|
Name |
Accession |
Description |
Interval |
E-value |
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
2-335 |
0e+00 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 538.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 2 KFLDQCKIYVRSGNGGGGAVSFRREKYIEYggpdggdggrggdVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHGA 81
Cdd:PRK12299 1 KFIDEAKIYVKAGDGGNGCVSFRREKFIPFggpdggdggrggsVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 82 AGDDVLLKVPVGTQVLEEDKETLIADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKLIAD 161
Cdd:PRK12299 81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAVL 241
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 242 IHLVDATQDDIAGAWTTIRGELEAYGDELADKSEILALNKVDALDPETRKAKAAELQ-AVSGIKPMLVSGVSGEGVTELL 320
Cdd:PRK12299 241 LHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDEEEEREKRAALElAALGGPVFLISAVTGEGLDELL 320
|
330
....*....|....*
gi 261266718 321 RAAFTQVRIRRGETP 335
Cdd:PRK12299 321 RALWELLEEARREEE 335
|
|
| Obg |
COG0536 |
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
3-347 |
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: 519.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 3 FLDQCKIYVRSGNGGGGAVSFRREKYIEYggpdggdggrggdVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHGAA 82
Cdd:COG0536 1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKggpdggdggrggdVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 83 GDDVLLKVPVGTQVLEEDKETLIADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKLIADV 162
Cdd:COG0536 81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVVAKGGRGGLGNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 163 GLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAVLI 242
Cdd:COG0536 161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 243 HLVDATQDD---IAGAWTTIRGELEAYGDELADKSEILALNKVDALDPETRKAKAAELQAvSGIKPMLVSGVSGEGVTEL 319
Cdd:COG0536 241 HVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLDAEELEELKAELEK-LGGPVFPISAVTGEGLDEL 319
|
330 340
....*....|....*....|....*...
gi 261266718 320 LRAAFTQVRirrgETPAEAAIDEAPEEE 347
Cdd:COG0536 320 LYALAELLE----ELRAEEAEEEEEVEE 343
|
|
| Obg_CgtA |
TIGR02729 |
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
3-327 |
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: 503.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 3 FLDQCKIYVRSGNGGGGAVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHGAA 82
Cdd:TIGR02729 1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 83 GDDVLLKVPVGTQVLEEDKETLIADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKLIADV 162
Cdd:TIGR02729 81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 163 GLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAVLI 242
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 243 HLVDATQD---DIAGAWTTIRGELEAYGDELADKSEILALNKVDALDPETRKAKAAELQAVSGIKPMLVSGVSGEGVTEL 319
Cdd:TIGR02729 241 HLIDISPEdgsDPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLDEEELEELLKELKKELGKPVFPISALTGEGLDEL 320
|
....*...
gi 261266718 320 LRAAFTQV 327
Cdd:TIGR02729 321 LDALAELL 328
|
|
| obgE |
PRK12298 |
GTPase CgtA; Reviewed |
1-345 |
4.41e-160 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 453.56 E-value: 4.41e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 1 MKFLDQCKIYVRSGNGGGGAVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHG 80
Cdd:PRK12298 1 MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 81 AAGDDVLLKVPVGTQVLEEDKETLIADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKLIA 160
Cdd:PRK12298 81 KRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 161 DVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAV 240
Cdd:PRK12298 161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 241 LIHLVDAT---QDDIAGAWTTIRGELEAYGDELADKSEILALNKVDALDPETRKAKAAELQAVSG--IKPMLVSGVSGEG 315
Cdd:PRK12298 241 LLHLIDIApidGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDEEEAEERAKAIVEALGweGPVYLISAASGLG 320
|
330 340 350
....*....|....*....|....*....|
gi 261266718 316 VTELLRAAFTQVRIRRGETPAEAAIDEAPE 345
Cdd:PRK12298 321 VKELCWDLMTFIEENPREEAEEAEAPEKVE 350
|
|
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
2-347 |
9.43e-153 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 436.07 E-value: 9.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 2 KFLDQCKIYVRSGNGGGGAVSFRREKYIEYggpdggdggrggdVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHGA 81
Cdd:PRK12297 1 MFIDQAKIYVKAGDGGDGMVSFRREKYVPKggpdggdggkggsVIFVADEGLRTLLDFRYKRHFKAENGENGMGKNMHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 82 AGDDVLLKVPVGTQVLEEDKETLIADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKLIAD 161
Cdd:PRK12297 81 NGEDLIIKVPVGTVVKDAETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGEERELRLELKLLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAVL 241
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 242 IHLVDAT---QDDIAGAWTTIRGELEAYGDELADKSEILALNKVDALDpetRKAKAAELQAVSGIKPMLVSGVSGEGVTE 318
Cdd:PRK12297 241 VHVIDMSgseGRDPIEDYEKINKELKLYNPRLLERPQIVVANKMDLPE---AEENLEEFKEKLGPKVFPISALTGQGLDE 317
|
330 340
....*....|....*....|....*....
gi 261266718 319 LLRAAFTQVRirrgETPAEAAIDEAPEEE 347
Cdd:PRK12297 318 LLYAVAELLE----ETPEFPLEEEEVEEE 342
|
|
| obgE |
PRK12296 |
GTPase CgtA; Reviewed |
1-353 |
2.17e-102 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 310.65 E-value: 2.17e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 1 MKFLDQCKIYVRSGNGGGGAVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHG 80
Cdd:PRK12296 2 PRFVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTLLDFHFRPHRKATNGKPGMGDNRDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 81 AAGDDVLLKVPVGTQVLEEDKETLiADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKLIA 160
Cdd:PRK12296 82 AAGEDLVLPVPDGTVVLDEDGEVL-ADLVGAGTRFVAAAGGRGGLGNAALASKARKAPGFALLGEPGEERDLVLELKSVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 161 DVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDlSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAV 240
Cdd:PRK12296 161 DVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQ-AGDTRFTVADVPGLIPGASEGKGLGLDFLRHIERCAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 241 LIHLVD-ATQD-------DIAgawtTIRGELEAYGD---------ELADKSEILALNKVDAldPEtrkakAAELqaVSGI 303
Cdd:PRK12296 240 LVHVVDcATLEpgrdplsDID----ALEAELAAYAPaldgdlglgDLAERPRLVVLNKIDV--PD-----AREL--AEFV 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261266718 304 KPML---------VSGVSGEGVTELLRAAFTQVRIRRGETPAEA---------AIDEA-----PEEETPGGWQ 353
Cdd:PRK12296 307 RPELeargwpvfeVSAASREGLRELSFALAELVEEARAAEPEAEptrivirpkAVDDAgftveRDGDGEGGFR 379
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
160-327 |
1.12e-86 |
|
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: 258.89 E-value: 1.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 160 ADVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSA 239
Cdd:cd01898 1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 240 VLIHLVDAT-QDDIAGAWTTIRGELEAYGDELADKSEILALNKVDALDPETRKAK-AAELQAVSGIKPMLVSGVSGEGVT 317
Cdd:cd01898 81 VLLHVIDLSgEDDPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKlKELLKELKGKKVFPISALTGEGLD 160
|
170
....*....|
gi 261266718 318 ELLRAAFTQV 327
Cdd:cd01898 161 ELLKKLAKLL 170
|
|
| GTP1_OBG |
pfam01018 |
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ... |
5-158 |
4.23e-67 |
|
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: 208.35 E-value: 4.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 5 DQCKIYVRSGNGGGGAVSFRREKYIEYGGPDGGDGGRGGDVWIEAVEGLNTLIDYRYQQHFKAGTGVHGMGRGRHGAAGD 84
Cdd:pfam01018 2 DRAKIKVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKRHFKAENGENGGGKNCHGKNGE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261266718 85 DVLLKVPVGTQVLEEDKETLIADLDTAGMTLRLAKGGNGGWGNLHFKGPVNQAPKYANPGQDGEELWVWLRLKL 158
Cdd:pfam01018 82 DLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
163-323 |
3.63e-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: 139.45 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 163 GLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAVLI 242
Cdd:cd01881 1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 243 HLVDATQD---DIAGAWTTIRGELEAYGDELADKSEILALNKVDALDPETRKaKAAELQAVSGIKPMLVSGVSGEGVTEL 319
Cdd:cd01881 81 HVIDASEDcvgDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMASENNLK-RLKLDKLKRGIPVVPTSALTRLGLDRV 159
|
....
gi 261266718 320 LRAA 323
Cdd:cd01881 160 IRTI 163
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
161-281 |
1.25e-31 |
|
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: 115.02 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 161 DVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERFVLADIPGLIEGASEGAGLGTRFLGHvERSAV 240
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELK-GKQIILVDTPGLIEGASEGEGLGRAFLAI-IEADL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 261266718 241 LIHLVDATQDdiagaWTTIRGELEAYGDElADKSEILALNK 281
Cdd:pfam01926 79 ILFVVDSEEG-----ITPLDEELLELLRE-NKKPIILVLNK 113
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
162-248 |
1.65e-26 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 108.74 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGV---------VDLSTS-----------ERFV---LADIPGLI 218
Cdd:PRK09602 4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecpcKELGVKcnprngkcidgTRFIpveLIDVAGLV 83
|
90 100 110
....*....|....*....|....*....|
gi 261266718 219 EGASEGAGLGTRFLGHVERSAVLIHLVDAT 248
Cdd:PRK09602 84 PGAHEGRGLGNQFLDDLRQADALIHVVDAS 113
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
162-248 |
2.50e-26 |
|
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: 106.54 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGV---------VDLSTSE-----------RFV---LADIPGLI 218
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrvecpcKELGVSCnprygkcidgkRYVpveLIDVAGLV 80
|
90 100 110
....*....|....*....|....*....|
gi 261266718 219 EGASEGAGLGTRFLGHVERSAVLIHLVDAT 248
Cdd:cd01899 81 PGAHEGKGLGNQFLDDLRDADVLIHVVDAS 110
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
160-319 |
3.96e-24 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 101.41 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 160 ADVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDlstsERFV---LADIPGLIEGASEGAGLGTRFLGhVE 236
Cdd:COG1163 64 ATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLE----YKGAkiqILDVPGLIEGAASGKGRGKEVLS-VV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 237 RSAVLIHLV------------------------------------------------DATQDDIAG---------AWTTI 259
Cdd:COG1163 139 RNADLILIVldvfeleqydvlkeelydagirlnkpppdvtiekkgkggirvnstgklDLDEEDIKKilreygivnADVLI 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261266718 260 RGELEAygDELAD--------KSEILALNKVDALDPETRKAKAAELQavSGIKPMLVSGVSGEGVTEL 319
Cdd:COG1163 219 REDVTL--DDLIDalmgnrvyKPAIVVVNKIDLADEEYVEELKSKLP--DGVPVIFISAEKGIGLEEL 282
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
160-267 |
2.83e-23 |
|
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: 96.46 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 160 ADVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLaDIPGLIEGASEGAGLGTRFLGhVERSA 239
Cdd:cd01896 1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLL-DLPGIIEGASDGKGRGRQVIA-VARTA 78
|
90 100
....*....|....*....|....*....
gi 261266718 240 VLIHLV-DATQDDIAGAwtTIRGELEAYG 267
Cdd:cd01896 79 DLILIVlDATKPEGQRE--ILERELEGVG 105
|
|
| YchF |
cd01900 |
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
162-251 |
6.27e-21 |
|
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: 90.98 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERF-VLA----------------DIPGLIEGASEG 224
Cdd:cd01900 1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVPVP-DERLdKLAeivkpkkivpatiefvDIAGLVKGASKG 79
|
90 100
....*....|....*....|....*..
gi 261266718 225 AGLGTRFLGHVERSAVLIHLVDATQDD 251
Cdd:cd01900 80 EGLGNKFLSHIREVDAIAHVVRCFEDD 106
|
|
| GTP1 |
COG0012 |
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ... |
162-251 |
1.76e-20 |
|
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439783 [Multi-domain] Cd Length: 362 Bit Score: 91.24 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVV-----------DLSTSER-------FVlaDIPGLIEGASE 223
Cdd:COG0012 3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVpvpderldklaEIVKPKKivpatieFV--DIAGLVKGASK 80
|
90 100
....*....|....*....|....*...
gi 261266718 224 GAGLGTRFLGHVERSAVLIHLVDATQDD 251
Cdd:COG0012 81 GEGLGNQFLANIREVDAIVHVVRCFEDD 108
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
162-312 |
8.19e-20 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 89.62 E-value: 8.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERF-----------------VLADIPGLIEGASEG 224
Cdd:PTZ00258 24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVP-DERFdwlckhfkpksivpaqlDITDIAGLVKGASEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 225 AGLGTRFLGHVERSAVLIHLVDATQD-DIA---GAWTTIRgELEAYGDEL--AD----KSEILALNKVDALDPeTRKAKA 294
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVRAFEDeDIThveGEIDPVR-DLEIISSELilKDlefvEKRLDELTKKRKKKK-KKKEEK 180
|
170
....*....|....*...
gi 261266718 295 AELQAVSGIKPMLVSGVS 312
Cdd:PTZ00258 181 VELDVLKKVLEWLEEGKP 198
|
|
| Nog1 |
COG1084 |
GTP-binding protein, GTP1/Obg family [General function prediction only]; |
166-324 |
3.01e-18 |
|
GTP-binding protein, GTP1/Obg family [General function prediction only];
Pssm-ID: 440701 [Multi-domain] Cd Length: 330 Bit Score: 84.11 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 166 GLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERFVLADIPGLIE-GASEgaglgtrfLGHVERSAV--LI 242
Cdd:COG1084 167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERG-HGRYQVIDTPGLLDrPLSE--------RNEIERQAIlaLK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 243 HL-------VDATQDdiagAWTTIRGELEAYGD--ELADKSEILALNKVDALDPEtrkakaaELQAVSGIKPMLVSGVSG 313
Cdd:COG1084 238 HLadvilflFDPSET----CGYSLEEQLNLLEEirSLFDVPVIVVINKIDLSDEE-------ELKEAEEEADIKISALTG 306
|
170
....*....|.
gi 261266718 314 EGVTELLRAAF 324
Cdd:COG1084 307 EGVDELLDELI 317
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
163-327 |
5.97e-18 |
|
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: 79.98 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 163 GLVGLPNAGKSTFLAAAT-AARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIEGASEGAGLGTRFLGHVERSAVL 241
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLgQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 242 IHLVDATQDdiagawttiRGELEAYGDEL--ADKSEILALNKVDALDPETRKAKAAE--LQAVSGIKPMLVSGVSGEGVT 317
Cdd:cd00880 81 LLVVDSDLT---------PVEEEAKLGLLreRGKPVLLVLNKIDLVPESEEEELLRErkLELLPDLPVIAVSALPGEGID 151
|
170
....*....|
gi 261266718 318 ELLRAAFTQV 327
Cdd:cd00880 152 ELRKKIAELL 161
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
164-324 |
7.94e-15 |
|
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: 71.44 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 164 LVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERFVLADIPGL----------IEGASEGAglgtrfLG 233
Cdd:cd01897 5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYK-YLRWQVIDTPGIldrpleerntIEMQAITA------LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 234 HVeRSAVLiHLVDATQDdiAGawTTIRGELEAYGD--ELADKSEILALNKVDALDPETRKAKAAELQAVsGIKPMLVSGV 311
Cdd:cd01897 78 HL-RAAVL-FFIDPSET--CG--YSIEEQLSLFKEikPLFNKPVIVVLNKIDLLTEEDLSEIEKELEKE-GEEVIKISTL 150
|
170
....*....|...
gi 261266718 312 SGEGVTELLRAAF 324
Cdd:cd01897 151 TEEGVDELKNKAC 163
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
163-322 |
9.11e-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: 70.95 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 163 GLVGLPNAGKSTFL-AAATAARPKIADYPFTTLTPNLGVVDLSTSER-FVLADIPGLIEGASEGAGLGTRFLghVERSAV 240
Cdd:cd00882 1 VVVGRGGVGKSSLLnALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVkLVLVDTPGLDEFGGLGREELARLL--LRGADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 241 LIHLVDATQDDIAGAWTTIRgeLEAYGDElaDKSEILALNKVDALDPETRKAKAAELQAV--SGIKPMLVSGVSGEGVTE 318
Cdd:cd00882 79 ILLVVDSTDRESEEDAKLLI--LRRLRKE--GIPIILVGNKIDLLEEREVEELLRLEELAkiLGVPVFEVSAKTGEGVDE 154
|
....
gi 261266718 319 LLRA 322
Cdd:cd00882 155 LFEK 158
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
162-327 |
1.87e-13 |
|
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: 68.25 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLAD----I----PGLIEGasegaglgtrF-- 231
Cdd:cd01878 44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDtvgfIrdlpHQLVEA----------Frs 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 232 -LGHVERSAVLIHLVDATQDDIAGAWTTIR---GELEAygdelADKSEILALNKVDALDPETRKAKAAELQavsgIKPML 307
Cdd:cd01878 114 tLEEVAEADLLLHVVDASDPDREEQIETVEevlKELGA-----DDIPIILVLNKIDLLDDEELEERLRAGR----PDAVF 184
|
170 180
....*....|....*....|
gi 261266718 308 VSGVSGEGVTELLRAAFTQV 327
Cdd:cd01878 185 ISAKTGEGLDLLKEAIEELL 204
|
|
| GTP_HflX |
TIGR03156 |
GTP-binding protein HflX; This protein family is one of a number of homologous small, ... |
162-327 |
1.53e-12 |
|
GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General]
Pssm-ID: 274455 [Multi-domain] Cd Length: 351 Bit Score: 67.88 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIegasegaglgtRFLGH------- 234
Cdd:TIGR03156 192 VALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVLLTDTVGFI-----------RDLPHelvaafr 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 235 -----VERSAVLIHLVDATQDDIAGAWTTIRGELEAYGdeLADKSEILALNKVDALDPETRKAKAAEL-QAVsgikpmLV 308
Cdd:TIGR03156 261 atleeVREADLLLHVVDASDPDREEQIEAVEKVLEELG--AEDIPQLLVYNKIDLLDEPRIERLEEGYpEAV------FV 332
|
170
....*....|....*....
gi 261266718 309 SGVSGEGVtELLRAAFTQV 327
Cdd:TIGR03156 333 SAKTGEGL-DLLLEAIAER 350
|
|
| HflX |
COG2262 |
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ... |
162-322 |
2.00e-12 |
|
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441863 [Multi-domain] Cd Length: 419 Bit Score: 67.80 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIegasegaglgtRFLGH--VE--R 237
Cdd:COG2262 202 VALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDTVGFI-----------RKLPHqlVEafR 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 238 S-------A-VLIHLVDATQDDIAGAWTTIR---GELEAygdelADKSEILALNKVDALDPETRKAKAAELQavsgiKPM 306
Cdd:COG2262 271 StleevreAdLLLHVVDASDPDFEEQIETVNevlEELGA-----DDKPIILVFNKIDLLDDEELERLRAGYP-----DAV 340
|
170
....*....|....*.
gi 261266718 307 LVSGVSGEGVTELLRA 322
Cdd:COG2262 341 FISAKTGEGIDELLEA 356
|
|
| TIGR00092 |
TIGR00092 |
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in ... |
163-252 |
4.77e-11 |
|
GTP-binding protein YchF; This predicted GTP-binding protein is found in a single copy in every complete bacterial genome, and is found in Eukaryotes. A more distantly related protein, separated from this model, is found in the archaea. It is known to bind GTP and double-stranded nucleic acid. It is suggested to belong to a nucleoprotein complex and act as a translation factor. [Unknown function, General]
Pssm-ID: 129200 [Multi-domain] Cd Length: 368 Bit Score: 63.26 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 163 GLVGLPNAGKSTFLAAATAAR-PKIADYPFTTLTPNLGVVDLS----------------TSERFVLADIPGLIEGASEGA 225
Cdd:TIGR00092 6 GIVGLPNVGKSTLFAATTNLLgNEAANPPFTTIEPNAGVVNPSdprldllaiyikpekvPPTTTEFVDIAGLVGGASKGE 85
|
90 100
....*....|....*....|....*..
gi 261266718 226 GLGTRFLGHVERSAVLIHLVDATQDDI 252
Cdd:TIGR00092 86 GLGNQFLANIREVDIIQHVVRCFEDDI 112
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
162-322 |
6.55e-10 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 59.23 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAArpKIA---DYPFTTLTPNLGVVdlsTSER--FVLADIPGLIEGASEgagLGtRFLGHVE 236
Cdd:COG1159 6 VAIVGRPNVGKSTLLNALVGQ--KVSivsPKPQTTRHRIRGIV---TREDaqIVFVDTPGIHKPKRK---LG-RRMNKAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 237 RSA-----VLIHLVDATQddiagawtTIRGELEAYGDELADKSE--ILALNKVDALDPETRKAKAAELQAVSGIKPML-V 308
Cdd:COG1159 77 WSAledvdVILFVVDATE--------KIGEGDEFILELLKKLKTpvILVINKIDLVKKEELLPLLAEYSELLDFAEIVpI 148
|
170
....*....|....
gi 261266718 309 SGVSGEGVTELLRA 322
Cdd:COG1159 149 SALKGDNVDELLDE 162
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
162-323 |
9.17e-09 |
|
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: 53.99 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERFVLADIPGL--IEGASEGAGLGTRFLGHvERSA 239
Cdd:pfam02421 3 IALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYK-GYEIEIVDLPGIysLSPYSEEERVARDYLLN-EKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 240 VLIHLVDATQDDiagawttiRG--------ELEaygdeladKSEILALNKVDALDPETRKAKAAELQAVSGIKPMLVSGV 311
Cdd:pfam02421 81 VIVNVVDATNLE--------RNlyltlqllELG--------LPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSAR 144
|
170
....*....|..
gi 261266718 312 SGEGVTELLRAA 323
Cdd:pfam02421 145 KGEGIDELLDAI 156
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
162-320 |
1.32e-08 |
|
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: 53.62 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAArpKIA---DYPFTTLTPNLGVVdlsTSER--FVLADIPGLIEGASegaGLGTRFLGHVE 236
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGQ--KISivsPKPQTTRNRIRGIY---TDDDaqIIFVDTPGIHKPKK---KLGERMVKAAW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 237 RSA----VLIHLVDATQDdiagawttiRGELEAY-GDELADKSE--ILALNKVDAL-DPETRKAKAAELQAVSGIKPML- 307
Cdd:cd04163 78 SALkdvdLVLFVVDASEW---------IGEGDEFiLELLKKSKTpvILVLNKIDLVkDKEDLLPLLEKLKELHPFAEIFp 148
|
170
....*....|...
gi 261266718 308 VSGVSGEGVTELL 320
Cdd:cd04163 149 ISALKGENVDELL 161
|
|
| PRK11058 |
PRK11058 |
GTPase HflX; Provisional |
159-326 |
6.51e-08 |
|
GTPase HflX; Provisional
Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 53.95 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 159 IADVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLSTSERFVLADIPGLIegasegaglgtRFLGH---- 234
Cdd:PRK11058 197 VPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFI-----------RHLPHdlva 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 235 --------VERSAVLIHLVDATQDDIA---GAWTTIRGELEAygDELadkSEILALNKVDALDPETRKAKAAELQavsgi 303
Cdd:PRK11058 266 afkatlqeTRQATLLLHVVDAADVRVQeniEAVNTVLEEIDA--HEI---PTLLVMNKIDMLDDFEPRIDRDEEN----- 335
|
170 180
....*....|....*....|....*
gi 261266718 304 KPMLV--SGVSGEGVtELLRAAFTQ 326
Cdd:PRK11058 336 KPIRVwlSAQTGAGI-PLLFQALTE 359
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
162-349 |
1.59e-07 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 52.74 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTF---LaaataARPKIA---DYPFTTLTPNLGVVDLSTSErFVLADIPGlIEGASEGaglgtrFLGHV 235
Cdd:PRK00093 4 VAIVGRPNVGKSTLfnrL-----TGKRDAivaDTPGVTRDRIYGEAEWLGRE-FILIDTGG-IEPDDDG------FEKQI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 236 ERSA--------VLIHLVDA----TQDDiagawttirgelEAYGDEL--ADKSEILALNKVDALDPETRKAKAAELqavs 301
Cdd:PRK00093 71 REQAelaieeadVILFVVDGraglTPAD------------EEIAKILrkSNKPVILVVNKVDGPDEEADAYEFYSL---- 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 261266718 302 GI-KPMLVSGVSGEGVTELLraaftqvrirrgetpaEAAIDEAPEEETP 349
Cdd:PRK00093 135 GLgEPYPISAEHGRGIGDLL----------------DAILEELPEEEEE 167
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
162-322 |
4.89e-07 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 50.43 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAArpKIA---DYPFTTLTPNLGVVdlsTSER--FVLADIPGLIEgaSEGAgLGtRFLGHVE 236
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGQ--KISivsPKPQTTRHRIRGIV---TEDDaqIIFVDTPGIHK--PKRA-LN-RAMNKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 237 RSA-----VLIHLVDATQDdiagawttIRGELEAYGDELADKSE--ILALNKVDAL-DPETRKAKAAELQAVSGIKPML- 307
Cdd:PRK00089 79 WSSlkdvdLVLFVVDADEK--------IGPGDEFILEKLKKVKTpvILVLNKIDLVkDKEELLPLLEELSELMDFAEIVp 150
|
170
....*....|....*
gi 261266718 308 VSGVSGEGVTELLRA 322
Cdd:PRK00089 151 ISALKGDNVDELLDV 165
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
164-323 |
5.55e-07 |
|
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: 48.61 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 164 LVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERFVLADIPGL--IEGASEGAGLGTRFLGHvERSAVL 241
Cdd:cd01879 2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLG-GKEIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 242 IHLVDATQDDIAGAWTTirgeleaygdELAD--KSEILALNKVDaldpETRKAK----AAELQAVSGIKPMLVSGVSGEG 315
Cdd:cd01879 80 VNVVDATNLERNLYLTL----------QLLElgLPVVVALNMID----EAEKRGikidLDKLSELLGVPVVPTSARKGEG 145
|
....*...
gi 261266718 316 VTELLRAA 323
Cdd:cd01879 146 IDELLDAI 153
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
162-351 |
3.16e-06 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 48.48 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTF---LaaataARPKIA---DYPFTTLTPNLGVVDLSTSErFVLADIPGLIEGASEGaglgtrFLGHV 235
Cdd:COG1160 5 VAIVGRPNVGKSTLfnrL-----TGRRDAivdDTPGVTRDRIYGEAEWGGRE-FTLIDTGGIEPDDDDG------LEAEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 236 ERSA--------VLIHLVDA----TQDDiagawttirgelEAYGDEL--ADKSEILALNKVDALDPETRKAKAAELqavs 301
Cdd:COG1160 73 REQAelaieeadVILFVVDGraglTPLD------------EEIAKLLrrSGKPVILVVNKVDGPKREADAAEFYSL---- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 261266718 302 GI-KPMLVSGVSGEGVTELLRAAFtqvrirrgetpaeAAIDEAPEEETPGG 351
Cdd:COG1160 137 GLgEPIPISAEHGRGVGDLLDAVL-------------ELLPEEEEEEEEDD 174
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
162-325 |
2.00e-05 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 44.35 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAA-RPKIADYPFTTLTPnlgvVDLSTS---ERFVLADIPGLIEGASEGAGL----GTRFLG 233
Cdd:cd01895 5 IAIIGRPNVGKSSLLNALLGEeRVIVSDIAGTTRDS----IDVPFEydgQKYTLIDTAGIRKKGKVTEGIekysVLRTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 234 HVERSAVLIHLVDAT-----QDdiagawTTIRGELEAYGdeladKSEILALNKVDAL--DPETRKAKAAELQA----VSG 302
Cdd:cd01895 81 AIERADVVLLVLDASegiteQD------LRIAGLILEEG-----KALIIVVNKWDLVekDEKTMKEFEKELRRklpfLDY 149
|
170 180
....*....|....*....|...
gi 261266718 303 IKPMLVSGVSGEGVTELLRAAFT 325
Cdd:cd01895 150 APIVFISALTGQGVDKLFDAIKE 172
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
164-323 |
2.09e-05 |
|
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: 43.96 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 164 LVGLPNAGKST-F--LaaataARPKIA---DYPFTTLTPNLGVVDLSTSErFVLADIPGlIEGASEGaglgtrFLGHVER 237
Cdd:cd01894 2 IVGRPNVGKSTlFnrL-----TGRRDAivsDTPGVTRDRKYGEAEWGGRE-FILIDTGG-IEPDDEG------ISKEIRE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 238 SA--------VLIHLVDA----TQDDIagawttirgeleaygdELAD---KSE---ILALNKVDALDPETRKAKAAELqa 299
Cdd:cd01894 69 QAeiaieeadVILFVVDGreglTPADE----------------EIAKylrKSKkpvILVVNKIDNIKEEEEAAEFYSL-- 130
|
170 180
....*....|....*....|....*
gi 261266718 300 vsGI-KPMLVSGVSGEGVTELLRAA 323
Cdd:cd01894 131 --GFgEPIPISAEHGRGIGDLLDAI 153
|
|
| FeoB |
COG0370 |
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
162-347 |
2.59e-05 |
|
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 45.88 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNLGVVDLStSERFVLADIPGL--IEGASEGAGLGTRFLgHVERSA 239
Cdd:COG0370 6 IALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLK-GKEIELVDLPGTysLSAYSPDEKVARDFL-LEEKPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 240 VLIHLVDATQddiagawttirgeLE----------AYGDELadkseILALNKVDaldpETRKAK----AAELQAVSGIKP 305
Cdd:COG0370 84 VVVNVVDATN-------------LErnlyltlqllELGIPV-----VLALNMMD----EAEKKGikidVEKLSKLLGVPV 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 261266718 306 MLVSGVSGEGVTELLRAAftqVRIRRGETPAEAAIDEAPEEE 347
Cdd:COG0370 142 VPTSARKGKGIDELKEAI---IEAAEGKKPRPLRIDYPEEIE 180
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
162-323 |
1.83e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 43.11 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLaaataarpkiadypfttltpN--LGvvdlstSERFVLADIPG--------LIEgaSEG------- 224
Cdd:PRK00093 176 IAIIGRPNVGKSSLI--------------------NalLG------EERVIVSDIAGttrdsidtPFE--RDGqkytlid 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 225 -AGL--------GT------RFLGHVERSAVLIHLVDAT-----QDdiagawTTIRGELEAYGdeladKSEILALNKVDA 284
Cdd:PRK00093 228 tAGIrrkgkvteGVekysviRTLKAIERADVVLLVIDATegiteQD------LRIAGLALEAG-----RALVIVVNKWDL 296
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 261266718 285 LDPETRKAKAAELQA----VSGIKPMLVSGVSGEGVTELLRAA 323
Cdd:PRK00093 297 VDEKTMEEFKKELRRrlpfLDYAPIVFISALTGQGVDKLLEAI 339
|
|
| era |
TIGR00436 |
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
162-333 |
2.49e-04 |
|
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]
Pssm-ID: 129528 [Multi-domain] Cd Length: 270 Bit Score: 42.38 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAAATAARPKI-ADYPFTTLTPNLGVVDLSTSErFVLADIPGLIEgasEGAGLGtRFLGHVERSA- 239
Cdd:TIGR00436 3 VAILGRPNVGKSTLLNQLHGQKISItSPKAQTTRNRISGIHTTGASQ-IIFIDTPGFHE---KKHSLN-RLMMKEARSAi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 240 ----VLIHLVDATQddiagaWTtirGELEAYGDEL--ADKSEILALNKVDALDPETRKAKAAELQAVSGIKPML-VSGVS 312
Cdd:TIGR00436 78 ggvdLILFVVDSDQ------WN---GDGEFVLTKLqnLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVpISALT 148
|
170 180
....*....|....*....|.
gi 261266718 313 GEGVTELlrAAFTQVRIRRGE 333
Cdd:TIGR00436 149 GDNTSFL--AAFIEVHLPEGP 167
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
162-319 |
3.33e-04 |
|
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: 40.82 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLAA-ATAARPKIADYPFTTLTPNLGVVDL-STSERFVLADIPGLIEGASEGAGLGTRFLGHVERSA 239
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSlLGNKGSITEYYPGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 240 VLIHLVDAtqDDIAGAWT-TIRGELEaygdelADKSEILALNKVD----ALDPETRKaKAAELQAVSGIKPmlvSGVSGE 314
Cdd:TIGR00231 84 IVILVLDV--EEILEKQTkEIIHHAD------SGVPIILVGNKIDlkdaDLKTHVAS-EFAKLNGEPIIPL---SAETGK 151
|
....*
gi 261266718 315 GVTEL 319
Cdd:TIGR00231 152 NIDSA 156
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
162-325 |
2.12e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 39.62 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 162 VGLVGLPNAGKSTFLaaataarpkiadypfttltpN--LGvvdlstSERFVLADIPG--------LIEgaSEG------- 224
Cdd:COG1160 178 IAIVGRPNVGKSSLI--------------------NalLG------EERVIVSDIAGttrdsidtPFE--RDGkkytlid 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 225 -AGL--------GT------RFLGHVERSAVLIHLVDAT-----QDdiagawTTIRGELEAYGdeladKSEILALNKVDA 284
Cdd:COG1160 230 tAGIrrkgkvdeGIekysvlRTLRAIERADVVLLVIDATegiteQD------LKIAGLALEAG-----KALVIVVNKWDL 298
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 261266718 285 LDPETRKAKA------AELQAVSGIKPMLVSGVSGEGVTELLRAAFT 325
Cdd:COG1160 299 VEKDRKTREElekeirRRLPFLDYAPIVFISALTGQGVDKLLEAVDE 345
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
160-288 |
5.24e-03 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 37.59 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261266718 160 ADVGLVGLPNAGKSTFLAAATAARPKIADYPFTTLTPNlgVVDLSTserFVLADIPGL--IEGASEGA-----GLGTRFL 232
Cdd:PRK04213 10 PEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPN--HYDWGD---FILTDLPGFgfMSGVPKEVqekikDEIVRYI 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261266718 233 -GHVERSAVLIHLVDATQ-DDIAGAWTTiRGE----LEAYG--DELaDKSEILALNKVDALDPE 288
Cdd:PRK04213 85 eDNADRILAAVLVVDGKSfIEIIERWEG-RGEipidVEMFDflREL-GIPPIVAVNKMDKIKNR 146
|
|
| |
