPIVVINKIDRPDARPDEVVDE--VFDLFIELGATDEQLdF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 322 PV---SALTG----------DNLMALAEATvaLAEMLELKADPNGPVegtviesftdkgRGLVTT----------AI--I 376
Cdd:COG1217 162 PVvyaSARNGwasldlddpgEDLTPLFDTI--LEHVPAPEVDPDGPL------------QMLVTNldysdyvgriAIgrI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 53729339 377 QRGTLRKG-SVLVAGKCWAKVR------LMFDENGKT-IDEAYPSMPVGITG 420
Cdd:COG1217 228 FRGTIKKGqQVALIKRDGKVEKgkitklFGFEGLERVeVEEAEAGDIVAIAG 279
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
184-334 |
1.58e-13 |
|
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: 69.92 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 184 TImGHVDHGKTTLLDKFRKTQVAAVETG----------------GITqhIGAFLVSLPSGEK-ITFLDTPGHAAF-SAMR 245
Cdd:cd01884 7 TI-GHVDHGKTTLTAAITKVLAKKGGAKakkydeidkapeekarGIT--INTAHVEYETANRhYAHVDCPGHADYiKNMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 246 ARGAQVtDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPEKVK------KELLaydvvcEDYGGDV 318
Cdd:cd01884 84 TGAAQM-DGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMVD-DEELLElvemevRELL------SKYGFDG 155
|
170
....*....|....*.
gi 53729339 319 QAVPVsaLTGDNLMAL 334
Cdd:cd01884 156 DDTPI--VRGSALKAL 169
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
183-300 |
1.65e-13 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 74.22 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF----RKT-QVAAVETG-------------GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSA 243
Cdd:PRK13351 11 IGILAHIDAGKTTLTERIlfytGKIhKMGEVEDGttvtdwmpqeqerGIT--IESAATSCDWDNhRINLIDTPGHIDFTG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 53729339 244 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKV 300
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKV 145
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
185-331 |
4.91e-12 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 65.98 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTL---------------LDKFRKtqvAAVETG-------------------GITQHIGAFLVSLPSgEKI 230
Cdd:cd01883 4 VIGHVDAGKSTLtghllyklggvdkrtIEKYEK---EAKEMGkesfkyawvldklkeererGVTIDVGLAKFETEK-YRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 231 TFLDTPGHAAF-SAMRArGAQVTDIVVLVVAADDG-------VMKQTVESIQHAKDAQVP-IILAVNKCDKAEADPEK-- 299
Cdd:cd01883 80 TIIDAPGHRDFvKNMIT-GASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKqLIVAVNKMDDVTVNWSQer 158
|
170 180 190
....*....|....*....|....*....|....*
gi 53729339 300 ---VKKELLAYDVVCEDYGGDVQAVPVSALTGDNL 331
Cdd:cd01883 159 ydeIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNL 193
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
183-304 |
1.72e-11 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 65.31 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF-RKTQV----AAVETGG---------ITQHIGAFLVSLP---SGEKITFLDTPGHAAFSAmR 245
Cdd:cd04170 2 IALVGHSGSGKTTLAEALlYATGAidrlGRVEDGNtvsdydpeeKKRKMSIETSVAPlewNGHKINLIDTPGYADFVG-E 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 246 ARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL 304
Cdd:cd04170 81 TLSAlRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAAL 140
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
230-354 |
2.98e-11 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 65.01 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 230 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKaeAD 296
Cdd:COG1159 53 IVFVDTPGihkpkrklgrrmnKAAWSALED-----VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VK 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 53729339 297 PEKVKKELLAYdvvcEDYGGDVQAVPVSALTGDNLMALAEatvALAEMLelkadPNGP 354
Cdd:COG1159 126 KEELLPLLAEY----SELLDFAEIVPISALKGDNVDELLD---EIAKLL-----PEGP 171
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
183-382 |
3.05e-11 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 66.66 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF----------RKTQVAAVETGGITQHIGAFLVSLPSGEK-----ITFLDTPGHAAFSAMRAR 247
Cdd:PRK10218 8 IAIIAHVDHGKTTLVDKLlqqsgtfdsrAETQERVMDSNDLEKERGITILAKNTAIKwndyrINIVDTPGHADFGGEVER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 248 GAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL--LAYDVVCEDYGGDVQAVPVSA 325
Cdd:PRK10218 88 VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVfdLFVNLDATDEQLDFPIVYASA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53729339 326 LTG----------DNLMALAEATVALAEMLELkaDPNGPVEGTVIESFTDKGRGLVTTAIIQRGTLR 382
Cdd:PRK10218 168 LNGiagldhedmaEDMTPLYQAIVDHVPAPDV--DLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVK 232
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
187-346 |
5.11e-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: 62.59 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 187 GHVDHGKTTLL-------DKFRKTQVAAVETGGITQHIG-----AFLV-SLP----------------SGEKITFL--DT 235
Cdd:cd04166 6 GSVDDGKSTLIgrllydsKSIFEDQLAALERSKSSGTQGekldlALLVdGLQaereqgitidvayryfSTPKRKFIiaDT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 236 PGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT-----VES---IQHakdaqvpIILAVNKCDKAEADPEkvkkellAY 307
Cdd:cd04166 86 PGHEQYTRNMVTGASTADLAILLVDARKGVLEQTrrhsyIASllgIRH-------VVVAVNKMDLVDYDEE-------VF 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 53729339 308 DVVCEDYGG--------DVQAVPVSALTGDNLMALAEATV-----ALAEMLE 346
Cdd:cd04166 152 EEIKADYLAfaaslgieDITFIPISALEGDNVVSRSENMPwykgpTLLEHLE 203
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
234-419 |
6.73e-11 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 65.72 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 234 DTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdaqvpIILAVNKCDKAEADPEKvkkell 305
Cdd:PRK05506 110 DTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTrrhsfiasLLGIRH-------VVLAVNKMDLVDYDQEV------ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 306 aYDVVCEDYG--------GDVQAVPVSALTGDNLMALAEAT--------VALAEMLELKADPNG-----PVEgTVIESFT 364
Cdd:PRK05506 177 -FDEIVADYRafaaklglHDVTFIPISALKGDNVVTRSARMpwyegpslLEHLETVEIASDRNLkdfrfPVQ-YVNRPNL 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 53729339 365 DKgRGLVTTaiIQRGTLRKG---SVLVAGKCwAKVRLMFDENGKtIDEAYPSMPVGIT 419
Cdd:PRK05506 255 DF-RGFAGT--VASGVVRPGdevVVLPSGKT-SRVKRIVTPDGD-LDEAFAGQAVTLT 307
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
179-387 |
7.12e-11 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 65.02 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 179 RSPVVTI--MGHVDHGKTTLL---------------DKFRKTQVAAVETG-GITqhIGAFLVSLPSGEK-ITFLDTPGHA 239
Cdd:PLN03126 78 KKPHVNIgtIGHVDHGKTTLTaaltmalasmggsapKKYDEIDAAPEERArGIT--INTATVEYETENRhYAHVDCPGHA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 240 AFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPE-------KVKKELLAYdvvc 311
Cdd:PLN03126 156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVD-DEEllelvelEVRELLSSY---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 312 EDYGGDVQAVPVSALT-------------GDN--------LMALAEATVALAE-MLELkadpngPVEGTVIESFTDKGRG 369
Cdd:PLN03126 231 EFPGDDIPIISGSALLalealmenpnikrGDNkwvdkiyeLMDAVDSYIPIPQrQTDL------PFLLAVEDVFSITGRG 304
|
250
....*....|....*...
gi 53729339 370 LVTTAIIQRGTLRKGSVL 387
Cdd:PLN03126 305 TVATGRVERGTVKVGETV 322
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
183-346 |
7.44e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 61.54 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKFRKTQVAAVETG---GITqhIGAFLVSLPSGE-KITFLDTPGHAAFSAMRA------RGAqvt 252
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLstnGVT--IDKKELKLDGLDvDLVIWDTPGQDEFRETRQfyarqlTGA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 253 DIVVLVVaadDGVMKQTVESI--------QHAKDAqvPIILAVNKCDkaEADPEKVKKELLAYDVVCEDYGGDVqaVPVS 324
Cdd:COG1100 81 SLYLFVV---DGTREETLQSLyelleslrRLGKKS--PIILVLNKID--LYDEEEIEDEERLKEALSEDNIVEV--VATS 151
|
170 180
....*....|....*....|....*.
gi 53729339 325 ALTGDNLM----ALAEATVALAEMLE 346
Cdd:COG1100 152 AKTGEGVEelfaALAEILRGEGDSLD 177
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
187-419 |
8.77e-11 |
|
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: 64.72 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 187 GHVDHGKTTLL------------DkfrktQVAAVET-----GgiTQHIG-AFLV-SLPSgEK---IT------------- 231
Cdd:COG2895 24 GSVDDGKSTLIgrllydtksifeD-----QLAALERdskkrG--TQEIDlALLTdGLQA-EReqgITidvayryfstpkr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 232 -FL--DTPGHAAFSamR--ARGAQVTDIVVLVVAADDGVMKQT-----VES---IQHakdaqvpIILAVNKCDKAEADPE 298
Cdd:COG2895 96 kFIiaDTPGHEQYT--RnmVTGASTADLAILLIDARKGVLEQTrrhsyIASllgIRH-------VVVAVNKMDLVDYSEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 299 kvkkellAYDVVCEDYGG--------DVQAVPVSALTGDNLMALAEAT-----VALAEMLE---LKADPNG-----PVEg 357
Cdd:COG2895 167 -------VFEEIVADYRAfaaklgleDITFIPISALKGDNVVERSENMpwydgPTLLEHLEtveVAEDRNDapfrfPVQ- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53729339 358 TVIEsFTDKGRGLVTTaiIQRGTLRKG---SVLVAGKCwAKVR--LMFDENgktIDEAYPSMPVGIT 419
Cdd:COG2895 239 YVNR-PNLDFRGYAGT--IASGTVRVGdevVVLPSGKT-STVKsiVTFDGD---LEEAFAGQSVTLT 298
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
183-305 |
8.78e-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: 62.25 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLD---------------KFRKTQVAAVE-TGGITqhIGAFLVSL--------PSGEK--ITFLDTP 236
Cdd:cd01885 3 ICIIAHVDHGKTTLSDsllasagiiseklagKARYLDTREDEqERGIT--IKSSAISLyfeyeeekMDGNDylINLIDSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53729339 237 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA----EADPEKVKKELL 305
Cdd:cd01885 81 GHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLilelKLSPEEAYQRLL 153
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
175-339 |
9.33e-11 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 63.63 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 175 LLTPRSPVVTIMGHVDHGKTTLLDKFRKTQVAAVetgGI----TQHIGAFLVSLPSGEKITFLDTPG-------HAAFSA 243
Cdd:COG3596 34 LVELPPPVIALVGKTGAGKSSLINALFGAEVAEV---GVgrpcTREIQRYRLESDGLPGLVLLDTPGlgevnerDREYRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 244 MRARGAQVtDIVVLVVAADDGVMKQTVESIQ--HAKDAQVPIILAVNKCDKAE-----------ADPEKVK--KELLAYd 308
Cdd:COG3596 111 LRELLPEA-DLILWVVKADDRALATDEEFLQalRAQYPDPPVLVVLTQVDRLEperewdppynwPSPPKEQniRRALEA- 188
|
170 180 190
....*....|....*....|....*....|....*
gi 53729339 309 vVCEDYGGDVQAV-PVSALTGD---NLMALAEATV 339
Cdd:COG3596 189 -IAEQLGVPIDRViPVSAAEDRtgyGLEELVDALA 222
|
|
| tufA |
CHL00071 |
elongation factor Tu |
184-384 |
1.58e-10 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 63.82 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 184 TImGHVDHGKTTLLDKFrkTQVAAVETGGITQHIgAFLVSLPSgEK---ITF----------------LDTPGHAAFSAM 244
Cdd:CHL00071 17 TI-GHVDHGKTTLTAAI--TMTLAAKGGAKAKKY-DEIDSAPE-EKargITIntahveyetenrhyahVDCPGHADYVKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 245 RARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEaDPE-------KVKKELLAYdvvceDYGG 316
Cdd:CHL00071 92 MITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVD-DEEllelvelEVRELLSKY-----DFPG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 317 DvqAVPVsaLTGDNLMALaEATVALAEM-----------LEL-----------KADPNGPVEGTVIESFTDKGRGLVTTA 374
Cdd:CHL00071 166 D--DIPI--VSGSALLAL-EALTENPKIkrgenkwvdkiYNLmdavdsyiptpERDTDKPFLMAIEDVFSITGRGTVATG 240
|
250
....*....|
gi 53729339 375 IIQRGTLRKG 384
Cdd:CHL00071 241 RIERGTVKVG 250
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
230-342 |
6.94e-10 |
|
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: 58.63 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 230 ITFLDTPG-------------HAAFSAMRarGAqvtDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEaD 296
Cdd:cd04163 53 IIFVDTPGihkpkkklgermvKAAWSALK--DV---DLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVK-D 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 53729339 297 PEKVKKELLAYdvvcEDYGGDVQAVPVSALTGDNLMALAEATVALA 342
Cdd:cd04163 127 KEDLLPLLEKL----KELHPFAEIFPISALKGENVDELLEYIVEYL 168
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
230-354 |
7.72e-10 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 60.45 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 230 ITFLDTPG-------------HAAFSAMRArgaqvTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEaD 296
Cdd:PRK00089 55 IIFVDTPGihkpkralnramnKAAWSSLKD-----VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVK-D 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 53729339 297 PEKVKKELLAYdvvcEDYGGDVQAVPVSALTGDNLMALAEatvALAEMLelkadPNGP 354
Cdd:PRK00089 129 KEELLPLLEEL----SELMDFAEIVPISALKGDNVDELLD---VIAKYL-----PEGP 174
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
226-347 |
2.73e-09 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 59.93 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 226 SGEKITFL--DTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQT--------VESIQHakdaqvpIILAVNKCDKAEA 295
Cdd:PRK05124 103 STEKRKFIiaDTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTrrhsfiatLLGIKH-------LVVAVNKMDLVDY 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53729339 296 DP---EKVKKELLAYdvvCEDYGG--DVQAVPVSALTGDNLMALAEAT-----VALAEMLEL 347
Cdd:PRK05124 176 SEevfERIREDYLTF---AEQLPGnlDIRFVPLSALEGDNVVSQSESMpwysgPTLLEVLET 234
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
185-304 |
2.74e-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: 58.66 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKF-----RKTQVAAVETG-------------GITqhIGAFLVSLP-SGEKITFLDTPGHAAFSAMR 245
Cdd:cd01886 4 IIAHIDAGKTTTTERIlyytgRIHKIGEVHGGgatmdwmeqererGIT--IQSAATTCFwKDHRINIIDTPGHVDFTIEV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 53729339 246 ARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKEL 304
Cdd:cd01886 82 ERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQI 140
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
183-289 |
4.99e-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: 54.55 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF--RKTQVAAVEtgGITQHIGAFLVSLpSGEKITFLDTPG-----HAAFSAMRA-RGAQVTDI 254
Cdd:pfam01926 2 VALVGRPNVGKSTLINALtgAKAIVSDYP--GTTRDPNEGRLEL-KGKQIILVDTPGliegaSEGEGLGRAfLAIIEADL 78
|
90 100 110
....*....|....*....|....*....|....*
gi 53729339 255 VVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNK 289
Cdd:pfam01926 79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
185-305 |
3.77e-08 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 56.80 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLD-----------KFRKTQVA----AVETG-GITqhIGAFLVSLP---SGEK--ITFLDTPGHAAFSA 243
Cdd:PRK07560 25 IIAHIDHGKTTLSDnllagagmiseELAGEQLAldfdEEEQArGIT--IKAANVSMVheyEGKEylINLIDTPGHVDFGG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53729339 244 MRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA----EADPEKVKKELL 305
Cdd:PRK07560 103 DVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLikelKLTPQEMQQRLL 168
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
227-337 |
4.79e-08 |
|
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: 53.21 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 227 GEKITFLDTPG----------HAAFSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEA 295
Cdd:cd01895 49 GQKYTLIDTAGirkkgkvtegIEKYSVLRTLKAiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEK 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 53729339 296 DP---EKVKKEL------LAYdvvcedyggdVQAVPVSALTGDNLMALAEA 337
Cdd:cd01895 129 DEktmKEFEKELrrklpfLDY----------APIVFISALTGQGVDKLFDA 169
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
181-418 |
7.10e-08 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 55.24 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 181 PVVTI--MGHVDHGKTTLldkfrktqVAAVeTG------------GITQHIG----------------AFLVSlPSGE-- 228
Cdd:PRK04000 8 PEVNIgmVGHVDHGKTTL--------VQAL-TGvwtdrhseelkrGITIRLGyadatirkcpdceepeAYTTE-PKCPnc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 229 --------KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGV-MKQTVE--------SIQHakdaqvpIILAVNKCD 291
Cdd:PRK04000 78 gsetellrRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEhlmaldiiGIKN-------IVIVQNKID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 292 KAeaDPEKVK------KELLAyDVVCEDyggdVQAVPVSALTGDNLMALAEatvALAEMLEL-KADPNGPVEGTVIESFT 364
Cdd:PRK04000 151 LV--SKERALenyeqiKEFVK-GTVAEN----APIIPVSALHKVNIDALIE---AIEEEIPTpERDLDKPPRMYVARSFD 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53729339 365 --------DKGRGLVTTAIIQRGTLRKGS---------VLVAGKC-W----AKVR-LMFdeNGKTIDEAYPSMPVGI 418
Cdd:PRK04000 221 vnkpgtppEKLKGGVIGGSLIQGVLKVGDeieirpgikVEEGGKTkWepitTKIVsLRA--GGEKVEEARPGGLVGV 295
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
227-337 |
1.47e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 54.26 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 227 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEA 295
Cdd:COG1160 222 GKKYTLIDTAGirrkgkvDEGiekYSVLRTLRAiERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEK 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 53729339 296 DP---EKVKKEL------LAYdvvcedyggdVQAVPVSALTG---DNLMALAEA 337
Cdd:COG1160 302 DRktrEELEKEIrrrlpfLDY----------APIVFISALTGqgvDKLLEAVDE 345
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
222-337 |
4.78e-07 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 50.92 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 222 VSLPSGEKITFLDTPG------H---AAFSAM--RARGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDA-QVPIILA 286
Cdd:cd01878 83 IKLPGGREVLLTDTVGfirdlpHqlvEAFRSTleEVAEA---DLLLHVVdASDPDREEQieTVEEVLKELGAdDIPIILV 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 53729339 287 VNKCDKaeADPEKVKKELLAydvvcedygGDVQAVPVSALTGDNLMALAEA 337
Cdd:cd01878 160 LNKIDL--LDDEELEERLRA---------GRPDAVFISAKTGEGLDLLKEA 199
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
184-322 |
1.02e-06 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 52.36 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 184 TIMGHVDHGKTTLLDKF--RKTQVAAVETG--------------GITqhIGAFLVSL------PSGEK-----ITFLDTP 236
Cdd:PTZ00416 23 SVIAHVDHGKSTLTDSLvcKAGIISSKNAGdarftdtradeqerGIT--IKSTGISLyyehdlEDGDDkqpflINLIDSP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 237 GHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA----EADPEKV----KKELLAYD 308
Cdd:PTZ00416 101 GHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAilelQLDPEEIyqnfVKTIENVN 180
|
170
....*....|....*...
gi 53729339 309 VVCEDYG----GDVQAVP 322
Cdd:PTZ00416 181 VIIATYNdelmGDVQVYP 198
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
182-296 |
1.49e-06 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 51.72 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 182 VVTIMGHVDHGKTTLLDKFRKTQVAAVE-TGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRARGA 249
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAVVEdTPGVTRD----RVSYDaewAGTDFKLVDTGGweadvegiDSAIASQAQIAV 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 53729339 250 QVTDIVVLVVAADDGvMKQTVESI-QHAKDAQVPIILAVNKCDKAEAD 296
Cdd:PRK09518 353 SLADAVVFVVDGQVG-LTSTDERIvRMLRRAGKPVVLAVNKIDDQASE 399
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
192-341 |
1.70e-06 |
|
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: 48.20 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 192 GKTTLLDKFRKTQVAAVE-TGGITQ--HIGAFLVSlpsGEKITFLDTPGHAAFS-----AMRA---RGAQVTDIVVLVVA 260
Cdd:cd01894 9 GKSTLFNRLTGRRDAIVSdTPGVTRdrKYGEAEWG---GREFILIDTGGIEPDDegiskEIREqaeIAIEEADVILFVVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 261 ADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEkvKKELLAYDVvcedygGDVqaVPVSALTGDNLMALAEATVA 340
Cdd:cd01894 86 GREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEE--AAEFYSLGF------GEP--IPISAEHGRGIGDLLDAILE 155
|
.
gi 53729339 341 L 341
Cdd:cd01894 156 L 156
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
222-346 |
3.54e-06 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 50.09 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 222 VSLPSGEKITFLDTPG------H---AAFsamRA-----RGAqvtDIVVLVV-AADDGVMKQ--TVESIQHAKDAQ-VPI 283
Cdd:COG2262 241 LELPDGRPVLLTDTVGfirklpHqlvEAF---RStleevREA---DLLLHVVdASDPDFEEQieTVNEVLEELGADdKPI 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53729339 284 ILAVNKCDKAEADPEKvkkellaydvvcEDYGGDVQAVPVSALTGDNLMALAEatvALAEMLE 346
Cdd:COG2262 315 ILVFNKIDLLDDEELE------------RLRAGYPDAVFISAKTGEGIDELLE---AIEERLP 362
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
185-304 |
9.11e-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: 47.98 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKF---------------RKTQVAAV-------ETGGITqhIGAFLVSLP-SGEKITFLDTPGHAAF 241
Cdd:cd04169 7 IISHPDAGKTTLTEKLllfggaiqeagavkaRKSRKHATsdwmeieKQRGIS--VTSSVMQFEyKGCVINLLDTPGHEDF 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 53729339 242 SAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADP----EKVKKEL 304
Cdd:cd04169 85 SEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPlellDEIENEL 151
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
192-331 |
1.04e-05 |
|
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: 46.35 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 192 GKTTLLDK-FRKTQVAAV-ETGGITQHIGAFLVslpsGEKITFLDTPG--HAAFS-AMRARGAQVTD----------IVV 256
Cdd:cd01876 11 GKSSLINAlTNRKKLARTsKTPGRTQLINFFNV----GDKFRLVDLPGygYAKVSkEVREKWGKLIEeylenrenlkGVV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53729339 257 LVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKaeADPEKVKKELLAYDVVCEDYGGDVQAVPVSALTGDNL 331
Cdd:cd01876 87 LLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADK--LKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGI 159
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
183-293 |
1.62e-05 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 48.18 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF---------------RKTQVAAVETG-GIT---------QHIGAFLVSLPSGEK------IT 231
Cdd:PLN00116 22 MSVIAHVDHGKSTLTDSLvaaagiiaqevagdvRMTDTRADEAErGITikstgislyYEMTDESLKDFKGERdgneylIN 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53729339 232 FLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKA 293
Cdd:PLN00116 102 LIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDRC 163
|
|
| Ras_dva |
cd04147 |
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ... |
183-291 |
2.46e-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: 45.98 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKF---------RKTqvaaVETggitQHIGAFLVSlpsGEKITF--LDTPGHAAFSAMRARGAQV 251
Cdd:cd04147 2 LVFMGAAGVGKTALIQRFlydtfepkhRRT----VEE----LHSKEYEVA---GVKVTIdiLDTSGSYSFPAMRKLSIQN 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 53729339 252 TDIVVLVVAADDGVMKQTVESI-----QHAKDAQVPIILAVNKCD 291
Cdd:cd04147 71 GDAFALVYSVDDPESFEEVKRLreeilEVKEDKFVPIVVVGNKID 115
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
227-336 |
4.08e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 46.58 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 227 GEKITFLDTPG-------HAA---FSAMRARGA-QVTDIVVLVVAADDGVMKQtVESI-QHAKDAQVPIILAVNKCDKAE 294
Cdd:PRK00093 220 GQKYTLIDTAGirrkgkvTEGvekYSVIRTLKAiERADVVLLVIDATEGITEQ-DLRIaGLALEAGRALVIVVNKWDLVD 298
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 53729339 295 ADP-EKVKKEL---LAYDvvceDYggdVQAVPVSALTG---DNLMALAE 336
Cdd:PRK00093 299 EKTmEEFKKELrrrLPFL----DY---APIVFISALTGqgvDKLLEAID 340
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
183-332 |
8.94e-05 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 45.51 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTL---------------LDKFRKTqvaAVETG-------------------GITQHIGAFLVSLPSGE 228
Cdd:PTZ00141 10 LVVIGHVDSGKSTTtghliykcggidkrtIEKFEKE---AAEMGkgsfkyawvldklkaererGITIDIALWKFETPKYY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 229 kITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMK-------QTVESIQHAKDAQVP-IILAVNK-----CDKAEA 295
Cdd:PTZ00141 87 -FTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKqMIVCINKmddktVNYSQE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 53729339 296 DPEKVKKELLAYdvvCEDYG---GDVQAVPVSALTGDNLM 332
Cdd:PTZ00141 166 RYDEIKKEVSAY---LKKVGynpEKVPFIPISGWQGDNMI 202
|
|
| SR_beta |
cd04105 |
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ... |
181-305 |
1.38e-04 |
|
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.
Pssm-ID: 206691 [Multi-domain] Cd Length: 202 Bit Score: 43.46 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 181 PVVTIMGHVDHGKTTLL-----DKFRKTQVAavetggITQHIGAFLVSLPSGEKITFLDTPGHAAFSAM-------RARG 248
Cdd:cd04105 1 PTVLLLGPSDSGKTALFtklttGKVRSTVTS------IEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKlleylkaSLKA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53729339 249 aqvtdiVVLVV--AADDGVMKQTVE------SIQHAKDAQVPIILAVNKCDKAEADPEKVKKELL 305
Cdd:cd04105 75 ------IVFVVdsATFQKNIRDVAEflydilTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELL 133
|
|
| IF2_IF5B_II |
cd03701 |
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ... |
354-434 |
2.59e-04 |
|
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents domain II of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologue aeIF5B. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.
Pssm-ID: 293902 [Multi-domain] Cd Length: 96 Bit Score: 40.73 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 354 PVEGTVIESFTDKGRGLVTTAIIQRGTLRKGSVLVAGKC----WAKVRLMFD----------ENGKTIDEAYPSMPVGIT 419
Cdd:cd03701 1 EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESkdviYTRIRALLDpdpleemesrKKGNKRKEVGAASGVKIL 80
|
90
....*....|....*.
gi 53729339 420 GW-RDLPSAGEEILEV 434
Cdd:cd03701 81 GFgQELPHAGDPLEVV 96
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
181-354 |
4.65e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 43.42 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 181 PVVTIMGHVDHGKTTLLDKFRKTQVAAVE-TGGITQHigafLVSLP---SGEKITFLDTPG--------HAAFSAMRARG 248
Cdd:PRK03003 39 PVVAVVGRPNVGKSTLVNRILGRREAVVEdVPGVTRD----RVSYDaewNGRRFTVVDTGGwepdakglQASVAEQAEVA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 249 AQVTDIVVLVV-------AADDGVMKQTVESiqhakdaQVPIILAVNKCD--KAEADpekvKKELLAYdvvcedygGDVQ 319
Cdd:PRK03003 115 MRTADAVLFVVdatvgatATDEAVARVLRRS-------GKPVILAANKVDdeRGEAD----AAALWSL--------GLGE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 53729339 320 AVPVSAL----TGDNLMALAEatvALAEMLELKADPNGP 354
Cdd:PRK03003 176 PHPVSALhgrgVGDLLDAVLA---ALPEVPRVGSASGGP 211
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
180-355 |
6.56e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 42.70 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 180 SPVVTIMGH--VdhGKTTLLDKFRKTQVAAVE-TGGIT--QHIG-AFLvslpSGEKITFLDTPG-----HAAFSA-MRAr 247
Cdd:COG1160 2 SPVVAIVGRpnV--GKSTLFNRLTGRRDAIVDdTPGVTrdRIYGeAEW----GGREFTLIDTGGiepddDDGLEAeIRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 248 gaQVT------DIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEAdpekvkkELLAYDVvcedYG---GDV 318
Cdd:COG1160 75 --QAElaieeaDVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKR-------EADAAEF----YSlglGEP 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 53729339 319 qaVPVSALTGDNLMALAEATVALAEMLELKADPNGPV 355
Cdd:COG1160 142 --IPISAEHGRGVGDLLDAVLELLPEEEEEEEEDDPI 176
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
180-355 |
8.47e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.34 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 180 SPVVTIMG--HVdhGKTTLLDKFRKTQVAAVE-TGGITQ--HIG-AFLvslpSGEKITFLDTPG-----HAAFSAMRArg 248
Cdd:PRK00093 1 KPVVAIVGrpNV--GKSTLFNRLTGKRDAIVAdTPGVTRdrIYGeAEW----LGREFILIDTGGiepddDGFEKQIRE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 249 aQVT------DIVVLVVAADDGVMKQTVESIQHAKDAQVPIILAVNKCDKAEADpekvkkellayDVVCEDYG---GDVq 319
Cdd:PRK00093 73 -QAElaieeaDVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEE-----------ADAYEFYSlglGEP- 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 53729339 320 aVPVSALTGDNLMALAEATVALAEMLELKADPNGPV 355
Cdd:PRK00093 140 -YPISAEHGRGIGDLLDAILEELPEEEEEDEEDEPI 174
|
|
| Rhes_like |
cd04143 |
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ... |
229-344 |
1.24e-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: 41.27 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 229 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAK---------DAQVPIILAVNKCDKAEa 295
Cdd:cd04143 49 QLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNResfeEVCRLREQILETKsclknktkeNVKIPMVICGNKADRDF- 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 53729339 296 dPEKVKKellayDVVCEDYGGDVQAV--PVSALTGDNLMALAEATVALAEM 344
Cdd:cd04143 128 -PREVQR-----DEVEQLVGGDENCAyfEVSAKKNSNLDEMFRALFSLAKL 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
395-510 |
1.56e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 395 KVRLMFDENGKTIDEAYPSMPvGITGWRDlpSAGEEILEVESEPRAREVVDWRKYEQEQEKGQEDLKIIEEKRKEHKEAH 474
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEME-QIRAEQE--EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
90 100 110
....*....|....*....|....*....|....*..
gi 53729339 475 QKAREKYGHLLWKKRSIL-RFLERKEQIPLKPKEKRE 510
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILeKELEERKQAMIEEERKRK 516
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
253-343 |
2.15e-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: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 253 DIVVLVVaadDGVMKQTVESIQ-HAKDAQVPIILAVNKCDKAEADPEKVKKELLAydvvcedyggdvqAVPVSALTGDNL 331
Cdd:cd04164 84 DLVLLVV---DASEGLDEEDLEiLELPAKKPVIVVLNKSDLLSDAEGISELNGKP-------------IIAISAKTGEGI 147
|
90
....*....|..
gi 53729339 332 MALAEATVALAE 343
Cdd:cd04164 148 DELKEALLELAG 159
|
|
| RalA_RalB |
cd04139 |
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ... |
222-331 |
2.32e-03 |
|
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: 39.33 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 222 VSLPSGE-KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDGVMKQTVESI-----QHAKDAQVPIILAVNKCDKAea 295
Cdd:cd04139 41 VVLDGEEvQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDMESFTALAEFreqilRVKEDDNVPLLLVGNKCDLE-- 118
|
90 100 110
....*....|....*....|....*....|....*.
gi 53729339 296 dpEKVKKELLAYDVVCEDYGgdVQAVPVSALTGDNL 331
Cdd:cd04139 119 --DKRQVSVEEAANLAEQWG--VNYVETSAKTRANV 150
|
|
| Ras |
pfam00071 |
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ... |
187-330 |
2.40e-03 |
|
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.
Pssm-ID: 425451 [Multi-domain] Cd Length: 162 Bit Score: 39.42 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 187 GHVdhGKTTLL-----DKFRKTQVAAVETGGITQHIGAFlvslpsGEKITF--LDTPGHAAFSAMRA---RGAQVTDIVV 256
Cdd:pfam00071 8 GGV--GKSSLLirftqNKFPEEYIPTIGVDFYTKTIEVD------GKTVKLqiWDTAGQERFRALRPlyyRGADGFLLVY 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 53729339 257 LVVAAD--DGVMKQtVESIQHAKDAQVPIILAVNKCD---KAEADPEKVKKellaydvVCEDYGgdVQAVPVSALTGDN 330
Cdd:pfam00071 80 DITSRDsfENVKKW-VEEILRHADENVPIVLVGNKCDledQRVVSTEEGEA-------LAKELG--LPFMETSAKTNEN 148
|
|
| Ras |
cd00876 |
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ... |
229-291 |
2.62e-03 |
|
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Pssm-ID: 206642 [Multi-domain] Cd Length: 160 Bit Score: 39.05 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53729339 229 KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDG----VMKQTVESIQHAKDAQ-VPIILAVNKCD 291
Cdd:cd00876 48 TLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSResfeEIKNIREQILRVKDKEdVPIVLVGNKCD 115
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
183-347 |
2.87e-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: 39.45 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKFRKTQV---AAVETGGITQHIGaflVSLPSGekITFLDTPGhaaFSAMRARGAQVT------- 252
Cdd:cd09912 3 LAVVGEFSAGKSTLLNALLGEEVlptGVTPTTAVITVLR---YGLLKG--VVLVDTPG---LNSTIEHHTEITesflpra 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 253 DIVVLVVAADDGVMKQTVESIQHAKDAQVP-IILAVNKCDKAEADPEKVKKELLAYDVVCEDYGG-DVQAVPVSALtgDN 330
Cdd:cd09912 75 DAVIFVLSADQPLTESEREFLKEILKWSGKkIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGgEPRIFPVSAK--EA 152
|
170
....*....|....*..
gi 53729339 331 LMALAEATVALAEMLEL 347
Cdd:cd09912 153 LEARLQGDEELLEQSGF 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
429-512 |
4.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 429 EEILEVESEPRAREVvdwRKYEQEqeKGQEDLKIIEEKRKEHKEAHQKAREKYGHLLWKKRSILRFLERKEQIPLKPKEK 508
Cdd:PTZ00121 1203 EAARKAEEERKAEEA---RKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
....
gi 53729339 509 RERD 512
Cdd:PTZ00121 1278 RKAD 1281
|
|
| Sar1 |
cd00879 |
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ... |
192-322 |
4.64e-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: 38.80 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 192 GKTTLLDKFRKTQVAAVETggiTQHigaflvslPSGEKITF-------LDTPGHAAfsAMRARG---AQVTDIVVLVVAA 261
Cdd:cd00879 31 GKTTLLHMLKDDRLAQHVP---TLH--------PTSEELTIgnvkfttFDLGGHEQ--ARRVWKdyfPEVDGIVFLVDAA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53729339 262 DdgvmkqtVESIQHAKD-----------AQVPIILAVNKCDKAEADPEKVKKELLAYDVVCEDYGGDVQAVP 322
Cdd:cd00879 98 D-------PERFQESKEeldsllndeelANVPILILGNKIDKPGAVSEEELREALGLYGTTTGKGGVSLKVS 162
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
192-331 |
4.94e-03 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 38.33 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 192 GKTTLLDKFRKTQVAAVETGgitqhIGAFLVSLPSGE-KITFLDTPGHAAFSAMRARGAQVTDIVVLVVAADDgvMKQTV 270
Cdd:cd00878 11 GKTTILYKLKLGEVVTTIPT-----IGFNVETVEYKNvKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSD--RERIE 83
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53729339 271 ESIQ-------HAKDAQVPIILAVNKCDKAEADPEKVKKELLAydvVCEDYGGDVQAVPVSALTGDNL 331
Cdd:cd00878 84 EAKNelhkllnEEELKGAPLLILANKQDLPGALTESELIELLG---LESIKGRRWHIQPCSAVTGDGL 148
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|
| Roc |
pfam08477 |
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ... |
192-291 |
5.32e-03 |
|
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.
Pssm-ID: 462490 [Multi-domain] Cd Length: 114 Bit Score: 37.49 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 192 GKTTLL-----DKFRKTQVAaveTGGITQHIGAFLVSLPSGEKITFL--DTPGHAAFSAMRA---RGAQvtdIVVLVVaa 261
Cdd:pfam08477 11 GKTSLLkrfvdDTFDPKYKS---TIGVDFKTKTVLENDDNGKKIKLNiwDTAGQERFRSLHPfyyRGAA---AALLVY-- 82
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90 100 110
....*....|....*....|....*....|...
gi 53729339 262 dDGVMKQTVES-IQHAKD--AQVPIILAVNKCD 291
Cdd:pfam08477 83 -DSRTFSNLKYwLRELKKyaGNSPVILVGNKID 114
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|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
185-328 |
5.55e-03 |
|
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.
Pssm-ID: 206668 [Multi-domain] Cd Length: 167 Bit Score: 38.14 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 185 IMGHVDHGKTTLLDKFR--KTQVAAVETGGITQHIGafLVSLPSGEKITFLDTPG--HAAFSAmRARGAQVTD------- 253
Cdd:cd01881 2 LVGLPNVGKSTLLSALTsaKVEIASYPFTTLEPNVG--VFEFGDGVDIQIIDLPGllDGASEG-RGLGEQILAhlyrsdl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 254 IVVLVVAADDGVM-----KQTVESIQHAKDAQV---PIILAVNKCDKAEADPEKVKKEllayDVVCEDYggdvQAVPVSA 325
Cdd:cd01881 79 ILHVIDASEDCVGdpledQKTLNEEVSGSFLFLknkPEMIVANKIDMASENNLKRLKL----DKLKRGI----PVVPTSA 150
|
...
gi 53729339 326 LTG 328
Cdd:cd01881 151 LTR 153
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
279-346 |
6.32e-03 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 39.70 E-value: 6.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 279 AQVPIILAVNKCDKAEADpEKVK--KELLAYDVVcedyggdvqavPVSALTGDNLMALAEATvalAEMLE 346
Cdd:PRK12297 273 LERPQIVVANKMDLPEAE-ENLEefKEKLGPKVF-----------PISALTGQGLDELLYAV---AELLE 327
|
|
| ARLTS1 |
cd04156 |
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ... |
183-344 |
7.86e-03 |
|
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.
Pssm-ID: 133356 [Multi-domain] Cd Length: 160 Bit Score: 37.78 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 183 VTIMGHVDHGKTTLLDKFRktqvaavetggitqhIGAFLVSLPS-GEKITFLDTPGHAAFSAMRARGAQV---------- 251
Cdd:cd04156 2 VLLLGLDSAGKSTLLYKLK---------------HAELVTTIPTvGFNVEMLQLEKHLSLTVWDVGGQEKmrtvwkcyle 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53729339 252 -TDIVVLVVAADDG-----VMKQTVESIQHAKDAQVPIILAVNKCDKAEADPEKVKKELLAYDVVCEDYGGDVQavPVSA 325
Cdd:cd04156 67 nTDGLVYVVDSSDEarldeSQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSDRDWYVQ--PCSA 144
|
170
....*....|....*....
gi 53729339 326 LTGDnlmALAEATVALAEM 344
Cdd:cd04156 145 VTGE---GLAEAFRKLASF 160
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