|
Name |
Accession |
Description |
Interval |
E-value |
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
1-428 |
0e+00 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 731.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 1 MFVDQVKIYVKGGDGGNGMVAYRREKYVpkggpaggdggkgadVVFVVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGR 80
Cdd:PRK12297 1 MFIDQAKIYVKAGDGGDGMVSFRREKYVpkggpdggdggkggsVIFVADEGLRTLLDFRYKRHFKAENGENGMGKNMHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 81 KSEDLLVKIPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLAD 160
Cdd:PRK12297 81 NGEDLIIKVPVGTVVKDAETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGEERELRLELKLLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVI 240
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 241 VHVIDMSGLEGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAFKEKVGdeVKIFPISAVTRQGVRDL 320
Cdd:PRK12297 241 VHVIDMSGSEGRDPIEDYEKINKELKLYNPRLLERPQIVVANKMDLPEAEENLEEFKEKLG--PKVFPISALTGQGLDEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 321 LFEVANLIETTPEFPIHEVADESDtsVMYKFDTEGVKFEITRESDGTFVISGYDIEKTFKMTDFSRDESIRRFARQMRGM 400
Cdd:PRK12297 319 LYAVAELLEETPEFPLEEEEVEEE--VYYKFEEEEKDFTITRDEDGVFVVSGEKIERLFKMTNFNRDESLRRFARQLRKM 396
|
410 420
....*....|....*....|....*...
gi 1005571658 401 GIDEALRARGAKDGDIVKILEYEFEFID 428
Cdd:PRK12297 397 GVDDALREAGAKDGDTVRIGDFEFEFVD 424
|
|
| Obg |
COG0536 |
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
2-344 |
0e+00 |
|
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair];
Pssm-ID: 440302 [Multi-domain] Cd Length: 343 Bit Score: 549.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 2 FVDQVKIYVKGGDGGNGMVAYRREKYVpkggpaggdggkgadVVFVVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGRK 81
Cdd:COG0536 1 FVDEAKIYVKAGDGGNGCVSFRREKYVpkggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 82 SEDLLVKIPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLADV 161
Cdd:COG0536 81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVVAKGGRGGLGNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 162 GLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVIV 241
Cdd:COG0536 161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 242 HVIDMSGLEGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEEnLQAFKEKVGDE-VKIFPISAVTRQGVRDL 320
Cdd:COG0536 241 HVVDAAPLDGRDPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEE-LEELKAELEKLgGPVFPISAVTGEGLDEL 319
|
330 340
....*....|....*....|....
gi 1005571658 321 LFEVANLIETTPEFPIHEVADESD 344
Cdd:COG0536 320 LYALAELLEELRAEEAEEEEEVEE 343
|
|
| Obg_CgtA |
TIGR02729 |
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
2-328 |
0e+00 |
|
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: 513.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 2 FVDQVKIYVKGGDGGNGMVAYRREKYVPKGGPAGGDGGKGADVVFVVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGRK 81
Cdd:TIGR02729 1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 82 SEDLLVKIPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLADV 161
Cdd:TIGR02729 81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 162 GLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVIV 241
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 242 HVIDMSGLEGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEEnLQAFKEKVGDE--VKIFPISAVTRQGVRD 319
Cdd:TIGR02729 241 HLIDISPEDGSDPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLDEEE-LEELLKELKKElgKPVFPISALTGEGLDE 319
|
....*....
gi 1005571658 320 LLFEVANLI 328
Cdd:TIGR02729 320 LLDALAELL 328
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
1-333 |
2.33e-167 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 473.02 E-value: 2.33e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 1 MFVDQVKIYVKGGDGGNGMVAYRREKYVpkggpaggdggkgadVVFVVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGR 80
Cdd:PRK12299 1 KFIDEAKIYVKAGDGGNGCVSFRREKFIpfggpdggdggrggsVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 81 KSEDLLVKIPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLAD 160
Cdd:PRK12299 81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVI 240
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 241 VHVIDMSgleGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAFKEKV--GDEVKIFPISAVTRQGVR 318
Cdd:PRK12299 241 LHLVDIE---AVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDEEEEREKRAALElaALGGPVFLISAVTGEGLD 317
|
330
....*....|....*
gi 1005571658 319 DLLFEVANLIETTPE 333
Cdd:PRK12299 318 ELLRALWELLEEARR 332
|
|
| obgE |
PRK12298 |
GTPase CgtA; Reviewed |
1-349 |
1.05e-147 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 425.05 E-value: 1.05e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 1 MFVDQVKIYVKGGDGGNGMVAYRREKYVPKGGPAGGDGGKGADVVFVVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGR 80
Cdd:PRK12298 2 KFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 81 KSEDLLVKIPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLAD 160
Cdd:PRK12298 82 RGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVI 240
Cdd:PRK12298 162 VGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 241 VHVIDMSGLEGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPD---AEENLQAFKEKVGDEVKIFPISAVTRQGV 317
Cdd:PRK12298 242 LHLIDIAPIDGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDeeeAEERAKAIVEALGWEGPVYLISAASGLGV 321
|
330 340 350
....*....|....*....|....*....|..
gi 1005571658 318 RDLLFEVANLIETTPEFPIHEVADESDTSVMY 349
Cdd:PRK12298 322 KELCWDLMTFIEENPREEAEEAEAPEKVEFMW 353
|
|
| obgE |
PRK12296 |
GTPase CgtA; Reviewed |
2-419 |
2.53e-143 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 418.12 E-value: 2.53e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 2 FVDQVKIYVKGGDGGNGMVAYRREKYVPKGGPAGGDGGKGADVVFVVEEGLRTLMDFRYQRHFKADRGQHGMSKGQHGRK 81
Cdd:PRK12296 4 FVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTLLDFHFRPHRKATNGKPGMGDNRDGAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 82 SEDLLVKIPPGTVVKDEkTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQERDVILELKVLADV 161
Cdd:PRK12296 84 GEDLVLPVPDGTVVLDE-DGEVLADLVGAGTRFVAAAGGRGGLGNAALASKARKAPGFALLGEPGEERDLVLELKSVADV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 162 GLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRsFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVIV 241
Cdd:PRK12296 163 GLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTR-FTVADVPGLIPGASEGKGLGLDFLRHIERCAVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 242 HVIDMSGLE-GRDPYEDYVTINNELKEY---------NLRLTERPQVVVANKMDMPDAEENLQAFKEKVGDE-VKIFPIS 310
Cdd:PRK12296 242 HVVDCATLEpGRDPLSDIDALEAELAAYapaldgdlgLGDLAERPRLVVLNKIDVPDARELAEFVRPELEARgWPVFEVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 311 AVTRQGVRDLLFEVANLIETTPEfpiHEVADESDTSVMYKFDTEGVKFEITRESD--GTFVISGYDIEKTFKMTDFSRDE 388
Cdd:PRK12296 322 AASREGLRELSFALAELVEEARA---AEPEAEPTRIVIRPKAVDDAGFTVERDGDgeGGFRVRGEKPERWVRQTDFDNDE 398
|
410 420 430
....*....|....*....|....*....|.
gi 1005571658 389 SIRRFARQMRGMGIDEALRARGAKDGDIVKI 419
Cdd:PRK12296 399 AVGYLADRLARLGVEDELLKAGARPGDAVTI 429
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
159-328 |
4.17e-98 |
|
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: 290.48 E-value: 4.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 159 ADVGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTR 238
Cdd:cd01898 1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 239 VIVHVIDMSGLEgrDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAFKEKVGD--EVKIFPISAVTRQG 316
Cdd:cd01898 81 VLLHVIDLSGED--DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKElkGKKVFPISALTGEG 158
|
170
....*....|..
gi 1005571658 317 VRDLLFEVANLI 328
Cdd:cd01898 159 LDELLKKLAKLL 170
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
162-328 |
5.13e-69 |
|
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: 216.11 E-value: 5.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 162 GLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVIV 241
Cdd:cd01881 1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 242 HVIDMSGLEGRDPYEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAFKEKVGDEVKIFPISAVTRQGVRDLL 321
Cdd:cd01881 81 HVIDASEDCVGDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMASENNLKRLKLDKLKRGIPVVPTSALTRLGLDRVI 160
|
....*..
gi 1005571658 322 FEVANLI 328
Cdd:cd01881 161 RTIRKLL 167
|
|
| GTP1_OBG |
pfam01018 |
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ... |
3-157 |
1.08e-65 |
|
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together.
Pssm-ID: 460027 [Multi-domain] Cd Length: 155 Bit Score: 206.81 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 3 VDQVKIYVKGGDGGNGMVAYRREKYVpkggpaggdggkgAD-------------VVFVVEEGLRTLMDFRYQRHFKADRG 69
Cdd:pfam01018 1 VDRAKIKVKAGDGGNGCVSFRREKYV-------------PKggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 70 QHGMSKGQHGRKSEDLLVKIPPGTVVKDEKTGQILADLVTHGQTAVIAKGGRGGRGNSRFATATNPAPEIAENGEPGQER 149
Cdd:pfam01018 68 ENGGGKNCHGKNGEDLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEER 147
|
....*...
gi 1005571658 150 DVILELKV 157
Cdd:pfam01018 148 WLELELKL 155
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
162-327 |
2.14e-30 |
|
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: 115.04 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 162 GLVGFPSVGKSTLL-SVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIERTRVI 240
Cdd:cd00880 1 AIFGRPNVGKSSLLnALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 241 VHVIDmsglEGRDPYEDYVTINnelkeyNLRLTERPQVVVANKMDMPDAEENLQA---FKEKVGDEVKIFPISAVTRQGV 317
Cdd:cd00880 81 LLVVD----SDLTPVEEEAKLG------LLRERGKPVLLVLNKIDLVPESEEEELlreRKLELLPDLPVIAVSALPGEGI 150
|
170
....*....|
gi 1005571658 318 RDLLFEVANL 327
Cdd:cd00880 151 DELRKKIAEL 160
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
160-283 |
9.37e-30 |
|
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: 111.56 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 160 DVGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETgDNRSFVMADLPGLIEGAHAGVGLGHQFLRHIErTRV 239
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLEL-KGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1005571658 240 IVHVIDMSglegrdpyEDYVTINNELKEYnLRLTERPQVVVANK 283
Cdd:pfam01926 79 ILFVVDSE--------EGITPLDEELLEL-LRENKKPIILVLNK 113
|
|
| Obg_CgtA_exten |
TIGR03595 |
Obg family GTPase CgtA, C-terminal extension; CgtA (see model TIGR02729) is a broadly ... |
358-426 |
1.29e-26 |
|
Obg family GTPase CgtA, C-terminal extension; CgtA (see model TIGR02729) is a broadly conserved member of the obg family of GTPases associated with ribosome maturation. This model represents a unique C-terminal domain found in some but not all sequences of CgtA. This region is preceded, and may be followed, by a region of low-complexity sequence.
Pssm-ID: 274668 [Multi-domain] Cd Length: 69 Bit Score: 101.43 E-value: 1.29e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005571658 358 FEITRESDGTFVISGYDIEKTFKMTDFSRDESIRRFARQMRGMGIDEALRARGAKDGDIVKILEYEFEF 426
Cdd:TIGR03595 1 FEIERDGDGVFVVSGKKIERWVAKTPFNNDEALRRFARKLKKLGVEDALRKAGAKAGDTVRIGDFEFEW 69
|
|
| DUF1967 |
pfam09269 |
Domain of unknown function (DUF1967); Members of this family contain a four-stranded beta ... |
360-426 |
1.73e-26 |
|
Domain of unknown function (DUF1967); Members of this family contain a four-stranded beta sheet and three alpha helices flanked by an additional beta strand. They are predominantly found in the bacterial GTP-binding protein Obg, and are still functionally uncharacterized.
Pssm-ID: 462733 [Multi-domain] Cd Length: 67 Bit Score: 100.91 E-value: 1.73e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005571658 360 ITRESDGTFVISGYDIEKTFKMTDFSRDESIRRFARQMRGMGIDEALRARGAKDGDIVKILEYEFEF 426
Cdd:pfam09269 1 IEEDEEGVFVVEGPKIERLVRMTNFDNEESLRRFQRVLKKLGVEDALRKAGAKEGDTVRIGDFEFEY 67
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
161-356 |
3.12e-25 |
|
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: 105.00 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGV-------------VETGDNRSFVMA----------DLPGLI 217
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrvecpckelgVSCNPRYGKCIDgkryvpveliDVAGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 218 EGAHAGVGLGHQFLRHIERTRVIVHVIDMSG----------LEGRDPYEDYVTINNELKEY---NLR------------- 271
Cdd:cd01899 81 PGAHEGKGLGNQFLDDLRDADVLIHVVDASGgtdaegngveTGGYDPLEDIEFLENEIDMWiygILErnwekivrkakae 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 272 -------LTER--------------------------------------------PQVVVANKMDMPDAEENLQAFKEKV 300
Cdd:cd01899 161 ktdiveaLSEQlsgfgvnedvviealeelelpadlskwddedllrlarelrkrrkPMVIAANKADIPDAEENISKLRLKY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005571658 301 GDEVkIFPISAVTRQGVRDLlfEVANLIETTPEFPIHEVADES-------------DTSVMYKFDTEGV 356
Cdd:cd01899 241 PDEI-VVPTSAEAELALRRA--AKQGLIKYVPGDSDFEITDEDglsdkqrealeniRDEVLDRFGSTGV 306
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
161-311 |
9.78e-24 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 102.19 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGV---------VETG-----------DNRSFV---MADLPGLI 217
Cdd:PRK09602 4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecpcKELGvkcnprngkciDGTRFIpveLIDVAGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 218 EGAHAGVGLGHQFLRHIERTRVIVHVIDMSG---LEGR-------DPYEDYVTINNELKEY------------------- 268
Cdd:PRK09602 84 PGAHEGRGLGNQFLDDLRQADALIHVVDASGstdEEGNpvepgshDPVEDIKFLEEELDMWiygileknwekfsrkaqae 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 269 ------------------------------------------------NLRLTERPQVVVANKMDMPDAEENLQAFKEKV 300
Cdd:PRK09602 164 kfdieealaeqlsglgineehvkealrelglpedpskwtdedllelarELRKISKPMVIAANKADLPPAEENIERLKEEK 243
|
250
....*....|.
gi 1005571658 301 GDEVkiFPISA 311
Cdd:PRK09602 244 YYIV--VPTSA 252
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
159-328 |
1.72e-22 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 97.95 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 159 ADVGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRsFVMADLPGLIEGAHAGVGLGHQFLRHIERTR 238
Cdd:COG1163 64 ATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAK-IQILDVPGLIEGAASGKGRGKEVLSVVRNAD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 239 VIVHVIDMSGLEGRD-----------------PY-----------------------EDYVTINNELKEYNLRLTER--- 275
Cdd:COG1163 143 LILIVLDVFELEQYDvlkeelydagirlnkppPDvtiekkgkggirvnstgkldldeEDIKKILREYGIVNADVLIRedv 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005571658 276 ----------------PQVVVANKMDMPDaEENLQAFKEKVGDEVKIFPISAVTRQGVRDL---LFEVANLI 328
Cdd:COG1163 223 tlddlidalmgnrvykPAIVVVNKIDLAD-EEYVEELKSKLPDGVPVIFISAEKGIGLEELkeeIFEELGLI 293
|
|
| YchF |
cd01900 |
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
161-265 |
7.83e-20 |
|
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.
Pssm-ID: 206687 [Multi-domain] Cd Length: 274 Bit Score: 88.67 E-value: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNR------------------SFVmaDLPGLIEGAHA 222
Cdd:cd01900 1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVPDERldklaeivkpkkivpatiEFV--DIAGLVKGASK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1005571658 223 GVGLGHQFLRHIERTRVIVHVI------DMSGLEGR-DPYEDYVTINNEL 265
Cdd:cd01900 79 GEGLGNKFLSHIREVDAIAHVVrcfeddDITHVEGSvDPVRDIEIINTEL 128
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
159-283 |
7.85e-20 |
|
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: 87.99 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 159 ADVGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRsFVMADLPGLIEGAHAGVGLGHQFLRHIERTR 238
Cdd:cd01896 1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAK-IQLLDLPGIIEGASDGKGRGRQVIAVARTAD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1005571658 239 VIVHVIDMSGLEGrdpyeDYVTINNELKEYNLRLT-ERPQVVVANK 283
Cdd:cd01896 80 LILIVLDATKPEG-----QREILERELEGVGIRLNkKPPNVTIKKK 120
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
161-265 |
1.25e-18 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 86.92 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNR-----------SFVMA-----DLPGLIEGAHAGV 224
Cdd:PTZ00258 24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERfdwlckhfkpkSIVPAqlditDIAGLVKGASEGE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1005571658 225 GLGHQFLRHIERTRVIVHVI------DMSGLEGR-DPYEDYVTINNEL 265
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVrafedeDITHVEGEiDPVRDLEIISSEL 151
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
163-329 |
1.25e-18 |
|
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: 82.61 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 163 LVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMaDLPGLiegahagvgLGHQF------------ 230
Cdd:cd01897 5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVI-DTPGI---------LDRPLeerntiemqait 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 231 -LRHIerTRVIVHVIDMSGLEGRdPYEDYVTINNELKEynlrLTERPQVVVANKMDMPDAEENLQAFKEKVGDEVKIFPI 309
Cdd:cd01897 75 aLAHL--RAAVLFFIDPSETCGY-SIEEQLSLFKEIKP----LFNKPVIVVLNKIDLLTEEDLSEIEKELEKEGEEVIKI 147
|
170 180
....*....|....*....|
gi 1005571658 310 SAVTRQGVRDLLFEVANLIE 329
Cdd:cd01897 148 STLTEEGVDELKNKACELLL 167
|
|
| Nog1 |
COG1084 |
GTP-binding protein, GTP1/Obg family [General function prediction only]; |
165-335 |
2.50e-18 |
|
GTP-binding protein, GTP1/Obg family [General function prediction only];
Pssm-ID: 440701 [Multi-domain] Cd Length: 330 Bit Score: 85.27 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 165 GFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRsFVMADLPGL----------IE----GAhagvglghqf 230
Cdd:COG1084 167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR-YQVIDTPGLldrplserneIErqaiLA---------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 231 LRHIerTRVIVHVIDMSGLEGRdPYEDYVTINNELKEynlrLTERPQVVVANKMDMPDAEEnlqafkEKVGDEVKIFPIS 310
Cdd:COG1084 236 LKHL--ADVILFLFDPSETCGY-SLEEQLNLLEEIRS----LFDVPVIVVINKIDLSDEEE------LKEAEEEADIKIS 302
|
170 180
....*....|....*....|....*
gi 1005571658 311 AVTRQGVRDLLFEVANLIETTPEFP 335
Cdd:COG1084 303 ALTGEGVDELLDELIEALEEEPELP 327
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
162-326 |
2.68e-18 |
|
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: 81.73 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 162 GLVGFPSVGKSTLL-SVVSSARPKIAEYHFTTIVPNLGVVET-GDNRSFVMADLPGLIEGAHAGvgLGHQFLRHIERTRV 239
Cdd:cd00882 1 VVVGRGGVGKSSLLnALLGGEVGEVSDVPGTTRDPDVYVKELdKGKVKLVLVDTPGLDEFGGLG--REELARLLLRGADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 240 IVHVIDMSglegRDPYEDYVTinnELKEYNLRLTERPQVVVANKMDMPDA---EENLQAFKEKVGDEVKIFPISAVTRQG 316
Cdd:cd00882 79 ILLVVDST----DRESEEDAK---LLILRRLRKEGIPIILVGNKIDLLEErevEELLRLEELAKILGVPVFEVSAKTGEG 151
|
170
....*....|
gi 1005571658 317 VRDLLFEVAN 326
Cdd:cd00882 152 VDELFEKLIE 161
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
161-363 |
4.65e-14 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 72.33 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLL--------SVVSSaRPKiaeyhfTT---IvpnLGVVeTGDNRSFVMADLPGLIEGAHAgvgLGhQ 229
Cdd:COG1159 6 VAIVGRPNVGKSTLLnalvgqkvSIVSP-KPQ------TTrhrI---RGIV-TREDAQIVFVDTPGIHKPKRK---LG-R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 230 FLRH-----IERTRVIVHVIDMSglEGRDPYEDYvtINNELKEynlrlTERPQVVVANKMDMPDAE---ENLQAFKEKvG 301
Cdd:COG1159 71 RMNKaawsaLEDVDVILFVVDAT--EKIGEGDEF--ILELLKK-----LKTPVILVINKIDLVKKEellPLLAEYSEL-L 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005571658 302 DEVKIFPISAVTRQGVRDLLFEVANLIettPE----FPIHEVADESDtsvmykfdtegvKF---EITRE 363
Cdd:COG1159 141 DFAEIVPISALKGDNVDELLDEIAKLL---PEgppyYPEDQITDRPE------------RFlaaEIIRE 194
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
161-321 |
1.02e-13 |
|
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: 68.64 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLL--------SVVSsarPKIAeyhfTTIVPNLGVVeTGDNRSFVMADLPGLIEGAHagvGLGHQFLR 232
Cdd:cd04163 6 VAIIGRPNVGKSTLLnalvgqkiSIVS---PKPQ----TTRNRIRGIY-TDDDAQIIFVDTPGIHKPKK---KLGERMVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 233 HIERT----RVIVHVIDMSglEGRDPYEDYvtINNELKEYNlrlteRPQVVVANKMDMPDAEENLQAFKEKV---GDEVK 305
Cdd:cd04163 75 AAWSAlkdvDLVLFVVDAS--EWIGEGDEF--ILELLKKSK-----TPVILVLNKIDLVKDKEDLLPLLEKLkelHPFAE 145
|
170
....*....|....*.
gi 1005571658 306 IFPISAVTRQGVRDLL 321
Cdd:cd04163 146 IFPISALKGENVDELL 161
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
161-364 |
2.59e-11 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 63.91 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLL--------SVVSSaRPKiaeyhfTTIVPNLGVVeTGDNRSFVMADLPGLIEGAHAgvgLGhQFLR 232
Cdd:PRK00089 8 VAIVGRPNVGKSTLLnalvgqkiSIVSP-KPQ------TTRHRIRGIV-TEDDAQIIFVDTPGIHKPKRA---LN-RAMN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 233 H-----IERTRVIVHVIDmsGLEGRDPYEDYVtinneLKeyNLRLTERPQVVVANKMDMPDAEENLQAFKEKV---GDEV 304
Cdd:PRK00089 76 KaawssLKDVDLVLFVVD--ADEKIGPGDEFI-----LE--KLKKVKTPVILVLNKIDLVKDKEELLPLLEELselMDFA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005571658 305 KIFPISAVTRQGVRDLLfevANLIETTPE----FPIHEVADESDtSVMYKfdtegvkfEITRES 364
Cdd:PRK00089 147 EIVPISALKGDNVDELL---DVIAKYLPEgppyYPEDQITDRPE-RFLAA--------EIIREK 198
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
161-320 |
3.81e-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: 61.23 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFV--MADLPGLIEGAHAGVGLGHQFLRHIERTR 238
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKfnLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 239 VIVHVIDM-SGLEgrdpyEDYVTINNELKeynlrlTERPQVVVANKMDMPDAEenlqaFKEKVGDEV------KIFPISA 311
Cdd:TIGR00231 84 IVILVLDVeEILE-----KQTKEIIHHAD------SGVPIILVGNKIDLKDAD-----LKTHVASEFaklngePIIPLSA 147
|
....*....
gi 1005571658 312 VTRQGVRDL 320
Cdd:TIGR00231 148 ETGKNIDSA 156
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
163-329 |
4.91e-11 |
|
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: 60.93 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 163 LVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDnRSFVMADLPGL--IEGAHAGVGLGHQFLRHiERTRVI 240
Cdd:cd01879 2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGG-KEIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 241 VHVIDMSGLEgRdpyedyvtinnelkeyNLRLT------ERPQVVVANKMDMpdAEE-----NLQAFKEKVGdeVKIFPI 309
Cdd:cd01879 80 VNVVDATNLE-R----------------NLYLTlqllelGLPVVVALNMIDE--AEKrgikiDLDKLSELLG--VPVVPT 138
|
170 180
....*....|....*....|
gi 1005571658 310 SAVTRQGVRDLLFEVANLIE 329
Cdd:cd01879 139 SARKGEGIDELLDAIAKLAE 158
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
161-328 |
1.59e-10 |
|
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: 60.17 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGahagvgLGHQ----FLRHIER 236
Cdd:cd01878 44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRD------LPHQlveaFRSTLEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 237 TR---VIVHVIDMSglegrDP-YEDYV-TINNELKEynLRLTERPQVVVANKMDMPDAEENLQAFKEKVGDEVkifPISA 311
Cdd:cd01878 118 VAeadLLLHVVDAS-----DPdREEQIeTVEEVLKE--LGADDIPIILVLNKIDLLDDEELEERLRAGRPDAV---FISA 187
|
170
....*....|....*..
gi 1005571658 312 VTRQGVRDLLFEVANLI 328
Cdd:cd01878 188 KTGEGLDLLKEAIEELL 204
|
|
| era |
TIGR00436 |
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
161-344 |
2.06e-08 |
|
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: 55.09 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEGAHAGVGL----GHQFLRHIEr 236
Cdd:TIGR00436 3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKHSLNRLmmkeARSAIGGVD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 237 trVIVHVIDMSGLEGRDPYedyvtINNELKEynlrlTERPQVVVANKMDM--PDAEENLQAFKEKVGDEVKIFPISAVTR 314
Cdd:TIGR00436 82 --LILFVVDSDQWNGDGEF-----VLTKLQN-----LKRPVVLTRNKLDNkfKDKLLPLIDKYAILEDFKDIVPISALTG 149
|
170 180 190
....*....|....*....|....*....|.
gi 1005571658 315 QGVRDLL-FEVANLIETTPEFPIHEVADESD 344
Cdd:TIGR00436 150 DNTSFLAaFIEVHLPEGPFRYPEDYVTDQPD 180
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
163-321 |
7.73e-08 |
|
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.
Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 51.42 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 163 LVGFPSVGKSTLLSvvssarpKIAEYHFTTIVPNLGV-VETGD--NRSFVMADlpgliegahagVGlGHQFLRHI----- 234
Cdd:cd00878 4 MLGLDGAGKTTILY-------KLKLGEVVTTIPTIGFnVETVEykNVKFTVWD-----------VG-GQDKIRPLwkhyy 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 235 ERTRVIVHVIDMSglegrDPyEDYVTINNELKEY--NLRLTERPQVVVANKMDMPDA------EENLQAFKEKvGDEVKI 306
Cdd:cd00878 65 ENTDGLIFVVDSS-----DR-ERIEEAKNELHKLlnEEELKGAPLLILANKQDLPGAlteselIELLGLESIK-GRRWHI 137
|
170
....*....|....*
gi 1005571658 307 FPISAVTRQGVRDLL 321
Cdd:cd00878 138 QPCSAVTGDGLDEGL 152
|
|
| PRK11058 |
PRK11058 |
GTPase HflX; Provisional |
161-323 |
2.06e-07 |
|
GTPase HflX; Provisional
Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 52.80 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNLGVVETGDNRSFVMADLPGLIEG-AHAGVGLGHQFLRHIERTRV 239
Cdd:PRK11058 200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHlPHDLVAAFKATLQETRQATL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 240 IVHVIDMSGLEGRdpyEDYVTINNELKEynLRLTERPQVVVANKMDMpdaeenLQAFKEKVGDEVKIFPI----SAVTRQ 315
Cdd:PRK11058 280 LLHVVDAADVRVQ---ENIEAVNTVLEE--IDAHEIPTLLVMNKIDM------LDDFEPRIDRDEENKPIrvwlSAQTGA 348
|
....*...
gi 1005571658 316 GVrDLLFE 323
Cdd:PRK11058 349 GI-PLLFQ 355
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
161-321 |
2.24e-07 |
|
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: 50.51 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLL--------SVVSSarpkIAEyhfTTIVPNLGVVETgDNRSFVMADLPGLIEGAHagVGLGHQF-- 230
Cdd:cd01895 5 IAIIGRPNVGKSSLLnallgeerVIVSD----IAG---TTRDSIDVPFEY-DGQKYTLIDTAGIRKKGK--VTEGIEKys 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 231 ----LRHIERTRVIVHVIDMS-GLEGRDpyedyVTINNELKEYNlrlteRPQVVVANKMD-MPDAEENLQAFKEKVG--- 301
Cdd:cd01895 75 vlrtLKAIERADVVLLVLDASeGITEQD-----LRIAGLILEEG-----KALIIVVNKWDlVEKDEKTMKEFEKELRrkl 144
|
170 180
....*....|....*....|...
gi 1005571658 302 ---DEVKIFPISAVTRQGVRDLL 321
Cdd:cd01895 145 pflDYAPIVFISALTGQGVDKLF 167
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
163-321 |
2.44e-07 |
|
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: 50.13 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 163 LVGFPSVGKSTL--------LSVVSSarpkiaeyhfttiVPNL------GVVETGDnRSFVMADLPGLIEGAHagvGLGH 228
Cdd:cd01894 2 IVGRPNVGKSTLfnrltgrrDAIVSD-------------TPGVtrdrkyGEAEWGG-REFILIDTGGIEPDDE---GISK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 229 ----QFLRHIERTRVIVHVIDmsGLEGRDPyEDYvtinnELKEYnLRLTERPQVVVANKMDMPDAEENLQAFkEKVGDEv 304
Cdd:cd01894 65 eireQAEIAIEEADVILFVVD--GREGLTP-ADE-----EIAKY-LRKSKKPVILVVNKIDNIKEEEEAAEF-YSLGFG- 133
|
170
....*....|....*..
gi 1005571658 305 KIFPISAVTRQGVRDLL 321
Cdd:cd01894 134 EPIPISAEHGRGIGDLL 150
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
161-338 |
2.49e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 52.74 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTL---LsvvssARPKIAeyhfttIV---PNL------GVVETGDnRSFVMADLPGLIEGAHagvGLGH 228
Cdd:PRK00093 4 VAIVGRPNVGKSTLfnrL-----TGKRDA------IVadtPGVtrdriyGEAEWLG-REFILIDTGGIEPDDD---GFEK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 229 ----QFLRHIERTRVIVHVIDmsGLEGRDPyEDYvtinnELKEYnLRLTERPQVVVANKMDMPDAEENLQAFKE-KVGDe 303
Cdd:PRK00093 69 qireQAELAIEEADVILFVVD--GRAGLTP-ADE-----EIAKI-LRKSNKPVILVVNKVDGPDEEADAYEFYSlGLGE- 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1005571658 304 vkIFPISAVTRQGVRDLLFEVANLIETTPEFPIHE 338
Cdd:PRK00093 139 --PYPISAEHGRGIGDLLDAILEELPEEEEEDEED 171
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
161-333 |
2.51e-07 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 52.72 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTL---LsvvssARPKIAeyhfttIV---PNL------GVVETGDnRSFVMADLPGLIEGAHAGVgLGH 228
Cdd:COG1160 5 VAIVGRPNVGKSTLfnrL-----TGRRDA------IVddtPGVtrdriyGEAEWGG-REFTLIDTGGIEPDDDDGL-EAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 229 ---QFLRHIERTRVIVHVIDmsGLEGRDPyEDYvtinnELKEYnLRLTERPQVVVANKMDMPDAEENLQAFKE-KVGDev 304
Cdd:COG1160 72 ireQAELAIEEADVILFVVD--GRAGLTP-LDE-----EIAKL-LRRSGKPVILVVNKVDGPKREADAAEFYSlGLGE-- 140
|
170 180
....*....|....*....|....*....
gi 1005571658 305 kIFPISAVTRQGVRDLLFEVANLIETTPE 333
Cdd:COG1160 141 -PIPISAEHGRGVGDLLDAVLELLPEEEE 168
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
161-320 |
2.99e-07 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 50.36 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSVVSSARPKIAEYHFT---TIVpNLGVVETGDNRSFVMADLPGLIEGAHAgvglGHQFLRHIERT 237
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTngvTID-KKELKLDGLDVDLVIWDTPGQDEFRET----RQFYARQLTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 238 RVIVHVIDmsgleGRDPyEDYVTINNELKEYNLRLTERPQVVVANKMDMPDAEE--NLQAFKEKVGDE--VKIFPISAVT 313
Cdd:COG1100 81 SLYLFVVD-----GTRE-ETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEieDEERLKEALSEDniVEVVATSAKT 154
|
....*..
gi 1005571658 314 RQGVRDL 320
Cdd:COG1100 155 GEGVEEL 161
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
161-328 |
2.74e-06 |
|
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: 47.12 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLS--------VVSSARPkiaeyhFTTIVPNLgvVETGDNRSFVmaDLPG----------------L 216
Cdd:cd01876 2 VAFAGRSNVGKSSLINaltnrkklARTSKTP------GRTQLINF--FNVGDKFRLV--DLPGygyakvskevrekwgkL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 217 IEgahagvglghQFLRHIERTRVIVHVIDMSglegRDPYEDYVTINNELKEYNLrlterPQVVVANKMDM---PDAEENL 293
Cdd:cd01876 72 IE----------EYLENRENLKGVVLLIDAR----HGPTPIDLEMLEFLEELGI-----PFLIVLTKADKlkkSELAKVL 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 1005571658 294 QAFKEKVG---DEVKIFPISAVTRQGVRDLLFEVANLI 328
Cdd:cd01876 133 KKIKEELNlfnILPPVILFSSKKGTGIDELRALIAEWL 170
|
|
| ARLTS1 |
cd04156 |
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ... |
161-327 |
1.93e-05 |
|
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.
Pssm-ID: 133356 [Multi-domain] Cd Length: 160 Bit Score: 44.71 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSvvssaRPKIAEYhFTTIvPNLGV-VEtgdnrsfvMADLPGLIEGAHAGVGlGHQFLR-----HI 234
Cdd:cd04156 2 VLLLGLDSAGKSTLLY-----KLKHAEL-VTTI-PTVGFnVE--------MLQLEKHLSLTVWDVG-GQEKMRtvwkcYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 235 ERTRVIVHVIDMSGLEGRDpyEDYVTINNELKEYNLRltERPQVVVANKMDMPDA---EENLQAFK-EKVGDEVKIF--P 308
Cdd:cd04156 66 ENTDGLVYVVDSSDEARLD--ESQKELKHILKNEHIK--GVPVVLLANKQDLPGAltaEEITRRFKlKKYCSDRDWYvqP 141
|
170
....*....|....*....
gi 1005571658 309 ISAVTRQGVRDLLFEVANL 327
Cdd:cd04156 142 CSAVTGEGLAEAFRKLASF 160
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
156-311 |
5.44e-05 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 43.75 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 156 KVLADVGLVGFPSVGKSTLLSVVSSARPKIAEYHFTTIVPNlgvveTGDNRSFVMADLPGLieGAHAGVGLGHQ------ 229
Cdd:PRK04213 7 DRKPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPN-----HYDWGDFILTDLPGF--GFMSGVPKEVQekikde 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 230 FLRHIE----RTRVIVHVID-MSGLEGRDPYE--DYVTINNELKEYnLRLTERPQVVVANKMD-MPDAEENLQAFKEKVG 301
Cdd:PRK04213 80 IVRYIEdnadRILAAVLVVDgKSFIEIIERWEgrGEIPIDVEMFDF-LRELGIPPIVAVNKMDkIKNRDEVLDEIAERLG 158
|
170
....*....|....*...
gi 1005571658 302 --------DEVkIFPISA 311
Cdd:PRK04213 159 lyppwrqwQDI-IAPISA 175
|
|
| MMR_HSR1_C |
pfam08438 |
GTPase of unknown function C-terminal; This domain is found at the C-terminus of pfam01926 in ... |
280-356 |
6.19e-05 |
|
GTPase of unknown function C-terminal; This domain is found at the C-terminus of pfam01926 in archaeal and eukaryotic GTP-binding proteins. The C-terminal domain of the GTP-binding proteins is necessary 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 nucleotides.
Pssm-ID: 429998 [Multi-domain] Cd Length: 109 Bit Score: 42.13 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 280 VANKMDMPDAEENLQAFKEKvGDEVKIFPISAVT----RQGVRdllfevANLIETTP---EFPIHEVADESD-------- 344
Cdd:pfam08438 1 AANKADLPAADENIEKLKEK-YPDHIVVPTSAEAelalRKAAK------AGLIDYLPgdsDFEIKEDGLLSEkqkkalen 73
|
90
....*....|....
gi 1005571658 345 --TSVMYKFDTEGV 356
Cdd:pfam08438 74 irDLVLKRYGSTGV 87
|
|
| PRK09518 |
PRK09518 |
bifunctional cytidylate kinase/GTPase Der; Reviewed |
156-332 |
1.08e-04 |
|
bifunctional cytidylate kinase/GTPase Der; Reviewed
Pssm-ID: 236546 [Multi-domain] Cd Length: 712 Bit Score: 44.40 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 156 KVLADVGLVGFPSVGKSTLLSVVSSARPKIAEYhfTTIVPNLGVVETGD--NRSFVMADLPGL---IEGAHAGVglGHQF 230
Cdd:PRK09518 273 KAVGVVAIVGRPNVGKSTLVNRILGRREAVVED--TPGVTRDRVSYDAEwaGTDFKLVDTGGWeadVEGIDSAI--ASQA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 231 LRHIERTRVIVHVIDmsGLEGrdpyedyVTINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAF-KEKVGDEvkiFPI 309
Cdd:PRK09518 349 QIAVSLADAVVFVVD--GQVG-------LTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYDAAEFwKLGLGEP---YPI 416
|
170 180
....*....|....*....|...
gi 1005571658 310 SAVTRQGVRDLLFEVANLIETTP 332
Cdd:PRK09518 417 SAMHGRGVGDLLDEALDSLKVAE 439
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
276-330 |
3.28e-04 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 41.30 E-value: 3.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005571658 276 PQVVVANKMD-MPDAEENLQAFK----------EKVGDEVKIFPISAVTRQGVRDLLFEVANLIET 330
Cdd:cd01887 103 PIIVAINKIDkPYGTEADPERVKnelselglvgEEWGGDVSIVPISAKTGEGIDDLLEAILLLAEV 168
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
163-321 |
3.39e-04 |
|
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: 40.94 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 163 LVGFPSVGKSTLLSVVssARPKIAeyhfttIVPNL-G----VVETG---DNRSFVMADLPGL------IEgaHAGvglgh 228
Cdd:cd04164 8 IAGKPNVGKSSLLNAL--AGRDRA------IVSDIaGttrdVIEEEidlGGIPVRLIDTAGLretedeIE--KIG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 229 qflrhIERTR-------VIVHVIDMSGLegrdpyedyvtINNELKEYNLRLTERPQVVVANKMDMPDAEENLQAFKEKvg 301
Cdd:cd04164 73 -----IERAReaieeadLVLLVVDASEG-----------LDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISELNGK-- 134
|
170 180
....*....|....*....|
gi 1005571658 302 devKIFPISAVTRQGVRDLL 321
Cdd:cd04164 135 ---PIIAISAKTGEGIDELK 151
|
|
| Arf |
pfam00025 |
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together |
163-321 |
3.66e-04 |
|
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
Pssm-ID: 459636 [Multi-domain] Cd Length: 160 Bit Score: 41.06 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 163 LVGFPSVGKSTLLSvvssaRPKIAEyhFTTIVPNLGV-VET--GDNRSFVMADlpgliegahagVGlGHQFLR-----HI 234
Cdd:pfam00025 5 ILGLDNAGKTTILY-----KLKLGE--IVTTIPTIGFnVETvtYKNVKFTVWD-----------VG-GQESLRplwrnYF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 235 ERTRVIVHVIDMSglegrdpyeDYVTINNELKEYNLRLTER-----PQVVVANKMDMPDAeENLQAFKEKVG-DEVK--- 305
Cdd:pfam00025 66 PNTDAVIFVVDSA---------DRDRIEEAKEELHALLNEEeladaPLLILANKQDLPGA-MSEAEIRELLGlHELKdrp 135
|
170
....*....|....*...
gi 1005571658 306 --IFPISAVTRQGVRDLL 321
Cdd:pfam00025 136 weIQGCSAVTGEGLDEGL 153
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
276-330 |
5.99e-04 |
|
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: 40.59 E-value: 5.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005571658 276 PQVVVANKMDMPDAEEnLQAFKEKV-----------GDEVKIFPISAVTRQGVRDLLFEVANLIET 330
Cdd:pfam00009 123 PIIVFINKMDRVDGAE-LEEVVEEVsrellekygedGEFVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
231-321 |
6.98e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 41.57 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 231 LRHIERTRVIVHVIDmsGLEGrdpyedyvtinneLKEYNLRLTE------RPQVVVANKMDMPDAEEnLQAFKEKVGDE- 303
Cdd:PRK00093 250 LKAIERADVVLLVID--ATEG-------------ITEQDLRIAGlaleagRALVIVVNKWDLVDEKT-MEEFKKELRRRl 313
|
90 100
....*....|....*....|...
gi 1005571658 304 -----VKIFPISAVTRQGVRDLL 321
Cdd:PRK00093 314 pfldyAPIVFISALTGQGVDKLL 336
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
234-330 |
7.41e-04 |
|
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: 41.59 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 234 IERTR-------VIVHVIDMSglegRDPYEDYVTINNELKEynlrlteRPQVVVANKMDMPDAEENlqafKEKVGDEVKI 306
Cdd:COG0486 283 IERAReaieeadLVLLLLDAS----EPLTEEDEEILEKLKD-------KPVIVVLNKIDLPSEADG----ELKSLPGEPV 347
|
90 100
....*....|....*....|....
gi 1005571658 307 FPISAVTRQGVRDLLFEVANLIET 330
Cdd:COG0486 348 IAISAKTGEGIDELKEAILELVGE 371
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
231-321 |
1.26e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 40.78 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 231 LRHIERTRVIVHVID-MSGLEGRDpyedyVTINNELKEYNlrlteRPQVVVANKMD-MPDAEENLQAFKEKVGDE----- 303
Cdd:COG1160 252 LRAIERADVVLLVIDaTEGITEQD-----LKIAGLALEAG-----KALVIVVNKWDlVEKDRKTREELEKEIRRRlpfld 321
|
90
....*....|....*....
gi 1005571658 304 -VKIFPISAVTRQGVRDLL 321
Cdd:COG1160 322 yAPIVFISALTGQGVDKLL 340
|
|
| PRK03003 |
PRK03003 |
GTP-binding protein Der; Reviewed |
138-344 |
1.73e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 179525 [Multi-domain] Cd Length: 472 Bit Score: 40.34 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 138 EIAENGEPGQERDVILELKVLAdvgLVGFPSVGKSTLLSVVSSARPKIAEYhfttiVPnlGVveTGD---------NRSF 208
Cdd:PRK03003 21 ELDDEDLAELEAAEGGPLPVVA---VVGRPNVGKSTLVNRILGRREAVVED-----VP--GV--TRDrvsydaewnGRRF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 209 VMADLPGL---IEGAHAGVGlgHQFLRHIERTRVIVHVID-MSGLEGRDpyEDYVTInnelkeynLRLTERPQVVVANKM 284
Cdd:PRK03003 89 TVVDTGGWepdAKGLQASVA--EQAEVAMRTADAVLFVVDaTVGATATD--EAVARV--------LRRSGKPVILAANKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005571658 285 DMPDAEENLQAFKE-KVGDEvkiFPISAVTRQGVRDLLFEVanlIETTPEFPihEVADESD 344
Cdd:PRK03003 157 DDERGEADAAALWSlGLGEP---HPVSALHGRGVGDLLDAV---LAALPEVP--RVGSASG 209
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
228-328 |
2.12e-03 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 39.17 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 228 HQFLRHIERTR----VIVHVIDMSGLEGrdpyedyvTINNELKEYNlrlTERPQVVVANKMDM--PDAeeNLQAFKEKVG 301
Cdd:cd01855 21 EDFLEILSTLLndnaLVVHVVDIFDFPG--------SLIPGLAELI---GAKPVILVGNKIDLlpKDV--KPNRLKQWVK 87
|
90 100 110
....*....|....*....|....*....|....*
gi 1005571658 302 DEVK--------IFPISAVTRQGVRDLLFEVANLI 328
Cdd:cd01855 88 KRLKigglkikdVILVSAKKGWGVEELIEEIKKLA 122
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
161-333 |
2.93e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.36 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTL--------LSVVSSARP---KIAEYHFttivpnlgvvETGDNRSFVMADLPGL--IEGAHAGVglg 227
Cdd:COG3596 42 IALVGKTGAGKSSLinalfgaeVAEVGVGRPctrEIQRYRL----------ESDGLPGLVLLDTPGLgeVNERDREY--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 228 HQFLRHIERTRVIVHVIDmsgleGRDPY----EDYVtinNELKEYNLRLterPQVVVANKMDM--PDAEEN--------- 292
Cdd:COG3596 109 RELRELLPEADLILWVVK-----ADDRAlatdEEFL---QALRAQYPDP---PVLVVLTQVDRlePEREWDppynwpspp 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005571658 293 --------LQAFKEKVGDEVK-IFPISA---VTRQGVRDLlfeVANLIETTPE 333
Cdd:COG3596 178 keqnirraLEAIAEQLGVPIDrVIPVSAaedRTGYGLEEL---VDALAEALPE 227
|
|
| HSR1_MMR1 |
cd01857 |
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ... |
161-217 |
3.49e-03 |
|
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.
Pssm-ID: 206750 [Multi-domain] Cd Length: 140 Bit Score: 37.60 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005571658 161 VGLVGFPSVGKSTLLS------VVSSARPKIAEYHFTTIVPNLGVvetgdnrsfVMADLPGLI 217
Cdd:cd01857 85 IGLVGYPNVGKSSLINalvgskKVSVSSTPGKTKHFQTIFLEPGI---------TLCDCPGLV 138
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
234-321 |
4.73e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 38.94 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 234 IERTR-------VIVHVIDMSGLEGRDPYEDYVTINNElkeynlrlterPQVVVANKMDMPDAEENLQAFKEKVgdevki 306
Cdd:PRK05291 285 IERSReaieeadLVLLVLDASEPLTEEDDEILEELKDK-----------PVIVVLNKADLTGEIDLEEENGKPV------ 347
|
90
....*....|....*
gi 1005571658 307 FPISAVTRQGVRDLL 321
Cdd:PRK05291 348 IRISAKTGEGIDELR 362
|
|
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
270-337 |
5.91e-03 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 39.13 E-value: 5.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005571658 270 LRLTERPQVVVA-NKMDMPDAEEnLQAFKEKVGDEVK--------IFPISAVTRQGVRDLLFEVANLIETTPEFPIH 337
Cdd:COG3276 99 LDLLGIKRGIVVlTKADLVDEEW-LELVEEEIRELLAgtfledapIVPVSAVTGEGIDELRAALDALAAAVPARDAD 174
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
161-329 |
6.42e-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: 37.66 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 161 VGLVGFPSVGKSTLLSV---VSSARPKIAEYHFT-------------TIVPNLGVVETGDNR-SFVmaDLPGliegaHAg 223
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSllyQTGAIDRRGTRKETfldtlkeerergiTIKTGVVEFEWPKRRiNFI--DTPG-----HE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571658 224 vglghQFLRHIERTRVI----VHVIDMS-GLEGRdpYEDYVTInnelkeynLRLTERPQVVVANKMDMP---DAEENLQA 295
Cdd:cd00881 74 -----DFSKETVRGLAQadgaLLVVDANeGVEPQ--TREHLNI--------ALAGGLPIIVAVNKIDRVgeeDFDEVLRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005571658 296 FKEKVG---------DEVKIFPISAVTRQGVRDLLFEVANLIE 329
Cdd:cd00881 139 IKELLKligftflkgKDVPIIPISALTGEGIEELLDAIVEHLP 181
|
|
| |
