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Conserved domains on  [gi|2217279553|ref|XP_047281998|]
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ribosome biogenesis protein BMS1 homolog isoform X4 [Homo sapiens]

Protein Classification

BMS1 and AARP2CN domain-containing protein( domain architecture ID 10111837)

BMS1 and AARP2CN domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
44-273 2.25e-169

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: 490.31  E-value: 2.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  44 AFAVQSAVRMARSFHRTQDLKTKKHHIPVVDRTPLEPPPIVVVVMGPPKVGKSTLIQCLIRNFTRQKLTEIRGPVTIVSG 123
Cdd:cd01882     1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 124 KKRRLTIIECGCDINMMIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMGVLTHLDSFKHNKQLKKTKKRLK 203
Cdd:cd01882    81 KKRRLTFIECPNDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 204 HRFWTEVYPGAKLFYLSGMVHGEYQNQEIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTN 273
Cdd:cd01882   161 HRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIREN 230
AARP2CN smart00785
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
231-317 1.25e-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: 135.38  E-value: 1.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  231 EIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNpediRTNIKCDRKVSLYGYLRGAHLKNKSQIHMPGVGDFAVSDI 310
Cdd:smart00785   1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITD----EEDPKVDRTLVVYGYVRGTGLNANQLVHIPGLGDFQISKI 76

                   ....*..
gi 2217279553  311 SFLPDPC 317
Cdd:smart00785  77 EALPDPC 83
 
Name Accession Description Interval E-value
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
44-273 2.25e-169

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: 490.31  E-value: 2.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  44 AFAVQSAVRMARSFHRTQDLKTKKHHIPVVDRTPLEPPPIVVVVMGPPKVGKSTLIQCLIRNFTRQKLTEIRGPVTIVSG 123
Cdd:cd01882     1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 124 KKRRLTIIECGCDINMMIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMGVLTHLDSFKHNKQLKKTKKRLK 203
Cdd:cd01882    81 KKRRLTFIECPNDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 204 HRFWTEVYPGAKLFYLSGMVHGEYQNQEIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTN 273
Cdd:cd01882   161 HRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIREN 230
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
41-410 4.28e-137

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 435.71  E-value: 4.28e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553   41 NPKAFAVQSAVRMARSFHRTQDLKTKKHHIPVVDRTPLE-PPPIVVVVMGPPKVGKSTLIQCLIRNFTRQKLTEIRGPVT 119
Cdd:COG5192     27 NAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDlPPPFIVAVVGPPGTGKSTLIRSLVRRFTKQTIDEIRGPIT 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  120 IVSGKKRRLTIIECGCDINMMIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMGVLTHLDSFKHNKQLKKTK 199
Cdd:COG5192    107 VVSGKTRRITFLECPSDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILISHGMPRVLGVVTHLDLFKNPSTLRSIK 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  200 KRLKHRFWTEVYPGAKLFYLSGMVHGEYQNQEIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTNIKCDRK 279
Cdd:COG5192    187 KRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNMHPYVLADRVDDLTLPVDIEQNPKVGRK 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  280 VSLYGYLRGAHL-KNKSQIHMPGVGDFAVSDISFLPDPCALPEQQK--KRCLNEKEKLVYAPLSGVGGVLYDKDAVYVDL 356
Cdd:COG5192    267 ITVYGYLHGTGLpRKDMEVHIPGVGDFRMADVEVLIDPCPPPDADHgrRRRLSLKSKLIYSPMSDIGGILKDKDRVYIEV 346
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217279553  357 GGSHVFQD---EVGPTHELVQSLISTHStiDAKMASSRVTLFSDSKPLG-----SEDIDNQG 410
Cdd:COG5192    347 PTSNFSKDensEAGEGEKMKMQLQEIEQ--DPGVDGVGLQLFSNSDAIDtvdreSSEIDNVG 406
AARP2CN pfam08142
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
231-316 3.16e-43

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: 151.12  E-value: 3.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 231 EIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTNIKCDRKVSLYGYLRGAHLKNKSQIHMPGVGDFAVSDI 310
Cdd:pfam08142   1 EILNLLRFISVQKPRPLSWRDTRPYLLADRVEDITDPEDIRENPKCDGTLVVYGYVRGTPLKVNQLVHIPGLGDFQISKI 80

                  ....*.
gi 2217279553 311 SFLPDP 316
Cdd:pfam08142  81 EALPDP 86
AARP2CN smart00785
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
231-317 1.25e-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: 135.38  E-value: 1.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  231 EIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNpediRTNIKCDRKVSLYGYLRGAHLKNKSQIHMPGVGDFAVSDI 310
Cdd:smart00785   1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITD----EEDPKVDRTLVVYGYVRGTGLNANQLVHIPGLGDFQISKI 76

                   ....*..
gi 2217279553  311 SFLPDPC 317
Cdd:smart00785  77 EALPDPC 83
 
Name Accession Description Interval E-value
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
44-273 2.25e-169

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: 490.31  E-value: 2.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  44 AFAVQSAVRMARSFHRTQDLKTKKHHIPVVDRTPLEPPPIVVVVMGPPKVGKSTLIQCLIRNFTRQKLTEIRGPVTIVSG 123
Cdd:cd01882     1 AFAVQSAVRAARQFQRTQDLEEKKLHVPVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIKRYTKQNLSDIKGPITIVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 124 KKRRLTIIECGCDINMMIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMGVLTHLDSFKHNKQLKKTKKRLK 203
Cdd:cd01882    81 KKRRLTFIECPNDINSMIDVAKIADLVLLLIDGSYGFEMETFEFLNILQVHGFPKVMGVLTHLDKFKNNKTLRKTKKRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 204 HRFWTEVYPGAKLFYLSGMVHGEYQNQEIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTN 273
Cdd:cd01882   161 HRFWTEVYDGAKLFYLSGIVHGRYPKTEILNLARFISVMKFRPLNWRNSHPYVLADRMEDLTNPEDIREN 230
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
41-410 4.28e-137

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 435.71  E-value: 4.28e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553   41 NPKAFAVQSAVRMARSFHRTQDLKTKKHHIPVVDRTPLE-PPPIVVVVMGPPKVGKSTLIQCLIRNFTRQKLTEIRGPVT 119
Cdd:COG5192     27 NAKAFAVAAIGQMARQAMRTADIEEKKLHVPMVDRTPKDlPPPFIVAVVGPPGTGKSTLIRSLVRRFTKQTIDEIRGPIT 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  120 IVSGKKRRLTIIECGCDINMMIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMGVLTHLDSFKHNKQLKKTK 199
Cdd:COG5192    107 VVSGKTRRITFLECPSDLHQMIDVAKIADLVLLLIDGNFGFEMETMEFLNILISHGMPRVLGVVTHLDLFKNPSTLRSIK 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  200 KRLKHRFWTEVYPGAKLFYLSGMVHGEYQNQEIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTNIKCDRK 279
Cdd:COG5192    187 KRLKHRFWTEIYQGAKLFYLSGVENGRYPDREILNLSRFISVMKFRPLEWRNMHPYVLADRVDDLTLPVDIEQNPKVGRK 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  280 VSLYGYLRGAHL-KNKSQIHMPGVGDFAVSDISFLPDPCALPEQQK--KRCLNEKEKLVYAPLSGVGGVLYDKDAVYVDL 356
Cdd:COG5192    267 ITVYGYLHGTGLpRKDMEVHIPGVGDFRMADVEVLIDPCPPPDADHgrRRRLSLKSKLIYSPMSDIGGILKDKDRVYIEV 346
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217279553  357 GGSHVFQD---EVGPTHELVQSLISTHStiDAKMASSRVTLFSDSKPLG-----SEDIDNQG 410
Cdd:COG5192    347 PTSNFSKDensEAGEGEKMKMQLQEIEQ--DPGVDGVGLQLFSNSDAIDtvdreSSEIDNVG 406
AARP2CN pfam08142
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
231-316 3.16e-43

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: 151.12  E-value: 3.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 231 EIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNPEDIRTNIKCDRKVSLYGYLRGAHLKNKSQIHMPGVGDFAVSDI 310
Cdd:pfam08142   1 EILNLLRFISVQKPRPLSWRDTRPYLLADRVEDITDPEDIRENPKCDGTLVVYGYVRGTPLKVNQLVHIPGLGDFQISKI 80

                  ....*.
gi 2217279553 311 SFLPDP 316
Cdd:pfam08142  81 EALPDP 86
AARP2CN smart00785
AARP2CN (NUC121) domain; This domain is the central domain of AARP2. It is weakly similar to ...
231-317 1.25e-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: 135.38  E-value: 1.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  231 EIHNLGRFITVMKFRPLTWQTSHPYILADRMEDLTNpediRTNIKCDRKVSLYGYLRGAHLKNKSQIHMPGVGDFAVSDI 310
Cdd:smart00785   1 EILNLLRFLSVMKPRPLSWRDQHPYMLADRVEDITD----EEDPKVDRTLVVYGYVRGTGLNANQLVHIPGLGDFQISKI 76

                   ....*..
gi 2217279553  311 SFLPDPC 317
Cdd:smart00785  77 EALPDPC 83
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
85-227 1.45e-16

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: 78.49  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  85 VVVMGPPKVGKSTLIQCLI-------RNFTRQKLT------EIRGPVTIVSG------KKRRLTIIECGCD---INMMID 142
Cdd:cd00881     2 VGVIGHVDHGKTTLTGSLLyqtgaidRRGTRKETFldtlkeERERGITIKTGvvefewPKRRINFIDTPGHedfSKETVR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 143 LAKVADLVLMLIDASFGFEMETFEFLNICQvHGFPKIMGVLTHLDSFKHNK---QLKKTKKRLKHRFWTEVYP-GAKLFY 218
Cdd:cd00881    82 GLAQADGALLVVDANEGVEPQTREHLNIAL-AGGLPIIVAVNKIDRVGEEDfdeVLREIKELLKLIGFTFLKGkDVPIIP 160

                  ....*....
gi 2217279553 219 LSGmVHGEY 227
Cdd:cd00881   161 ISA-LTGEG 168
YeeP COG3596
Predicted GTPase [General function prediction only];
53-187 9.51e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 48.61  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  53 MARSFHRTQDLKTKKHHIPVVDRTPL---------EPPPIVVVVMGPPKVGKSTLIQCLirnfTRQKLTEI--RGPVT-- 119
Cdd:COG3596     1 MSTEVSSLTERLEALKRLPQVLRELLaealerllvELPPPVIALVGKTGAGKSSLINAL----FGAEVAEVgvGRPCTre 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 120 -----IVSGKKRRLTIIEC-GCD--------INMMIDLAKVADLVLMLIDAS-FGFEMEtFEFLN-ICQVHGFPKIMGVL 183
Cdd:COG3596    77 iqryrLESDGLPGLVLLDTpGLGevnerdreYRELRELLPEADLILWVVKADdRALATD-EEFLQaLRAQYPDPPVLVVL 155

                  ....
gi 2217279553 184 THLD 187
Cdd:COG3596   156 TQVD 159
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
85-184 1.61e-05

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: 44.92  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  85 VVVMGPPKVGKSTLIQCLIRnfTRQKLTEI----RGPVTI-VSGKKRRLTIIEC-----GCDINMMIDLAKV----ADLV 150
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTG--AKAIVSDYpgttRDPNEGrLELKGKQIILVDTpglieGASEGEGLGRAFLaiieADLI 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217279553 151 LMLIDASFGFEMETFEFLNICQVHGFPKIMgVLT 184
Cdd:pfam01926  80 LFVVDSEEGITPLDEELLELLRENKKPIIL-VLN 112
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
85-209 3.23e-05

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 45.19  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  85 VVVMGPPKVGKSTLIQCLIRnftRQKLTEirgpvtiVS---GKKRRLTIIECGCDInMMIDL-----AKVAD-------- 148
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTN---RKKLAR-------TSktpGRTQLINFFNVGDKF-RLVDLpgygyAKVSKevrekwgk 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217279553 149 -------------LVLMLIDASFGFEMETFEFLNICQVHGFPKIMgVLTHLDSFKHN---KQLKKTKKRLKHRFWTE 209
Cdd:cd01876    71 lieeylenrenlkGVVLLIDARHGPTPIDLEMLEFLEELGIPFLI-VLTKADKLKKSelaKVLKKIKEELNLFNILP 146
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
86-187 9.49e-05

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: 43.60  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  86 VVMGPPKVGKSTLIQCLIRNftRQKLTEIRGPVTI--------VSGKKRRLTII------ECGC--DINMMIDLAKVADL 149
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGG--EVGEVSDVPGTTRdpdvyvkeLDKGKVKLVLVdtpgldEFGGlgREELARLLLRGADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217279553 150 VLMLIDASFG--FEMETFEFLNICQVHGFPKIMgVLTHLD 187
Cdd:cd00882    79 ILLVVDSTDResEEDAKLLILRRLRKEGIPIIL-VGNKID 117
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
85-220 1.64e-04

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: 43.22  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  85 VVVMGPPKVGKSTLIQCLIR----------NFTRQKlteIRGPVT-------------IVSGKKRRltiiecgcdINMMI 141
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGqkisivspkpQTTRNR---IRGIYTdddaqiifvdtpgIHKPKKKL---------GERMV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553 142 DLA----KVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMgVLTHLDSFKHNKQLKKTKkrlkhRFWTEVYPGAKLF 217
Cdd:cd04163    74 KAAwsalKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVIL-VLNKIDLVKDKEDLLPLL-----EKLKELHPFAEIF 147

                  ...
gi 2217279553 218 YLS 220
Cdd:cd04163   148 PIS 150
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
86-206 7.74e-03

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: 38.00  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  86 VVMGPPKVGKSTLIQCLirnfTRQKLTEI-------RGPVT--IVSGKKRRLTII------ECGCDINMM----IDLAKV 146
Cdd:cd00880     1 AIFGRPNVGKSSLLNAL----LGQNVGIVspipgttRDPVRkeWELLPLGPVVLIdtpgldEEGGLGRERveeaRQVADR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217279553 147 ADLVLMLIDASFGF--EMETFEFLNICQVhgfpKIMGVLTHLDSFKHNKQLKKTKKRLKHRF 206
Cdd:cd00880    77 ADLVLLVVDSDLTPveEEAKLGLLRERGK----PVLLVLNKIDLVPESEEEELLRERKLELL 134
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
51-104 7.81e-03

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: 38.28  E-value: 7.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217279553  51 VRMARSFHRTQDLKTKKHHIPvvdrtplepPPIVVVVMGPPKVGKSTLIQCLIR 104
Cdd:cd01856    93 LKKAKKLLKENEKLKAKGLLP---------RPLRAMVVGIPNVGKSTLINRLRG 137
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
85-210 9.76e-03

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: 38.27  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279553  85 VVVMGPPKVGKSTLIQCLI-----------RNFTRQKLT-----EIRGPVTI------VSGKKRRLTIIEC-G-CD-INM 139
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytgaiskrgeVKGEGEAGLdnlpeERERGITIksaavsFETKDYLINLIDTpGhVDfVKE 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217279553 140 MIDLAKVADLVLMLIDASFGFEMETFEFLNICQVHGFPKIMgVLTHLDSFKHNKqLKKTKKRLKHRFWTEV 210
Cdd:pfam00009  86 VIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIV-FINKMDRVDGAE-LEEVVEEVSRELLEKY 154
 
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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