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Conserved domains on  [gi|6325039|ref|NP_015107|]
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GTPase BMS1 [Saccharomyces cerevisiae S288C]

Protein Classification

BMS1 family protein( domain architecture ID 11474123)

BMS1 family protein similar to Saccharomyces cerevisiae ribosome biogenesis protein BMS1, which may act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
1-1182 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: 1656.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     1 MEQSNKQHRKAKEKNTAKKKLHTQGHNAKAFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDDPPPFIVAVVGPPGT 80
Cdd:COG5192    1 MDEKKAKHSKAEKKKLKKVMDGKVGNNAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDLPPPFIVAVVGPPGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    81 GKTTLIRSLVRRMTKSTLNDIQGPITVVSGKHRRLTFLECPaDDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQ 160
Cdd:COG5192   81 GKSTLIRSLVRRFTKQTIDEIRGPITVVSGKTRRITFLECP-SDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   161 HHGMPRVLGVATHLDLFKSQSTLRASKKRLKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNE 240
Cdd:COG5192  160 SHGMPRVLGVVTHLDLFKNPSTLRSIKKRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   241 HPYMLADRFTDLTHPELIEtQGLQIDRKVAIYGYLHGTPLPSAPGTrVHIAGVGDFSVAQIEKLPDPCPTPfyqqklddf 320
Cdd:COG5192  240 HPYVLADRVDDLTLPVDIE-QNPKVGRKITVYGYLHGTGLPRKDME-VHIPGVGDFRMADVEVLIDPCPPP--------- 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   321 erekmkeeakangeitTASTTRRRkRLDDKDKLIYAPMSDVGGVLMDKDAVYIDIGKKNeePSFVPGQERGEGEKLMTGL 400
Cdd:COG5192  309 ----------------DADHGRRR-RLSLKSKLIYSPMSDIGGILKDKDRVYIEVPTSN--FSKDENSEAGEGEKMKMQL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   401 QSVEQSIAekFDGVGLQLFSNgTELHEVADHEGMDVESgeesieddegksKGRTSLRKPriYGKPVQEEDADIDNLPSDE 480
Cdd:COG5192  370 QEIEQDPG--VDGVGLQLFSN-SDAIDTVDRESSEIDN------------VGRKTRRQP--TGKAIAEETSREDELSFDD 432
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   481 EPYTNDDDVQDSEPRMVEIDFNNTGEQGAEKLALETDSEFEESEDEFSWERTAANKLKKTESKKRTWNIGKLIYMDNISP 560
Cdd:COG5192  433 SDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESLSP 512
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   561 EECIRRWRGEDDDSKDESDIEEDVDDDFFRkkdgtVTKEGNKDHAVDLEKFVPyfDTFEKLAKKWKSVDAIKERFLGAGI 640
Cdd:COG5192  513 EECIEEYKGESAKSSESDLVVQDEPEDFFD-----VSKVANESISSNHEKLME--SEFEELKKKWSSLAQLKSRFQKDAT 585
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   641 LgndnktksDSNEGGEELYgdfEDLEDGNpseqAEDNSDKESEDEDENEDTNGdddNSFTNFDAEEKKDLTMEQEREMNA 720
Cdd:COG5192  586 L--------DSIEGEEELI---QDDEKGN----FEDLEDEENSSDNEMEESRG---SSVTAENEESADEVDYETEREENA 647
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   721 AKKEKLRAQFEIEEgenfKEDDENNEYDtWYELQKAKISKQLEINNIEYQEMTPEQRQRIEGFKAGSYVRIVFEKVPMEF 800
Cdd:COG5192  648 RKKEELRGNFELEE----RGDPEKKDVD-WYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYRAGRYVRIVLSHVPLEF 722
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   801 VKNFNPKFPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDSRTRTRMLKYTPEHTY 880
Cdd:COG5192  723 VDEFNSRYPIVLGGLLPAEKEMGIVQGRIKRHRWHKKILKTNDPLIFSVGWRRFQSIPVYSMKDSRTRNRMLKYTPEHMH 802
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   881 CNAAFYGPLCSPNTPFCGVQivanSDTGNgFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVAR 960
Cdd:COG5192  803 CNVSFYGPVVPPNTGFCAVQ----SEKGD-FRVLALGTITDVNGDAKLVKKLKLVGYPKQIVQNTVFVRDMFTSDLEVLK 877
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   961 FEGAQIKTVSGIRGEIKRALSKpEGHYRAAFEDKILMSDIVILRSWYPVRVKKFYNPVTSLLLkektEWKGLRLTGQIRA 1040
Cdd:COG5192  878 FEGASLKAVSGLRGQVKGPHGK-NGEYRAVFEGKMLMSDIITLRCFVPVEVHRIFIPVDNLLG----KWRGLRRLHEIRE 952
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039  1041 AMNLETPSNPDSAYHKIERVERHFNGLKVPKAVQKELPFKsqihqmkpQKKKTYMAKRAVVLGGDEKKARSFIQKVLTIS 1120
Cdd:COG5192  953 SLGLTHSYAPQNDSSSEEMGYGAEEDYSLPREIESKLPLD--------KRSIAVVSRRIELPVPPECREKHEIKDRIVKE 1024
                       1130      1140      1150      1160      1170      1180
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325039  1121 KAKDSKRKEQKASQRKERLKKLAKMEEEKSQRDKEKKKEYFAQNGKRttmggddesRPRKMR 1182
Cdd:COG5192 1025 RIKDQEEKERMESLQRAKEEEIGKKEKEREQRIRKTIHDNYKEMAKK---------RLKKKR 1077
 
Name Accession Description Interval E-value
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
1-1182 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: 1656.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     1 MEQSNKQHRKAKEKNTAKKKLHTQGHNAKAFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDDPPPFIVAVVGPPGT 80
Cdd:COG5192    1 MDEKKAKHSKAEKKKLKKVMDGKVGNNAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDLPPPFIVAVVGPPGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    81 GKTTLIRSLVRRMTKSTLNDIQGPITVVSGKHRRLTFLECPaDDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQ 160
Cdd:COG5192   81 GKSTLIRSLVRRFTKQTIDEIRGPITVVSGKTRRITFLECP-SDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   161 HHGMPRVLGVATHLDLFKSQSTLRASKKRLKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNE 240
Cdd:COG5192  160 SHGMPRVLGVVTHLDLFKNPSTLRSIKKRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   241 HPYMLADRFTDLTHPELIEtQGLQIDRKVAIYGYLHGTPLPSAPGTrVHIAGVGDFSVAQIEKLPDPCPTPfyqqklddf 320
Cdd:COG5192  240 HPYVLADRVDDLTLPVDIE-QNPKVGRKITVYGYLHGTGLPRKDME-VHIPGVGDFRMADVEVLIDPCPPP--------- 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   321 erekmkeeakangeitTASTTRRRkRLDDKDKLIYAPMSDVGGVLMDKDAVYIDIGKKNeePSFVPGQERGEGEKLMTGL 400
Cdd:COG5192  309 ----------------DADHGRRR-RLSLKSKLIYSPMSDIGGILKDKDRVYIEVPTSN--FSKDENSEAGEGEKMKMQL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   401 QSVEQSIAekFDGVGLQLFSNgTELHEVADHEGMDVESgeesieddegksKGRTSLRKPriYGKPVQEEDADIDNLPSDE 480
Cdd:COG5192  370 QEIEQDPG--VDGVGLQLFSN-SDAIDTVDRESSEIDN------------VGRKTRRQP--TGKAIAEETSREDELSFDD 432
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   481 EPYTNDDDVQDSEPRMVEIDFNNTGEQGAEKLALETDSEFEESEDEFSWERTAANKLKKTESKKRTWNIGKLIYMDNISP 560
Cdd:COG5192  433 SDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESLSP 512
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   561 EECIRRWRGEDDDSKDESDIEEDVDDDFFRkkdgtVTKEGNKDHAVDLEKFVPyfDTFEKLAKKWKSVDAIKERFLGAGI 640
Cdd:COG5192  513 EECIEEYKGESAKSSESDLVVQDEPEDFFD-----VSKVANESISSNHEKLME--SEFEELKKKWSSLAQLKSRFQKDAT 585
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   641 LgndnktksDSNEGGEELYgdfEDLEDGNpseqAEDNSDKESEDEDENEDTNGdddNSFTNFDAEEKKDLTMEQEREMNA 720
Cdd:COG5192  586 L--------DSIEGEEELI---QDDEKGN----FEDLEDEENSSDNEMEESRG---SSVTAENEESADEVDYETEREENA 647
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   721 AKKEKLRAQFEIEEgenfKEDDENNEYDtWYELQKAKISKQLEINNIEYQEMTPEQRQRIEGFKAGSYVRIVFEKVPMEF 800
Cdd:COG5192  648 RKKEELRGNFELEE----RGDPEKKDVD-WYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYRAGRYVRIVLSHVPLEF 722
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   801 VKNFNPKFPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDSRTRTRMLKYTPEHTY 880
Cdd:COG5192  723 VDEFNSRYPIVLGGLLPAEKEMGIVQGRIKRHRWHKKILKTNDPLIFSVGWRRFQSIPVYSMKDSRTRNRMLKYTPEHMH 802
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   881 CNAAFYGPLCSPNTPFCGVQivanSDTGNgFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVAR 960
Cdd:COG5192  803 CNVSFYGPVVPPNTGFCAVQ----SEKGD-FRVLALGTITDVNGDAKLVKKLKLVGYPKQIVQNTVFVRDMFTSDLEVLK 877
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   961 FEGAQIKTVSGIRGEIKRALSKpEGHYRAAFEDKILMSDIVILRSWYPVRVKKFYNPVTSLLLkektEWKGLRLTGQIRA 1040
Cdd:COG5192  878 FEGASLKAVSGLRGQVKGPHGK-NGEYRAVFEGKMLMSDIITLRCFVPVEVHRIFIPVDNLLG----KWRGLRRLHEIRE 952
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039  1041 AMNLETPSNPDSAYHKIERVERHFNGLKVPKAVQKELPFKsqihqmkpQKKKTYMAKRAVVLGGDEKKARSFIQKVLTIS 1120
Cdd:COG5192  953 SLGLTHSYAPQNDSSSEEMGYGAEEDYSLPREIESKLPLD--------KRSIAVVSRRIELPVPPECREKHEIKDRIVKE 1024
                       1130      1140      1150      1160      1170      1180
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325039  1121 KAKDSKRKEQKASQRKERLKKLAKMEEEKSQRDKEKKKEYFAQNGKRttmggddesRPRKMR 1182
Cdd:COG5192 1025 RIKDQEEKERMESLQRAKEEEIGKKEKEREQRIRKTIHDNYKEMAKK---------RLKKKR 1077
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
30-261 2.06e-151

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: 452.56  E-value: 2.06e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    30 AFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDdPPPFIVAVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGPITVVS 109
Cdd:cd01882    1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEE-PPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   110 GKHRRLTFLECPaDDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLGVATHLDLFKSQSTLRASKKR 189
Cdd:cd01882   80 GKKRRLTFIECP-NDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325039   190 LKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHPELIETQ 261
Cdd:cd01882  159 LKHRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIREN 230
RIBIOP_C pfam04950
40S ribosome biogenesis protein Tsr1 and BMS1 C-terminal; RIBIOP_C is a family of eukaryotic ...
709-1009 1.31e-104

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: 330.96  E-value: 1.31e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     709 DLTMEQEREMNAAKKEKLRAQF--EIEEGENFKEDDEN-NEYDTWYELQKAKISKQLEInnieyqemtpeqrqriEGFKA 785
Cdd:pfam04950    2 ETPPDVPARERFAKYRGLKSFRtsPWDPKENLPDDYARiFQFENYKRTKKRVLKEALNG----------------AEVRP 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     786 GSYVRIVFEKVPMEFVKNFnpkfPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDS 865
Cdd:pfam04950   66 GTYVRIYIKNVPCEFVENF----PLIVGGLLPHEHKMSVVNFRIKRHRWYEKPLKSKDPLIFQVGWRRFQINPIFSQADN 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     866 RTRTRMLKYT-PEHTyCNAAFYGPLCSPNTPFCGVQivANSDTGNGFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKN 944
Cdd:pfam04950  142 NNRHKYERYLhPGHM-CVATFYGPITFPNTPVLAFK--ELSSSTGGFRLVATGTVLNVDPSRIIVKRIILTGHPFKIHKK 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325039     945 TAFIKDMFSSAMEVARFEGAQIKTVSGIRGEIKRALSKpEGHYRAAFEDKILMSDIVILRSWYPV 1009
Cdd:pfam04950  219 TATVRYMFFNPEDVAWFKPVELRTKSGRRGHIKESLGT-HGYFKATFDGKILQQDTVFMSLYKRV 282
AARP2CN smart00785
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
219-308 2.87e-37

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: 134.61  E-value: 2.87e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      219 EILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHpelieTQGLQIDRKVAIYGYLHGTPLPsaPGTRVHIAGVGDFSV 298
Cdd:smart00785    1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITD-----EEDPKVDRTLVVYGYVRGTGLN--ANQLVHIPGLGDFQI 73
                            90
                    ....*....|
gi 6325039      299 AQIEKLPDPC 308
Cdd:smart00785   74 SKIEALPDPC 83
 
Name Accession Description Interval E-value
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
1-1182 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: 1656.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     1 MEQSNKQHRKAKEKNTAKKKLHTQGHNAKAFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDDPPPFIVAVVGPPGT 80
Cdd:COG5192    1 MDEKKAKHSKAEKKKLKKVMDGKVGNNAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDLPPPFIVAVVGPPGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    81 GKTTLIRSLVRRMTKSTLNDIQGPITVVSGKHRRLTFLECPaDDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQ 160
Cdd:COG5192   81 GKSTLIRSLVRRFTKQTIDEIRGPITVVSGKTRRITFLECP-SDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   161 HHGMPRVLGVATHLDLFKSQSTLRASKKRLKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNE 240
Cdd:COG5192  160 SHGMPRVLGVVTHLDLFKNPSTLRSIKKRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   241 HPYMLADRFTDLTHPELIEtQGLQIDRKVAIYGYLHGTPLPSAPGTrVHIAGVGDFSVAQIEKLPDPCPTPfyqqklddf 320
Cdd:COG5192  240 HPYVLADRVDDLTLPVDIE-QNPKVGRKITVYGYLHGTGLPRKDME-VHIPGVGDFRMADVEVLIDPCPPP--------- 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   321 erekmkeeakangeitTASTTRRRkRLDDKDKLIYAPMSDVGGVLMDKDAVYIDIGKKNeePSFVPGQERGEGEKLMTGL 400
Cdd:COG5192  309 ----------------DADHGRRR-RLSLKSKLIYSPMSDIGGILKDKDRVYIEVPTSN--FSKDENSEAGEGEKMKMQL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   401 QSVEQSIAekFDGVGLQLFSNgTELHEVADHEGMDVESgeesieddegksKGRTSLRKPriYGKPVQEEDADIDNLPSDE 480
Cdd:COG5192  370 QEIEQDPG--VDGVGLQLFSN-SDAIDTVDRESSEIDN------------VGRKTRRQP--TGKAIAEETSREDELSFDD 432
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   481 EPYTNDDDVQDSEPRMVEIDFNNTGEQGAEKLALETDSEFEESEDEFSWERTAANKLKKTESKKRTWNIGKLIYMDNISP 560
Cdd:COG5192  433 SDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESLSP 512
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   561 EECIRRWRGEDDDSKDESDIEEDVDDDFFRkkdgtVTKEGNKDHAVDLEKFVPyfDTFEKLAKKWKSVDAIKERFLGAGI 640
Cdd:COG5192  513 EECIEEYKGESAKSSESDLVVQDEPEDFFD-----VSKVANESISSNHEKLME--SEFEELKKKWSSLAQLKSRFQKDAT 585
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   641 LgndnktksDSNEGGEELYgdfEDLEDGNpseqAEDNSDKESEDEDENEDTNGdddNSFTNFDAEEKKDLTMEQEREMNA 720
Cdd:COG5192  586 L--------DSIEGEEELI---QDDEKGN----FEDLEDEENSSDNEMEESRG---SSVTAENEESADEVDYETEREENA 647
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   721 AKKEKLRAQFEIEEgenfKEDDENNEYDtWYELQKAKISKQLEINNIEYQEMTPEQRQRIEGFKAGSYVRIVFEKVPMEF 800
Cdd:COG5192  648 RKKEELRGNFELEE----RGDPEKKDVD-WYTEEKRKIEEQLKINRSEFETMVPESRVVIEGYRAGRYVRIVLSHVPLEF 722
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   801 VKNFNPKFPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDSRTRTRMLKYTPEHTY 880
Cdd:COG5192  723 VDEFNSRYPIVLGGLLPAEKEMGIVQGRIKRHRWHKKILKTNDPLIFSVGWRRFQSIPVYSMKDSRTRNRMLKYTPEHMH 802
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   881 CNAAFYGPLCSPNTPFCGVQivanSDTGNgFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVAR 960
Cdd:COG5192  803 CNVSFYGPVVPPNTGFCAVQ----SEKGD-FRVLALGTITDVNGDAKLVKKLKLVGYPKQIVQNTVFVRDMFTSDLEVLK 877
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   961 FEGAQIKTVSGIRGEIKRALSKpEGHYRAAFEDKILMSDIVILRSWYPVRVKKFYNPVTSLLLkektEWKGLRLTGQIRA 1040
Cdd:COG5192  878 FEGASLKAVSGLRGQVKGPHGK-NGEYRAVFEGKMLMSDIITLRCFVPVEVHRIFIPVDNLLG----KWRGLRRLHEIRE 952
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039  1041 AMNLETPSNPDSAYHKIERVERHFNGLKVPKAVQKELPFKsqihqmkpQKKKTYMAKRAVVLGGDEKKARSFIQKVLTIS 1120
Cdd:COG5192  953 SLGLTHSYAPQNDSSSEEMGYGAEEDYSLPREIESKLPLD--------KRSIAVVSRRIELPVPPECREKHEIKDRIVKE 1024
                       1130      1140      1150      1160      1170      1180
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325039  1121 KAKDSKRKEQKASQRKERLKKLAKMEEEKSQRDKEKKKEYFAQNGKRttmggddesRPRKMR 1182
Cdd:COG5192 1025 RIKDQEEKERMESLQRAKEEEIGKKEKEREQRIRKTIHDNYKEMAKK---------RLKKKR 1077
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
30-261 2.06e-151

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: 452.56  E-value: 2.06e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    30 AFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDdPPPFIVAVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGPITVVS 109
Cdd:cd01882    1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEE-PPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   110 GKHRRLTFLECPaDDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLGVATHLDLFKSQSTLRASKKR 189
Cdd:cd01882   80 GKKRRLTFIECP-NDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325039   190 LKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHPELIETQ 261
Cdd:cd01882  159 LKHRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIREN 230
RIBIOP_C pfam04950
40S ribosome biogenesis protein Tsr1 and BMS1 C-terminal; RIBIOP_C is a family of eukaryotic ...
709-1009 1.31e-104

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: 330.96  E-value: 1.31e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     709 DLTMEQEREMNAAKKEKLRAQF--EIEEGENFKEDDEN-NEYDTWYELQKAKISKQLEInnieyqemtpeqrqriEGFKA 785
Cdd:pfam04950    2 ETPPDVPARERFAKYRGLKSFRtsPWDPKENLPDDYARiFQFENYKRTKKRVLKEALNG----------------AEVRP 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     786 GSYVRIVFEKVPMEFVKNFnpkfPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDS 865
Cdd:pfam04950   66 GTYVRIYIKNVPCEFVENF----PLIVGGLLPHEHKMSVVNFRIKRHRWYEKPLKSKDPLIFQVGWRRFQINPIFSQADN 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     866 RTRTRMLKYT-PEHTyCNAAFYGPLCSPNTPFCGVQivANSDTGNGFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKN 944
Cdd:pfam04950  142 NNRHKYERYLhPGHM-CVATFYGPITFPNTPVLAFK--ELSSSTGGFRLVATGTVLNVDPSRIIVKRIILTGHPFKIHKK 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325039     945 TAFIKDMFSSAMEVARFEGAQIKTVSGIRGEIKRALSKpEGHYRAAFEDKILMSDIVILRSWYPV 1009
Cdd:pfam04950  219 TATVRYMFFNPEDVAWFKPVELRTKSGRRGHIKESLGT-HGYFKATFDGKILQQDTVFMSLYKRV 282
AARP2CN pfam08142
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
219-307 8.95e-41

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: 144.57  E-value: 8.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039     219 EILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHPELIETQGlQIDRKVAIYGYLHGTPLpsAPGTRVHIAGVGDFSV 298
Cdd:pfam08142    1 EILNLLRFISVQKPRPLSWRDTRPYLLADRVEDITDPEDIRENP-KCDGTLVVYGYVRGTPL--KVNQLVHIPGLGDFQI 77

                   ....*....
gi 6325039     299 AQIEKLPDP 307
Cdd:pfam08142   78 SKIEALPDP 86
AARP2CN smart00785
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
219-308 2.87e-37

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: 134.61  E-value: 2.87e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      219 EILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHpelieTQGLQIDRKVAIYGYLHGTPLPsaPGTRVHIAGVGDFSV 298
Cdd:smart00785    1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITD-----EEDPKVDRTLVVYGYVRGTGLN--ANQLVHIPGLGDFQI 73
                            90
                    ....*....|
gi 6325039      299 AQIEKLPDPC 308
Cdd:smart00785   74 SKIEALPDPC 83
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
71-222 2.21e-22

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: 95.82  E-value: 2.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    71 IVAVVGPPGTGKTTLIRSLV--------RRMTKSTLNDIQGP-----ITVVSG------KHRRLTFLECP--ADDLNAMI 129
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLyqtgaidrRGTRKETFLDTLKEerergITIKTGvvefewPKRRINFIDTPghEDFSKETV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   130 DIAKIADLVLLLIDGNFGFEMETMEFLNIAQhHGMPRVLGVATHLDLF---KSQSTLRASKKRLKHRFWTEV-YQGAKLF 205
Cdd:cd00881   81 RGLAQADGALLVVDANEGVEPQTREHLNIAL-AGGLPIIVAVNKIDRVgeeDFDEVLREIKELLKLIGFTFLkGKDVPII 159
                        170
                 ....*....|....*...
gi 6325039   206 YLSGVIN-GRYPDREILN 222
Cdd:cd00881  160 PISALTGeGIEELLDAIV 177
COG5177 COG5177
Uncharacterized conserved protein [Function unknown];
586-1003 1.07e-17

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227504 [Multi-domain]  Cd Length: 769  Bit Score: 88.60  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   586 DDFFRKKDGTVTKEGNKDHAVDLEKFVPYFDTFEKLAKKWKSVDAikerFLGAGILGNDNKTKSDSNEGGEELYGDFEDL 665
Cdd:COG5177  343 EDLRSDYDEDFEYDGLTTVRIDDHGFLPGREQTSKKAAVPKGTSF----YQAKWAEDEEEEDGQCNDEESTMSAIDDDDP 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   666 EDGNPSEQAEDNSDKESEDEDENEDTNGDDDNSFTNFDAEEKKDLTMEQEREM--NAAKKEKLR----------AQFEIE 733
Cdd:COG5177  419 KENDNEEVAGDEESAIDDNEGFEELSPEEEERQLREFRDMEKEDREFPDEAELqpSESAIERYKeyrglrnlytCSWRSD 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   734 EgenfKEDDENNEYDTWYELQKAKISKQLEINNIEYQEMTPEQRQRIegfkagsyvrivFEKVPMEFVKNFN-PKFPIVM 812
Cdd:COG5177  499 E----KDPSFPEEWKSLVFFDNYRNAKNLVVKKDNESVAPDGQMVRI------------KLRFPKFLYEGLIePQILLVV 562
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   813 GGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDSRT--RTRMLKYTPEHTYCNAAFYGPLC 890
Cdd:COG5177  563 YGLLEYEDKKTVHNFSLQRHFEYEVPLKSEESMVVQLGHRRVDICPLISKGSNSPnnNQKYFRRLKPLESGVASFIGPIS 642
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039   891 SPNTPfcgVQIVANSDT-GNGFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVARFEGAQIKTV 969
Cdd:COG5177  643 FGLSP---VIIFKKSALdELSATLLASGGMNNFDGDRVIAKRAVLTGHPFKNHKRYVTVRYMFFSPEDVMWFKNIQLFTK 719
                        410       420       430
                 ....*....|....*....|....*....|....
gi 6325039   970 SGIRGEIKRALSKpEGHYRAAFEDKILMSDIVIL 1003
Cdd:COG5177  720 RGRTGFIKEPLGT-HGYFKATFSGKIKSQDKVAM 752
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
73-176 5.22e-08

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: 53.61  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    73 AVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGPITVVSGKH------RRLTFLECP-------ADDLNAMIDIAKIADLVL 139
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKeldkgkVKLVLVDTPgldefggLGREELARLLLRGADLIL 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6325039   140 LLIDGNFG--FEMETMEFLNIAQHHGMPRVLgVATHLDL 176
Cdd:cd00882   81 LVVDSTDResEEDAKLLILRRLRKEGIPIIL-VGNKIDL 118
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
72-168 1.29e-07

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: 51.08  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      72 VAVVGPPGTGKTTLIRSLVRRMTKS------TLNDIQGPITvVSGKHRRLT----FLECPADDLNAMIDIAKI--ADLVL 139
Cdd:pfam01926    2 VALVGRPNVGKSTLINALTGAKAIVsdypgtTRDPNEGRLE-LKGKQIILVdtpgLIEGASEGEGLGRAFLAIieADLIL 80
                           90       100
                   ....*....|....*....|....*....
gi 6325039     140 LLIDGNFGFEMETMEFLNIAQHHGMPRVL 168
Cdd:pfam01926   81 FVVDSEEGITPLDEELLELLRENKKPIIL 109
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
71-201 2.50e-06

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: 49.06  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      71 IVAVVGPPGTGKTTLIRSLVR---RMTKSTLNDIQGP-------------ITV------VSGKHRRLTFLECP--ADDLN 126
Cdd:pfam00009    5 NIGIIGHVDHGKTTLTDRLLYytgAISKRGEVKGEGEagldnlpeerergITIksaavsFETKDYLINLIDTPghVDFVK 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325039     127 AMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLgVATHLDLfKSQSTLRASKKRLKHRFWTEVYQG 201
Cdd:pfam00009   85 EVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIV-FINKMDR-VDGAELEEVVEEVSRELLEKYGED 157
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
72-208 6.21e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 48.05  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    72 VAVVGPPGTGKTTLIRSLVRRMTksTLNDIQGPITVVSGKHRrltfLECPADDLNAMI-DIA----------------KI 134
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIF--SLEKYLSTNGVTIDKKE----LKLDGLDVDLVIwDTPgqdefretrqfyarqlTG 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325039   135 ADLVLLLIDGNFGFEMETMEFL--NIAQHHGMPRVLGVATHLDLFKSQStlRASKKRLKHRFwtEVYQGAKLFYLS 208
Cdd:COG1100   80 ASLYLFVVDGTREETLQSLYELleSLRRLGKKSPIILVLNKIDLYDEEE--IEDEERLKEAL--SEDNIVEVVATS 151
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
72-208 1.96e-05

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: 46.30  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    72 VAVVGPPGTGKTTLIRSLVRR----MTK---STLNDIQGPIT-------------VVSGKHRRLTFLecpaddLNAMIDI 131
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQkisiVSPkpqTTRNRIRGIYTdddaqiifvdtpgIHKPKKKLGERM------VKAAWSA 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325039   132 AKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLgVATHLDLFKSQSTLraskkrLKH-RFWTEVYQGAKLFYLS 208
Cdd:cd04163   80 LKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVIL-VLNKIDLVKDKEDL------LPLlEKLKELHPFAEIFPIS 150
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
73-176 2.04e-05

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: 46.08  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    73 AVVGPPGTGKTTLIRSLVRRMTKSTlNDIQG----PITVVSGKH--RRLTFLECP----ADDLNAM-----IDIAKIADL 137
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIV-SPIPGttrdPVRKEWELLplGPVVLIDTPgldeEGGLGRErveeaRQVADRADL 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6325039   138 VLLLIDGNFGFEmETMEFLNIAQHHGMPrVLGVATHLDL 176
Cdd:cd00880   80 VLLVVDSDLTPV-EEEAKLGLLRERGKP-VLLVLNKIDL 116
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
74-143 2.49e-05

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 44.89  E-value: 2.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      74 VVGPPGTGKTTLIRSLVRRMtkstlndiQGPITVVSGKHRRLTFLECPADDLNAMIDIAKIADLVLLLID 143
Cdd:pfam00004    3 LYGPPGTGKTTLAKAVAKEL--------GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFID 64
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
72-193 4.75e-05

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: 46.43  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    72 VAVVGPPGTGKTTLIRSLVRRM----------TKSTLND-----------IQ-GPITVVSGKHrRLTFLECPADD----- 124
Cdd:cd04170    2 IALVGHSGSGKTTLAEALLYATgaidrlgrveDGNTVSDydpeekkrkmsIEtSVAPLEWNGH-KINLIDTPGYAdfvge 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325039   125 -LNAMidiaKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLgVATHLDLFKS--QSTLRASKKRLKHR 193
Cdd:cd04170   81 tLSAL----RAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRII-FINKMDRARAdfDKTLAALREAFGRP 147
AAA_22 pfam13401
AAA domain;
71-168 1.50e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.71  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      71 IVAVVGPPGTGKTTLIRSLVRR-------------MTKSTLNDIQgpITVVSGKHRRLTFLECPADDLNAMIDIAK-IAD 136
Cdd:pfam13401    7 ILVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlPSGTSPKDLL--RALLRALGLPLSGRLSKEELLAALQQLLLaLAV 84
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 6325039     137 LVLLLIDG--NFGFEMetMEFLNI---AQHHGMPRVL 168
Cdd:pfam13401   85 AVVLIIDEaqHLSLEA--LEELRDllnLSSKLLQLIL 119
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
68-143 2.31e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 2.31e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039       68 PPFIVAVVGPPGTGKTTLIRSLVRRMTKST----LNDIQGPITVVSGKHRRLTFLECP-----ADDLNAMIDIAKIADLV 138
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGggviYIDGEDILEEVLDQLLLIIVGGKKasgsgELRLRLALALARKLKPD 80

                    ....*
gi 6325039      139 LLLID 143
Cdd:smart00382   81 VLILD 85
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
71-112 4.81e-04

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 41.07  E-value: 4.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 6325039    71 IVAVVGPPGTGKTTLIRSLVRRMTKSTLNDiqgPITVVSGKH 112
Cdd:cd17934    1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGK---RVLVTAQSN 39
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
72-193 7.59e-04

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 41.14  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      72 VAVVGPPGTGKTTLIRSLVRRMTKSTLN--DIQGPItVVSGKHRRLTFLECPADDLNAMIDIAKIA-----DLVlllIDG 144
Cdd:pfam13671    2 ILLVGLPGSGKSTLARRLLEELGAVRLSsdDERKRL-FGEGRPSISYYTDATDRTYERLHELARIAlragrPVI---LDA 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 6325039     145 NFGFEMETMEFLNIAQHHGMPRVLgvathLDLFKSQSTLRAskkRLKHR 193
Cdd:pfam13671   78 TNLRRDERARLLALAREYGVPVRI-----VVFEAPEEVLRE---RLAAR 118
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
71-93 1.42e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 41.70  E-value: 1.42e-03
                         10        20
                 ....*....|....*....|...
gi 6325039    71 IVAVVGPPGTGKTTLIRSLVRRM 93
Cdd:COG3267   45 FVVLTGEVGTGKTTLLRRLLERL 67
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
67-143 1.56e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.21  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    67 PPPFIVAVVGPPGTGKTTLIRSLVRRmtkstLNDIQGPITVVSGKHRRLTFLECPADDLNA---MIDIAKIADLVLLLID 143
Cdd:cd00009   17 PPPKNLLLYGPPGTGKTTLARAIANE-----LFRPGAPFLYLNASDLLEGLVVAELFGHFLvrlLFELAEKAKPGVLFID 91
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
59-116 2.63e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.18  E-value: 2.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325039      59 VDRTPEDDPPpfIVAVVGPPGTGKTTLIRSLVRRMTKSTlndiqgpITVVSGKHRRLT 116
Cdd:pfam13191   16 LDRVRSGRPP--SVLLTGEAGTGKTTLLRELLRALERDG-------GYFLRGKCDENL 64
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
71-139 3.01e-03

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 39.78  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    71 IVAVVGPPGTGKTTLIRSLVRRMTKSTLN-----------DIQGP-------------ITVVSGKHRRLTFLECPAD-DL 125
Cdd:COG1763    3 VLGIVGYSGSGKTTLLEKLIPELKARGLRvgtikhahhdfDIDTPgkdsyrhreagadEVLVASPERWALMTELPEEpSL 82
                         90
                 ....*....|....
gi 6325039   126 NAMIDIAKIADLVL 139
Cdd:COG1763   83 DELLARLDDVDLVL 96
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
40-141 4.77e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 39.94  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    40 ARTMQRSSDVNERKLHVPMVDRTPEDDPPPFIVAVVGPPGTGKTTLIRSLVRRMTKSTlndIQGPITVVSGK-HRRLTFL 118
Cdd:COG2401   27 VAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP---VAGCVDVPDNQfGREASLI 103
                         90       100
                 ....*....|....*....|....*...
gi 6325039   119 EC--PADDLNAMIDI---AKIADLVLLL 141
Cdd:COG2401  104 DAigRKGDFKDAVELlnaVGLSDAVLWL 131
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1056-1181 5.98e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 5.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039    1056 KIERVERHFNGLKVPKAVQKElpfksqiHQMKPQKKKTYMAKravvLGGDEKKARSFIQKVLTISKAKDSKRKEQKASQR 1135
Cdd:pfam17380  390 KNERVRQELEAARKVKILEEE-------RQRKIQQQKVEMEQ----IRAEQEEARQREVRRLEEERAREMERVRLEEQER 458
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 6325039    1136 KERLKKLAKMEEE----KSQRDKEKKKEYFAQNGKRTTMGGDDESRPRKM 1181
Cdd:pfam17380  459 QQQVERLRQQEEErkrkKLELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
72-144 6.08e-03

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 38.83  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325039      72 VAVVGPPGTGKTTLIRSLVRRMTKSTLN-DIQGPITVVSGKHRRLTFLECPAD-------DLNAMID-----IAKIADLV 138
Cdd:pfam05729    3 VILQGEAGSGKTTLLQKLALLWAQGKLPqGFDFVFFLPCRELSRSGNARSLADllfsqwpEPAAPVSevwavILELPERL 82

                   ....*.
gi 6325039     139 LLLIDG 144
Cdd:pfam05729   83 LLILDG 88
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
69-93 8.75e-03

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 38.89  E-value: 8.75e-03
                         10        20
                 ....*....|....*....|....*
gi 6325039    69 PFIVAVVGPPGTGKTTLIRSLVRRM 93
Cdd:COG0378   13 VLAVNLMGSPGSGKTTLLEKTIRAL 37
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
69-104 9.40e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 39.25  E-value: 9.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 6325039      69 PFIVAVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGP 104
Cdd:pfam13086   13 SHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAG 48
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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