|
Name |
Accession |
Description |
Interval |
E-value |
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
551-1054 |
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: 956.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 551 VVRPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVPsGDRVTFLDTPGHAAFSAMRARGANVTDIVV 630
Cdd:COG0532 1 VPRPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-GGKITFLDTPGHEAFTAMRARGAQVTDIVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 631 LVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELLQHEVVVEALGGETQIIEVSAKTGLGLDSLIE 710
Cdd:COG0532 80 LVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDKPGANPDRVKQELAEHGLVPEEWGGDTIFVPVSAKTGEGIDELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 711 AILLQAEVLDLRANPDRTAEGVVIEAKLDKGRGPVATVLVKRGTLKRGDIIVAGASWGRVRALINERNEQLPEAGPSEPV 790
Cdd:COG0532 160 MILLQAEVLELKANPDRPARGTVIEAKLDKGRGPVATVLVQNGTLKVGDIVVAGTAYGRVRAMFDDRGKRVKEAGPSTPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 791 EILGLDAAPDPGEAFAVVESDARAREITEYRQRIKREKTLAPVGAISLTDMMSKLAEKKVKELQLIIKADVQGSAEAIIG 870
Cdd:COG0532 240 EILGLSGVPQAGDEFVVVEDEKKAREIAEKRQQKAREKKLARQKRVSLEDLFSQIKEGEVKELNLILKADVQGSVEALKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 871 SLEKVGNDEVRARIIHSGAGAITESDVQLAKGSNSPIIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDDIKGVLSGML 950
Cdd:COG0532 320 SLEKLSTDEVKVNIIHSGVGAITESDVNLAAASNAIIIGFNVRPDAKARKLAEREGVDIRYYSIIYDLIDDVKAAMEGML 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 951 APIQRETFLGNAEVLEVFDITKVGKVAGCRVTEGRVEKGARVRILRDNVVIQEmGVLSTLKRFKDEVNSVVVGQECGMAF 1030
Cdd:COG0532 400 EPEYKEEILGRAEVREVFKVSKVGTIAGCYVTEGKIKRNAKVRVLRDGVVIYE-GELESLKRFKDDVKEVRAGYECGIGL 478
|
490 500
....*....|....*....|....
gi 557835801 1031 NGFQDLKAGDFIECFTVEEIKRTL 1054
Cdd:COG0532 479 KNFNDIKEGDIIEAFEMEEVKRTL 502
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
469-1054 |
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: 790.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 469 VSRDVIIPDVITVQELSNRMAVRAVDIIKMLMKQGMMLKINDVIDTDTAELVATEFGHTVKRVSESDVMEGFIDAEDHDD 548
Cdd:TIGR00487 2 KPSVIVIGGTLTVSELANKMNIKVSDIIKKLMLLGVMVTINQVLDKETAELVAEEFGVKVEVRVTLEETEAEEQDEDSGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 549 DTVVRPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVPSGDRVTFLDTPGHAAFSAMRARGANVTDI 628
Cdd:TIGR00487 82 LLVERPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHVENEDGKMITFLDTPGHEAFTSMRARGAKVTDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 629 VVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELLQHEVVVEALGGETQIIEVSAKTGLGLDSL 708
Cdd:TIGR00487 162 VVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANPDRVKQELSEYGLVPEDWGGDTIFVPVSALTGDGIDEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 709 IEAILLQAEVLDLRANPDRTAEGVVIEAKLDKGRGPVATVLVKRGTLKRGDIIVAGASWGRVRALINERNEQLPEAGPSE 788
Cdd:TIGR00487 242 LDMILLQSEVEELKANPNGQASGVVIEAQLDKGRGPVATVLVQSGTLRVGDIVVVGAAYGRVRAMIDENGKSVKEAGPSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 789 PVEILGLDAAPDPGEAFAVVESDARAREITEYRQRIKREKTLAPVGAISLTDMMSKLAEKKVKELQLIIKADVQGSAEAI 868
Cdd:TIGR00487 322 PVEILGLSDVPAAGDEFIVFKDEKDARLVAEKRAGKLRQKALSRSVKVTLDNLFEQIKEGELKELNIILKADVQGSLEAI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 869 IGSLEKVGNDEVRARIIHSGAGAITESDVQLAKGSNSPIIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDDIKGVLSG 948
Cdd:TIGR00487 402 KNSLEKLNNEEVKVKVIHSGVGGITETDISLASASNAIIIGFNVRPDATAKNVAEAENVDIRYYSVIYKLIDEIRAAMKG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 949 MLAPIQRETFLGNAEVLEVFDITKVGKVAGCRVTEGRVEKGARVRILRDNVVIQEmGVLSTLKRFKDEVNSVVVGQECGM 1028
Cdd:TIGR00487 482 MLDPEYEEEIIGQAEVRQVFNVPKIGNIAGCYVTEGVIKRGNPLRVIRDGVVIFE-GEIDSLKRFKDDVKEVSNGYECGI 560
|
570 580
....*....|....*....|....*.
gi 557835801 1029 AFNGFQDLKAGDFIECFTVEEIKRTL 1054
Cdd:TIGR00487 561 GIKNYNDIKEGDIIEAFEVQEVKRTL 586
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
470-1054 |
0e+00 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 593.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 470 SRDVIIPDVITVQELSNRMAVRAVDIIKMLMKQGMMLKINDVIDTDTAELVATEFGHTVKRVSESDVMEgfIDAEDHDDD 549
Cdd:CHL00189 157 PKSISIHSPLTIQELSTLLCIPETEIIKSLFLKGISVTVNQIIDISIISQVADDFGINIISEEKNNINE--KTSNLDNTS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 550 -----TVVRPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVPSGD---RVTFLDTPGHAAFSAMRAR 621
Cdd:CHL00189 235 aftenSINRPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGAYEVEFEYKDenqKIVFLDTPGHEAFSSMRSR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 622 GANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELLQHEVVVEALGGETQIIEVSAKT 701
Cdd:CHL00189 315 GANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKWGGDTPMIPISASQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 702 GLGLDSLIEAILLQAEVLDLRANPDRTAEGVVIEAKLDKGRGPVATVLVKRGTLKRGDIIVAGASWGRVRALINERNEQL 781
Cdd:CHL00189 395 GTNIDKLLETILLLAEIEDLKADPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIGTSYAKIRGMINSLGNKI 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 782 PEAGPSEPVEILGLDAAPDPGEAFAVVESDARAReitEYRQRIKREKTLAPVGAISLTDMMSKLAEKKVKELQLIIKADV 861
Cdd:CHL00189 475 NLATPSSVVEIWGLSSVPATGEHFQVFNSEKEAK---LKIIKNKENNKKDTTKRITLSTTKTINKKDNKKQINLIIKTDT 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 862 QGSAEAIIGSLEKVGNDEVRARIIHSGAGAITESDVQLAKGSNSPIIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDD 941
Cdd:CHL00189 552 QGSIEAIINSISQIPQKKVQLNILYASLGEVTETDVEFASTTNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLEY 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 942 IKGVLSGMLAPIQRETFLGNAEVLEVFDITKvGKVAGCRVTEGRVEKGARVRILRDNVVIQEmGVLSTLKRFKDEVNSVV 1021
Cdd:CHL00189 632 IEALMEDLLDPEYKKVPIGEAEVKTVFPLAK-RFVAGCRVTEGKITKNALIKVIRENKLIYE-GKITSLKRVKEDVEEAQ 709
|
570 580 590
....*....|....*....|....*....|...
gi 557835801 1022 VGQECGMAFNGFQDLKAGDFIECFTVEEIKRTL 1054
Cdd:CHL00189 710 EGNECGIFIEEFQLWQSGDKIHAFELIPKKKSL 742
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
555-719 |
2.02e-99 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 310.17 E-value: 2.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 555 PVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVP-SGDRVTFLDTPGHAAFSAMRARGANVTDIVVLVV 633
Cdd:cd01887 1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPIDvKIPGITFIDTPGHEAFTNMRARGASVTDIAILVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 634 AADDGVMPQTIEAINHARSAKTPIIVAVNKMDK---HEANPQRVINELLQHEVVVEALGGETQIIEVSAKTGLGLDSLIE 710
Cdd:cd01887 81 AADDGVMPQTIEAINHAKAANVPIIVAINKIDKpygTEADPERVKNELSELGLVGEEWGGDVSIVPISAKTGEGIDDLLE 160
|
....*....
gi 557835801 711 AILLQAEVL 719
Cdd:cd01887 161 AILLLAEVL 169
|
|
| PRK04004 |
PRK04004 |
translation initiation factor IF-2; Validated |
552-1032 |
6.66e-71 |
|
translation initiation factor IF-2; Validated
Pssm-ID: 235195 [Multi-domain] Cd Length: 586 Bit Score: 247.40 E-value: 6.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 552 VRPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVP-----SGDRVT------------FLDTPGHAA 614
Cdd:PRK04004 4 LRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDviekiAGPLKKplpiklkipgllFIDTPGHEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 615 FSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK------HEANP---------QRVINELL 679
Cdd:PRK04004 84 FTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRipgwksTEDAPflesiekqsQRVQQELE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 680 Q--HEVVVE--ALGGETQ-------------IIEVSAKTGLGLDSLIeAIL-------LQAEvldLRANPDRTAEGVVIE 735
Cdd:PRK04004 164 EklYELIGQlsELGFSADrfdrvkdftktvaIVPVSAKTGEGIPDLL-MVLaglaqryLEER---LKIDVEGPGKGTVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 736 AKLDKGRGPVATVLVKRGTLKRGDIIVAGASWG----RVRALI-----------NERNEQLPEAGPSEPVEIlgldAAPD 800
Cdd:PRK04004 240 VKEERGLGTTIDVILYDGTLRKGDTIVVGGKDGpivtKVRALLkprpldemrdpEDKFKPVDEVVAAAGVKI----SAPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 801 PGEAFA-----VVESDararEITEYRQRIKREktlapvgaisLTDMMSKLAEKKVkelqlIIKADVQGSAEAIIGSLEKV 875
Cdd:PRK04004 316 LEDALAgsplrVVRDE----DVEEVKEEVEEE----------IEEIRIETDEEGV-----VVKADTLGSLEALVNELREE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 876 GNDEVRARIihsgaGAITESDV---QLAKGSN---SPIIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDDIKGVLSGM 949
Cdd:PRK04004 377 GIPIRKADV-----GDISKRDVieaSTVAEKDplyGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 950 lapiqREtflgnAEVLEVFD-ITKVGK---------------VAGCRVTEGRVEKGARVrILRDNvviQEMGVLSTLKRF 1013
Cdd:PRK04004 452 -----KE-----AEKEKILEkIVRPAKirilpgyvfrqsdpaIVGVEVLGGTIKPGVPL-IKEDG---KRVGTIKQIQDQ 517
|
570
....*....|....*....
gi 557835801 1014 KDEVNSVVVGQECGMAFNG 1032
Cdd:PRK04004 518 GENVKEAKAGMEVAISIDG 536
|
|
| IF-2 |
pfam11987 |
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main ... |
827-943 |
1.90e-57 |
|
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: 193.42 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 827 EKTLAPVGAISLTDMMSKLAEKkVKELQLIIKADVQGSAEAIIGSLEKVGNDEVRARIIHSGAGAITESDVQLAKGSNSP 906
Cdd:pfam11987 1 EEELAAKKKVSLEDLFSQIKEE-VKELNLIIKADVQGSLEALKESLEKLSNDEVKVNIIHSGVGAITESDVMLASASNAI 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 557835801 907 IIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDDIK 943
Cdd:pfam11987 80 IIGFNVRPDAKARKLAEKEGVDIRYYNIIYDLIDDVK 116
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
552-958 |
5.73e-51 |
|
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: 190.03 E-value: 5.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 552 VRPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVP-----SGD-------RVT-----FLDTPGHAA 614
Cdd:TIGR00491 2 LRQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGASEVPTDviekiCGDllksfkiKLKipgllFIDTPGHEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 615 FSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK------HEANP----------------- 671
Cdd:TIGR00491 82 FTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRipgwksHEGYPflesinkqeqrvrqnld 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 672 QRVINELLQ-HEVVVEA--------LGGETQIIEVSAKTGLGLDSL--IEAILLQAEVLD-LRANPDRTAEGVVIEAKLD 739
Cdd:TIGR00491 162 KQVYNLVIQlAEQGFNAerfdrirdFTKTVAIIPVSAKTGEGIPELlaILAGLAQNYLENkLKLAIEGPAKGTILEVKEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 740 KGRGPVATVLVKRGTLKRGDIIVAGASWG----RVRALINE------RNEQLPEAGPSEPVEILGLDAAPdPGE------ 803
Cdd:TIGR00491 242 QGLGYTIDAVIYDGILRKGDIIVLAGIDDvivtRVRAILKPrplqemRLARKKFAQVDEVYAAAGVKVAA-PNLdtvlag 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 804 AFAVVESDaraREITEYRQRIKREktlapVGAISLtdmmsklaekKVKELQLIIKADVQGSAEAIIGSLEKVGNDEVRAR 883
Cdd:TIGR00491 321 SPIVVENN---EEIEKYKEEIQKE-----VEEIKI----------YTDEEGIVVKADTLGSLEALVNELRRRGIPIKKAD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 884 IihsgaGAITESDV---QLAKGSN---SPIIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDDIKGVLSGMLAPIQRET 957
Cdd:TIGR00491 383 I-----GDVSKRDVveaEIVKQEAkeyGAIAAFNVKPLPGAEIEAEKYDIKLFSDNIIYQLMENFEKWIEDIEESEKRKT 457
|
.
gi 557835801 958 F 958
Cdd:TIGR00491 458 L 458
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
568-1032 |
3.62e-47 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 183.93 E-value: 3.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 568 TSLLDALRKADVATGEAGGITQHIGAYQVRVPSGDRVT-----------------FLDTPGHAAFSAMRARGANVTDIVV 630
Cdd:PRK14845 475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICgpllkllkaeikipgllFIDTPGHEAFTSLRKRGGSLADLAV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 631 LVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK------HEANP---------QRVINELLQ--HEVV--------- 684
Cdd:PRK14845 555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLipgwniSEDEPfllnfneqdQHALTELEIklYELIgklyelgfd 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 685 ------VEALGGETQIIEVSAKTGLGLDSLIEAIL-LQAEVLD--LRANPDRTAEGVVIEAKLDKGRGPVATVLVKRGTL 755
Cdd:PRK14845 635 adrfdrVQDFTRTVAIVPVSAKTGEGIPELLMMVAgLAQKYLEerLKLNVEGYAKGTILEVKEEKGLGTTIDAIIYDGTL 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 756 KRGDIIVAG----ASWGRVRALINER---------------NEQLPEAGpsepVEIlgldAAPDPGEAFA--VVESDARA 814
Cdd:PRK14845 715 RRGDTIVVGgpddVIVTKVRALLKPKpldeirdprdkfdpvDEVTAAAG----VKI----AAPGLEEVLAgsPIRIVPTK 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 815 REITEYRQRIKREKTLAPVgaisltdmmsklaekKVKELQLIIKADVQGSAEAIIGSLEKVGndevrARIIHSGAGAITE 894
Cdd:PRK14845 787 EKIEKAKEEVMKEVEEAKI---------------ETDKEGILIKADTLGSLEALANELRKAG-----IPIKKAEVGDITK 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 895 SDVQLA---KGSN---SPIIGFNVRASKQARDLAEREGVEIRYYAIIYDLIDDIKGVLSGMLAPIQRE-----TFLGNAE 963
Cdd:PRK14845 847 KDVIEAlsyKQENplyGVILGFNVKVLPEAQEEAEKYGVKIFVDNIIYKLVEDYTEWVKEEEEKKKRElfeklIKPGIIR 926
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557835801 964 VLE--VFDITKVGkVAGCRVTEGRVEKGarVRILRDNVviQEMGVLSTLKRFKDEVNSVVVGQECGMAFNG 1032
Cdd:PRK14845 927 LLPdcIFRRSNPA-IVGVEVLEGTLRVG--VTLIKEDG--MKVGTVRSIKDRGENVKEAKAGKAVAIAIEG 992
|
|
| IF2_mtIF2_II |
cd03702 |
Domain II of bacterial and mitochondrial Initiation Factor 2; This family represents domain II ... |
729-823 |
4.59e-45 |
|
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: 157.20 E-value: 4.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 729 AEGVVIEAKLDKGRGPVATVLVKRGTLKRGDIIVAGASWGRVRALINERNEQLPEAGPSEPVEILGLDAAPDPGEAFAVV 808
Cdd:cd03702 2 ARGVVIESKLDKGRGPVATVLVQNGTLKVGDILVAGTTYGKVRAMIDDNGKRIKEAGPSTPVEILGLNGVPQAGDKFIVV 81
|
90
....*....|....*
gi 557835801 809 ESDARAREITEYRQR 823
Cdd:cd03702 82 DSEKEAREIAEKRQE 96
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
557-712 |
6.89e-44 |
|
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: 157.30 E-value: 6.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATGEAG-------------------GITQHIGAyqVRVPSGDR-VTFLDTPGHAAFS 616
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLLYYTGAISKRGevkgegeagldnlpeererGITIKSAA--VSFETKDYlINLIDTPGHVDFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 617 AMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK-HEANPQRVINELLQHEVVVEALGGE-TQI 694
Cdd:pfam00009 84 KEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRvDGAELEEVVEEVSRELLEKYGEDGEfVPV 163
|
170
....*....|....*...
gi 557835801 695 IEVSAKTGLGLDSLIEAI 712
Cdd:pfam00009 164 VPGSALKGEGVQTLLDAL 181
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
557-717 |
2.29e-40 |
|
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: 147.06 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL---------------RKADVATGE-AGGITQHIGAyqVRVPSGD-RVTFLDTPGHAAFSAMR 619
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLlyqtgaidrrgtrkeTFLDTLKEErERGITIKTGV--VEFEWPKrRINFIDTPGHEDFSKET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK-HEANPQRV---INELLQHEVVVEALGGETQII 695
Cdd:cd00881 80 VRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRvGEEDFDEVlreIKELLKLIGFTFLKGKDVPII 159
|
170 180
....*....|....*....|..
gi 557835801 696 EVSAKTGLGLDSLIEAILLQAE 717
Cdd:cd00881 160 PISALTGEGIEELLDAIVEHLP 181
|
|
| mtIF2_IVc |
cd03692 |
C2 subdomain of domain IV in mitochondrial translation initiation factor 2; This model ... |
960-1044 |
2.04e-35 |
|
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: 129.15 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 960 GNAEVLEVFDITKVGKVAGCRVTEGRVEKGARVRILRDNVVIQEmGVLSTLKRFKDEVNSVVVGQECGMAFNGFQDLKAG 1039
Cdd:cd03692 1 GEAEVRAVFKISKVGTIAGCYVTEGKIKRNAKVRVLRDGEVIYE-GKISSLKRFKDDVKEVKKGYECGITLENFNDIKEG 79
|
....*
gi 557835801 1040 DFIEC 1044
Cdd:cd03692 80 DIIEA 84
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
554-713 |
3.62e-29 |
|
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: 114.39 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 554 PPVVAVMGHVDHGKTSLLDALRKADVATGEAG-GITQHIGAYQVRV-PSGDRVTFLDTPGHAAFSAMR-------ARGAN 624
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYpGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRrlyypqvERSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 625 VTDIVVLVVAADDGVMPQTIEAINHARSaKTPIIVAVNKMDKheanpqrVINELLQHEV-VVEALGGETqIIEVSAKTGL 703
Cdd:TIGR00231 81 VFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKIDL-------KDADLKTHVAsEFAKLNGEP-IIPLSAETGK 151
|
170
....*....|
gi 557835801 704 GLDSLIEAIL 713
Cdd:TIGR00231 152 NIDSAFKIVE 161
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
556-713 |
3.57e-28 |
|
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: 111.54 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 556 VVAVMGHVDHGKTSLLDALrkadvaTGEAG---------GITQHIGAYQVRVPSGDRVTFLDTPGHAAF-SAMRArGANV 625
Cdd:cd04171 1 IIGTAGHIDHGKTTLIKAL------TGIETdrlpeekkrGITIDLGFAYLDLPDGKRLGFIDVPGHEKFvKNMLA-GAGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 626 TDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKheANPQRVinELLQHEV--VVEALGGET-QIIEVSAKT 701
Cdd:cd04171 74 IDAVLLVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADL--VDEDRL--ELVEEEIleLLAGTFLADaPIFPVSSVT 149
|
170
....*....|..
gi 557835801 702 GLGLDSLIEAIL 713
Cdd:cd04171 150 GEGIEELKNYLD 161
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
558-713 |
5.45e-24 |
|
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: 99.45 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 558 AVMGHVDHGKTSLLDALRKADVA-TGEAGGITQHIGAYQVRVPSGDR-VTFLDTPGHAAFSAMRARG-----ANVTDIVV 630
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGeVSDVPGTTRDPDVYVKELDKGKVkLVLVDTPGLDEFGGLGREElarllLRGADLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 631 LVVAADDGVMPQTIEA--INHARSAKTPIIVAVNKMDKHEANPQRVINELLQhevvvEALGGETQIIEVSAKTGLGLDSL 708
Cdd:cd00882 81 LVVDSTDRESEEDAKLliLRRLRKEGIPIILVGNKIDLLEEREVEELLRLEE-----LAKILGVPVFEVSAKTGEGVDEL 155
|
....*
gi 557835801 709 IEAIL 713
Cdd:cd00882 156 FEKLI 160
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
556-773 |
5.73e-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: 108.08 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 556 VVAVMGHVDHGKTSLLDALrkadvaTGEAG---------GITQHIG-AYqVRVPSGDRVTFLDTPGHAAF-SAMRArGAN 624
Cdd:COG3276 2 IIGTAGHIDHGKTTLVKAL------TGIDTdrlkeekkrGITIDLGfAY-LPLPDGRRLGFVDVPGHEKFiKNMLA-GAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 625 VTDIVVLVVAADDGVMPQTIE--------AINHarsaktpIIVAVNKMDKheANPQRVinELLQHEvVVEALGG----ET 692
Cdd:COG3276 74 GIDLVLLVVAADEGVMPQTREhlaildllGIKR-------GIVVLTKADL--VDEEWL--ELVEEE-IRELLAGtfleDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 693 QIIEVSAKTGLGLDSLIEAILLQAEVLdlranPDRTAEGVvieAKL--D-----KGRGPVATVLVKRGTLKRGD-IIVAG 764
Cdd:COG3276 142 PIVPVSAVTGEGIDELRAALDALAAAV-----PARDADGP---FRLpiDrvfsiKGFGTVVTGTLLSGTVRVGDeLELLP 213
|
250
....*....|
gi 557835801 765 ASW-GRVRAL 773
Cdd:COG3276 214 SGKpVRVRGI 223
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
556-762 |
2.23e-23 |
|
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: 106.11 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 556 VVAVMGHVDHGKTSLLDAL---RKADVATGEAGGITQHIG-AYqvrVPSGDRV-TFLDTPGHAAFSAMRARGANVTDIVV 630
Cdd:TIGR00475 2 IIATAGHVDHGKTTLLKALtgiAADRLPEEKKRGMTIDLGfAY---FPLPDYRlGFIDVPGHEKFISNAIAGGGGIDAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 631 LVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEANPQRVINELLQHEVVVEALGGETQIIEVSAKTGLGLDSLI 709
Cdd:TIGR00475 79 LVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLKNAKIFKTSAKTGQGIGELK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 710 EAILLQAEVLD-LRAN-PDRTAegvVIEAKLDKGRGPVATVLVKRGTLKRGDIIV 762
Cdd:TIGR00475 159 KELKNLLESLDiKRIQkPLRMA---IDRAFKVKGAGTVVTGTAFSGEVKVGDNLR 210
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
557-708 |
2.64e-21 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 92.66 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATGEAG----------------GITqhIGAYQVRVPSGD-RVTFLDTPGHAAFSAMR 619
Cdd:cd01891 5 IAIIAHVDHGKTTLVDALLKQSGTFRENEevgervmdsndlererGIT--ILAKNTAITYKDtKINIIDTPGHADFGGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELlqHEVVVEALGGETQ----II 695
Cdd:cd01891 83 ERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEV--FDLFLELNATDEQldfpIV 160
|
170
....*....|...
gi 557835801 696 EVSAKTGLGLDSL 708
Cdd:cd01891 161 YASAKNGWASLNL 173
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
557-798 |
2.13e-19 |
|
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: 93.52 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKAdvatgeaGGITQHIGAYQVRV-PSGD---------------------RVTFLDTPGHAA 614
Cdd:TIGR01394 4 IAIIAHVDHGKTTLVDALLKQ-------SGTFRANEAVAERVmDSNDlerergitilakntairyngtKINIVDTPGHAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 615 FSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELlqHEVVVEALGGETQ- 693
Cdd:TIGR01394 77 FGGEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDRPSARPDEVVDEV--FDLFAELGADDEQl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 694 ---IIEVSAKTGLG----------LDSLIEAILlqAEVLDLRANPDRTAEGVVIEAKLDKGRGPVATVLVKRGTLKRG-D 759
Cdd:TIGR01394 155 dfpIVYASGRAGWAsldlddpsdnMAPLFDAIV--RHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGqQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 557835801 760 IIVAGAS----WGRVRALIN----ERNEqLPEAGPSEPVEILGLDAA 798
Cdd:TIGR01394 233 VALMKRDgtieNGRISKLLGfeglERVE-IDEAGAGDIVAVAGLEDI 278
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
558-716 |
4.13e-19 |
|
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: 85.38 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 558 AVMGHVDHGKTSLLDALRKADVA-TGEAGGITQHIGAYQVRVPSGDRVTFLDTPG-------HAAFSAMRARGANVTDIV 629
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNVGiVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 630 VLVVAADdgvMPQTIEAINH--ARSAKTPIIVAVNKMDKHEANPQRVINELLqhevvVEALGGETQIIEVSAKTGLGLDS 707
Cdd:cd00880 81 LLVVDSD---LTPVEEEAKLglLRERGKPVLLVLNKIDLVPESEEEELLRER-----KLELLPDLPVIAVSALPGEGIDE 152
|
....*....
gi 557835801 708 LIEAILLQA 716
Cdd:cd00880 153 LRKKIAELL 161
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
557-712 |
6.64e-19 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 85.88 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALrkADVATGEA---------GGITQHIG--AYQVRVPSGD-----------RVTFLDTPGHAa 614
Cdd:cd01889 3 VGLLGHVDSGKTSLAKAL--SEIASTAAfdknpqsqeRGITLDLGfsSFEVDKPKHLednenpqienyQITLVDCPGHA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 615 fSAMRA--RGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK-HEANPQRVINELLQ--HEVVVEALG 689
Cdd:cd01889 80 -SLIRTiiGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLiPEEERKRKIEKMKKrlQKTLEKTRL 158
|
170 180
....*....|....*....|...
gi 557835801 690 GETQIIEVSAKTGLGLDSLIEAI 712
Cdd:cd01889 159 KDSPIIPVSAKPGEGEAELGGEL 181
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
558-712 |
1.44e-16 |
|
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: 78.73 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 558 AVMGHVDHGKTSLLDALRKADVATGEAG---------------GITqhIGAYQVRVP--SGDRVTFL----DTPGHAAFS 616
Cdd:cd01890 4 SIIAHIDHGKSTLADRLLELTGTVSEREmkeqvldsmdlererGIT--IKAQAVRLFykAKDGEEYLlnliDTPGHVDFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 617 AMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELlqhevvVEALGGET-QII 695
Cdd:cd01890 82 YEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEI------EDVLGLDAsEAI 155
|
170
....*....|....*..
gi 557835801 696 EVSAKTGLGLDSLIEAI 712
Cdd:cd01890 156 LVSAKTGLGVEDLLEAI 172
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
557-678 |
4.42e-16 |
|
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: 83.17 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL--------RKADVATGEA----------GGITQHIGAYQVRVpSGDRVTFLDTPGHAAF--- 615
Cdd:COG0480 12 IGIVAHIDAGKTTLTERIlfytgaihRIGEVHDGNTvmdwmpeeqeRGITITSAATTCEW-KGHKINIIDTPGHVDFtge 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 616 --SAMRarganVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINEL 678
Cdd:COG0480 91 veRSLR-----VLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQL 150
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
557-684 |
6.02e-16 |
|
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: 79.17 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATGEAGGI-------------TQHIGAYQVRVPS----GDRVTFLDTPGHAAFSAmR 619
Cdd:cd04170 2 IALVGHSGSGKTTLAEALLYATGAIDRLGRVedgntvsdydpeeKKRKMSIETSVAPlewnGHKINLIDTPGYADFVG-E 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557835801 620 ARGA-NVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINEL---LQHEVV 684
Cdd:cd04170 81 TLSAlRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALreaFGRPVV 149
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
557-786 |
6.10e-16 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 81.51 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSL---------------LDALRKADVATGEAG----------------GITQHIGAYQVRVPSGDrVT 605
Cdd:PRK12317 9 LAVIGHVDHGKSTLvgrllyetgaidehiIEELREEAKEKGKESfkfawvmdrlkeererGVTIDLAHKKFETDKYY-FT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 606 FLDTPGHAAFSAMRARGANVTDIVVLVVAADD--GVMPQTIEainHARSAKT----PIIVAVNKMDKHEANPQR---VIN 676
Cdd:PRK12317 88 IVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTRE---HVFLARTlginQLIVAINKMDAVNYDEKRyeeVKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 677 ELLQhevVVEALG---GETQIIEVSAKTGlglDSLIEA----------ILLqaEVLDLRANPDRTaegvvIEAKLdkgRG 743
Cdd:PRK12317 165 EVSK---LLKMVGykpDDIPFIPVSAFEG---DNVVKKsenmpwyngpTLL--EALDNLKPPEKP-----TDKPL---RI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 557835801 744 P---------VATVLVKR---GTLKRGDIIV---AGASwGRVRAlINERNEQLPEAGP 786
Cdd:PRK12317 229 PiqdvysisgVGTVPVGRvetGVLKVGDKVVfmpAGVV-GEVKS-IEMHHEELPQAEP 284
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
557-786 |
9.03e-16 |
|
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: 80.75 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSL---------------LDALRKADVATGEAG----------------GITQHIGAYQVRVPSGDrVT 605
Cdd:COG5256 10 LVVIGHVDHGKSTLvgrllyetgaidehiIEKYEEEAEKKGKESfkfawvmdrlkeererGVTIDLAHKKFETDKYY-FT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 606 FLDTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEainHARSAKT----PIIVAVNKMDKHEANPQR---VINEL 678
Cdd:COG5256 89 IIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTRE---HAFLARTlginQLIVAVNKMDAVNYSEKRyeeVKEEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 679 LQhevVVEALG---GETQIIEVSAKTGlglDSLIEA----------ILLQAevLDLRANPDRTaegvvIEAKLdkgRGP- 744
Cdd:COG5256 166 SK---LLKMVGykvDKIPFIPVSAWKG---DNVVKKsdnmpwyngpTLLEA--LDNLKEPEKP-----VDKPL---RIPi 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 557835801 745 --------VATVLVKR---GTLKRGDIIV---AGASwGRVRAlINERNEQLPEAGP 786
Cdd:COG5256 230 qdvysisgIGTVPVGRvetGVLKVGDKVVfmpAGVV-GEVKS-IEMHHEELEQAEP 283
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
556-773 |
1.33e-15 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 81.25 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 556 VVAVMGHVDHGKTSLLDALRKADVA---TGEAGGITQHIG-AYQVRvPSGDRVTFLDTPGHAAFSAMRARGANVTDIVVL 631
Cdd:PRK10512 2 IIATAGHVDHGKTTLLQAITGVNADrlpEEKKRGMTIDLGyAYWPQ-PDGRVLGFIDVPGHEKFLSNMLAGVGGIDHALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 632 VVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKheANPQRVINELLQHEVVVEALG-GETQIIEVSAKTGLGLDSLI 709
Cdd:PRK10512 81 VVACDDGVMAQTREHLAILQLTGNPmLTVALTKADR--VDEARIAEVRRQVKAVLREYGfAEAKLFVTAATEGRGIDALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 557835801 710 EAILLQAEVLDlraNPDRTAEGVVIEAKLDKGRGPVATVLVKRGTLKRGDII-VAGASWG-RVRAL 773
Cdd:PRK10512 159 EHLLQLPEREH---AAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLwLTGVNKPmRVRGL 221
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
557-796 |
1.42e-15 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 81.22 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKAdvatgeAG----------------------GITqhIGAYQVRVPSGD-RVTFLDTPGHA 613
Cdd:COG1217 9 IAIIAHVDHGKTTLVDALLKQ------SGtfrenqevaervmdsndlererGIT--ILAKNTAVRYKGvKINIVDTPGHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 614 AFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELLqhEVVVEaLGG-ET 692
Cdd:COG1217 81 DFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDARPDEVVDEVF--DLFIE-LGAtDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 693 Q----IIEVSAKTGL----------GLDSLIEAIL-------------LQAEVLDLRANPdrtaegvvieaklDKGRgpV 745
Cdd:COG1217 158 QldfpVVYASARNGWasldlddpgeDLTPLFDTILehvpapevdpdgpLQMLVTNLDYSD-------------YVGR--I 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 746 ATVLVKRGTLKRGD-IIVAGASWGRVRALIN--------ERNEqLPEAGPSEPVEILGLD 796
Cdd:COG1217 223 AIGRIFRGTIKKGQqVALIKRDGKVEKGKITklfgfeglERVE-VEEAEAGDIVAIAGIE 281
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
557-742 |
1.83e-15 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 81.15 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL--------RKADVATGEA----------GGITqhIGAYQVRVPSGD-RVTFLDTPGHAAFSA 617
Cdd:PRK13351 11 IGILAHIDAGKTTLTERIlfytgkihKMGEVEDGTTvtdwmpqeqeRGIT--IESAATSCDWDNhRINLIDTPGHIDFTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 618 MRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELlqhevvVEALGGETQIIEV 697
Cdd:PRK13351 89 EVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDI------EERFGKRPLPLQL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 557835801 698 SAKTGLGLDSLIEAILLQAEVLDLRANPDRTAEGVVIEAKLDKGR 742
Cdd:PRK13351 163 PIGSEDGFEGVVDLITEPELHFSEGDGGSTVEEGPIPEELLEEVE 207
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
557-759 |
3.66e-15 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 78.83 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRK--ADVATGEAG--------------GITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:PRK12736 15 IGTIGHVDHGKTTLTAAITKvlAERGLNQAKdydsidaapeekerGIT--INTAHVEYETEKRhYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEaNPQRVinELLQHEvVVEAL------GGET 692
Cdd:PRK12736 93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPyLVVFLNKVDLVD-DEELL--ELVEME-VRELLseydfpGDDI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557835801 693 QIIEVSAKTGL-GLDSLIEAIL-LQAEVLDLRANPDRTAEGVVIEAKLD----KGRGPVATVLVKRGTLKRGD 759
Cdd:PRK12736 169 PVIRGSALKALeGDPKWEDAIMeLMDAVDEYIPTPERDTDKPFLMPVEDvftiTGRGTVVTGRVERGTVKVGD 241
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
560-685 |
3.70e-15 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 80.17 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 560 MGHVDHGKTSLLDAL--------RKADVATGEAG----------GITQHIGAYQVRVpSGDRVTFLDTPGHAAFSAMRAR 621
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfytgaihRIGEVEDGTTTmdfmpeererGISITSAATTCEW-KGHKINLIDTPGHVDFTGEVER 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557835801 622 GANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINEL---LQHEVVV 685
Cdd:PRK12740 80 ALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLqekLGAPVVP 146
|
|
| IF2_N |
pfam04760 |
Translation initiation factor IF-2, N-terminal region; This conserved feature at the ... |
476-527 |
5.67e-15 |
|
Translation initiation factor IF-2, N-terminal region; This conserved feature at the N-terminus of bacterial translation initiation factor IF2 has recently had its structure solved. It shows structural similarity to the tRNA anticodon Stem Contact Fold domains of the methionyl-tRNA and glutaminyl-tRNA synthetases, and a similar fold is also found in the B5 domain of the phenylalanine-tRNA synthetase.
Pssm-ID: 428110 [Multi-domain] Cd Length: 52 Bit Score: 69.80 E-value: 5.67e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 557835801 476 PDVITVQELSNRMAVRAVDIIKMLMKQGMMLKINDVIDTDTAELVATEFGHT 527
Cdd:pfam04760 1 MEKIRVYELAKELGVSSKELIKKLFKLGIMKSHNSTLDEETAELLAEEFGVE 52
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
557-759 |
5.84e-15 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 78.28 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKA---------------DVATGE-AGGITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:TIGR00485 15 VGTIGHVDHGKTTLTAAITTVlakeggaaaraydqiDNAPEEkARGIT--INTAHVEYETETRhYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKheANPQRVInELLQHEvVVEAL------GGET 692
Cdd:TIGR00485 93 ITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDM--VDDEELL-ELVEME-VRELLsqydfpGDDT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557835801 693 QIIEVSAKTGL-GLDSLIEAIL-LQAEVLDLRANPDRTAEGVVIEAKLD----KGRGPVATVLVKRGTLKRGD 759
Cdd:TIGR00485 169 PIIRGSALKALeGDAEWEAKILeLMDAVDEYIPTPEREIDKPFLLPIEDvfsiTGRGTVVTGRVERGIIKVGE 241
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
557-719 |
9.39e-15 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 73.48 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATGEAGGiTQHIGAYQVRVP-SGDRVTFL--DTPGHAAFSAMRA------RGAnvtD 627
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLS-TNGVTIDKKELKlDGLDVDLViwDTPGQDEFRETRQfyarqlTGA---S 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 628 IVVLVVaadDGVMPQTIEAINHARSA------KTPIIVAVNKMDKHEA----NPQRVINELLQHEVVvealggetQIIEV 697
Cdd:COG1100 82 LYLFVV---DGTREETLQSLYELLESlrrlgkKSPIILVLNKIDLYDEeeieDEERLKEALSEDNIV--------EVVAT 150
|
170 180
....*....|....*....|..
gi 557835801 698 SAKTGLGLDSLIEAIllqAEVL 719
Cdd:COG1100 151 SAKTGEGVEELFAAL---AEIL 169
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
557-665 |
3.14e-14 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 72.23 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKA---------------DVATGE-AGGITqhIGAYQVRVPSGDRV-TFLDTPGHAAFSAMR 619
Cdd:cd01884 5 VGTIGHVDHGKTTLTAAITKVlakkggakakkydeiDKAPEEkARGIT--INTAHVEYETANRHyAHVDCPGHADYIKNM 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMD 665
Cdd:cd01884 83 ITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKAD 129
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
557-666 |
3.61e-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: 72.69 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL-RKADVATGEAGGITQHIGAYQVRVPSGDR----------------------VTFLDTPGHA 613
Cdd:cd04167 3 VCIAGHLHHGKTSLLDMLiEQTHKRTPSVKLGWKPLRYTDTRKDEQERgisiksnpislvledskgksylINIIDTPGHV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 557835801 614 AFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK 666
Cdd:cd04167 83 NFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
553-713 |
6.62e-14 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 74.03 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 553 RPPVVAVMGHVDHGKTSLLDALRKADVA-TGEAGGITQHIGAYQVRVPSGDRVTFLDTPG-------HAAFSAMRARGAN 624
Cdd:COG3596 38 PPPVIALVGKTGAGKSSLINALFGAEVAeVGVGRPCTREIQRYRLESDGLPGLVLLDTPGlgevnerDREYRELRELLPE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 625 VtDIVVLVVAADDGVMPQTIEAIN--HARSAKTPIIVAVNKMDK----HEANPQRV---------INELLqhEVVVEALG 689
Cdd:COG3596 118 A-DLILWVVKADDRALATDEEFLQalRAQYPDPPVLVVLTQVDRlepeREWDPPYNwpsppkeqnIRRAL--EAIAEQLG 194
|
170 180
....*....|....*....|....*...
gi 557835801 690 G-ETQIIEVSAK---TGLGLDSLIEAIL 713
Cdd:COG3596 195 VpIDRVIPVSAAedrTGYGLEELVDALA 222
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
557-759 |
1.38e-13 |
|
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: 74.03 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKA---------------DVATGEAG-GITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:COG0050 15 IGTIGHVDHGKTTLTAAITKVlakkggakakaydqiDKAPEEKErGIT--INTSHVEYETEKRhYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEaNPQRVinELLQHEvVVEAL------GGET 692
Cdd:COG0050 93 ITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELL--ELVEME-VRELLskygfpGDDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 693 QIIEVSAKTGLGLDSL---IEAILLQAEVLDLRA-NPDRtaegvvieaKLDK-------------GRGPVATVLVKRGTL 755
Cdd:COG0050 169 PIIRGSALKALEGDPDpewEKKILELMDAVDSYIpEPER---------DTDKpflmpvedvfsitGRGTVVTGRVERGII 239
|
....
gi 557835801 756 KRGD 759
Cdd:COG0050 240 KVGD 243
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
557-663 |
1.84e-13 |
|
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: 67.64 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRvPSGDRVTFLDTPG-----HAAFSAMRARGANV-TDIVV 630
Cdd:pfam01926 2 VALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLE-LKGKQIILVDTPGliegaSEGEGLGRAFLAIIeADLIL 80
|
90 100 110
....*....|....*....|....*....|...
gi 557835801 631 LVVAADDGVMPQTIEAINHARSAKTPIIVAVNK 663
Cdd:pfam01926 81 FVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
557-759 |
2.12e-13 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 73.71 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATG----------------EAGGITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:PLN03127 64 VGTIGHVDHGKTTLTAAITKVLAEEGkakavafdeidkapeeKARGIT--IATAHVEYETAKRhYAHVDCPGHADYVKNM 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEaNPQRVinELLQHEvVVEAL------GGET 692
Cdd:PLN03127 142 ITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPsLVVFLNKVDVVD-DEELL--ELVEME-LRELLsfykfpGDEI 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 693 QIIEVSAKTGL-GLDSLI--EAIL-LQAEVLDLRANPDRTAEGVVIEAKLD----KGRGPVATVLVKRGTLKRGD 759
Cdd:PLN03127 218 PIIRGSALSALqGTNDEIgkNAILkLMDAVDEYIPEPVRVLDKPFLMPIEDvfsiQGRGTVATGRVEQGTIKVGE 292
|
|
| tufA |
CHL00071 |
elongation factor Tu |
557-761 |
4.77e-13 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 72.30 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKA---------------DVATGE-AGGITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:CHL00071 15 IGTIGHVDHGKTTLTAAITMTlaakggakakkydeiDSAPEEkARGIT--INTAHVEYETENRhYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEANPqrvINELLQHEvVVEAL------GGET 692
Cdd:CHL00071 93 ITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVDDEE---LLELVELE-VRELLskydfpGDDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 693 QIIEVSA-----------KTGLGLDSLIEAILLQAEVLDLR-ANPDRTAEGVVIEAKLD----KGRGPVATVLVKRGTLK 756
Cdd:CHL00071 169 PIVSGSAllalealtenpKIKRGENKWVDKIYNLMDAVDSYiPTPERDTDKPFLMAIEDvfsiTGRGTVATGRIERGTVK 248
|
....*
gi 557835801 757 RGDII 761
Cdd:CHL00071 249 VGDTV 253
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
515-764 |
6.14e-13 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 72.66 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 515 DTAELVATEFGHTVKRVSESDV-MEGFI------DAEDHDDDTVVrppvVAVMGHVDHGKTSLLDAL------------- 574
Cdd:COG5258 80 DVLSLLAEEIGAKIEDVETWEVgDGGLVgvvtirEGKEKDPEHIV----VGVAGHVDHGKSTLVGTLvtgklddgnggtr 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 575 -----RKADVATGEAGGITQHIGAYQ----VRVPSGDR--------------VTFLDTPGHAAFSAMRARG--ANVTDIV 629
Cdd:COG5258 156 sfldvQPHEVERGLSADLSYAVYGFDddgpVRMKNPLRktdrarvveesdklVSFVDTVGHEPWLRTTIRGlvGQKLDYG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 630 VLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKheANPQRV------INELLQ------------HEV--VVEALG 689
Cdd:COG5258 236 LLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDK--VDDERVeevereIENLLRivgrtplevesrHDVdaAIEEIN 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557835801 690 GE-TQIIEVSAKTGLGLDSLIEAILLqaevLDLRANPDRTAEGVVIEAKLD-KGRGPVATVLVKRGTLKRGDIIVAG 764
Cdd:COG5258 314 GRvVPILKTSAVTGEGLDLLDELFER----LPKRATDEDEPFLMYIDRIYNvTGVGTVVSGTVKSGKVEAGDELLIG 386
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
606-713 |
1.19e-12 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 69.63 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 606 FLDTPG-------------HAAFSAMRArganvTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKheANPQ 672
Cdd:COG1159 55 FVDTPGihkpkrklgrrmnKAAWSALED-----VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDL--VKKE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557835801 673 rvinELLQHEVVVEALGGETQIIEVSAKTGLGLDSLIEAIL 713
Cdd:COG1159 128 ----ELLPLLAEYSELLDFAEIVPISALKGDNVDELLDEIA 164
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
557-761 |
1.32e-12 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 71.18 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATG----------------EAGGITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:PLN03126 84 IGTIGHVDHGKTTLTAALTMALASMGgsapkkydeidaapeeRARGIT--INTATVEYETENRhYAHVDCPGHADYVKNM 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEANPQRVINELLQHEVVV--EALGGETQIIE 696
Cdd:PLN03126 162 ITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVDDEELLELVELEVRELLSsyEFPGDDIPIIS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 697 VSAKTGL-----------GLDSLIEAIL-LQAEVLDLRANPDRTAEGVVIEAKLD----KGRGPVATVLVKRGTLKRGDI 760
Cdd:PLN03126 242 GSALLALealmenpnikrGDNKWVDKIYeLMDAVDSYIPIPQRQTDLPFLLAVEDvfsiTGRGTVATGRVERGTVKVGET 321
|
.
gi 557835801 761 I 761
Cdd:PLN03126 322 V 322
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
557-759 |
2.59e-12 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 69.83 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRK--ADVATGEAG--------------GITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:PRK00049 15 VGTIGHVDHGKTTLTAAITKvlAKKGGAEAKaydqidkapeekarGIT--INTAHVEYETEKRhYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEaNPQRVinELLQHEvVVEAL------GGET 692
Cdd:PRK00049 93 ITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELL--ELVEME-VRELLskydfpGDDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 693 QIIEVSAKTGL-GLDSLI--EAILLQAEVLDLR-ANPDRtaegvvieaKLDK-------------GRGPVATVLVKRGTL 755
Cdd:PRK00049 169 PIIRGSALKALeGDDDEEweKKILELMDAVDSYiPTPER---------AIDKpflmpiedvfsisGRGTVVTGRVERGII 239
|
....
gi 557835801 756 KRGD 759
Cdd:PRK00049 240 KVGE 243
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
557-678 |
3.36e-12 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 66.87 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL------RKADVA-----------------TGEAGGITQHIGaYQVRVPSGD--RVTFLDTPG 611
Cdd:cd01885 3 ICIIAHVDHGKTTLSDSLlasagiISEKLAgkaryldtredeqergiTIKSSAISLYFE-YEEEKMDGNdyLINLIDSPG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557835801 612 HAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDkheanpqRVINEL 678
Cdd:cd01885 82 HVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKID-------RLILEL 141
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
557-670 |
3.53e-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: 67.13 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSL---------------LDALRKADVATGEAG----------------GITQHIGAYQVRVPSgDRVT 605
Cdd:cd01883 2 LVVIGHVDAGKSTLtghllyklggvdkrtIEKYEKEAKEMGKESfkyawvldklkeererGVTIDVGLAKFETEK-YRFT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557835801 606 FLDTPGHAAF-SAMRArGANVTDIVVLVVAADDG-------VMPQTIEainHARSAKT----PIIVAVNKMDKHEAN 670
Cdd:cd01883 81 IIDAPGHRDFvKNMIT-GASQADVAVLVVSARKGefeagfeKGGQTRE---HALLARTlgvkQLIVAVNKMDDVTVN 153
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
606-713 |
4.32e-12 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 68.15 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 606 FLDTPG-------------HAAFSAMRArganvTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKheANPQ 672
Cdd:PRK00089 57 FVDTPGihkpkralnramnKAAWSSLKD-----VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL--VKDK 129
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557835801 673 rviNELLQHEVVVEALGGETQIIEVSAKTGLGLDSLIEAIL 713
Cdd:PRK00089 130 ---EELLPLLEELSELMDFAEIVPISALKGDNVDELLDVIA 167
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
557-759 |
4.51e-12 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 69.10 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADVATGEAG----------------GITqhIGAYQVRVPSGDR-VTFLDTPGHAAFSAMR 619
Cdd:PRK12735 15 VGTIGHVDHGKTTLTAAITKVLAKKGGGEakaydqidnapeekarGIT--INTSHVEYETANRhYAHVDCPGHADYVKNM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTP-IIVAVNKMDKHEaNPQRVinELLQHEvVVEAL------GGET 692
Cdd:PRK12735 93 ITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPyIVVFLNKCDMVD-DEELL--ELVEME-VRELLskydfpGDDT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 693 QIIEVSAKTGL-GLDSLI--EAILLQAEVLDLR-ANPDRTAEGVVIEAKLD----KGRGPVATVLVKRGTLKRGD 759
Cdd:PRK12735 169 PIIRGSALKALeGDDDEEweAKILELMDAVDSYiPEPERAIDKPFLMPIEDvfsiSGRGTVVTGRVERGIVKVGD 243
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
606-713 |
4.90e-12 |
|
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: 65.18 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 606 FLDTPG-------------HAAFSAMRarGAnvtDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKheANPQ 672
Cdd:cd04163 55 FVDTPGihkpkkklgermvKAAWSALK--DV---DLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDL--VKDK 127
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557835801 673 rviNELLQHEVVVEALGGETQIIEVSAKTGLGLDSLIEAIL 713
Cdd:cd04163 128 ---EDLLPLLEKLKELHPFAEIFPISALKGENVDELLEYIV 165
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
553-691 |
7.25e-12 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 69.32 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 553 RPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRV---PSGDRVTFLDTPGHAAFSAMRARGANVTDIV 629
Cdd:COG5180 398 RGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVPGdaeSVSGPAGLADQAGAAASTAMADFVAPVTDAT 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557835801 630 VLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELLQHEVVVEALGGE 691
Cdd:COG5180 478 PVDVADVLGVRPDAILGGNVAPASGLDAETRIIEAEGAPATEDFVAAELSELREAAEEKTGD 539
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
557-713 |
8.80e-12 |
|
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: 64.45 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL--RKADVATGEAGGITQHIGAYQVrvpsGDRVTFLDTPG--HAAFS-AMRARGANVTD---- 627
Cdd:cd01876 2 VAFAGRSNVGKSSLINALtnRKKLARTSKTPGRTQLINFFNV----GDKFRLVDLPGygYAKVSkEVREKWGKLIEeyle 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 628 ------IVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHeaNPQRVINELLQHEVVVEALGGETQIIEVSAKT 701
Cdd:cd01876 78 nrenlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKL--KKSELAKVLKKIKEELNLFNILPPVILFSSKK 155
|
170
....*....|..
gi 557835801 702 GLGLDSLIEAIL 713
Cdd:cd01876 156 GTGIDELRALIA 167
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
557-771 |
1.09e-11 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 68.97 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADvATGEAGGITQH---------------IGAYQVRVPSGD-RVTFLDTPGHAAFSAMRA 620
Cdd:PRK10218 8 IAIIAHVDHGKTTLVDKLLQQS-GTFDSRAETQErvmdsndlekergitILAKNTAIKWNDyRINIVDTPGHADFGGEVE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 621 RGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINELLQHEVVVEALGGETQ--IIEVS 698
Cdd:PRK10218 87 RVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDfpIVYAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 699 AKTGL-GLD--SLIEAIL-LQAEVLDLRANPDRTAEGVVIE--AKLDKGR--GPVATVLVKRGTLKRGDIIVAGASWGRV 770
Cdd:PRK10218 167 ALNGIaGLDheDMAEDMTpLYQAIVDHVPAPDVDLDGPFQMqiSQLDYNSyvGVIGIGRIKRGKVKPNQQVTIIDSEGKT 246
|
.
gi 557835801 771 R 771
Cdd:PRK10218 247 R 247
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
557-722 |
3.53e-11 |
|
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: 62.95 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKADV-------ATgeagGITQHIgAYQVRvpsgDRVTFLDTPGhaaFSAMRARGANVT--- 626
Cdd:cd09912 3 LAVVGEFSAGKSTLLNALLGEEVlptgvtpTT----AVITVL-RYGLL----KGVVLVDTPG---LNSTIEHHTEITesf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 627 ----DIVVLVVAADDgvmPQT---IEAINHARSA-KTPIIVAVNKMDKHEANPQRVINELLQHEVVVEALGGET-QIIEV 697
Cdd:cd09912 71 lpraDAVIFVLSADQ---PLTeseREFLKEILKWsGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGGEpRIFPV 147
|
170 180
....*....|....*....|....*.
gi 557835801 698 SAKTGL-GLDSLIEAILLQAEVLDLR 722
Cdd:cd09912 148 SAKEALeARLQGDEELLEQSGFEELE 173
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
561-712 |
1.31e-10 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 61.90 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 561 GHVDHGKTSLLDALR--KADVATGEAG-GITQHIG-------------------AYQVRVPSGD-------RVTFLDTPG 611
Cdd:cd01888 7 GHVAHGKTTLVKALSgvWTVRHKEELKrNITIKLGyanakiykcpncgcprpydTPECECPGCGgetklvrHVSFVDCPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 612 HAAFSAMRARGANVTDIVVLVVAADDGV-MPQTIE--------AINHarsaktpIIVAVNKMD---KHEANPQ-RVINEL 678
Cdd:cd01888 87 HEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEhlaaleimGLKH-------IIILQNKIDlvkEEQALENyEQIKEF 159
|
170 180 190
....*....|....*....|....*....|....
gi 557835801 679 LQHEVVVEAlggetQIIEVSAKTGLGLDSLIEAI 712
Cdd:cd01888 160 VKGTIAENA-----PIIPISAQLKYNIDVLCEYI 188
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
557-713 |
2.64e-10 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 60.52 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKAD-VATGEAGGITQHIgayqVRVP---SGDRVTFLDTPG----------HAAFSAMRARG 622
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGEErVIVSDIAGTTRDS----IDVPfeyDGQKYTLIDTAGirkkgkvtegIEKYSVLRTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 623 A-NVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEaNPQRVINELLQHevVVEALG--GETQIIEVSA 699
Cdd:cd01895 81 AiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVE-KDEKTMKEFEKE--LRRKLPflDYAPIVFISA 157
|
170
....*....|....
gi 557835801 700 KTGLGLDSLIEAIL 713
Cdd:cd01895 158 LTGQGVDKLFDAIK 171
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
557-712 |
5.40e-10 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 62.56 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALrkadvaTGE---------AGGITQHIG----------------AYQV--RVPSGD------- 602
Cdd:PRK04000 12 IGMVGHVDHGKTTLVQAL------TGVwtdrhseelKRGITIRLGyadatirkcpdceepeAYTTepKCPNCGsetellr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 603 RVTFLDTPGHAAFSAMRARGANVTDIVVLVVAADDGV-MPQTIE--------AINHarsaktpIIVAVNKMD---KHEAN 670
Cdd:PRK04000 86 RVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEhlmaldiiGIKN-------IVIVQNKIDlvsKERAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 557835801 671 PQ-RVINELLQHEVVVEAlggetQIIEVSAKTGLGLDSLIEAI 712
Cdd:PRK04000 159 ENyEQIKEFVKGTVAENA-----PIIPVSALHKVNIDALIEAI 196
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
181-388 |
3.93e-09 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 60.61 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 181 AAEPAPQPvqksPIEEALSRPAQRAPREGHREGFrddrgprTEHPQGDRPQG--QYGDRPRPQGDRPQGDRPPFNRDRPQ 258
Cdd:PRK14086 92 AGEPAPPP----PHARRTSEPELPRPGRRPYEGY-------GGPRADDRPPGlpRQDQLPTARPAYPAYQQRPEPGAWPR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 259 GDRPQGNYGDRSPRPQGDrPQGNYGERTPRPQGDRPPFNRDRPQGDRPQgdrpafnRDGNRDRPQGDRPQGDRGPRPqgd 338
Cdd:PRK14086 161 AADDYGWQQQRLGFPPRA-PYASPASYAPEQERDREPYDAGRPEYDQRR-------RDYDHPRPDWDRPRRDRTDRP--- 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 557835801 339 rGPRP-AGETVRYSANSPRPPRAPA-GVAPNAPavsevdrirssrGTPAGRP 388
Cdd:PRK14086 230 -EPPPgAGHVHRGGPGPPERDDAPVvPIRPSAP------------GPLAAQP 268
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
559-685 |
4.58e-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: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 559 VMGHVDHGKTSLLD-------ALRKA-DVATGEAG----------GITqhIGAYQVRVPSGD-RVTFLDTPGHAAFSAMR 619
Cdd:cd01886 4 IIAHIDAGKTTTTErilyytgRIHKIgEVHGGGATmdwmeqererGIT--IQSAATTCFWKDhRINIIDTPGHVDFTIEV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557835801 620 ARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINEL---LQHEVVV 685
Cdd:cd01886 82 ERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIrekLGANPVP 150
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
107-338 |
5.40e-09 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 60.30 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 107 QSGANLGGLRQEEVERRNRVVEAARQDQERREADARRAAEVRAREEAARRAAEPAPQASAPAPAAPSAPVEAPRAAEPAP 186
Cdd:PRK12678 59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 187 QPVQ-KSPIEEALSRPAQRAPREGHREGFRDDRGPRTEHPQGDRPQGQYGDRPRPQGDRPQGDRPPFNRDRPQGDRpQGN 265
Cdd:PRK12678 139 RGAArKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR-REE 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557835801 266 YGDRSPRPQGDRPQGNYGERTPRPQGDRPPFNRDRPQGDRPQGDRPAFNRDGNRDRPQGDRPQGDRGPRPQGD 338
Cdd:PRK12678 218 RGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELRED 290
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
555-712 |
5.97e-09 |
|
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: 57.08 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 555 PVVAVMGHVDHGKTSLLDALRKADV-------ATGEAggiTqhigAYQVRVPSGDRVTFLDTPG------H---AAFSAM 618
Cdd:cd01878 42 PTVALVGYTNAGKSTLFNALTGADVlaedqlfATLDP---T----TRRIKLPGGREVLLTDTVGfirdlpHqlvEAFRST 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 619 --RARGAnvtDIVVLVVAADDGVMPQTIEAINH------ARSAktPIIVAVNKMDKHEANPQRVINELLQHEVVVealgg 690
Cdd:cd01878 115 leEVAEA---DLLLHVVDASDPDREEQIETVEEvlkelgADDI--PIILVLNKIDLLDDEELEERLRAGRPDAVF----- 184
|
170 180
....*....|....*....|..
gi 557835801 691 etqiieVSAKTGLGLDSLIEAI 712
Cdd:cd01878 185 ------ISAKTGEGLDLLKEAI 200
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
601-678 |
6.84e-09 |
|
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: 57.99 E-value: 6.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557835801 601 GDRVTFLDTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANPQRVINEL 678
Cdd:cd04169 70 GCVINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEI 147
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
964-1043 |
9.48e-09 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 53.04 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 964 VLEVFDITKVGKVAGCRVTEGRVEKGARVRILRDNVViqemGVLSTLKRFKDEVNSVVVGQECGMAFNGFQDLKAGDFIE 1043
Cdd:cd01342 5 VFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGIT----GRVTSIERFHEEVDEAKAGDIVGIGILGVKDILTGDTLT 80
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
217-344 |
1.25e-08 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 55.43 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 217 DRGPRTEHPQGDRPQGQYGDRP--RPQGDRPQGDRPPFNRDRPQGDRPQGNYGDRSPRPQGDRPQGNygertPRPQGDRP 294
Cdd:pfam15240 43 GQGPQGPPPGGFPPQPPASDDPpgPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGG-----NQQQGPPP 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 557835801 295 PFNrdrPQGDRPQGDRPAfNRDGNRDRP---QGDRPQGDRGPRPQGDRGPRPA 344
Cdd:pfam15240 118 PGK---PQGPPPQGGGPP-PQGGNQQGPpppPPGNPQGPPQRPPQPGNPQGPP 166
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
128-342 |
1.31e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 59.15 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 128 EAARQDQERREADARRAAEVRAREEAARRAAEPAPQASAPAPAAPSAPVEAPRAAEPAPQPVQKSPIEEALSRPAQRAPR 207
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 208 EGhREGFRDDRGPRTEHPQGDRPQGQYGDRPRPQGDRPQGDRPPFNRDRPQGDRPQGNYGDRSPRPQGDRPQGNYGERTP 287
Cdd:PRK12678 136 AA-RRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDR 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 288 RPQGDRppfNRDRPQGDRPQGDRPAFNRDGNRDRPQGDRPQGDRGPRpQGDRGPR 342
Cdd:PRK12678 215 REERGR---RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGR-GGRRGRR 265
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
627-713 |
1.86e-08 |
|
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: 54.75 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 627 DIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEanpqrvinellQHEVVVE--ALG-GEtqIIEVSAKTGL 703
Cdd:cd01894 78 DVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIK-----------EEEEAAEfySLGfGE--PIPISAEHGR 144
|
90
....*....|
gi 557835801 704 GLDSLIEAIL 713
Cdd:cd01894 145 GIGDLLDAIL 154
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
627-713 |
6.49e-08 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 56.19 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 627 DIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEanpqrvinellQHEVVVE--ALG-GEtqIIEVSAKTGL 703
Cdd:COG1160 84 DVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPK-----------READAAEfySLGlGE--PIPISAEHGR 150
|
90
....*....|
gi 557835801 704 GLDSLIEAIL 713
Cdd:COG1160 151 GVGDLLDAVL 160
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
566-713 |
7.22e-08 |
|
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: 52.88 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 566 GKTSLLDALRKADVA--TGEAGG----ITQHIgayqvrVPSGDRVTFLDTPG--------------HAAFSAMRArganv 625
Cdd:cd04164 15 GKSSLLNALAGRDRAivSDIAGTtrdvIEEEI------DLGGIPVRLIDTAGlretedeiekigieRAREAIEEA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 626 tDIVVLVVaadDGVMPQTIE-AINHARSAKTPIIVAVNKMDkheanpqrvineLLQHEVVVEALGGETqIIEVSAKTGLG 704
Cdd:cd04164 84 -DLVLLVV---DASEGLDEEdLEILELPAKKPVIVVLNKSD------------LLSDAEGISELNGKP-IIAISAKTGEG 146
|
....*....
gi 557835801 705 LDSLIEAIL 713
Cdd:cd04164 147 IDELKEALL 155
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
557-709 |
7.27e-08 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 54.22 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL------------------RKADVATGEAGGITQ-HIG--------AYQVRVP---------- 599
Cdd:cd04165 2 VAVVGNVDAGKSTLLGVLtqgeldngrgkarlnlfrHKHEVESGRTSSVSNdILGfdsdgevvNYPDNHLgeldveicek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 600 SGDRVTFLDTPGHAAF--SAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEANP-QRVIN 676
Cdd:cd04165 82 SSKVVTFIDLAGHERYlkTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVlQETLK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 557835801 677 ELL-----------------QHEVVVEALGGETQ----IIEVSAKTGLGLDSLI 709
Cdd:cd04165 162 DLKrllkspgvrklpvpvksKDDVVLSASNLSSGrvvpIFQVSNVTGEGLDLLR 215
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
559-682 |
1.08e-07 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 56.21 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 559 VMGHVDHGKTSLLDAL--RKADVATGEAG--------------GITqhIGA------YQVRVPSGDR-----VTFLDTPG 611
Cdd:PTZ00416 24 VIAHVDHGKSTLTDSLvcKAGIISSKNAGdarftdtradeqerGIT--IKStgislyYEHDLEDGDDkqpflINLIDSPG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557835801 612 HAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDkheanpqRVINElLQHE 682
Cdd:PTZ00416 102 HVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVD-------RAILE-LQLD 164
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
557-678 |
3.05e-07 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 54.52 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL---------------RKADVATGEAG-GITqhIGAYQVRVP---SGDR--VTFLDTPGHAAF 615
Cdd:TIGR00490 22 IGIVAHIDHGKTTLSDNLlagagmiseelagqqLYLDFDEQEQErGIT--INAANVSMVheyEGNEylINLIDTPGHVDF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557835801 616 SAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDkheanpqRVINEL 678
Cdd:TIGR00490 100 GGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVD-------RLINEL 155
|
|
| IF2_IF5B_II |
cd03701 |
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ... |
729-796 |
3.80e-07 |
|
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: 49.21 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 729 AEGVVIEAKLDKGRGPVATVLVKRGTLKRGDIIVAGAS----WGRVRALINERN----------EQLPEAGPSEPVEILG 794
Cdd:cd03701 2 PRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESkdviYTRIRALLDPDPleemesrkkgNKRKEVGAASGVKILG 81
|
..
gi 557835801 795 LD 796
Cdd:cd03701 82 FG 83
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
180-359 |
5.78e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 53.75 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 180 RAAEPAPQPVQKSPIEEALSRPAQRAPREGHREgfrddrgprTEHPQGDRPQGQYGDRPRPQGDRPQGDRPPFNRDRPQG 259
Cdd:PRK12678 85 AAARQAEQPAAEAAAAKAEAAPAARAAAAAAAE---------AASAPEAAQARERRERGEAARRGAARKAGEGGEQPATE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 260 DRPQGnyGDRSPRPQGDRPQGNyGERTPRPQGDRPPfNRDRPQGDRPQGDRPAFNRDGNRDRPQGDRPQGDRGPRPQGDR 339
Cdd:PRK12678 156 ARADA--AERTEEEERDERRRR-GDREDRQAEAERG-ERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180
....*....|....*....|
gi 557835801 340 GPRPAGETVRYSANSPRPPR 359
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRD 251
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
558-712 |
6.53e-07 |
|
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: 50.47 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 558 AVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRVPSGDRVTFLDTPG--HAAFSAMR-----ARGANVTDIVV 630
Cdd:cd01881 1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGllDGASEGRGlgeqiLAHLYRSDLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 631 LVVAA--DDGVMP-QTIEAIN-------HARSAKtPIIVAVNKMDK-HEANPQRVINELLQHEVVVealggetqiIEVSA 699
Cdd:cd01881 81 HVIDAseDCVGDPlEDQKTLNeevsgsfLFLKNK-PEMIVANKIDMaSENNLKRLKLDKLKRGIPV---------VPTSA 150
|
170
....*....|...
gi 557835801 700 KTGLGLDSLIEAI 712
Cdd:cd01881 151 LTRLGLDRVIRTI 163
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
627-713 |
7.01e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 53.13 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 627 DIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDKHEanpqrvinellQHEVVVE--ALG-GEtqIIEVSAKTGL 703
Cdd:PRK00093 82 DVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPD-----------EEADAYEfySLGlGE--PYPISAEHGR 148
|
90
....*....|
gi 557835801 704 GLDSLIEAIL 713
Cdd:PRK00093 149 GIGDLLDAIL 158
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
171-419 |
7.62e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 171 APSAPVEAPRAAEPAPQPvqkSPIEEALSRPAQR--APREGHRegfrddrgPRTEHPQGDRPQGQYGDRPRPQGDRPQgD 248
Cdd:PHA03247 2558 AAPPAAPDRSVPPPRPAP---RPSEPAVTSRARRpdAPPQSAR--------PRAPVDDRGDPRGPAPPSPLPPDTHAP-D 2625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 249 RPPFNRdRPQGDRPQGNYGDRSPRPQGDRPQGNYGE----RTPRPQGdRPPFNRDRPQGDRPQGDRPAFNRDGNRDRPQG 324
Cdd:PHA03247 2626 PPPPSP-SPAANEPDPHPPPTVPPPERPRDDPAPGRvsrpRRARRLG-RAAQASSPPQRPRRRAARPTVGSLTSLADPPP 2703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 325 DRPQGDRGPRPQGDRGPRPAGeTVRYSANSPRPPRAPAGVA-PNAPAVSEVDRIRSSRGTPAGRPLGARAgddddrnkRG 403
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPG-PAAARQASPALPAAPAPPAvPAGPATPGGPARPARPPTTAGPPAPAPP--------AA 2774
|
250
....*....|....*.
gi 557835801 404 KVGAPTKAVSQTRGEP 419
Cdd:PHA03247 2775 PAAGPPRRLTRPAVAS 2790
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
87-328 |
9.49e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 52.98 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 87 QGGQSQNNGPRPSQNSGPRPQSGANLGGLRQEEVERRNRVVEAARQDQERREADARRAAEVRAREEAARRAAEPAPQASA 166
Cdd:PRK12678 59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 167 PAPAAPSAPVEAPRAAEPAPQPVQKSPIEEALSRPAQRAPREGHREGFRDDRGPRTEhpQGDRPQGQYGDRPRPQGDRPQ 246
Cdd:PRK12678 139 RGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREE--RGRDGDDRDRRDRREQGDRRE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 247 GDRPPFNRDRPQGDRPQGNYGDRSPRPQGDRPQGNYGERTPRpQGDRPPFNRDRpqgDRpqgdrpafNRDGNRDRPQGDR 326
Cdd:PRK12678 217 ERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGR-GGRRGRRFRDR---DR--------RGRRGGDGGNERE 284
|
..
gi 557835801 327 PQ 328
Cdd:PRK12678 285 PE 286
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
557-678 |
1.12e-06 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 52.56 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDALRKA------DVAtGEA-----------GGITqhIGAYQVRVP---SGDR--VTFLDTPGHAA 614
Cdd:PRK07560 23 IGIIAHIDHGKTTLSDNLLAGagmiseELA-GEQlaldfdeeeqaRGIT--IKAANVSMVheyEGKEylINLIDTPGHVD 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557835801 615 FSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDkheanpqRVINEL 678
Cdd:PRK07560 100 FGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVD-------RLIKEL 156
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
50-388 |
1.71e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.48 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 50 VETKRRIGTPPPGAPGSANPAPRPTADSNL-------AKPRPPQQGGQSQNNGPRPSQNSGPRPQSGANLGGLRQEEVER 122
Cdd:PHA03307 61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWslstlapASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 123 RNRVVEAARQDQERREADARRAAEVRAREEAARRAAEPAPQASAPAPA-APSAPVEAPRAAEPAPQPVQKSPIEEALSRP 201
Cdd:PHA03307 141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSpPAEPPPSTPPAAASPRPPRRSSPISASASSP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 202 AQRAPREG------------HREGFRDDRGPRTEHPqgdRPQGQYGDRPRPQGDRPQGDRPPFnrdRPQGDRPQGNYGDR 269
Cdd:PHA03307 221 APAPGRSAaddagasssdssSSESSGCGWGPENECP---LPRPAPITLPTRIWEASGWNGPSS---RPGPASSSSSPRER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 270 SPRPQGDRPQGNYGERTPRPQGDR-------PPFNRDRPQGDRPQGDRPAfnRDGNRDRPQGDRPQGDRGPRPQGDRGPR 342
Cdd:PHA03307 295 SPSPSPSSPGSGPAPSSPRASSSSsssressSSSTSSSSESSRGAAVSPG--PSPSRSPSPSRPPPPADPSSPRKRPRPS 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 557835801 343 PAGETVRYSANSPRPPRApagvapnAPAVSEVDRIRSSRG-TPAGRP 388
Cdd:PHA03307 373 RAPSSPAASAGRPTRRRA-------RAAVAGRARRRDATGrFPAGRP 412
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
557-666 |
1.90e-06 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 52.03 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 557 VAVMGHVDHGKTSLLDAL---------------RKADVATGEAG-GIT---------QHIGAYQVRVPSGDR------VT 605
Cdd:PLN00116 22 MSVIAHVDHGKSTLTDSLvaaagiiaqevagdvRMTDTRADEAErGITikstgislyYEMTDESLKDFKGERdgneylIN 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557835801 606 FLDTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMDK 666
Cdd:PLN00116 102 LIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
627-734 |
2.25e-06 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 50.94 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 627 DIVVLVVAADDGVMPQTIEaINHARSAKTPIIVAVNKMDkheanpqrvinelLQHEVVVEALGGETQIIEVSAKTGLGLD 706
Cdd:pfam12631 175 DLVLLVLDASRPLDEEDLE-ILELLKDKKPIIVVLNKSD-------------LLGEIDELEELKGKPVLAISAKTGEGLD 240
|
90 100
....*....|....*....|....*...
gi 557835801 707 SLIEAIllqaevLDLRANPDRTAEGVVI 734
Cdd:pfam12631 241 ELEEAI------KELFLAGEIASDGPII 262
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
553-712 |
2.40e-06 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 49.53 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 553 RPPVVAVMGHVDHGKTSLLDALRKADVATGEAGGITQHIGAYQVRvpsgdRVTFLDTPGhaaFSAMRARGANV-----TD 627
Cdd:PRK04213 8 RKPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPNHYDWG-----DFILTDLPG---FGFMSGVPKEVqekikDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 628 IV-------------VLVV---AADD--------GVMPQTIEAINHARSAKTPIIVAVNKMDKHEaNPQRVINELlqhev 683
Cdd:PRK04213 80 IVryiednadrilaaVLVVdgkSFIEiierwegrGEIPIDVEMFDFLRELGIPPIVAVNKMDKIK-NRDEVLDEI----- 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 557835801 684 vVEALGGET-------QIIEVSAKTGlGLDSLIEAI 712
Cdd:PRK04213 154 -AERLGLYPpwrqwqdIIAPISAKKG-GIEELKEAI 187
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
566-710 |
2.82e-06 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 48.34 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 566 GKTSLLDALRKADVATgeaggITQHIGaYQVR-VPSGD-RVTFLDTPGHAAFSAMRARGANVTDIVVLVV-AADDGVMPQ 642
Cdd:cd00878 11 GKTTILYKLKLGEVVT-----TIPTIG-FNVEtVEYKNvKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVdSSDRERIEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557835801 643 TIE----AINHARSAKTPIIVAVNKMDKHEANPQRVINELLQHEvvvEALGGETQIIEVSAKTGLGLDSLIE 710
Cdd:cd00878 85 AKNelhkLLNEEELKGAPLLILANKQDLPGALTESELIELLGLE---SIKGRRWHIQPCSAVTGDGLDEGLD 153
|
|
| IF2_assoc |
pfam08364 |
Bacterial translation initiation factor IF-2 associated region; Most of the sequences in this ... |
18-55 |
4.94e-06 |
|
Bacterial translation initiation factor IF-2 associated region; Most of the sequences in this alignment come from bacterial translation initiation factors (IF-2, also pfam04760), but the domain is also found in the eukaryotic translation initiation factor 4 gamma in yeast and in a hypothetical Euglenozoa protein of unknown function.
Pssm-ID: 429947 [Multi-domain] Cd Length: 39 Bit Score: 44.06 E-value: 4.94e-06
10 20 30
....*....|....*....|....*....|....*...
gi 557835801 18 RAPLSLKPRTggnvsTGTVKQSFSHGRSKTVVVETKRR 55
Cdd:pfam08364 1 PKKLTLKRKT-----TSEVKQSFSHGRSKTVQVEVRKK 33
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
627-713 |
6.00e-06 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 50.06 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 627 DIVVLVVAADDGVMPQTIEAInhARSAKTPIIVAVNKMDkheanpqrvineLLQHEVVVEALGGETQIIEVSAKTGLGLD 706
Cdd:COG0486 294 DLVLLLLDASEPLTEEDEEIL--EKLKDKPVIVVLNKID------------LPSEADGELKSLPGEPVIAISAKTGEGID 359
|
....*..
gi 557835801 707 SLIEAIL 713
Cdd:COG0486 360 ELKEAIL 366
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
561-665 |
6.49e-06 |
|
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: 48.33 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 561 GHVDHGKTSL---------------LDALRKADVATGEAG-----------------GITQHIgAYqvRVPSGDRVTFL- 607
Cdd:cd04166 6 GSVDDGKSTLigrllydsksifedqLAALERSKSSGTQGEkldlallvdglqaereqGITIDV-AY--RYFSTPKRKFIi 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557835801 608 -DTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQT--------IEAINHarsaktpIIVAVNKMD 665
Cdd:cd04166 83 aDTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTrrhsyiasLLGIRH-------VVVAVNKMD 142
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
555-712 |
9.46e-06 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 49.31 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 555 PVVAVMGHVDHGKTSLLDALRKADV-------ATgeaggitqhigayQVRVPSGDRVTFLDTPG------H---AAFSA- 617
Cdd:COG2262 200 PTVALVGYTNAGKSTLFNRLTGADVlaedklfATldp-------ttrRLELPDGRPVLLTDTVGfirklpHqlvEAFRSt 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 618 -MRARGAnvtDIVVLVV-AADDGVMPQ------TIEAINharSAKTPIIVAVNKMDkheanpqrvineLLQHEVVVEALG 689
Cdd:COG2262 273 lEEVREA---DLLLHVVdASDPDFEEQietvneVLEELG---ADDKPIILVFNKID------------LLDDEELERLRA 334
|
170 180
....*....|....*....|...
gi 557835801 690 GETQIIEVSAKTGLGLDSLIEAI 712
Cdd:COG2262 335 GYPDAVFISAKTGEGIDELLEAI 357
|
|
| Ras_dva |
cd04147 |
Ras - dorsal-ventral anterior localization (Ras-dva) family; Ras-dva subfamily. Ras-dva (Ras - ... |
559-716 |
1.17e-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: 47.14 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 559 VMGHVDHGKTSLLDALRKADVATGEAGGITQ-HIGAYqvrVPSGDRVTF--LDTPGHAAFSAMRARGANVTDIVVLVVAA 635
Cdd:cd04147 4 FMGAAGVGKTALIQRFLYDTFEPKHRRTVEElHSKEY---EVAGVKVTIdiLDTSGSYSFPAMRKLSIQNGDAFALVYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 636 DDgvmPQTIEAINHARS--------AKTPIIVAVNKMDKHeanPQRVInELLQHEVVVEaLGGETQIIEVSAKTGLGLDS 707
Cdd:cd04147 81 DD---PESFEEVKRLREeilevkedKFVPIVVVGNKIDSL---AERQV-EAADALSTVE-LDWNNGFVEASAKDNENVTE 152
|
....*....
gi 557835801 708 LIEAILLQA 716
Cdd:cd04147 153 VFKELLQQA 161
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
182-303 |
1.19e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 49.68 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 182 AEPAPQPVQKSPIEEALSRPAQRAPREGHREGFRDDRGPRTEHPQG--DRPQGQYGDRPRPQGdRPQGDRPPfnRDRPQG 259
Cdd:PHA03378 667 TQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGraQRPAAATGRARPPAA-APGRARPP--AAAPGR 743
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 557835801 260 DRPQGNYGDRSPRPQG-----DRPQGNYGERTPRPQGDRPPFNRDRPQG 303
Cdd:PHA03378 744 ARPPAAAPGRARPPAAapgraRPPAAAPGAPTPQPPPQAPPAPQQRPRG 792
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
535-722 |
1.32e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 48.89 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 535 DVMEGFIDAEDHDDDTvvRPPVVAVMGHVDHGKTSLLDALRKAD--VATGEAGgITqhigayqvR----VP---SGDRVT 605
Cdd:PRK00093 156 AILEELPEEEEEDEED--EPIKIAIIGRPNVGKSSLINALLGEErvIVSDIAG-TT--------RdsidTPferDGQKYT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 606 FLDTPG-------HAA---FSAMRARGA-NVTDIVVLVVAADDGVMPQ--TIeaINHARSAKTPIIVAVNKMDKHEANPQ 672
Cdd:PRK00093 225 LIDTAGirrkgkvTEGvekYSVIRTLKAiERADVVLLVIDATEGITEQdlRI--AGLALEAGRALVIVVNKWDLVDEKTM 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 557835801 673 RVINELLQHEvvveaLG--GETQIIEVSAKTGLGLDSLIEAILLQAEVLDLR 722
Cdd:PRK00093 303 EEFKKELRRR-----LPflDYAPIVFISALTGQGVDKLLEAIDEAYENANRR 349
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
604-761 |
1.74e-05 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 48.46 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 604 VTFLDTPGHAAFSAMRARGANVTDIVVLVVAADDGV-MPQTIEAINHARSAK-TPIIVAVNKMDkheanpqrVINE---L 678
Cdd:PTZ00327 119 VSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKlKHIIILQNKID--------LVKEaqaQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 679 LQHEVVVEALGGETQ----IIEVSAKTGLGLDSLIEAILLQAEV--LDLRANPDRTaegvVIEA--------KLDKGRGP 744
Cdd:PTZ00327 191 DQYEEIRNFVKGTIAdnapIIPISAQLKYNIDVVLEYICTQIPIpkRDLTSPPRMI----VIRSfdvnkpgeDIENLKGG 266
|
170
....*....|....*..
gi 557835801 745 VATVLVKRGTLKRGDII 761
Cdd:PTZ00327 267 VAGGSILQGVLKVGDEI 283
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
559-790 |
2.14e-05 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 48.20 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 559 VMGHVDHGKTSLLDAL------------RKADVATGEAG-------------------GITQHIGAYQVRVPSGdRVTFL 607
Cdd:PTZ00141 12 VIGHVDSGKSTTTGHLiykcggidkrtiEKFEKEAAEMGkgsfkyawvldklkaererGITIDIALWKFETPKY-YFTII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 608 DTPGHAAFSAMRARGANVTDIVVLVVAADDGVMP-------QTIEainHARSAKT----PIIVAVNKMDKHEANPQRVIN 676
Cdd:PTZ00141 91 DAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTRE---HALLAFTlgvkQMIVCINKMDDKTVNYSQERY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 677 ELLQHEV--VVEALGGETQIIEVSAKTGLGLDSLIE----------AILLQAevLDLRANPDRTAEGVVIEAKLDKGR-G 743
Cdd:PTZ00141 168 DEIKKEVsaYLKKVGYNPEKVPFIPISGWQGDNMIEksdnmpwykgPTLLEA--LDTLEPPKRPVDKPLRLPLQDVYKiG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 557835801 744 PVATVLVKR---GTLKRGDIIVAGASwgrvrALINE------RNEQLPEAGPSEPV 790
Cdd:PTZ00141 246 GIGTVPVGRvetGILKPGMVVTFAPS-----GVTTEvksvemHHEQLAEAVPGDNV 296
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
223-359 |
2.21e-05 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 45.80 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 223 EHPQGDrPQGQYGDRPrPQGDRPQGDRPPfnrDRPQGDRPQGNygdrSPRPQGDRPQGNYGERTPRPQGDRPPfnrdrpQ 302
Cdd:pfam15240 44 QGPQGP-PPGGFPPQP-PASDDPPGPPPP---GGPQQPPPQGG----KQKPQGPPPQGGPRPPPGKPQGPPPQ------G 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 557835801 303 GDRPQGDRPAFNRDGNRDRPQGDRPQGDRGPRPQGDRGPRPAGETVRYS--ANSPRPPR 359
Cdd:pfam15240 109 GNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPqpGNPQGPPQ 167
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
601-713 |
2.75e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 47.71 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 601 GDRVTFLDTPG-------HAA---FSAMRARGA-NVTDIVVLVVAADDGVMPQ--TIeaINHARSAKTPIIVAVNKMD-- 665
Cdd:COG1160 222 GKKYTLIDTAGirrkgkvDEGiekYSVLRTLRAiERADVVLLVIDATEGITEQdlKI--AGLALEAGKALVIVVNKWDlv 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 557835801 666 KHEANPQRVINELLQHEV--VVEAlggetQIIEVSAKTGLGLDSLIEAIL 713
Cdd:COG1160 300 EKDRKTREELEKEIRRRLpfLDYA-----PIVFISALTGQGVDKLLEAVD 344
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
603-665 |
3.38e-05 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 47.82 E-value: 3.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557835801 603 RVTFLDTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMD 665
Cdd:PRK00741 80 LINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLD 142
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
566-713 |
4.54e-05 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 47.03 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 566 GKTSLLDALRKADVA--TGEAGG----ITQHIgayQVR-VPsgdrVTFLDTPG--HA-----------AFSAMRArgAnv 625
Cdd:PRK05291 227 GKSSLLNALLGEERAivTDIAGTtrdvIEEHI---NLDgIP----LRLIDTAGirETddevekigierSREAIEE--A-- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 626 tDIVVLVVAADDGVMPQTIEAINhaRSAKTPIIVAVNKMDKHEANPQRVINEllqhevvvealggeTQIIEVSAKTGLGL 705
Cdd:PRK05291 296 -DLVLLVLDASEPLTEEDDEILE--ELKDKPVIVVLNKADLTGEIDLEEENG--------------KPVIRISAKTGEGI 358
|
....*...
gi 557835801 706 DSLIEAIL 713
Cdd:PRK05291 359 DELREAIK 366
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
274-407 |
5.93e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 46.82 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 274 QGDRPQGNYGERTPR-PQGDRPPFNRDRPQGdrPQGDRPAFNRDGNRDRPQGDRPQGDRGPR-PQGDRGPR----PAGET 347
Cdd:NF038329 114 KGDGEKGEPGPAGPAgPAGEQGPRGDRGETG--PAGPAGPPGPQGERGEKGPAGPQGEAGPQgPAGKDGEAgakgPAGEK 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 348 VRYSANSPRPPRAPAGvaPNAPAVSEVDRIRSSRGTPAGRPLGARAGDDDDRNKRGKVGA 407
Cdd:NF038329 192 GPQGPRGETGPAGEQG--PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP 249
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
219-361 |
1.30e-04 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 43.87 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 219 GPRTEHPQGDRPQGQYGDRPRPQGDRPQGDRPPfnrdrPQGDRPQGNYGDRSP-RPQGDRPQGNYGERTPRPQGDRPPFN 297
Cdd:pfam15240 18 SSSEDVSQEDSPSLISEEEGQSQQGGQGPQGPP-----PGGFPPQPPASDDPPgPPPPGGPQQPPPQGGKQKPQGPPPQG 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557835801 298 RDRPQGDRPQGDRPAFNRDGNRDRPqgdrPQGDRGPRPQGDRGPRPAGETVRYSANSPRPPRAP 361
Cdd:pfam15240 93 GPRPPPGKPQGPPPQGGNQQQGPPP----PGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGP 152
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
566-713 |
1.36e-04 |
|
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.
Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 43.57 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 566 GKTSLLDALRKADVAtgeaggitqhIGAYQ----------VRVPSGDRVTFLDTPG-----HaafsamraRGANV----- 625
Cdd:cd01898 12 GKSTLLSAISNAKPK----------IADYPfttlvpnlgvVRVDDGRSFVIADIPGliegaS--------EGKGLghrfl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 626 -----TDIVVLVVAADDGVMP----QTI----EAINHARSAKtPIIVAVNKMDkheANPQRVINELLQHevVVEALGGEt 692
Cdd:cd01898 74 rhierTRVLLHVIDLSGEDDPvedyETIrnelEAYNPGLAEK-PRIVVLNKID---LLDAEERFEKLKE--LLKELKGK- 146
|
170 180
....*....|....*....|.
gi 557835801 693 QIIEVSAKTGLGLDSLIEAIL 713
Cdd:cd01898 147 KVFPISALTGEGLDELLKKLA 167
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
623-712 |
1.37e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 44.31 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 623 ANVtDIVVLVVAADDGVM-PQTIE-AINHARSAKTPIIVAVNKMDKHEANPqrvINELLQHevvVEALGgeTQIIEVSAK 700
Cdd:cd01854 1 ANV-DQVLIVFSLKEPFFnLRLLDrYLVAAEASGIEPVIVLNKADLVDDEE---LEELLEI---YEKLG--YPVLAVSAK 71
|
90
....*....|..
gi 557835801 701 TGLGLDSLIEAI 712
Cdd:cd01854 72 TGEGLDELRELL 83
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
974-1040 |
1.95e-04 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 40.71 E-value: 1.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557835801 974 GKVAGCRVTEGRVEKGARVRILrDNVVIQ--EMGVLSTLKRFKDEVNSVVVGQECGMAFN--GFQDLKAGD 1040
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRIL-PNGTGKkkIVTRVTSLLMFHAPLREAVAGDNAGLILAgvGLEDIRVGD 70
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
180-398 |
2.16e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 180 RAAEPAPQPVQKSPIEE-ALSRPAQRAPREGHREGFRDDRGPRteHPQGDRPQGQYGDRPRPQGDRPQGDRPPFNRDRPQ 258
Cdd:PHA03307 59 AAACDRFEPPTGPPPGPgTEAPANESRSTPTWSLSTLAPASPA--REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 259 GDRPQGNYGDRSPRPQ---------------------------------GDRPQGNYGERTPRPQGDRPPFNRDRPQGDR 305
Cdd:PHA03307 137 MLRPVGSPGPPPAASPpaagaspaavasdaassrqaalplsspeetaraPSSPPAEPPPSTPPAAASPRPPRRSSPISAS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 306 PQGDRPAFNRDGNRDRPQ-------------GDRPQGDRG-PRPQGDRGPRPAGETVRYSANSPRPPRAPAGVAPNAPAv 371
Cdd:PHA03307 217 ASSPAPAPGRSAADDAGAsssdssssessgcGWGPENECPlPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS- 295
|
250 260
....*....|....*....|....*....
gi 557835801 372 SEVDRIRSSRG--TPAGRPLGARAGDDDD 398
Cdd:PHA03307 296 PSPSPSSPGSGpaPSSPRASSSSSSSRES 324
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
537-665 |
2.74e-04 |
|
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: 44.69 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 537 MEGFIDA--EDHDDDTVVRppvVAVMGHVDHGKTSL---------------LDALRKADVATGEAG-------------- 585
Cdd:COG2895 1 MSTDIEAylAQHENKDLLR---FITCGSVDDGKSTLigrllydtksifedqLAALERDSKKRGTQEidlalltdglqaer 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 586 --GITqhIG-AYqvRVPSGDRVTFL--DTPGHAAFSamR--ARGANVTDIVVLVVAADDGVMPQT-----IEA---INHa 650
Cdd:COG2895 78 eqGIT--IDvAY--RYFSTPKRKFIiaDTPGHEQYT--RnmVTGASTADLAILLIDARKGVLEQTrrhsyIASllgIRH- 150
|
170
....*....|....*
gi 557835801 651 rsaktpIIVAVNKMD 665
Cdd:COG2895 151 ------VVVAVNKMD 159
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
32-251 |
2.92e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 32 STGTVKQSFSHGRSKTVVVETKR-----------RIGTPPPGAPGSANPAPRPtADSNLAKPRPPQQGGQSQNNGPRP-S 99
Cdd:PRK07764 553 STGGLARRFASPGNAEVLVTALAeelggdwqveaVVGPAPGAAGGEGPPAPAS-SGPPEEAARPAAPAAPAAPAAPAPaG 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 100 QNSGPRPQSGANLGGLRQEEVERRNRVVEAARQDqerreadARRAAEVRAREEAARRAAEPAPQASAPAPAAPSAPVEAP 179
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG-------GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA 704
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557835801 180 RAAEPAPQPVQKSPIEEALSRPAQRAPREGHREGFRDDRGPRtEHPQGDRPQGQYGDRPRPQGDRPQGDRPP 251
Cdd:PRK07764 705 PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD-DPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
586-699 |
4.14e-04 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 44.13 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 586 GITQHIgAYqvRVPSGDRVTFL--DTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQT--------IEAINHarsakt 655
Cdd:PRK05124 92 GITIDV-AY--RYFSTEKRKFIiaDTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTrrhsfiatLLGIKH------ 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 557835801 656 pIIVAVNKMDKHEANPQRVinELLQHE--VVVEALGGETQI--IEVSA 699
Cdd:PRK05124 163 -LVVAVNKMDLVDYSEEVF--ERIREDylTFAEQLPGNLDIrfVPLSA 207
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
629-712 |
4.78e-04 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 42.25 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 629 VVLVV-AAD-DGVMPQTIEAINHARsaktPIIVAVNKMD------KHEANPQRVINELLQHEVVVealggeTQIIEVSAK 700
Cdd:cd01855 37 VVHVVdIFDfPGSLIPGLAELIGAK----PVILVGNKIDllpkdvKPNRLKQWVKKRLKIGGLKI------KDVILVSAK 106
|
90
....*....|..
gi 557835801 701 TGLGLDSLIEAI 712
Cdd:cd01855 107 KGWGVEELIEEI 118
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
57-429 |
7.11e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 57 GTPPPGAPGSANPaprPTADSNLAKPRPpqqggqsqnnGPRPSqnsGPRPQSGANLGGLRQEEVerRNRVVEAARQDQER 136
Cdd:PHA03247 2549 GDPPPPLPPAAPP---AAPDRSVPPPRP----------APRPS---EPAVTSRARRPDAPPQSA--RPRAPVDDRGDPRG 2610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 137 READARRAAEVRAREEAARRAAEPAPQASAPAPAAPSAPVEAPRAaePAPQPVQKSPIEEALSRPAQRA--PREGHREGF 214
Cdd:PHA03247 2611 PAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDD--PAPGRVSRPRRARRLGRAAQASspPQRPRRRAA 2688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 215 RDDRGPRTE----HPQGDRPQgqygdrPRPQGDRPQGDRPPFNRDRPQGDRPQGnyGDRSPRPQGDRPQGNYGERTP-RP 289
Cdd:PHA03247 2689 RPTVGSLTSladpPPPPPTPE------PAPHALVSATPLPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPARPaRP 2760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 290 QGDRPPfNRDRPQGDRPQGDRPAFNRdgnrdrPQGDRPQGDRGPRPQGdRGPRPAGETVRYSANSPRPPRAPAGVAPNAP 369
Cdd:PHA03247 2761 PTTAGP-PAPAPPAAPAAGPPRRLTR------PAVASLSESRESLPSP-WDPADPPAAVLAPAAALPPAASPAGPLPPPT 2832
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 370 AVSEVDRIRSSRGTPAGRPLGARAGDDDDRNKRGKVGAPTKAVSQTRGEPKRREGRLTLQ 429
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVS 2892
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
200-295 |
7.12e-04 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 41.56 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 200 RPAQRAPREGHREGFRDDRGPRTEHPQGDRPQGQYGDRPRPQGDRPQGDRPPFNRDRPQGDRPQGnygdrSPRPQGDRPQ 279
Cdd:pfam15240 76 PPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQG-----PPPPPPGNPQ 150
|
90
....*....|....*.
gi 557835801 280 gnyGERTPRPQGDRPP 295
Cdd:pfam15240 151 ---GPPQRPPQPGNPQ 163
|
|
| RocCOR |
cd09914 |
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ... |
559-713 |
8.84e-04 |
|
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.
Pssm-ID: 206741 [Multi-domain] Cd Length: 161 Bit Score: 41.17 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 559 VMGHVDHGKTSLLDALRKA--DVATGEAGGItqHIGAYQVRVPSGDRVTF--LDTPGHAAFSA-----MRARGanvtdIV 629
Cdd:cd09914 6 LVGQGGVGKTSLCKQLIGEkfDGDESSTHGI--NVQDWKIPAPERKKIRLnvWDFGGQEIYHAthqffLTSRS-----LY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 630 VLVVAADDGVMPQTIE---AINHARSAKTPIIVAVNKMDkhEANPQRVINELLQHEVVVEalggETQIIEVSAKTGLGLD 706
Cdd:cd09914 79 LLVFDLRTGDEVSRVPywlRQIKAFGGVSPVILVGTHID--ESCDEDILKKALNKKFPAI----INDIHFVSCKNGKGIA 152
|
....*..
gi 557835801 707 SLIEAIL 713
Cdd:cd09914 153 ELKKAIA 159
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
180-360 |
1.28e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 180 RAAEPAPQPVQKSPIEEALSRPAQRAPREGHREGfrDDRGPRTEHPQGDRPQGQYGDRPRPQGDRPQGDRPPfnRDRPQG 259
Cdd:PHA03307 767 KLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPG--RLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPA--RPPGAA 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 260 DRP----QGNYGDRSPRPQGDRPQGNYGERtprpqGDRPPFNRDRPQGDRPQGDRPAFNRDGNRDRPQGDRPQGDRGPRP 335
Cdd:PHA03307 843 ARPpparSSESSKSKPAAAGGRARGKNGRR-----RPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMP 917
|
170 180 190
....*....|....*....|....*....|.
gi 557835801 336 QGDRGPR------PAGETVrysanSPRPPRA 360
Cdd:PHA03307 918 PGGPDPRggfrrvPPGDLH-----TPAPSAA 943
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
182-392 |
1.29e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 182 AEPAPQPVQKSPieealsrPAQRAPREGHREGFRDDRGPrtEHPQGDRPQGQYGDRPRPQGDRPQGDRPPFNRDRPQGDR 261
Cdd:PRK07764 619 AAPAAPAAPAPA-------GAAAAPAEASAAPAPGVAAP--EHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 262 PQGNYGDRSPRPQGDRPQGNYGERTPRPQGdrppfnrDRPQGDRPQGDRPAFNRDGNRDRPQGDRPQGDRGPRPQGDRGP 341
Cdd:PRK07764 690 PAAPAGAAPAQPAPAPAATPPAGQADDPAA-------QPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPP 762
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 342 RPAGETVrYSANSPRPPRAPAGVAPNAPAVSEVDRIRSSRGTPAG----RPLGAR 392
Cdd:PRK07764 763 APAPAAA-PAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMelleEELGAK 816
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
180-373 |
2.28e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 180 RAAEPAPQPVQKSPIEEALSRPAQRAPREGHREgfrddRGPRTEHPQGDRpQGQYGDRPRPQGDRPQGDRPPFNRDRPQG 259
Cdd:PRK12323 393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR-----RSPAPEALAAAR-QASARGPGGAPAPAPAPAAAPAAAARPAA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 260 DRPQGNygdrsPRPQGDRPQGNYGERTPRPQGDRPPFNRDRPqgdrpqGDRPAFNRDGNRDRPQGDRPQGDRGPRPQGDR 339
Cdd:PRK12323 467 AGPRPV-----AAAAAAAPARAAPAAAPAPADDDPPPWEELP------PEFASPAPAQPDAAPAGWVAESIPDPATADPD 535
|
170 180 190
....*....|....*....|....*....|....*
gi 557835801 340 GPRPAGETVRYSANSPRPPRAPAG-VAPNAPAVSE 373
Cdd:PRK12323 536 DAFETLAPAPAAAPAPRAAAATEPvVAPRPPRASA 570
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
530-665 |
2.30e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 41.88 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 530 RVSESDVMEGFIDAEDHDDDTVVRPPVVAVMGHVDHGKTSLLDAL---RKADVAtgEAGGITQHIGAYQVrVPSGDRVTF 606
Cdd:PRK03003 14 WADESDWELDDEDLAELEAAEGGPLPVVAVVGRPNVGKSTLVNRIlgrREAVVE--DVPGVTRDRVSYDA-EWNGRRFTV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557835801 607 LDTPG--------HAAFSAMRARGANVTDIVVLVVAADDGVMPQTIEAINHARSAKTPIIVAVNKMD 665
Cdd:PRK03003 91 VDTGGwepdakglQASVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVD 157
|
|
| aeIF5B_II |
cd03703 |
Domain II of archaeal and eukaryotic Initiation Factor 5; This family represents domain II of ... |
729-774 |
2.99e-03 |
|
Domain II of archaeal and eukaryotic Initiation Factor 5; This family represents domain II of archaeal and eukaryotic IF5B. aIF5B and eIF5B are homologs of prokaryotic Initiation Factor 2 (IF2). 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 joining of 60S subunits. 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 of EF1A, eEF1A and aeIF2gamma.
Pssm-ID: 293904 [Multi-domain] Cd Length: 111 Bit Score: 38.29 E-value: 2.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 557835801 729 AEGVVIEAKLDKGRGPVATVLVKRGTLKRGDIIVAGASWG----RVRALI 774
Cdd:cd03703 2 GKGTVLEVKEEEGLGTTIDVILYDGTLREGDTIVVGGLNGpivtKVRALL 51
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
270-386 |
3.96e-03 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 40.76 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 270 SPRPQGD---RPQGNYGERTPRPQGDRPPFNRDRPQGDRPQGDRPAFNRDG-NRDRPQGDRPQGdrgprpqgdrgpRPAG 345
Cdd:PHA03264 274 SPAPPGDdrpEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGpPRPAPDADRPEG------------WPSL 341
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557835801 346 ETVrysansPRPPRAPAgvapnAPAVSEVDRIRSSRGTPAG 386
Cdd:PHA03264 342 EAI------TFPPPTPA-----TPAVPRARPVIVGTGIAAA 371
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
238-414 |
5.92e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 238 PRPQGDRPQGDRPPFNRDRP-QGDRPQGnyGDRSPRPQGDRPQGNYGERTPRPQGDRPPFNRDRPQGDRPQGDRPAFNRD 316
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPeEAARPAA--PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 317 GNRDRPQGDRPQGD-RGPRPQGDRGPRPAGETVRYSANSPRPPRAPAGVAPNAPAVSEVDRIRSSRGTPAGRPLGARAGD 395
Cdd:PRK07764 668 GWPAKAGGAAPAAPpPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
170
....*....|....*....
gi 557835801 396 DDDRNKRGKVGAPTKAVSQ 414
Cdd:PRK07764 748 PPDPAGAPAQPPPPPAPAP 766
|
|
| Rhes_like |
cd04143 |
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ... |
607-712 |
6.03e-03 |
|
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.
Pssm-ID: 133343 [Multi-domain] Cd Length: 247 Bit Score: 39.73 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 607 LDTPGHAAFSAMRARGANVTDIVVLVVAADDGVMPQTI----EAINHARS---------AKTPIIVAVNKMDKHEanPQR 673
Cdd:cd04143 53 LDTSGNHPFPAMRRLSILTGDVFILVFSLDNRESFEEVcrlrEQILETKSclknktkenVKIPMVICGNKADRDF--PRE 130
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557835801 674 VinellQHEVVVEALGGETQ--IIEVSAKTGLGLDSLIEAI 712
Cdd:cd04143 131 V-----QRDEVEQLVGGDENcaYFEVSAKKNSNLDEMFRAL 166
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
642-720 |
6.62e-03 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 40.08 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 642 QTIEAINH------ARSAKTPIIVAVNKMDKHEAnpQRVINELLqhevvvEALGgeTQIIEVSAKTGLGLDSLIEAIllq 715
Cdd:PRK12297 256 EDYEKINKelklynPRLLERPQIVVANKMDLPEA--EENLEEFK------EKLG--PKVFPISALTGQGLDELLYAV--- 322
|
....*
gi 557835801 716 AEVLD 720
Cdd:PRK12297 323 AELLE 327
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
656-717 |
7.20e-03 |
|
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 206667 [Multi-domain] Cd Length: 159 Bit Score: 38.21 E-value: 7.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557835801 656 PIIVAVNKMDkhEANPQRV-IN-ELLQhevvvEALGgeTQIIEVSAKTGLGLDSLIEAILLQAE 717
Cdd:cd01879 104 PVVVALNMID--EAEKRGIkIDlDKLS-----ELLG--VPVVPTSARKGEGIDELLDAIAKLAE 158
|
|
| PHA00666 |
PHA00666 |
putative protease |
210-280 |
7.24e-03 |
|
putative protease
Pssm-ID: 222808 [Multi-domain] Cd Length: 233 Bit Score: 39.25 E-value: 7.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557835801 210 HREGFRDDRGPRTEHPQGDRPQGQYGDRPRPQGD--RPQGDR--PPFNRDRPQGDRPQGNYGDRSPRPqGDRPQG 280
Cdd:PHA00666 9 MRRLCNEQPGDGGSQPAASEPAAGAGDNPAPQGDptQEEGDKpqPAAGADKPEGDKKADGDKPEEKKP-GEKPEG 82
|
|
| Innate_immun |
pfam12782 |
Invertebrate innate immunity transcript family; The immune response of the purple sea urchin ... |
231-361 |
8.57e-03 |
|
Invertebrate innate immunity transcript family; The immune response of the purple sea urchin appears to be more complex than previously believed in that it uses immune-related gene families homologous to vertebrate Toll-like and NOD/NALP-like receptor families as well as C-type lectins and a rudimentary complement system. In addition, the species also produces this unusual family of mRNAs, also known as 185/333, which is strongly upregulated in response to pathogen challenge.
Pssm-ID: 432781 [Multi-domain] Cd Length: 291 Bit Score: 39.37 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557835801 231 QGQYGDRPRPQGDRPQgdrppfnrDRPQGDRPQGNYGDRSPRPQ--GDRPQGNYGERTPRPQGDRP----PFNRDRPQGD 304
Cdd:pfam12782 144 RGHHGHRQGPPQDRPE--------EQPFGQRNESSDEDGRPHPRhhGRHHQHHHRNHTEGHQGHNEtgdhPHRHHNKTGD 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557835801 305 RPQgDRPAFNRDGNRDRPQGDRPQGDR-----------GPRPQGDRgpRPAGETVRYSANSPRPPRAP 361
Cdd:pfam12782 216 GDQ-DRPMFEMRPFRFNPFGRKPFGDRpfgrrngteegSPRRDGQR--RPYGNRGRWGENESEEKEHP 280
|
|
| PRK05733 |
PRK05733 |
single-stranded DNA-binding protein; Provisional |
242-320 |
9.79e-03 |
|
single-stranded DNA-binding protein; Provisional
Pssm-ID: 235585 [Multi-domain] Cd Length: 172 Bit Score: 38.37 E-value: 9.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557835801 242 GDRPQGDRppfnrdrpQGDRPQGNYGDRSPRPQGDRPQgnygertPRPQGDRPPfnrdRPQGDRPQgdrPAFNRDGNRD 320
Cdd:PRK05733 112 GGRPQGDD--------QGGQGGGNYNQSAPRQQAQRPQ-------QAAQQQSRP----APQQPAPQ---PAADFDSFDD 168
|
|
| |
