|
Name |
Accession |
Description |
Interval |
E-value |
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
36-1147 |
0e+00 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 755.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 36 GKNVKAFAITKARSAEKRFRRKEDVLTKKHHIPLVDKTPEE-PPPVLIAVVGPPKVGKSTLINNLIKNFTRTNVTNINGP 114
Cdd:COG5192 25 GNNAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDlPPPFIVAVVGPPGTGKSTLIRSLVRRFTKQTIDEIRGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 115 ITIITSKKRRITLIECNNDINSMIDIAKCADLVLLMVDASFGFEMEIFEFLNICQVHGMPKIMGILTHLDTIKTAKAVKM 194
Cdd:COG5192 105 ITVVSGKTRRITFLECPSDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILISHGMPRVLGVVTHLDLFKNPSTLRS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 195 QKKVLKHRFWTEVYDGAKLFYLSGLIHGEYVRNEIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEQIRLNPKCD 274
Cdd:COG5192 185 IKKRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNMHPYVLADRVDDLTLPVDIEQNPKVG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 275 RDVVLYGYVRGVPLKKENM-VHVAGLGDMKIEELNALPDPCPLP--STEKKRNLLEKERLLYAPMSGVGGIVYDKDAVYI 351
Cdd:COG5192 265 RKITVYGYLHGTGLPRKDMeVHIPGVGDFRMADVEVLIDPCPPPdaDHGRRRRLSLKSKLIYSPMSDIGGILKDKDRVYI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 352 ELQGSHSHKraVENTEQQELVKSVIEKKET-LDVQIENQEFRLFSDGDVIKSREFQIDDDNY---------------NED 415
Cdd:COG5192 345 EVPTSNFSK--DENSEAGEGEKMKMQLQEIeQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNvgrktrrqptgkaiaEET 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 416 SENDEESDQDSGVEESDDETGGPSRIARTGWNPEDQSEdedddhdedddedddanglSDGYGTKKSSGFlssDEEDGNne 495
Cdd:COG5192 423 SREDELSFDDSDVSTSDENEDVDFTGKKGAINNEDESD-------------------NEEVAFDSDSQF---DESEGN-- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 496 rvsnsMAWKAGLASKARndYLERQATSKNLMKIVYGVFSKFK------KDREQEELEEDAENQDDDLLGGLFKSVAQKQA 569
Cdd:COG5192 479 -----LRWKEGLASKLA--YSQSGKRGRNIQKIFYDESLSPEecieeyKGESAKSSESDLVVQDEPEDFFDVSKVANESI 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 570 EILKKKTVQDVdegcfFEEYAdgvRDWtedENKKLIRNCFVTGKWKASEDAEELLKLDDmSDGDSEvygDFEDLETGEKH 649
Cdd:COG5192 552 SSNHEKLMESE-----FEELK---KKW---SSLAQLKSRFQKDATLDSIEGEEELIQDD-EKGNFE---DLEDEENSSDN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 650 AGKSDNGGQNKADENTDSKEGENTLKRklsrieEKNMSRTELMAkkmklkakfdAEYDNPEKDDQHiEGDHQYYEKLKAD 729
Cdd:COG5192 617 EMEESRGSSVTAENEESADEVDYETER------EENARKKEELR----------GNFELEERGDPE-KKDVDWYTEEKRK 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 730 ALRQSELNKKEFSNLDDEVRLNIEGYRAGLFVRLNFKNVPSEFVDHFDAQYPVLIGGLNMAEENVGYVTCKVKKHRWYKK 809
Cdd:COG5192 680 IEEQLKINRSEFETMVPESRVVIEGYRAGRYVRIVLSHVPLEFVDEFNSRYPIVLGGLLPAEKEMGIVQGRIKRHRWHKK 759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 810 ILKAGDPLIISLGWRRFQTVPIFAKVEDDLKHRYLKYTPNHVTCSVTFWGPITPQNTGILAIQSIAYDqqetkrlgFRVA 889
Cdd:COG5192 760 ILKTNDPLIFSVGWRRFQSIPVYSMKDSRTRNRMLKYTPEHMHCNVSFYGPVVPPNTGFCAVQSEKGD--------FRVL 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 890 ATGAVSESDKSAQIMKKLKLIGTPYKIYQKTAFIQGMFNSTLEVAKFEGAKIKTVSGIRGQIKKAVPPEGSFRATFEDRI 969
Cdd:COG5192 832 ALGTITDVNGDAKLVKKLKLVGYPKQIVQNTVFVRDMFTSDLEVLKFEGASLKAVSGLRGQVKGPHGKNGEYRAVFEGKM 911
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 970 VLSDIVFCRTWFKVNVPNFYAPVTNLLLppekkiKWVGMKTLSQLKRENNIQFEAKEDSSYKPIEREDLQFRPLVIPKSL 1049
Cdd:COG5192 912 LMSDIITLRCFVPVEVHRIFIPVDNLLG------KWRGLRRLHEIRESLGLTHSYAPQNDSSSEEMGYGAEEDYSLPREI 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 1050 QKALPYKDKpklgpinpKKPLDSGRvAVVHSPHEQKVNKMMK--MIKTNFENKEEKRKQLNKQKSEKYKKQKIDNDfrKL 1127
Cdd:COG5192 986 ESKLPLDKR--------SIAVVSRR-IELPVPPECREKHEIKdrIVKERIKDQEEKERMESLQRAKEEEIGKKEKE--RE 1054
|
1130 1140
....*....|....*....|
gi 1218236368 1128 QRQKELKKKVFKAISKMEAK 1147
Cdd:COG5192 1055 QRIRKTIHDNYKEMAKKRLK 1074
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
41-271 |
2.61e-145 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 436.00 E-value: 2.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 41 AFAITKARSAEKRFRRKEDVLTKKHHIPLVDKTPEEPPPVLIAVVGPPKVGKSTLINNLIKNFTRTNVTNINGPITIITS 120
Cdd:cd01882 1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 121 KKRRITLIECNNDINSMIDIAKCADLVLLMVDASFGFEMEIFEFLNICQVHGMPKIMGILTHLDTIKTAKAVKMQKKVLK 200
Cdd:cd01882 81 KKRRLTFIECPNDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKRLK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218236368 201 HRFWTEVYDGAKLFYLSGLIHGEYVRNEIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEQIRLNP 271
Cdd:cd01882 161 HRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIRENP 231
|
|
| RIBIOP_C |
pfam04950 |
40S ribosome biogenesis protein Tsr1 and BMS1 C-terminal; RIBIOP_C is a family of eukaryotic ... |
723-983 |
1.20e-102 |
|
40S ribosome biogenesis protein Tsr1 and BMS1 C-terminal; RIBIOP_C is a family of eukaryotic proteins from the C-terminus of pre-rRNA-processing protein or ribosome biogenesis proteins BMS1 and TSR1. These proteins act, in the nucleolus, as a molecular switch during maturation of the 40S ribosomal subunit. This domain, domain IV of translation elongation factor selb, adopts the same fold as translation proteins such as domain II of GTP-elongation factor Tu proteins.
Pssm-ID: 461497 [Multi-domain] Cd Length: 284 Bit Score: 325.18 E-value: 1.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 723 YEKLKAdaLRQSELNKKE-----------FSNLDDEVR------LNIEGYRAGLFVRLNFKNVPSEFVDHFdaqyPVLIG 785
Cdd:pfam04950 16 YRGLKS--FRTSPWDPKEnlpddyarifqFENYKRTKKrvlkeaLNGAEVRPGTYVRIYIKNVPCEFVENF----PLIVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 786 GLNMAEENVGYVTCKVKKHRWYKKILKAGDPLIISLGWRRFQTVPIFAKVEDDLKHRYLKYT-PNHvTCSVTFWGPITPQ 864
Cdd:pfam04950 90 GLLPHEHKMSVVNFRIKRHRWYEKPLKSKDPLIFQVGWRRFQINPIFSQADNNNRHKYERYLhPGH-MCVATFYGPITFP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 865 NTGILAIQsiaydQQETKRLGFRVAATGAVSESDKSAQIMKKLKLIGTPYKIYQKTAFIQGMFNSTLEVAKFEGAKIKTV 944
Cdd:pfam04950 169 NTPVLAFK-----ELSSSTGGFRLVATGTVLNVDPSRIIVKRIILTGHPFKIHKKTATVRYMFFNPEDVAWFKPVELRTK 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 1218236368 945 SGIRGQIKKAVPPEGSFRATFEDRIVLSDIVFCRTWFKV 983
Cdd:pfam04950 244 SGRRGHIKESLGTHGYFKATFDGKILQQDTVFMSLYKRV 282
|
|
| AARP2CN |
smart00785 |
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ... |
228-314 |
1.67e-39 |
|
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to the GTP-binding domain of elongation factor TU.
Pssm-ID: 129021 [Multi-domain] Cd Length: 83 Bit Score: 141.15 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 228 EIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEqirlNPKCDRDVVLYGYVRGVPLKKENMVHVAGLGDMKIEEL 307
Cdd:smart00785 1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITDEE----DPKVDRTLVVYGYVRGTGLNANQLVHIPGLGDFQISKI 76
|
....*..
gi 1218236368 308 NALPDPC 314
Cdd:smart00785 77 EALPDPC 83
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
82-232 |
4.15e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 56.21 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIK----------NFTRtnvTNINGpitIITSKKRRITLI------ECNNDIN-SMIDIAKCA 144
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGqkisivspkpQTTR---HRIRG---IVTEDDAQIIFVdtpgihKPKRALNrAMNKAAWSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 145 ----DLVLLMVDASFGFEMEIFEFLNICQVHGMPKImGILTHLDTIKTakavkmQKKVLKH-RFWTEVYDGAKLFYLSGL 219
Cdd:PRK00089 82 lkdvDLVLFVVDADEKIGPGDEFILEKLKKVKTPVI-LVLNKIDLVKD------KEELLPLlEELSELMDFAEIVPISAL 154
|
170
....*....|....*.
gi 1218236368 220 iHGEYV---RNEIKNL 232
Cdd:PRK00089 155 -KGDNVdelLDVIAKY 169
|
|
| era |
TIGR00436 |
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
82-154 |
7.20e-04 |
|
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]
Pssm-ID: 129528 [Multi-domain] Cd Length: 270 Bit Score: 42.76 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIK----------NFTR----TNVTNINGPITII-----TSKKRRITLIECNNDINSMIDIak 142
Cdd:TIGR00436 3 VAILGRPNVGKSTLLNQLHGqkisitspkaQTTRnrisGIHTTGASQIIFIdtpgfHEKKHSLNRLMMKEARSAIGGV-- 80
|
90
....*....|..
gi 1218236368 143 caDLVLLMVDAS 154
Cdd:TIGR00436 81 --DLILFVVDSD 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
36-1147 |
0e+00 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 755.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 36 GKNVKAFAITKARSAEKRFRRKEDVLTKKHHIPLVDKTPEE-PPPVLIAVVGPPKVGKSTLINNLIKNFTRTNVTNINGP 114
Cdd:COG5192 25 GNNAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDlPPPFIVAVVGPPGTGKSTLIRSLVRRFTKQTIDEIRGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 115 ITIITSKKRRITLIECNNDINSMIDIAKCADLVLLMVDASFGFEMEIFEFLNICQVHGMPKIMGILTHLDTIKTAKAVKM 194
Cdd:COG5192 105 ITVVSGKTRRITFLECPSDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILISHGMPRVLGVVTHLDLFKNPSTLRS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 195 QKKVLKHRFWTEVYDGAKLFYLSGLIHGEYVRNEIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEQIRLNPKCD 274
Cdd:COG5192 185 IKKRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNMHPYVLADRVDDLTLPVDIEQNPKVG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 275 RDVVLYGYVRGVPLKKENM-VHVAGLGDMKIEELNALPDPCPLP--STEKKRNLLEKERLLYAPMSGVGGIVYDKDAVYI 351
Cdd:COG5192 265 RKITVYGYLHGTGLPRKDMeVHIPGVGDFRMADVEVLIDPCPPPdaDHGRRRRLSLKSKLIYSPMSDIGGILKDKDRVYI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 352 ELQGSHSHKraVENTEQQELVKSVIEKKET-LDVQIENQEFRLFSDGDVIKSREFQIDDDNY---------------NED 415
Cdd:COG5192 345 EVPTSNFSK--DENSEAGEGEKMKMQLQEIeQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNvgrktrrqptgkaiaEET 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 416 SENDEESDQDSGVEESDDETGGPSRIARTGWNPEDQSEdedddhdedddedddanglSDGYGTKKSSGFlssDEEDGNne 495
Cdd:COG5192 423 SREDELSFDDSDVSTSDENEDVDFTGKKGAINNEDESD-------------------NEEVAFDSDSQF---DESEGN-- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 496 rvsnsMAWKAGLASKARndYLERQATSKNLMKIVYGVFSKFK------KDREQEELEEDAENQDDDLLGGLFKSVAQKQA 569
Cdd:COG5192 479 -----LRWKEGLASKLA--YSQSGKRGRNIQKIFYDESLSPEecieeyKGESAKSSESDLVVQDEPEDFFDVSKVANESI 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 570 EILKKKTVQDVdegcfFEEYAdgvRDWtedENKKLIRNCFVTGKWKASEDAEELLKLDDmSDGDSEvygDFEDLETGEKH 649
Cdd:COG5192 552 SSNHEKLMESE-----FEELK---KKW---SSLAQLKSRFQKDATLDSIEGEEELIQDD-EKGNFE---DLEDEENSSDN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 650 AGKSDNGGQNKADENTDSKEGENTLKRklsrieEKNMSRTELMAkkmklkakfdAEYDNPEKDDQHiEGDHQYYEKLKAD 729
Cdd:COG5192 617 EMEESRGSSVTAENEESADEVDYETER------EENARKKEELR----------GNFELEERGDPE-KKDVDWYTEEKRK 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 730 ALRQSELNKKEFSNLDDEVRLNIEGYRAGLFVRLNFKNVPSEFVDHFDAQYPVLIGGLNMAEENVGYVTCKVKKHRWYKK 809
Cdd:COG5192 680 IEEQLKINRSEFETMVPESRVVIEGYRAGRYVRIVLSHVPLEFVDEFNSRYPIVLGGLLPAEKEMGIVQGRIKRHRWHKK 759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 810 ILKAGDPLIISLGWRRFQTVPIFAKVEDDLKHRYLKYTPNHVTCSVTFWGPITPQNTGILAIQSIAYDqqetkrlgFRVA 889
Cdd:COG5192 760 ILKTNDPLIFSVGWRRFQSIPVYSMKDSRTRNRMLKYTPEHMHCNVSFYGPVVPPNTGFCAVQSEKGD--------FRVL 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 890 ATGAVSESDKSAQIMKKLKLIGTPYKIYQKTAFIQGMFNSTLEVAKFEGAKIKTVSGIRGQIKKAVPPEGSFRATFEDRI 969
Cdd:COG5192 832 ALGTITDVNGDAKLVKKLKLVGYPKQIVQNTVFVRDMFTSDLEVLKFEGASLKAVSGLRGQVKGPHGKNGEYRAVFEGKM 911
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 970 VLSDIVFCRTWFKVNVPNFYAPVTNLLLppekkiKWVGMKTLSQLKRENNIQFEAKEDSSYKPIEREDLQFRPLVIPKSL 1049
Cdd:COG5192 912 LMSDIITLRCFVPVEVHRIFIPVDNLLG------KWRGLRRLHEIRESLGLTHSYAPQNDSSSEEMGYGAEEDYSLPREI 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 1050 QKALPYKDKpklgpinpKKPLDSGRvAVVHSPHEQKVNKMMK--MIKTNFENKEEKRKQLNKQKSEKYKKQKIDNDfrKL 1127
Cdd:COG5192 986 ESKLPLDKR--------SIAVVSRR-IELPVPPECREKHEIKdrIVKERIKDQEEKERMESLQRAKEEEIGKKEKE--RE 1054
|
1130 1140
....*....|....*....|
gi 1218236368 1128 QRQKELKKKVFKAISKMEAK 1147
Cdd:COG5192 1055 QRIRKTIHDNYKEMAKKRLK 1074
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
41-271 |
2.61e-145 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 436.00 E-value: 2.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 41 AFAITKARSAEKRFRRKEDVLTKKHHIPLVDKTPEEPPPVLIAVVGPPKVGKSTLINNLIKNFTRTNVTNINGPITIITS 120
Cdd:cd01882 1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 121 KKRRITLIECNNDINSMIDIAKCADLVLLMVDASFGFEMEIFEFLNICQVHGMPKIMGILTHLDTIKTAKAVKMQKKVLK 200
Cdd:cd01882 81 KKRRLTFIECPNDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKRLK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218236368 201 HRFWTEVYDGAKLFYLSGLIHGEYVRNEIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEQIRLNP 271
Cdd:cd01882 161 HRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIRENP 231
|
|
| RIBIOP_C |
pfam04950 |
40S ribosome biogenesis protein Tsr1 and BMS1 C-terminal; RIBIOP_C is a family of eukaryotic ... |
723-983 |
1.20e-102 |
|
40S ribosome biogenesis protein Tsr1 and BMS1 C-terminal; RIBIOP_C is a family of eukaryotic proteins from the C-terminus of pre-rRNA-processing protein or ribosome biogenesis proteins BMS1 and TSR1. These proteins act, in the nucleolus, as a molecular switch during maturation of the 40S ribosomal subunit. This domain, domain IV of translation elongation factor selb, adopts the same fold as translation proteins such as domain II of GTP-elongation factor Tu proteins.
Pssm-ID: 461497 [Multi-domain] Cd Length: 284 Bit Score: 325.18 E-value: 1.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 723 YEKLKAdaLRQSELNKKE-----------FSNLDDEVR------LNIEGYRAGLFVRLNFKNVPSEFVDHFdaqyPVLIG 785
Cdd:pfam04950 16 YRGLKS--FRTSPWDPKEnlpddyarifqFENYKRTKKrvlkeaLNGAEVRPGTYVRIYIKNVPCEFVENF----PLIVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 786 GLNMAEENVGYVTCKVKKHRWYKKILKAGDPLIISLGWRRFQTVPIFAKVEDDLKHRYLKYT-PNHvTCSVTFWGPITPQ 864
Cdd:pfam04950 90 GLLPHEHKMSVVNFRIKRHRWYEKPLKSKDPLIFQVGWRRFQINPIFSQADNNNRHKYERYLhPGH-MCVATFYGPITFP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 865 NTGILAIQsiaydQQETKRLGFRVAATGAVSESDKSAQIMKKLKLIGTPYKIYQKTAFIQGMFNSTLEVAKFEGAKIKTV 944
Cdd:pfam04950 169 NTPVLAFK-----ELSSSTGGFRLVATGTVLNVDPSRIIVKRIILTGHPFKIHKKTATVRYMFFNPEDVAWFKPVELRTK 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 1218236368 945 SGIRGQIKKAVPPEGSFRATFEDRIVLSDIVFCRTWFKV 983
Cdd:pfam04950 244 SGRRGHIKESLGTHGYFKATFDGKILQQDTVFMSLYKRV 282
|
|
| AARP2CN |
pfam08142 |
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ... |
228-313 |
3.53e-42 |
|
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to the GTP-binding domain of elongation factor TU.
Pssm-ID: 462369 Cd Length: 86 Bit Score: 148.81 E-value: 3.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 228 EIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEQIRLNPKCDRDVVLYGYVRGVPLKKENMVHVAGLGDMKIEEL 307
Cdd:pfam08142 1 EILNLLRFISVQKPRPLSWRDTRPYLLADRVEDITDPEDIRENPKCDGTLVVYGYVRGTPLKVNQLVHIPGLGDFQISKI 80
|
....*.
gi 1218236368 308 NALPDP 313
Cdd:pfam08142 81 EALPDP 86
|
|
| AARP2CN |
smart00785 |
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ... |
228-314 |
1.67e-39 |
|
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to the GTP-binding domain of elongation factor TU.
Pssm-ID: 129021 [Multi-domain] Cd Length: 83 Bit Score: 141.15 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 228 EIKNLGRFISVMKFRPLSWRGAHSYILADRMEDITNSEqirlNPKCDRDVVLYGYVRGVPLKKENMVHVAGLGDMKIEEL 307
Cdd:smart00785 1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITDEE----DPKVDRTLVVYGYVRGTGLNANQLVHIPGLGDFQISKI 76
|
....*..
gi 1218236368 308 NALPDPC 314
Cdd:smart00785 77 EALPDPC 83
|
|
| COG5177 |
COG5177 |
Uncharacterized conserved protein [Function unknown]; |
757-975 |
6.35e-18 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 227504 [Multi-domain] Cd Length: 769 Bit Score: 89.37 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 757 AGLFVRLNFKNVPSEFVDHFDAQYPVLIGGLNMAEENVGYVTCKVKKHRWYKKILKAGDPLIISLGWRRFQTVPIFAKVE 836
Cdd:COG5177 535 DGQMVRIKLRFPKFLYEGLIEPQILLVVYGLLEYEDKKTVHNFSLQRHFEYEVPLKSEESMVVQLGHRRVDICPLISKGS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 837 D--DLKHRYLKYTPNHVTCSVTFWGPITPQNTGIlaiqsIAYDQQETKRLGFRVAATGAVSESDKSAQIMKKLKLIGTPY 914
Cdd:COG5177 615 NspNNNQKYFRRLKPLESGVASFIGPISFGLSPV-----IIFKKSALDELSATLLASGGMNNFDGDRVIAKRAVLTGHPF 689
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218236368 915 KIYQKTAFIQGMFNSTLEVAKFEGAKIKTVSGIRGQIKKAVPPEGSFRATFEDRIVLSDIV 975
Cdd:COG5177 690 KNHKRYVTVRYMFFSPEDVMWFKNIQLFTKRGRTGFIKEPLGTHGYFKATFSGKIKSQDKV 750
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
82-225 |
3.63e-15 |
|
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: 75.02 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLI-------------KNFTRTNVTNINGPITIITS------KKRRITLIECNNDINS---MID 139
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLLyqtgaidrrgtrkETFLDTLKEERERGITIKTGvvefewPKRRINFIDTPGHEDFskeTVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 140 IAKCADLVLLMVDASFGFEMEIFEFLNICQvHGMPKIMGILTHLDTIKTAKA--VKMQ-KKVLKHRFWTEV-YDGAKLFY 215
Cdd:cd00881 82 GLAQADGALLVVDANEGVEPQTREHLNIAL-AGGLPIIVAVNKIDRVGEEDFdeVLREiKELLKLIGFTFLkGKDVPIIP 160
|
170
....*....|
gi 1218236368 216 LSGLiHGEYV 225
Cdd:cd00881 161 ISAL-TGEGI 169
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
82-177 |
2.49e-10 |
|
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: 58.78 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIKnfTRTNVTNING----PITI-ITSKKRRITLIEC-----NNDINSMIDIAKC----ADLV 147
Cdd:pfam01926 2 VALVGRPNVGKSTLINALTG--AKAIVSDYPGttrdPNEGrLELKGKQIILVDTpglieGASEGEGLGRAFLaiieADLI 79
|
90 100 110
....*....|....*....|....*....|
gi 1218236368 148 LLMVDASFGFEMEIFEFLNICQVHGMPKIM 177
Cdd:pfam01926 80 LFVVDSEEGITPLDEELLELLRENKKPIIL 109
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
82-232 |
3.87e-10 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 59.78 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIK----------NFTRTNVTNI----NGPI----T--IITSKKRritLIEC-NNDINSMIDI 140
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGqkisivspkpQTTRNRIRGIytddDAQIifvdTpgIHKPKKK---LGERmVKAAWSALKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 141 akcADLVLLMVDASFGFEMEIFEFLNICQVHGMPKIMgILTHLDTIKTakavkmQKKVLKH-RFWTEVYDGAKLFYLSGL 219
Cdd:cd04163 83 ---VDLVLFVVDASEWIGEGDEFILELLKKSKTPVIL-VLNKIDLVKD------KEDLLPLlEKLKELHPFAEIFPISAL 152
|
170
....*....|....*.
gi 1218236368 220 iHGEYV---RNEIKNL 232
Cdd:cd04163 153 -KGENVdelLEYIVEY 167
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
82-232 |
4.15e-08 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 56.21 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIK----------NFTRtnvTNINGpitIITSKKRRITLI------ECNNDIN-SMIDIAKCA 144
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGqkisivspkpQTTR---HRIRG---IVTEDDAQIIFVdtpgihKPKRALNrAMNKAAWSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 145 ----DLVLLMVDASFGFEMEIFEFLNICQVHGMPKImGILTHLDTIKTakavkmQKKVLKH-RFWTEVYDGAKLFYLSGL 219
Cdd:PRK00089 82 lkdvDLVLFVVDADEKIGPGDEFILEKLKKVKTPVI-LVLNKIDLVKD------KEELLPLlEELSELMDFAEIVPISAL 154
|
170
....*....|....*.
gi 1218236368 220 iHGEYV---RNEIKNL 232
Cdd:PRK00089 155 -KGDNVdelLDVIAKY 169
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
66-158 |
1.38e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 55.42 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 66 HIPLVDKTPEEPPPVLIAVVGPPKVGKSTLINNLIKNfTRTNVTNING----PI-TIITSKKRRITLIecnnD------- 133
Cdd:COG1160 162 LLPEEEEEEEEDDPIKIAIVGRPNVGKSSLINALLGE-ERVIVSDIAGttrdSIdTPFERDGKKYTLI----Dtagirrk 236
|
90 100 110
....*....|....*....|....*....|....*..
gi 1218236368 134 --INSMID----------IAKcADLVLLMVDASFGFE 158
Cdd:COG1160 237 gkVDEGIEkysvlrtlraIER-ADVVLLVIDATEGIT 272
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
83-184 |
2.57e-07 |
|
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: 51.69 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 83 AVVGPPKVGKSTLINNLIKNfTRTNVTNINGPiTI--------ITSKKRRITLI--------ECNNDINSMIDIAKCADL 146
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGG-EVGEVSDVPGT-TRdpdvyvkeLDKGKVKLVLVdtpgldefGGLGREELARLLLRGADL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1218236368 147 VLLMVDASFG--FEMEIFEFLNICQVHGMPKIMgILTHLD 184
Cdd:cd00882 79 ILLVVDSTDResEEDAKLLILRRLRKEGIPIIL-VGNKID 117
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
66-158 |
2.47e-06 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 51.20 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 66 HIPLVDKTPEEPPPVLIAVVGPPKVGKSTLINNLIKNfTRTNVTNING----PITI-ITSKKRRITLIecnnD------- 133
Cdd:PRK00093 160 ELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGE-ERVIVSDIAGttrdSIDTpFERDGQKYTLI----Dtagirrk 234
|
90 100 110
....*....|....*....|....*....|....*..
gi 1218236368 134 --INSMID----------IAKcADLVLLMVDASFGFE 158
Cdd:PRK00093 235 gkVTEGVEkysvirtlkaIER-ADVVLLVIDATEGIT 270
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
83-158 |
2.51e-06 |
|
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: 48.78 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 83 AVVGPPKVGKSTLINNLIKNfTRTNVTNING----PIT--IITSKKRRITLI------ECNNDINSM----IDIAKCADL 146
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQ-NVGIVSPIPGttrdPVRkeWELLPLGPVVLIdtpgldEEGGLGRERveeaRQVADRADL 79
|
90
....*....|..
gi 1218236368 147 VLLMVDASFGFE 158
Cdd:cd00880 80 VLLVVDSDLTPV 91
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
82-232 |
7.30e-06 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 49.22 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLI--KnftrtnvtningpITIITSK----KRRIT-----------------LIECNNDIN-SM 137
Cdd:COG1159 6 VAIVGRPNVGKSTLLNALVgqK-------------VSIVSPKpqttRHRIRgivtredaqivfvdtpgIHKPKRKLGrRM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 138 IDIAKCA----DLVLLMVDASFGFEMEIFEFLNICQVHGMPKImGILTHLDTIKtakavkmQKKVLKH-RFWTEVYDGAK 212
Cdd:COG1159 73 NKAAWSAledvDVILFVVDATEKIGEGDEFILELLKKLKTPVI-LVINKIDLVK-------KEELLPLlAEYSELLDFAE 144
|
170 180
....*....|....*....|...
gi 1218236368 213 LFYLSGLiHGEYV---RNEIKNL 232
Cdd:COG1159 145 IVPISAL-KGDNVdelLDEIAKL 166
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
82-169 |
2.38e-05 |
|
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: 45.95 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIkNFTRTNVTNINGpitiitskkrriT---LIECNNDINSM----IDIA------------- 141
Cdd:cd04164 6 VVIAGKPNVGKSSLLNALA-GRDRAIVSDIAG------------TtrdVIEEEIDLGGIpvrlIDTAglretedeiekig 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 1218236368 142 --------KCADLVLLMVDASFGFEMEIFEFLNICQ 169
Cdd:cd04164 73 ierareaiEEADLVLLVVDASEGLDEEDLEILELPA 108
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
82-158 |
5.78e-05 |
|
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: 45.12 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIKNfTRTNVTNING----PITI-ITSKKRRITLIEC---------NNDINSM-----IDIAK 142
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGE-ERVIVSDIAGttrdSIDVpFEYDGQKYTLIDTagirkkgkvTEGIEKYsvlrtLKAIE 83
|
90
....*....|....*.
gi 1218236368 143 CADLVLLMVDASFGFE 158
Cdd:cd01895 84 RADVVLLVLDASEGIT 99
|
|
| YlqF |
cd01856 |
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ... |
37-101 |
8.85e-05 |
|
Circularly permuted YlqF GTPase; Proteins of the YlqF 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. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).
Pssm-ID: 206749 [Multi-domain] Cd Length: 171 Bit Score: 44.44 E-value: 8.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1218236368 37 KNVKAFAITKARSAEKRFRRKEDVLTKKHHIPLVDKTPEEPPPVLIAVVGPPKVGKSTLINNLIK 101
Cdd:cd01856 73 SQGEPVLFVNAKNGKGVKKLLKKAKKLLKENEKLKAKGLLPRPLRAMVVGIPNVGKSTLINRLRG 137
|
|
| era |
TIGR00436 |
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
82-154 |
7.20e-04 |
|
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]
Pssm-ID: 129528 [Multi-domain] Cd Length: 270 Bit Score: 42.76 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIK----------NFTR----TNVTNINGPITII-----TSKKRRITLIECNNDINSMIDIak 142
Cdd:TIGR00436 3 VAILGRPNVGKSTLLNQLHGqkisitspkaQTTRnrisGIHTTGASQIIFIdtpgfHEKKHSLNRLMMKEARSAIGGV-- 80
|
90
....*....|..
gi 1218236368 143 caDLVLLMVDAS 154
Cdd:TIGR00436 81 --DLILFVVDSD 90
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
83-165 |
8.01e-04 |
|
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: 41.27 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 83 AVVGPPKVGKSTLINNLIKnfTRTNVT-NINGpIT------IITSKKRRITLI-----ECNND-----INSMIDIA-KCA 144
Cdd:cd01894 1 AIVGRPNVGKSTLFNRLTG--RRDAIVsDTPG-VTrdrkygEAEWGGREFILIdtggiEPDDEgiskeIREQAEIAiEEA 77
|
90 100
....*....|....*....|....
gi 1218236368 145 DLVLLMVDASFGF---EMEIFEFL 165
Cdd:cd01894 78 DVILFVVDGREGLtpaDEEIAKYL 101
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
74-100 |
9.64e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 43.03 E-value: 9.64e-04
10 20
....*....|....*....|....*..
gi 1218236368 74 PEEPPPVLiAVVGPPKVGKSTLINNLI 100
Cdd:PRK03003 34 EGGPLPVV-AVVGRPNVGKSTLVNRIL 59
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
82-154 |
4.17e-03 |
|
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.
Pssm-ID: 206683 [Multi-domain] Cd Length: 233 Bit Score: 40.22 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIKNFTR------TNVTNINGpitIITSKKRRITLIecnnDINSMID--------------IA 141
Cdd:cd01896 3 VALVGFPSVGKSTLLSKLTNTKSEvaayefTTLTCVPG---VMEYKGAKIQLL----DLPGIIEgasdgkgrgrqviaVA 75
|
90
....*....|...
gi 1218236368 142 KCADLVLLMVDAS 154
Cdd:cd01896 76 RTADLILIVLDAT 88
|
|
| GTPase_YlqF |
TIGR03596 |
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ... |
77-102 |
5.21e-03 |
|
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]
Pssm-ID: 274669 [Multi-domain] Cd Length: 276 Bit Score: 40.18 E-value: 5.21e-03
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
82-206 |
6.34e-03 |
|
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: 39.03 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218236368 82 IAVVGPPKVGKSTLINNLIKN-----------FTRT-NVTNINGPITII---------TSKKRRitliecnNDINSMID- 139
Cdd:cd01876 2 VAFAGRSNVGKSSLINALTNRkklartsktpgRTQLiNFFNVGDKFRLVdlpgygyakVSKEVR-------EKWGKLIEe 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1218236368 140 -IAKCADL--VLLMVDASFGFEMEIFEFLNICQVHGMPKIMgILTHLDTIKT---AKAVKMQKKVLKHRFWTE 206
Cdd:cd01876 75 yLENRENLkgVVLLIDARHGPTPIDLEMLEFLEELGIPFLI-VLTKADKLKKselAKVLKKIKEELNLFNILP 146
|
|
| |
