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Conserved domains on  [gi|55953087|ref|NP_036473|]
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GTP-binding protein 4 [Homo sapiens]

Protein Classification

NOG1 family protein( domain architecture ID 11437690)

nucleolar GTP-binding protein 1 (NOG1) family protein which binds GTP, and may associate with ribosomal subunits and play a role in ribosomal RNA maturation

Gene Ontology:  GO:0005525|GO:0042273
PubMed:  11112701

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
6-339 8.30e-104

GTP-binding protein, GTP1/Obg family [General function prediction only];


:

Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 317.93  E-value: 8.30e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   6 FKKITVVPSAKDFIDLTLSKTQRKTPtvihKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILTDFPKLDDIHPFYADLMNI 85
Cdd:COG1084   3 FEKIPTVPTADELIDKAFRRAARAGR----AKRGLEKGREAEESRLRTAANILSDNLENIVRKFPDFDELHPFYRELADI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  86 LYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLyRCKQLKRAALGRMCTVIKRQKQSLEYLEQVRQHLSRLPTID 165
Cdd:COG1084  79 LVGVDELKKSLSAVSWASRKIKEISREYIRKIRRADSD-EARKLRKEAFGRIASVVRRIDDDLLFLNEARNKLRKLPDID 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 166 PNTRTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALA 245
Cdd:COG1084 158 PDLPTIVVAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLDRPLSERNEIERQAILALK 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 246 HLRAAVLYVMDLSEQCGHGLREQLELFQNIRPLFiNKPLIVVANKCDVKRIAELSEDdqkiftdlqsEGFPVIETSTLTE 325
Cdd:COG1084 238 HLADVILFLFDPSETCGYSLEEQLNLLEEIRSLF-DVPVIVVINKIDLSDEEELKEA----------EEEADIKISALTG 306

                       330
                ....*....|....
gi 55953087 326 EGVIKVKTEACDRL 339
Cdd:COG1084 307 EGVDELLDELIEAL 320
NOGCT pfam08155
NOGCT (NUC087) domain; This C terminal domain is found in the NOG subfamily of nucleolar ...
 398-446 8.15e-24

NOGCT (NUC087) domain; This C terminal domain is found in the NOG subfamily of nucleolar GTP-binding proteins.


:

Pssm-ID: 462381  Cd Length: 51  Bit Score: 94.48  E-value: 8.15e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 55953087   398 ERDLELEMGD--DYILDLQKYWDLMNLSEKHDKIPEIWEGHNIADYIDPAI 446
Cdd:pfam08155   1 ERDLEEENGGagVYNVDLKKKYDLKNPEWKYDIIPEIWDGKNVADFIDPDI 51
 
Name Accession Description Interval E-value
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
6-339 8.30e-104

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 317.93  E-value: 8.30e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   6 FKKITVVPSAKDFIDLTLSKTQRKTPtvihKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILTDFPKLDDIHPFYADLMNI 85
Cdd:COG1084   3 FEKIPTVPTADELIDKAFRRAARAGR----AKRGLEKGREAEESRLRTAANILSDNLENIVRKFPDFDELHPFYRELADI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  86 LYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLyRCKQLKRAALGRMCTVIKRQKQSLEYLEQVRQHLSRLPTID 165
Cdd:COG1084  79 LVGVDELKKSLSAVSWASRKIKEISREYIRKIRRADSD-EARKLRKEAFGRIASVVRRIDDDLLFLNEARNKLRKLPDID 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 166 PNTRTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALA 245
Cdd:COG1084 158 PDLPTIVVAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLDRPLSERNEIERQAILALK 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 246 HLRAAVLYVMDLSEQCGHGLREQLELFQNIRPLFiNKPLIVVANKCDVKRIAELSEDdqkiftdlqsEGFPVIETSTLTE 325
Cdd:COG1084 238 HLADVILFLFDPSETCGYSLEEQLNLLEEIRSLF-DVPVIVVINKIDLSDEEELKEA----------EEEADIKISALTG 306

                       330
                ....*....|....
gi 55953087 326 EGVIKVKTEACDRL 339
Cdd:COG1084 307 EGVDELLDELIEAL 320
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 169-340 1.42e-103

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 311.03  E-value: 1.42e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 169 RTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALAHLR 248
Cdd:cd01897   1 RTLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGILDRPLEERNTIEMQAITALAHLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 249 AAVLYVMDLSEQCGHGLREQLELFQNIRPLFiNKPLIVVANKCDVKRIAELSEddqkIFTDLQSEGFPVIETSTLTEEGV 328
Cdd:cd01897  81 AAVLFFIDPSETCGYSIEEQLSLFKEIKPLF-NKPVIVVLNKIDLLTEEDLSE----IEKELEKEGEEVIKISTLTEEGV 155

                       170
                ....*....|..
gi 55953087 329 IKVKTEACDRLL 340
Cdd:cd01897 156 DELKNKACELLL 167
NOG1_N pfam17835
NOG1 N-terminal helical domain; This domain is found at the N-terminus of NOG1 GTPase proteins.
 6-165 8.93e-54

NOG1 N-terminal helical domain; This domain is found at the N-terminus of NOG1 GTPase proteins.


Pssm-ID: 436080  Cd Length: 160  Bit Score: 181.06  E-value: 8.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087     6 FKKITVVPSAKDFIDLTLSKTQRKTPTVIHKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILTDFPKLDDIHPFYADLMNI 85
Cdd:pfam17835   1 FEKIPIVPTSEELIDSALRRAKRIGPTTKKKGNEINRLRNRYARQLDTAMKTLSDKLSTIVEKFPNLDELHPFYRELLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087    86 LYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLYRCKQLKRAALGRMCTVIKRQKQSLEYLEQVRQHLSRLPTID 165
Cdd:pfam17835  81 VAGKDEYKKSLGQVNTARKIIRKIGKEYANLLKKSGDKKEAEELRREAFGRVASVLRKIGPCLDFLEDIAKKLRKLPVID 160
NOGCT pfam08155
NOGCT (NUC087) domain; This C terminal domain is found in the NOG subfamily of nucleolar ...
 398-446 8.15e-24

NOGCT (NUC087) domain; This C terminal domain is found in the NOG subfamily of nucleolar GTP-binding proteins.


Pssm-ID: 462381  Cd Length: 51  Bit Score: 94.48  E-value: 8.15e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 55953087   398 ERDLELEMGD--DYILDLQKYWDLMNLSEKHDKIPEIWEGHNIADYIDPAI 446
Cdd:pfam08155   1 ERDLEEENGGagVYNVDLKKKYDLKNPEWKYDIIPEIWDGKNVADFIDPDI 51
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 173-328 9.30e-15

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 75.92  E-value: 9.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLR-WQVVDTPGIldhpledrntIEMQA------ITALA 245
Cdd:TIGR02729 162 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGL----------IEGASegaglgHRFLK 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   246 HL-RAAVL-YVMDLSEQCGHG-------LREQLELFqniRPLFINKPLIVVANKCDVKRIAELSEDDQKIftdLQSEGFP 316
Cdd:TIGR02729 232 HIeRTRVLlHLIDISPEDGSDpvedyeiIRNELKKY---SPELAEKPRIVVLNKIDLLDEEELEELLKEL---KKELGKP 305

                         170
                  ....*....|..
gi 55953087   317 VIETSTLTEEGV 328
Cdd:TIGR02729 306 VFPISALTGEGL 317
obgE PRK12299
GTPase CgtA; Reviewed
 173-347 2.41e-14

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 74.72  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTksLF-----VGHMDYKylRWQVVDTPGIldhpledrntIEMQA------I 241
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPFTT--LHpnlgvVRVDDYK--SFVIADIPGL----------IEGASegaglgH 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  242 TALAHL-RAAVL-YVMDLSEQCG----HGLREQLELFqniRPLFINKPLIVVANKCDVkrIAELSEDDQKIFTDLQSEGF 315
Cdd:PRK12299 229 RFLKHIeRTRLLlHLVDIEAVDPvedyKTIRNELEKY---SPELADKPRILVLNKIDL--LDEEEEREKRAALELAALGG 303

                        170       180       190
                 ....*....|....*....|....*....|..
gi 55953087  316 PVIETSTLTEEGVIKVKTEACDRLLAHRVETK 347
Cdd:PRK12299 304 PVFLISAVTGEGLDELLRALWELLEEARREEE 335
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 171-341 4.49e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 38.26  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087    171 LLLCGYPNVGKSSFINKVTRaDVDVQPYA------FTTKSLfvgHMDYKYLRWQVVDTPGildhplEDRntieMQAITAl 244
Cdd:smart00175   3 IILIGDSGVGKSSLLSRFTD-GKFSEQYKstigvdFKTKTI---EVDGKRVKLQIWDTAG------QER----FRSITS- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087    245 AHLRAA--VLYVMDLS-----EQCGHGLREQLELFQNirplfiNKPLIVVANKCDVKRIAELSEDDQKIFTdlQSEGFPV 317
Cdd:smart00175  68 SYYRGAvgALLVYDITnresfENLENWLKELREYASP------NVVIMLVGNKSDLEEQRQVSREEAEAFA--EEHGLPF 139

                          170       180
                   ....*....|....*....|....
gi 55953087    318 IETSTLTEEGVIKVKTEACDRLLA 341
Cdd:smart00175 140 FETSAKTNTNVEEAFEELAREILK 163
 
Name Accession Description Interval E-value
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
6-339 8.30e-104

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 317.93  E-value: 8.30e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   6 FKKITVVPSAKDFIDLTLSKTQRKTPtvihKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILTDFPKLDDIHPFYADLMNI 85
Cdd:COG1084   3 FEKIPTVPTADELIDKAFRRAARAGR----AKRGLEKGREAEESRLRTAANILSDNLENIVRKFPDFDELHPFYRELADI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  86 LYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLyRCKQLKRAALGRMCTVIKRQKQSLEYLEQVRQHLSRLPTID 165
Cdd:COG1084  79 LVGVDELKKSLSAVSWASRKIKEISREYIRKIRRADSD-EARKLRKEAFGRIASVVRRIDDDLLFLNEARNKLRKLPDID 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 166 PNTRTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALA 245
Cdd:COG1084 158 PDLPTIVVAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLDRPLSERNEIERQAILALK 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 246 HLRAAVLYVMDLSEQCGHGLREQLELFQNIRPLFiNKPLIVVANKCDVKRIAELSEDdqkiftdlqsEGFPVIETSTLTE 325
Cdd:COG1084 238 HLADVILFLFDPSETCGYSLEEQLNLLEEIRSLF-DVPVIVVINKIDLSDEEELKEA----------EEEADIKISALTG 306

                       330
                ....*....|....
gi 55953087 326 EGVIKVKTEACDRL 339
Cdd:COG1084 307 EGVDELLDELIEAL 320
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 169-340 1.42e-103

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 311.03  E-value: 1.42e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 169 RTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDRNTIEMQAITALAHLR 248
Cdd:cd01897   1 RTLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGILDRPLEERNTIEMQAITALAHLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 249 AAVLYVMDLSEQCGHGLREQLELFQNIRPLFiNKPLIVVANKCDVKRIAELSEddqkIFTDLQSEGFPVIETSTLTEEGV 328
Cdd:cd01897  81 AAVLFFIDPSETCGYSIEEQLSLFKEIKPLF-NKPVIVVLNKIDLLTEEDLSE----IEKELEKEGEEVIKISTLTEEGV 155

                       170
                ....*....|..
gi 55953087 329 IKVKTEACDRLL 340
Cdd:cd01897 156 DELKNKACELLL 167
NOG1_N pfam17835
NOG1 N-terminal helical domain; This domain is found at the N-terminus of NOG1 GTPase proteins.
 6-165 8.93e-54

NOG1 N-terminal helical domain; This domain is found at the N-terminus of NOG1 GTPase proteins.


Pssm-ID: 436080  Cd Length: 160  Bit Score: 181.06  E-value: 8.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087     6 FKKITVVPSAKDFIDLTLSKTQRKTPTVIHKHYQIHRIRHFYMRKVKFTQQNYHDRLSQILTDFPKLDDIHPFYADLMNI 85
Cdd:pfam17835   1 FEKIPIVPTSEELIDSALRRAKRIGPTTKKKGNEINRLRNRYARQLDTAMKTLSDKLSTIVEKFPNLDELHPFYRELLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087    86 LYDKDHYKLALGQINIAKNLVDNVAKDYVRLMKYGDSLYRCKQLKRAALGRMCTVIKRQKQSLEYLEQVRQHLSRLPTID 165
Cdd:pfam17835  81 VAGKDEYKKSLGQVNTARKIIRKIGKEYANLLKKSGDKKEAEELRREAFGRVASVLRKIGPCLDFLEDIAKKLRKLPVID 160
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 173-339 3.59e-40

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 144.46  E-value: 3.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYK-YLRWQVVDTPGILDHPLEDRNTIEmqAITALAHLRAAV 251
Cdd:cd01881   2 LVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGE--QILAHLYRSDLI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 252 LYVMDLSEQCGHG-LREQLELFQNIRPLFI---NKPLIVVANKCDVKRIAELSEDdqkiFTDLQSEGFPVIETSTLTEEG 327
Cdd:cd01881  80 LHVIDASEDCVGDpLEDQKTLNEEVSGSFLflkNKPEMIVANKIDMASENNLKRL----KLDKLKRGIPVVPTSALTRLG 155

                       170
                ....*....|..
gi 55953087 328 VIKVKTEACDRL 339
Cdd:cd01881 156 LDRVIRTIRKLL 167
NOG1 pfam06858
Nucleolar GTP-binding protein 1 (NOG1); This family represents a conserved region of ...
 235-292 1.18e-30

Nucleolar GTP-binding protein 1 (NOG1); This family represents a conserved region of approximately 60 residues in length within nucleolar GTP-binding protein 1 (NOG1). In S. cerevisiae, the NOG1 gene has been shown to be essential for cell viability, suggesting that NOG1 may play an important role in nucleolar functions. Family members include eukaryotic, bacterial and archaeal proteins.


Pssm-ID: 462021 [Multi-domain]  Cd Length: 58  Bit Score: 114.07  E-value: 1.18e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 55953087   235 TIEMQAITALAHLRAAVLYVMDLSEQCGHGLREQLELFQNIRPLFINKPLIVVANKCD 292
Cdd:pfam06858   1 EIEMQAIAALAHLADAVLFVIDPSETCGYSLEEQLSLFEEIKPLFANKPVIVVLNKID 58
NOGCT pfam08155
NOGCT (NUC087) domain; This C terminal domain is found in the NOG subfamily of nucleolar ...
 398-446 8.15e-24

NOGCT (NUC087) domain; This C terminal domain is found in the NOG subfamily of nucleolar GTP-binding proteins.


Pssm-ID: 462381  Cd Length: 51  Bit Score: 94.48  E-value: 8.15e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 55953087   398 ERDLELEMGD--DYILDLQKYWDLMNLSEKHDKIPEIWEGHNIADYIDPAI 446
Cdd:pfam08155   1 ERDLEEENGGagVYNVDLKKKYDLKNPEWKYDIIPEIWDGKNVADFIDPDI 51
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 175-290 1.45e-21

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: 89.99  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   175 GYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLEDrntiEMQAITALAHLRA-AVLY 253
Cdd:pfam01926   6 GRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEG----EGLGRAFLAIIEAdLILF 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 55953087   254 VMDLSEQCGHGLREQLELFQNirplfINKPLIVVANK 290
Cdd:pfam01926  82 VVDSEEGITPLDEELLELLRE-----NKKPIILVLNK 113
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 173-339 2.58e-18

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 82.47  E-value: 2.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYK-YLRWQVVDTPGIldhpledrntIEMQAITA------LA 245
Cdd:cd01898   5 LVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGL----------IEGASEGKglghrfLR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 246 HL-RAAVL-YVMDLSEQCG-----HGLREQLELFQnirPLFINKPLIVVANKCDVkriaelsEDDQKIFTDLQ-----SE 313
Cdd:cd01898  75 HIeRTRVLlHVIDLSGEDDpvedyETIRNELEAYN---PGLAEKPRIVVLNKIDL-------LDAEERFEKLKellkeLK 144

                       170       180
                ....*....|....*....|....*.
gi 55953087 314 GFPVIETSTLTEEGVIKVKTEACDRL 339
Cdd:cd01898 145 GKKVFPISALTGEGLDELLKKLAKLL 170
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 175-339 2.06e-15

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: 74.20  E-value: 2.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 175 GYPNVGKSSFINKVTRADV-DVQPYAFTTKslfvghmDYKYLRWQV--------VDTPGILDHPLEDRNTIEMqAITALA 245
Cdd:cd00880   4 GRPNVGKSSLLNALLGQNVgIVSPIPGTTR-------DPVRKEWELlplgpvvlIDTPGLDEEGGLGRERVEE-ARQVAD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 246 HLRaAVLYVMDLSeqcghglREQLELFQNIRPLF-INKPLIVVANKCDVkriaeLSEDDQK-IFTDLQSEGF---PVIET 320
Cdd:cd00880  76 RAD-LVLLVVDSD-------LTPVEEEAKLGLLReRGKPVLLVLNKIDL-----VPESEEEeLLRERKLELLpdlPVIAV 142

                       170
                ....*....|....*....
gi 55953087 321 STLTEEGVIKVKTEACDRL 339
Cdd:cd00880 143 SALPGEGIDELRKKIAELL 161
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 172-337 2.62e-15

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: 73.64  E-value: 2.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 172 LLCGYPNVGKSSFINKVTRADV-DVQPYAFTTKSLFVGHMDYKYLRWQV--VDTPGILDhplEDRNTIEMQAITALAHLR 248
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVgEVSDVPGTTRDPDVYVKELDKGKVKLvlVDTPGLDE---FGGLGREELARLLLRGAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 249 aAVLYVMDLSEqcghglreqLELFQNIRPLFI------NKPLIVVANKCDVKRIAELSEDDQKIFtDLQSEGFPVIETST 322
Cdd:cd00882  78 -LILLVVDSTD---------RESEEDAKLLILrrlrkeGIPIILVGNKIDLLEEREVEELLRLEE-LAKILGVPVFEVSA 146

                       170
                ....*....|....*
gi 55953087 323 LTEEGVIKVKTEACD 337
Cdd:cd00882 147 KTGEGVDELFEKLIE 161
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 173-328 9.30e-15

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 75.92  E-value: 9.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLR-WQVVDTPGIldhpledrntIEMQA------ITALA 245
Cdd:TIGR02729 162 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGL----------IEGASegaglgHRFLK 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   246 HL-RAAVL-YVMDLSEQCGHG-------LREQLELFqniRPLFINKPLIVVANKCDVKRIAELSEDDQKIftdLQSEGFP 316
Cdd:TIGR02729 232 HIeRTRVLlHLIDISPEDGSDpvedyeiIRNELKKY---SPELAEKPRIVVLNKIDLLDEEELEELLKEL---KKELGKP 305

                         170
                  ....*....|..
gi 55953087   317 VIETSTLTEEGV 328
Cdd:TIGR02729 306 VFPISALTGEGL 317
obgE PRK12299
GTPase CgtA; Reviewed
 173-347 2.41e-14

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 74.72  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTksLF-----VGHMDYKylRWQVVDTPGIldhpledrntIEMQA------I 241
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPFTT--LHpnlgvVRVDDYK--SFVIADIPGL----------IEGASegaglgH 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  242 TALAHL-RAAVL-YVMDLSEQCG----HGLREQLELFqniRPLFINKPLIVVANKCDVkrIAELSEDDQKIFTDLQSEGF 315
Cdd:PRK12299 229 RFLKHIeRTRLLlHLVDIEAVDPvedyKTIRNELEKY---SPELADKPRILVLNKIDL--LDEEEEREKRAALELAALGG 303

                        170       180       190
                 ....*....|....*....|....*....|..
gi 55953087  316 PVIETSTLTEEGVIKVKTEACDRLLAHRVETK 347
Cdd:PRK12299 304 PVFLISAVTGEGLDELLRALWELLEEARREEE 335
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
170-361 2.49e-14

Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 74.83  E-value: 2.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 170 TLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILDHPLE--DRNTIemqaitALAHL 247
Cdd:COG1163  65 TVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASgkGRGKE------VLSVV 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 248 RAA--VLYVMDLS----------------------------EQCGHG--------------------------------L 265
Cdd:COG1163 139 RNAdlILIVLDVFeleqydvlkeelydagirlnkpppdvtiEKKGKGgirvnstgkldldeedikkilreygivnadvlI 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 266 REQLELFQNIRPLFIN---KPLIVVANKCDVKRIAELSEDDQKIftdlqSEGFPVIETSTLTEEGVIKVKTEACDRLLAH 342
Cdd:COG1163 219 REDVTLDDLIDALMGNrvyKPAIVVVNKIDLADEEYVEELKSKL-----PDGVPVIFISAEKGIGLEELKEEIFEELGLI 293

                       250       260       270
                ....*....|....*....|....*....|...
gi 55953087 343 RVETK--------------MKGNKVNEVLNRLH 361
Cdd:COG1163 294 RVYLKppggkadmeeplilRKGSTVGDVCEKIH 326
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 175-328 3.09e-13

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: 67.90  E-value: 3.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 175 GYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVGHMDYKYLRWQVVDTPGIldhpledRNT---IEMQAIT-ALAHLRA 249
Cdd:cd04164  10 GKPNVGKSSLLNALAGRDRAiVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGL-------RETedeIEKIGIErAREAIEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 250 A--VLYVMDLSEqcghglrEQLELFQNIRPLFINKPLIVVANKCDvkriaeLSEDDQKIFTdlqSEGFPVIETSTLTEEG 327
Cdd:cd04164  83 AdlVLLVVDASE-------GLDEEDLEILELPAKKPVIVVLNKSD------LLSDAEGISE---LNGKPIIAISAKTGEG 146


                .
gi 55953087 328 V 328
Cdd:cd04164 147 I 147
obgE PRK12297
GTPase CgtA; Reviewed
 173-339 4.60e-13

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 71.29  E-value: 4.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVV-DTPGI--------------LDHpledrntIE 237
Cdd:PRK12297 163 LVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMaDIPGLiegasegvglghqfLRH-------IE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  238 mqaitalahlRAAVL-YVMDLSEQCGhglREQLELFQNIR-------PLFINKPLIVVANKCDVkriaelsEDDQKIFTD 309
Cdd:PRK12297 236 ----------RTRVIvHVIDMSGSEG---RDPIEDYEKINkelklynPRLLERPQIVVANKMDL-------PEAEENLEE 295

                        170       180       190
                 ....*....|....*....|....*....|.
gi 55953087  310 LQSE-GFPVIETSTLTEEGVIKVKTEACDRL 339
Cdd:PRK12297 296 FKEKlGPKVFPISALTGQGLDELLYAVAELL 326
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
167-341 3.36e-12

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 65.39  E-value: 3.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 167 NTRTLLLCGYPNVGKSSFINKVTRADVDVQPYA------FTTKSLFVGHMDYKYLrwqVVDTPGILD----HPLEDRNTI 236
Cdd:COG1100   2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLstngvtIDKKELKLDGLDVDLV---IWDTPGQDEfretRQFYARQLT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 237 EmqaitalahlRAAVLYVMDLSEQcgHGLREQLELFQNIRPLFINKPLIVVANKCDVKRIAELSEDDQKIFTDLQSEGFP 316
Cdd:COG1100  79 G----------ASLYLFVVDGTRE--ETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNIVE 146

                       170       180
                ....*....|....*....|....*
gi 55953087 317 VIETSTLTEEGVIKVKTEACDRLLA 341
Cdd:COG1100 147 VVATSAKTGEGVEELFAALAEILRG 171
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 168-331 3.73e-11

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 62.00  E-value: 3.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   168 TRTLLLCGYPNVGKSSFINKVTRADV-DVQPYAFTTKSLFVGHMDY--KYLRWQVVDTPGIldhplEDRNTIE---MQAI 241
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGsITEYYPGTTRNYVTTVIEEdgKTYKFNLLDTAGQ-----EDYDAIRrlyYPQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   242 TALAHLRAAVLYVMDLSEqcghGLREQLELFQNIRPLfiNKPLIVVANKCDvKRIAELSEDDQKIFtdLQSEGFPVIETS 321
Cdd:TIGR00231  76 ERSLRVFDIVILVLDVEE----ILEKQTKEIIHHADS--GVPIILVGNKID-LKDADLKTHVASEF--AKLNGEPIIPLS 146

                         170
                  ....*....|
gi 55953087   322 TLTEEGVIKV 331
Cdd:TIGR00231 147 AETGKNIDSA 156
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 173-227 1.10e-10

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: 62.18  E-value: 1.10e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55953087 173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILD 227
Cdd:cd01896   5 LVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIE 59
obgE PRK12298
GTPase CgtA; Reviewed
 173-418 1.79e-10

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 63.35  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTK--SLFVGHMDykylRWQ---VVDTPGIldhpledrntIEMQA------I 241
Cdd:PRK12298 164 LLGLPNAGKSTFIRAVSAAKPKVADYPFTTLvpNLGVVRVD----DERsfvVADIPGL----------IEGASegaglgI 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  242 TALAHL-RAAVL-YVMDLSEQCGHG-------LREQLELFQnirPLFINKPLIVVANKCDVKRIAELSEDDQKIFTDLQS 312
Cdd:PRK12298 230 RFLKHLeRCRVLlHLIDIAPIDGSDpvenariIINELEKYS---PKLAEKPRWLVFNKIDLLDEEEAEERAKAIVEALGW 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  313 EGfPVIETSTLTEEGvikvkteacdrllahrvetkmkgnkVNEVLNRLHLAIptrrddKERPPFIPEGVVARRK-RMETE 391
Cdd:PRK12298 307 EG-PVYLISAASGLG-------------------------VKELCWDLMTFI------EENPREEAEEAEAPEKvEFMWD 354

                        250       260
                 ....*....|....*....|....*..
gi 55953087  392 ESRKKRERDLELEMGDDYILDlqkyWD 418
Cdd:PRK12298 355 DYHREQLEEVEEEDDDDWDDD----WD 377
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 173-342 1.91e-10

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 63.54  E-value: 1.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVGHMDYKYLRWQVVDTPGIldhpledRNT---IEMQAIT-ALAHL 247
Cdd:COG0486 218 IVGRPNVGKSSLLNALLGEERAiVTDIAGTTRDVIEERINIGGIPVRLIDTAGL-------RETedeVEKIGIErAREAI 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 248 RAA--VLYVMDLSEqcghglrEQLELFQNIRPLFINKPLIVVANKCDvkriaeLSEDDQKIFTDLqsEGFPVIETSTLTE 325
Cdd:COG0486 291 EEAdlVLLLLDASE-------PLTEEDEEILEKLKDKPVIVVLNKID------LPSEADGELKSL--PGEPVIAISAKTG 355

                       170
                ....*....|....*..
gi 55953087 326 EGVikvkteacDRLLAH 342
Cdd:COG0486 356 EGI--------DELKEA 364
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 169-335 2.02e-10

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 59.39  E-value: 2.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   169 RTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILD-HPLedrnTIEmQAIT--ALA 245
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSlSPY----SEE-ERVArdYLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   246 HLRA-AVLYVMDLSEqcghgLREQLELFQNIRPLfiNKPLIVVANKCDVKRIAELSEDDQKiftdLQSE-GFPVIETSTL 323
Cdd:pfam02421  76 NEKPdVIVNVVDATN-----LERNLYLTLQLLEL--GLPVVLALNMMDEAEKKGIKIDIKK----LSELlGVPVVPTSAR 144

                         170
                  ....*....|..
gi 55953087   324 TEEGVIKVKTEA 335
Cdd:pfam02421 145 KGEGIDELLDAI 156
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
175-328 9.05e-10

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 61.28  E-value: 9.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  175 GYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVGHMDYKYLRWQVVDTPGIldhpledRNT---IEMQAIT-ALAHLRA 249
Cdd:PRK05291 222 GRPNVGKSSLLNALLGEERAiVTDIAGTTRDVIEEHINLDGIPLRLIDTAGI-------RETddeVEKIGIErSREAIEE 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  250 A--VLYVMDLSEQcghGLREQLELFQNIrplfINKPLIVVANKCDVKRIAELSEDDqkiftdlqseGFPVIETSTLTEEG 327
Cdd:PRK05291 295 AdlVLLVLDASEP---LTEEDDEILEEL----KDKPVIVVLNKADLTGEIDLEEEN----------GKPVIRISAKTGEG 357


                 .
gi 55953087  328 V 328
Cdd:PRK05291 358 I 358
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 175-292 2.95e-09

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: 56.29  E-value: 2.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 175 GYPNVGKSSFINKVTR---ADVDvqPYAFTTKSLFVGHMDYKYLRWQVVDTPGI--LDHPLEDRntIEMQAITALAhlRA 249
Cdd:cd01894   4 GRPNVGKSTLFNRLTGrrdAIVS--DTPGVTRDRKYGEAEWGGREFILIDTGGIepDDEGISKE--IREQAEIAIE--EA 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 55953087 250 -AVLYVMDLSEqcghGLREQ-LELFQNIRPLfiNKPLIVVANKCD 292
Cdd:cd01894  78 dVILFVVDGRE----GLTPAdEEIAKYLRKS--KKPVILVVNKID 116
YeeP COG3596
Predicted GTPase [General function prediction only];
141-292 7.76e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 57.47  E-value: 7.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 141 IKRQKQSLEylEQVRQHLSRLPTIDPNTRtLLLCGYPNVGKSSFINKVTRADV-----------DVQPYAFTTKSLfvgh 209
Cdd:COG3596  15 LKRLPQVLR--ELLAEALERLLVELPPPV-IALVGKTGAGKSSLINALFGAEVaevgvgrpctrEIQRYRLESDGL---- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 210 mdyKYLRwqVVDTPGILDHPLEDRNTIEMQAITALAHLraaVLYVMDLSEqcgHGLREQLELFQNIRPLFINKPLIVVAN 289
Cdd:COG3596  88 ---PGLV--LLDTPGLGEVNERDREYRELRELLPEADL---ILWVVKADD---RALATDEEFLQALRAQYPDPPVLVVLT 156


                ...
gi 55953087 290 KCD 292
Cdd:COG3596 157 QVD 159
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
151-357 8.64e-09

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 58.11  E-value: 8.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 151 LEQVRQHLSRLPTIDPNTRTLLLC--GYPNVGKSSFINKVTRAD-VDVQPYAFTTK-SLFVgHMDYKYLRWQVVDTPGIl 226
Cdd:COG1160 156 LDAVLELLPEEEEEEEEDDPIKIAivGRPNVGKSSLINALLGEErVIVSDIAGTTRdSIDT-PFERDGKKYTLIDTAGI- 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 227 dhpledR------NTIEMQAIT-ALAHLRAA--VLYVMDLSEqcghGLREQ-LELFQnirplFI---NKPLIVVANKCDv 293
Cdd:COG1160 234 ------RrkgkvdEGIEKYSVLrTLRAIERAdvVLLVIDATE----GITEQdLKIAG-----LAleaGKALVIVVNKWD- 297

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55953087 294 kriaeLSEDDQKIFTDLQSE---------GFPVIETSTLTEEGVIKVkTEACDRLLAHRvETKMKGNKVNEVL 357
Cdd:COG1160 298 -----LVEKDRKTREELEKEirrrlpfldYAPIVFISALTGQGVDKL-LEAVDEVYESA-NKRISTSKLNRVL 363
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 173-332 9.74e-09

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 54.77  E-value: 9.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGILD-HPledrNTIEmQAIT--ALAHLRA 249
Cdd:cd01879   2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSlTP----YSED-EKVArdFLLGEEP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 250 -AVLYVMDLSEqcghgLREQLELFQNIrpLFINKPLIVVANKCDvkriaELSEDDQKIFTDLQSE--GFPVIETSTLTEE 326
Cdd:cd01879  77 dLIVNVVDATN-----LERNLYLTLQL--LELGLPVVVALNMID-----EAEKRGIKIDLDKLSEllGVPVVPTSARKGE 144


                ....*.
gi 55953087 327 GVIKVK 332
Cdd:cd01879 145 GIDELL 150
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 175-337 2.39e-08

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 53.98  E-value: 2.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 175 GYPNVGKSSFINKVTRAD-VDVQPYAFTTK-SLFVgHMDYKYLRWQVVDTPGIldhpledR------NTIE-MQAITALA 245
Cdd:cd01895   9 GRPNVGKSSLLNALLGEErVIVSDIAGTTRdSIDV-PFEYDGQKYTLIDTAGI-------RkkgkvtEGIEkYSVLRTLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 246 HLRAA--VLYVMDLSEqcghGLREQ-LELFQnirplFI---NKPLIVVANKCDvkriaeLSEDDQKIFTDL--------- 310
Cdd:cd01895  81 AIERAdvVLLVLDASE----GITEQdLRIAG-----LIleeGKALIIVVNKWD------LVEKDEKTMKEFekelrrklp 145

                       170       180
                ....*....|....*....|....*..
gi 55953087 311 QSEGFPVIETSTLTEEGVIKVKTEACD 337
Cdd:cd01895 146 FLDYAPIVFISALTGQGVDKLFDAIKE 172
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 151-358 8.33e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 55.06  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  151 LEQVRQHLSRLPTIDPNTRTLLLC--GYPNVGKSSFINKVTRAD-VDVQPYAFTTK-SLFVgHMDYKYLRWQVVDTPGIl 226
Cdd:PRK00093 154 LDAILEELPEEEEEDEEDEPIKIAiiGRPNVGKSSLINALLGEErVIVSDIAGTTRdSIDT-PFERDGQKYTLIDTAGI- 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  227 dhpledR------NTIE-------MQAITAlAHLraaVLYVMDLSEqcghGLREQ-LELFQnirplFI---NKPLIVVAN 289
Cdd:PRK00093 232 ------RrkgkvtEGVEkysvirtLKAIER-ADV---VLLVIDATE----GITEQdLRIAG-----LAleaGRALVIVVN 292

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55953087  290 KCDVkriaeLSEDDQKIFT-DLQSE-----GFPVIETSTLTEEGVIKVKtEACDRLLAHRvETKMKGNKVNEVLN 358
Cdd:PRK00093 293 KWDL-----VDEKTMEEFKkELRRRlpfldYAPIVFISALTGQGVDKLL-EAIDEAYENA-NRRISTSVLNRVLE 360
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
173-301 1.12e-07

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 54.64  E-value: 1.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTR---ADVDVQPyaFTTKSLFVGHMDYKYLRWQVVDTPGIL---DHPLEDRntIEMQAITALAH 246
Cdd:COG1160   7 IVGRPNVGKSTLFNRLTGrrdAIVDDTP--GVTRDRIYGEAEWGGREFTLIDTGGIEpddDDGLEAE--IREQAELAIEE 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 55953087 247 lrA-AVLYVMDLSEqcghGLREQ-LELFQNIRPLfiNKPLIVVANKCD-VKRIAELSE 301
Cdd:COG1160  83 --AdVILFVVDGRA----GLTPLdEEIAKLLRRS--GKPVILVVNKVDgPKREADAAE 132
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 173-328 1.28e-07

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 54.02  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   173 LCGYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVGHMDYKYLRWQVVDTPGIldhpledRNT---IEMQAIT-ALAHL 247
Cdd:pfam12631  99 IVGKPNVGKSSLLNALLGEERAiVTDIPGTTRDVIEETINIGGIPLRLIDTAGI-------RETddeVEKIGIErAREAI 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   248 RAA--VLYVMDLSEQCGHGLREQLELFQNirplfiNKPLIVVANKCDVKriaelseddQKIFTDLQSEGFPVIETSTLTE 325
Cdd:pfam12631 172 EEAdlVLLVLDASRPLDEEDLEILELLKD------KKPIIVVLNKSDLL---------GEIDELEELKGKPVLAISAKTG 236


                  ...
gi 55953087   326 EGV 328
Cdd:pfam12631 237 EGL 239
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 175-415 3.19e-07

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 53.59  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   175 GYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGIldHPLEDRNTIEMQAITALAHLRA-AVLY 253
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGI--YSLTTFSLEEEVARDYLLNEKPdLVVN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   254 VMDLSEqcghgLREQLELFQNIrpLFINKPLIVVANKCDvkrIAElsedDQKIFtdlqsegfpvIETSTLTEE-GVIKVK 332
Cdd:TIGR00437  79 VVDASN-----LERNLYLTLQL--LELGIPMILALNLVD---EAE----KKGIR----------IDEEKLEERlGVPVVP 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   333 TEAcdrllahrvetkMKGNKVNEVLNRLHLAIPTRRDDKERPPFIPEGVVARR---KRMETEESRKKRERDLELEMGDDY 409
Cdd:TIGR00437 135 TSA------------TEGRGIERLKDAIRKAIGLKELKKRAIEIVPEAYQVVEvveGLIEIIYSISKRGLEILLGLLEDL 202


                  ....*.
gi 55953087   410 ILDLQK 415
Cdd:TIGR00437 203 SLEIEK 208
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
167-409 3.39e-07

Fe2+ transporter FeoB [Inorganic ion transport and metabolism];


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 53.59  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 167 NTRTLLLCGYPNVGKSSFINKVTRADVDVQPYAFTTKSLFVGHMDYKYLRWQVVDTPGI-------LDhpledrntiEMQ 239
Cdd:COG0370   2 KMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTyslsaysPD---------EKV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 240 AITALAHLRA-AVLYVMDLSEqcghgLREQLELFQNIRPLfiNKPLIVVANKCDV--KR-----IAELSEddqkiftDLq 311
Cdd:COG0370  73 ARDFLLEEKPdVVVNVVDATN-----LERNLYLTLQLLEL--GIPVVLALNMMDEaeKKgikidVEKLSK-------LL- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 312 seGFPVIETSTLTEEGVIKVKtEACDRLLAHRVETKMKGNKVNEVLNRLHLAIPTRRDDKERPP------FIPEGVVARR 385
Cdd:COG0370 138 --GVPVVPTSARKGKGIDELK-EAIIEAAEGKKPRPLRIDYPEEIEEAIEELEELLEEDGPYPSrwlaikLLEGDEEVLE 214

                       250       260
                ....*....|....*....|....
gi 55953087 386 KRMETEESRKKRERDLELEMGDDY 409
Cdd:COG0370 215 LLSELLELLEEIREELEEELGEDL 238
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 170-292 6.42e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.97  E-value: 6.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  170 TLLLCGYPNVGKSSFINKVTR---ADVDVQP-------YAFTTkslfvgHMDYKYLrwqVVDTPGIL--DHPLEDRntIE 237
Cdd:PRK00093   3 VVAIVGRPNVGKSTLFNRLTGkrdAIVADTPgvtrdriYGEAE------WLGREFI---LIDTGGIEpdDDGFEKQ--IR 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55953087  238 MQAITALAHlrA-AVLYVMDLSEqcghGLREQ-LELFQNIRPLfiNKPLIVVANKCD 292
Cdd:PRK00093  72 EQAELAIEE--AdVILFVVDGRA----GLTPAdEEIAKILRKS--NKPVILVVNKVD 120
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 175-328 2.25e-06

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: 48.23  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 175 GYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVG---HMDYkylrwQV--VDTPGIL--DHPLEDRntieM--QAITAL 244
Cdd:cd04163  10 GRPNVGKSTLLNALVGQKISiVSPKPQTTRNRIRGiytDDDA-----QIifVDTPGIHkpKKKLGER----MvkAAWSAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 245 AHlrA-AVLYVMDLSEQCGHGLREQLELFQNirplfINKPLIVVANKCD-VKRIAELSEDDQKI-FTDLQSEGFPVietS 321
Cdd:cd04163  81 KD--VdLVLFVVDASEWIGEGDEFILELLKK-----SKTPVILVLNKIDlVKDKEDLLPLLEKLkELHPFAEIFPI---S 150


                ....*..
gi 55953087 322 TLTEEGV 328
Cdd:cd04163 151 ALKGENV 157
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 219-340 2.14e-05

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: 45.59  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   219 VVDTPGildHplEDRnTIEMqaITALAHLRAAVLyVMDlseqCGHGLREQLElfQNIRPLFI-NKPLIVVANKCDVKRIA 297
Cdd:pfam00009  73 LIDTPG---H--VDF-VKEV--IRGLAQADGAIL-VVD----AVEGVMPQTR--EHLRLARQlGVPIIVFINKMDRVDGA 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 55953087   298 ELSEDDQKIFTDL------QSEGFPVIETSTLTEEGVIKVkTEACDRLL 340
Cdd:pfam00009 138 ELEEVVEEVSRELlekygeDGEFVPVVPGSALKGEGVQTL-LDALDEYL 185
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 136-328 3.75e-05

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 45.14  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 136 RMcTVIKRQkqsleyLEQVRQHL---------SRLPTIDpntrtllLCGYPNVGKSSFINKVTRADVDVQPYAF-----T 201
Cdd:cd01878  14 RI-AKLRKE------LEKVKKQRelqrarrkrSGVPTVA-------LVGYTNAGKSTLFNALTGADVLAEDQLFatldpT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 202 TKSLFVGHmDYKYLrwqVVDTPGILDH-PledrntieMQAITA----LAHLRAA--VLYVMDLSEQCghgLREQLELFQN 274
Cdd:cd01878  80 TRRIKLPG-GREVL---LTDTVGFIRDlP--------HQLVEAfrstLEEVAEAdlLLHVVDASDPD---REEQIETVEE 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 55953087 275 I-RPLFI-NKPLIVVANKCDVkriaelsEDDQKIFTDLQSEGFPVIETSTLTEEGV 328
Cdd:cd01878 145 VlKELGAdDIPIILVLNKIDL-------LDDEELEERLRAGRPDAVFISAKTGEGL 193
era PRK00089
GTPase Era; Reviewed
 175-339 3.98e-05

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 45.81  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  175 GYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVG-HMDYKYlrwQV--VDTPGIL--DHPLEDRntieMQAiTALAHLR 248
Cdd:PRK00089  12 GRPNVGKSTLLNALVGQKISiVSPKPQTTRHRIRGiVTEDDA---QIifVDTPGIHkpKRALNRA----MNK-AAWSSLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  249 AA--VLYVMDLSEQCGHGLREQLELFQNirplfINKPLIVVANKCD-VKRIAELSEDDQKIftdlqSEGFP---VIETST 322
Cdd:PRK00089  84 DVdlVLFVVDADEKIGPGDEFILEKLKK-----VKTPVILVLNKIDlVKDKEELLPLLEEL-----SELMDfaeIVPISA 153

                        170
                 ....*....|....*..
gi 55953087  323 LTEEGVIKVKTEACDRL 339
Cdd:PRK00089 154 LKGDNVDELLDVIAKYL 170
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 142-226 4.52e-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: 4.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 142 KRQKQSLEYLEQVRQHLSRLPTIDPNTRTL--LLCGYPNVGKSSFINKVT-RADVDVQPYAFTTKSlfvghmdykyLRW- 217
Cdd:cd01856  87 KGVKKLLKKAKKLLKENEKLKAKGLLPRPLraMVVGIPNVGKSTLINRLRgKKVAKVGNKPGVTRG----------QQWi 156

                        90
                ....*....|....*
gi 55953087 218 ------QVVDTPGIL 226
Cdd:cd01856 157 rigpniELLDTPGIL 171
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 173-202 5.30e-05

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 45.68  E-value: 5.30e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTRADVDVQPYAFTT 202
Cdd:cd01899   3 LVGKPNVGKSTFFNAATLADVEIANYPFTT 32
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
174-328 7.95e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 44.98  E-value: 7.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 174 CGY------PNVGKSSFINK--------VTRAdvdVQpyafTTKSLFVG-HMDYKYlrwQV--VDTPGIL--DHPLEDRn 234
Cdd:COG1159   3 SGFvaivgrPNVGKSTLLNAlvgqkvsiVSPK---PQ----TTRHRIRGiVTREDA---QIvfVDTPGIHkpKRKLGRR- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 235 tieMQAiTALAHLRAA--VLYVMDLSEQCGHGLREQLELFQNIrplfiNKPLIVVANKCD-VKR------IAELSEddQK 305
Cdd:COG1159  72 ---MNK-AAWSALEDVdvILFVVDATEKIGEGDEFILELLKKL-----KTPVILVINKIDlVKKeellplLAEYSE--LL 140

                       170       180
                ....*....|....*....|...
gi 55953087 306 IFTDlqsegfpVIETSTLTEEGV 328
Cdd:COG1159 141 DFAE-------IVPISALKGDNV 156
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 173-202 8.25e-05

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 45.18  E-value: 8.25e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 55953087  173 LCGYPNVGKSSFINKVTRADVDVQPYAFTT 202
Cdd:PRK09602   6 LVGKPNVGKSTFFNAATLADVEIANYPFTT 35
PLN03110 PLN03110
Rab GTPase; Provisional
 171-330 1.95e-04

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 42.99  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  171 LLLCGYPNVGKSSFINKVTRADVDVQPYA-----FTTKSLFVghmDYKYLRWQVVDTPGildhplEDRntieMQAITAlA 245
Cdd:PLN03110  15 IVLIGDSGVGKSNILSRFTRNEFCLESKStigveFATRTLQV---EGKTVKAQIWDTAG------QER----YRAITS-A 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087  246 HLRAAV--LYVMDLSEQcghglreqlELFQNI----RPLF----INKPLIVVANKCDVKRIAELSEDDQKIFTdlQSEGF 315
Cdd:PLN03110  81 YYRGAVgaLLVYDITKR---------QTFDNVqrwlRELRdhadSNIVIMMAGNKSDLNHLRSVAEEDGQALA--EKEGL 149

                        170
                 ....*....|....*
gi 55953087  316 PVIETSTLTEEGVIK 330
Cdd:PLN03110 150 SFLETSALEATNVEK 164
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 170-301 2.20e-04

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 42.53  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 170 TLLLCGYPNVGKSSFINKVTRADV---DVQPyafTTKSLFVghmdykyLRWQV------VDTPGILDHPLEDrntiemQA 240
Cdd:cd09912   2 LLAVVGEFSAGKSTLLNALLGEEVlptGVTP---TTAVITV-------LRYGLlkgvvlVDTPGLNSTIEHH------TE 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55953087 241 ITaLAHL-RA-AVLYVMDLSEQCGHGLREQLELFQNIRplfiNKPLIVVANKCDVKRIAELSE 301
Cdd:cd09912  66 IT-ESFLpRAdAVIFVLSADQPLTESEREFLKEILKWS----GKKIFFVLNKIDLLSEEELEE 123
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 171-292 4.12e-04

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 40.18  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   171 LLLCGYPNVGKSSFINKVTRADVDVQPYA-----FTTKSLFVGHMDYKYLRWQVVDTPGildhpLEdrntiEMQAITALa 245
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDTFDPKYKStigvdFKTKTVLENDDNGKKIKLNIWDTAG-----QE-----RFRSLHPF- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 55953087   246 HLRAAVLYVMDLSEQCGHGLREQLELFQNIRPlfiNKPLIVVANKCD 292
Cdd:pfam08477  71 YYRGAAAALLVYDSRTFSNLKYWLRELKKYAG---NSPVILVGNKID 114
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 175-225 5.16e-04

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 41.41  E-value: 5.16e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 55953087 175 GYPNVGKSSFIN--KVTRAdVDVQPYAFTTKSLFVGHMDyKYLRwqVVDTPGI 225
Cdd:cd04178 123 GYPNVGKSSVINslKRSRA-CNVGATPGVTKSMQEVHLD-KHVK--LLDSPGV 171
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 175-328 7.63e-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: 41.61  E-value: 7.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   175 GYPNVGKSSFINKVTRADVD-VQPYAFTTKSLFVG-HMDYKYlrwQV--VDTPGIlDHPLEDRNTIEMQAITALAHLRAA 250
Cdd:TIGR00436   7 GRPNVGKSTLLNQLHGQKISiTSPKAQTTRNRISGiHTTGAS---QIifIDTPGF-HEKKHSLNRLMMKEARSAIGGVDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087   251 VLYVMDLSEQCGHGlREQLELFQNIRplfinKPLIVVANKCDVK-RIAELSE-DDQKIFTDLQsegfPVIETSTLTEEGV 328
Cdd:TIGR00436  83 ILFVVDSDQWNGDG-EFVLTKLQNLK-----RPVVLTRNKLDNKfKDKLLPLiDKYAILEDFK----DIVPISALTGDNT 152
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 172-232 4.16e-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: 39.41  E-value: 4.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55953087   172 LLCGYPNVGKSSFINK-VTRADVDVQPYAFTTKSlfvghmdykyLRW-------QVVDTPGILDHPLED 232
Cdd:TIGR03596 122 MIVGIPNVGKSTLINRlAGKKVAKVGNRPGVTKG----------QQWiklsdnlELLDTPGILWPKFED 180
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 171-341 4.49e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 38.26  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087    171 LLLCGYPNVGKSSFINKVTRaDVDVQPYA------FTTKSLfvgHMDYKYLRWQVVDTPGildhplEDRntieMQAITAl 244
Cdd:smart00175   3 IILIGDSGVGKSSLLSRFTD-GKFSEQYKstigvdFKTKTI---EVDGKRVKLQIWDTAG------QER----FRSITS- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087    245 AHLRAA--VLYVMDLS-----EQCGHGLREQLELFQNirplfiNKPLIVVANKCDVKRIAELSEDDQKIFTdlQSEGFPV 317
Cdd:smart00175  68 SYYRGAvgALLVYDITnresfENLENWLKELREYASP------NVVIMLVGNKSDLEEQRQVSREEAEAFA--EEHGLPF 139

                          170       180
                   ....*....|....*....|....
gi 55953087    318 IETSTLTEEGVIKVKTEACDRLLA 341
Cdd:smart00175 140 FETSAKTNTNVEEAFEELAREILK 163
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 173-328 6.47e-03

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: 38.04  E-value: 6.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 173 LCGYPNVGKSSFINKVTRADVDVQPyAFTTKSLF---------------VGHMDYKYL--RWQVVDTPGildHplED--R 233
Cdd:cd00881   4 VIGHVDHGKTTLTGSLLYQTGAIDR-RGTRKETFldtlkeerergitikTGVVEFEWPkrRINFIDTPG---H--EDfsK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55953087 234 NTIemqaiTALAHLRAAVLyVMDLSEQCGHGLREQLELFqnirpLFINKPLIVVANKCD----------VKRIAELSEdd 303
Cdd:cd00881  78 ETV-----RGLAQADGALL-VVDANEGVEPQTREHLNIA-----LAGGLPIIVAVNKIDrvgeedfdevLREIKELLK-- 144

                       170       180
                ....*....|....*....|....*
gi 55953087 304 QKIFTDLQSEGFPVIETSTLTEEGV 328
Cdd:cd00881 145 LIGFTFLKGKDVPIIPISALTGEGI 169
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 169-225 7.88e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.18  E-value: 7.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55953087  169 RTLLLCGYPNVGKSSFINKVTRAD-VDVQPYAFTTK----SLFvgHMDYKylRWQVVDTPGI 225
Cdd:PRK03003 212 RRVALVGKPNVGKSSLLNKLAGEErSVVDDVAGTTVdpvdSLI--ELGGK--TWRFVDTAGL 269
 
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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