|
Name |
Accession |
Description |
Interval |
E-value |
| obgE |
PRK12297 |
GTPase CgtA; Reviewed |
3-437 |
0e+00 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237046 [Multi-domain] Cd Length: 424 Bit Score: 789.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 3 MFLDTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMHGR 82
Cdd:PRK12297 1 MFIDQAKIYVKAGDGGDGMVSFRREKYVPKGGPDGGDGGKGGSVIFVADEGLRTLLDFRYKRHFKAENGENGMGKNMHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 83 GAEDLIVRVPQGTTVRDADTGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKVLAD 162
Cdd:PRK12297 81 NGEDLIIKVPVGTVVKDAETGEVIADLVEPGQEVVVAKGGRGGRGNAHFATSTNQAPRIAENGEPGEERELRLELKLLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVI 242
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 243 LHVLDMSASEGRDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEAAENLEEFKKKLAanydefdelPQIFPISGIA 322
Cdd:PRK12297 241 VHVIDMSGSEGRDPIEDYEKINKELKLYNPRLLERPQIVVANKMDLPEAEENLEEFKEKLG---------PKVFPISALT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 323 HQGLENLLEATAELLEKTPEFLLYEEsdFQEEEAYYGFNPDEPEFDISRADDASWVLSGDKLEKLFIMTNFDRDESVMKF 402
Cdd:PRK12297 312 GQGLDELLYAVAELLEETPEFPLEEE--EVEEEVYYKFEEEEKDFTITRDEDGVFVVSGEKIERLFKMTNFNRDESLRRF 389
|
410 420 430
....*....|....*....|....*....|....*
gi 1929598373 403 ARQLRGMGVDEALRARGAKDGDTVRIGKFEFEFVD 437
Cdd:PRK12297 390 ARQLRKMGVDDALREAGAKDGDTVRIGDFEFEFVD 424
|
|
| Obg |
COG0536 |
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ... |
4-353 |
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: 574.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 4 FLDTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMHGRG 83
Cdd:COG0536 1 FVDEAKIYVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKRHFKAENGENGMGKNRTGKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 84 AEDLIVRVPQGTTVRDADTGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKVLADV 163
Cdd:COG0536 81 GEDLVIKVPVGTVVKDAETGEVLADLTEDGQRVVVAKGGRGGLGNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 164 GLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVIL 243
Cdd:COG0536 161 GLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 244 HVLDMSASEGRDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEaAENLEEFKKKLAANYDEfdelpqIFPISGIAH 323
Cdd:COG0536 241 HVVDAAPLDGRDPVEDYEIIRNELEAYSPELAEKPRIVVLNKIDLLD-AEELEELKAELEKLGGP------VFPISAVTG 313
|
330 340 350
....*....|....*....|....*....|
gi 1929598373 324 QGLENLLEATAELLEKTPEFLLYEESDFQE 353
Cdd:COG0536 314 EGLDELLYALAELLEELRAEEAEEEEEVEE 343
|
|
| Obg_CgtA |
TIGR02729 |
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ... |
4-337 |
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: 546.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 4 FLDTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMHGRG 83
Cdd:TIGR02729 1 FVDEAKIFVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGSVILEADENLNTLLDFRYQRHFKAENGENGMGKNRTGKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 84 AEDLIVRVPQGTTVRDADTGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKVLADV 163
Cdd:TIGR02729 81 GEDLVIKVPVGTVVYDADTGELLADLTEPGQRFLVAKGGRGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 164 GLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVIL 243
Cdd:TIGR02729 161 GLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 244 HVLDMSASEGRDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEaAENLEEFKKKLAANYDEfdelpQIFPISGIAH 323
Cdd:TIGR02729 241 HLIDISPEDGSDPVEDYEIIRNELKKYSPELAEKPRIVVLNKIDLLD-EEELEELLKELKKELGK-----PVFPISALTG 314
|
330
....*....|....
gi 1929598373 324 QGLENLLEATAELL 337
Cdd:TIGR02729 315 EGLDELLDALAELL 328
|
|
| obgE |
PRK12299 |
GTPase CgtA; Reviewed |
3-342 |
2.06e-177 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237048 [Multi-domain] Cd Length: 335 Bit Score: 498.83 E-value: 2.06e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 3 MFLDTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMHGR 82
Cdd:PRK12299 1 KFIDEAKIYVKAGDGGNGCVSFRREKFIPFGGPDGGDGGRGGSVILEADENLNTLIDFRYKRHFKAENGENGMGRNRTGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 83 GAEDLIVRVPQGTTVRDADTGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKVLAD 162
Cdd:PRK12299 81 SGKDLVLKVPVGTQIYDADTGELIADLTEHGQRFLVAKGGKGGLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVI 242
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 243 LHVLDMSaseGRDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEAAENLEEFKKKLAANYDEFdelpqIFPISGIA 322
Cdd:PRK12299 241 LHLVDIE---AVDPVEDYKTIRNELEKYSPELADKPRILVLNKIDLLDEEEEREKRAALELAALGGP-----VFLISAVT 312
|
330 340
....*....|....*....|
gi 1929598373 323 HQGLENLLEATAELLEKTPE 342
Cdd:PRK12299 313 GEGLDELLRALWELLEEARR 332
|
|
| obgE |
PRK12298 |
GTPase CgtA; Reviewed |
2-364 |
6.01e-149 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237047 [Multi-domain] Cd Length: 390 Bit Score: 428.52 E-value: 6.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 2 SMFLDTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMHG 81
Cdd:PRK12298 1 MKFVDEAKIRVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVYLEADENLNTLIDYRFERHFRAERGQNGQGRDCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 82 RGAEDLIVRVPQGTTVRDADTGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKVLA 161
Cdd:PRK12298 81 KRGKDITIKVPVGTRVIDADTGEVIGDLTEHGQRLLVAKGGWHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 162 DVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRV 241
Cdd:PRK12298 161 DVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 242 ILHVLDMSASEGRDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEAaenlEEFKKKLAANYDEFDELPQIFPISGI 321
Cdd:PRK12298 241 LLHLIDIAPIDGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDLLDE----EEAEERAKAIVEALGWEGPVYLISAA 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1929598373 322 AHQGLENLLEATAELLEKTPEfllyEESDFQEEEAYYGFNPDE 364
Cdd:PRK12298 317 SGLGVKELCWDLMTFIEENPR----EEAEEAEAPEKVEFMWDD 355
|
|
| obgE |
PRK12296 |
GTPase CgtA; Reviewed |
1-434 |
8.78e-145 |
|
GTPase CgtA; Reviewed
Pssm-ID: 237045 [Multi-domain] Cd Length: 500 Bit Score: 421.97 E-value: 8.78e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 1 MSMFLDTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMH 80
Cdd:PRK12296 1 MPRFVDRVVLHVKAGDGGNGCASVHREKFKPLGGPDGGNGGRGGSVVLVVDPQVTTLLDFHFRPHRKATNGKPGMGDNRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 81 GRGAEDLIVRVPQGTTVRDADtGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKVL 160
Cdd:PRK12296 81 GAAGEDLVLPVPDGTVVLDED-GEVLADLVGAGTRFVAAAGGRGGLGNAALASKARKAPGFALLGEPGEERDLVLELKSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 161 ADVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGeSFAVADLPGLIEGASQGVGLGTQFLRHIERTR 240
Cdd:PRK12296 160 ADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDT-RFTVADVPGLIPGASEGKGLGLDFLRHIERCA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 241 VILHVLDMSASE-GRDPYEDYVAINNELETY---------NLRLMERPQIIVANKMDMPEAAEnLEEFKKklaanyDEFD 310
Cdd:PRK12296 239 VLVHVVDCATLEpGRDPLSDIDALEAELAAYapaldgdlgLGDLAERPRLVVLNKIDVPDARE-LAEFVR------PELE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 311 EL-PQIFPISGIAHQGLENLLEATAELLEKtpefllYEESDFQEEEAYYGFNP---DEPEFDISRADDA--SWVLSGDKL 384
Cdd:PRK12296 312 ARgWPVFEVSAASREGLRELSFALAELVEE------ARAAEPEAEPTRIVIRPkavDDAGFTVERDGDGegGFRVRGEKP 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1929598373 385 EKLFIMTNFDRDESVMKFARQLRGMGVDEALRARGAKDGDTVRIGK-----FEFE 434
Cdd:PRK12296 386 ERWVRQTDFDNDEAVGYLADRLARLGVEDELLKAGARPGDAVTIGTgngvvFDWE 440
|
|
| Obg |
cd01898 |
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ... |
161-337 |
8.36e-92 |
|
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: 274.69 E-value: 8.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 161 ADVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTR 240
Cdd:cd01898 1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 241 VILHVLDMSASEgrDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEAAENLEEFKKKLAANYDEfdelpQIFPISG 320
Cdd:cd01898 81 VLLHVIDLSGED--DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKELKGK-----KVFPISA 153
|
170
....*....|....*..
gi 1929598373 321 IAHQGLENLLEATAELL 337
Cdd:cd01898 154 LTGEGLDELLKKLAKLL 170
|
|
| GTP1_OBG |
pfam01018 |
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ... |
6-159 |
4.87e-84 |
|
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: 254.19 E-value: 4.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 6 DTAKIKVKAGKGGDGMVAFRREKYVPNGGPWGGDGARGGDVVFVVDEGLRTLMDFRYNRRFKADDGEKGMTKGMHGRGAE 85
Cdd:pfam01018 2 DRAKIKVKAGDGGNGCVSFRREKYVPKGGPDGGDGGRGGDVILVADENLNTLLDFRYKRHFKAENGENGGGKNCHGKNGE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929598373 86 DLIVRVPQGTTVRDADTGKVITDLVENGQEFVIAHGGRGGRGNIRFATPKNPAPEISENGEPGEERNLELELKV 159
Cdd:pfam01018 82 DLIIKVPVGTVVKDAETGEVLADLTEPGQRVLVAKGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
|
|
| Obg_like |
cd01881 |
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ... |
164-337 |
1.48e-55 |
|
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: 181.44 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 164 GLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVIL 243
Cdd:cd01881 1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 244 HVLDMSASEGRDPYEDYVAINNELETYNLRLMERPQIIVANKMDMPEAAENLEEFKKKLAanydefDELPqIFPISGIAH 323
Cdd:cd01881 81 HVIDASEDCVGDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMASENNLKRLKLDKLK------RGIP-VVPTSALTR 153
|
170
....*....|....
gi 1929598373 324 QGLENLLEATAELL 337
Cdd:cd01881 154 LGLDRVIRTIRKLL 167
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
162-285 |
3.43e-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: 112.71 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 162 DVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGLIEGASQGVGLGTQFLRHIErTRV 241
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELK-GKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1929598373 242 ILHVLDMSasegrdpyEDYVAINNELETYnLRLMERPQIIVANK 285
Cdd:pfam01926 79 ILFVVDSE--------EGITPLDEELLEL-LRENKKPIILVLNK 113
|
|
| DUF1967 |
pfam09269 |
Domain of unknown function (DUF1967); Members of this family contain a four-stranded beta ... |
369-435 |
5.21e-27 |
|
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: 102.45 E-value: 5.21e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929598373 369 ISRADDASWVLSGDKLEKLFIMTNFDRDESVMKFARQLRGMGVDEALRARGAKDGDTVRIGKFEFEF 435
Cdd:pfam09269 1 IEEDEEGVFVVEGPKIERLVRMTNFDNEESLRRFQRVLKKLGVEDALRKAGAKEGDTVRIGDFEFEY 67
|
|
| Obg_CgtA_exten |
TIGR03595 |
Obg family GTPase CgtA, C-terminal extension; CgtA (see model TIGR02729) is a broadly ... |
367-435 |
3.25e-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: 100.66 E-value: 3.25e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929598373 367 FDISRADDASWVLSGDKLEKLFIMTNFDRDESVMKFARQLRGMGVDEALRARGAKDGDTVRIGKFEFEF 435
Cdd:TIGR03595 1 FEIERDGDGVFVVSGKKIERWVAKTPFNNDEALRRFARKLKKLGVEDALRKAGAKAGDTVRIGDFEFEW 69
|
|
| DRG |
cd01896 |
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ... |
161-285 |
2.50e-25 |
|
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: 103.39 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 161 ADVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGLIEGASQGVGLGTQFLRHIERTR 240
Cdd:cd01896 1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYK-GAKIQLLDLPGIIEGASDGKGRGRQVIAVARTAD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1929598373 241 VILHVLDmsASEGRDPYEdyvAINNELETYNLRL-MERPQIIVANK 285
Cdd:cd01896 80 LILIVLD--ATKPEGQRE---ILERELEGVGIRLnKKPPNVTIKKK 120
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
164-337 |
3.61e-24 |
|
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: 98.09 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 164 GLVGFPSVGKSTLLSVITAAKPKI-GAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQGVGLGTQFLRHIERTRVI 242
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 243 LHVLDmsasEGRDPYEDYVAINneletyNLRLMERPQIIVANKMDMPEAAENLEEFKKKLAAnydEFDELPqIFPISGIA 322
Cdd:cd00880 81 LLVVD----SDLTPVEEEAKLG------LLRERGKPVLLVLNKIDLVPESEEEELLRERKLE---LLPDLP-VIAVSALP 146
|
170
....*....|....*
gi 1929598373 323 HQGLENLLEATAELL 337
Cdd:cd00880 147 GEGIDELRKKIAELL 161
|
|
| PRK09602 |
PRK09602 |
translation-associated GTPase; Reviewed |
163-300 |
7.87e-24 |
|
translation-associated GTPase; Reviewed
Pssm-ID: 236584 [Multi-domain] Cd Length: 396 Bit Score: 102.58 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGM--VRTK------------------SGESFA---VADLPGLI 219
Cdd:PRK09602 4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayVRVEcpckelgvkcnprngkciDGTRFIpveLIDVAGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 220 EGASQGVGLGTQFLRHIERTRVILHVLDMSAS---EGR-------DPYEDYVAINNELETY------------------- 270
Cdd:PRK09602 84 PGAHEGRGLGNQFLDDLRQADALIHVVDASGStdeEGNpvepgshDPVEDIKFLEEELDMWiygileknwekfsrkaqae 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929598373 271 ------------------------------------------------NLRLMERPQIIVANKMDMPEAAENLEEFKK 300
Cdd:PRK09602 164 kfdieealaeqlsglgineehvkealrelglpedpskwtdedllelarELRKISKPMVIAANKADLPPAEENIERLKE 241
|
|
| Rbg1 |
COG1163 |
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis]; |
161-288 |
1.74e-22 |
|
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440777 [Multi-domain] Cd Length: 368 Bit Score: 98.33 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 161 ADVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGLIEGASQGVGLGTQFLRHIERTR 240
Cdd:COG1163 64 ATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYK-GAKIQILDVPGLIEGAASGKGRGKEVLSVVRNAD 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1929598373 241 VILHVLDmsASEGrdpyEDYVAINNELETYNLRLMERPQIIVANKMDM 288
Cdd:COG1163 143 LILIVLD--VFEL----EQYDVLKEELYDAGIRLNKPPPDVTIEKKGK 184
|
|
| Ygr210 |
cd01899 |
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ... |
163-353 |
3.72e-22 |
|
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: 96.53 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGM-------------VRTKSGESFAVA----------DLPGLI 219
Cdd:cd01899 1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrvecpckelgVSCNPRYGKCIDgkryvpveliDVAGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 220 EGASQGVGLGTQFLRHIERTRVILHVLDMSAS----------EGRDPYEDYVAINNELETY---NLR------------- 273
Cdd:cd01899 81 PGAHEGKGLGNQFLDDLRDADVLIHVVDASGGtdaegngvetGGYDPLEDIEFLENEIDMWiygILErnwekivrkakae 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 274 -------------------------------------------------LMER--PQIIVANKMDMPEAAENLEEFKKKl 302
Cdd:cd01899 161 ktdivealseqlsgfgvnedvviealeelelpadlskwddedllrlareLRKRrkPMVIAANKADIPDAEENISKLRLK- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1929598373 303 aanydefDELPQIFPISGIAHQGLENLleATAELLEKTPefllyEESDFQE 353
Cdd:cd01899 240 -------YPDEIVVPTSAEAELALRRA--AKQGLIKYVP-----GDSDFEI 276
|
|
| PTZ00258 |
PTZ00258 |
GTP-binding protein; Provisional |
163-300 |
4.51e-18 |
|
GTP-binding protein; Provisional
Pssm-ID: 240334 [Multi-domain] Cd Length: 390 Bit Score: 85.38 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMV--------------RTKS--GESFAVADLPGLIEGASQGV 226
Cdd:PTZ00258 24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVnvpderfdwlckhfKPKSivPAQLDITDIAGLVKGASEGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 227 GLGTQFLRHIERTRVILHVL------DMSASEGR-DPYEDYVAINNELETYNL----RLMERPQIIVANKMDMPEAAENL 295
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVrafedeDITHVEGEiDPVRDLEIISSELILKDLefveKRLDELTKKRKKKKKKKEEKVEL 183
|
....*
gi 1929598373 296 EEFKK 300
Cdd:PTZ00258 184 DVLKK 188
|
|
| YchF |
cd01900 |
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ... |
163-267 |
3.49e-16 |
|
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: 78.27 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMV-----R-------TKSGE----SFAVADLPGLIEGASQGV 226
Cdd:cd01900 1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVpvpdeRldklaeiVKPKKivpaTIEFVDIAGLVKGASKGE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1929598373 227 GLGTQFLRHIERTRVILHVL------DMSASEGR-DPYEDYVAINNEL 267
Cdd:cd01900 81 GLGNKFLSHIREVDAIAHVVrcfeddDITHVEGSvDPVRDIEIINTEL 128
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
164-335 |
5.89e-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: 72.10 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 164 GLVGFPSVGKSTLLSVITAAKPKI-GAYHFTTIVPNLGMVRT-KSGESFAVADLPGLIEGasQGVGLGTQFLRHIERTRV 241
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKELdKGKVKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 242 ILHVLDMSasegRDPYEDYVainNELETYNLRLMERPQIIVANKMDMPEAAENleefKKKLAANYDEFDELPQIFPISGI 321
Cdd:cd00882 79 ILLVVDST----DRESEEDA---KLLILRRLRKEGIPIILVGNKIDLLEEREV----EELLRLEELAKILGVPVFEVSAK 147
|
170
....*....|....
gi 1929598373 322 AHQGLENLLEATAE 335
Cdd:cd00882 148 TGEGVDELFEKLIE 161
|
|
| NOG |
cd01897 |
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
165-338 |
1.04e-13 |
|
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: 68.74 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 165 LVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGL----------IEgaSQGVGLgtqfLR 234
Cdd:cd01897 5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYK-YLRWQVIDTPGIldrpleerntIE--MQAITA----LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 235 HIerTRVILHVLDMSASEGRdPYEDYVAINNELETynlrLMERPQIIVANKMDMPEaaenLEEFKKKLAANYDEFDElpq 314
Cdd:cd01897 78 HL--RAAVLFFIDPSETCGY-SIEEQLSLFKEIKP----LFNKPVIVVLNKIDLLT----EEDLSEIEKELEKEGEE--- 143
|
170 180
....*....|....*....|....
gi 1929598373 315 IFPISGIAHQGLENLLEATAELLE 338
Cdd:cd01897 144 VIKISTLTEEGVDELKNKACELLL 167
|
|
| Nog1 |
COG1084 |
GTP-binding protein, GTP1/Obg family [General function prediction only]; |
167-342 |
1.46e-12 |
|
GTP-binding protein, GTP1/Obg family [General function prediction only];
Pssm-ID: 440701 [Multi-domain] Cd Length: 330 Bit Score: 68.32 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 167 GFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGEsFAVADLPGL----------IEgaSQGVGLgtqfLRHI 236
Cdd:COG1084 167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR-YQVIDTPGLldrplserneIE--RQAILA----LKHL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 237 erTRVILHVLDMSASEGRdPYEDYVAINNELETynlrLMERPQIIVANKMDMPEAaenlEEFKKKLAANYdefdelpqiF 316
Cdd:COG1084 240 --ADVILFLFDPSETCGY-SLEEQLNLLEEIRS----LFDVPVIVVINKIDLSDE----EELKEAEEEAD---------I 299
|
170 180
....*....|....*....|....*.
gi 1929598373 317 PISGIAHQGLENLLEATAELLEKTPE 342
Cdd:COG1084 300 KISALTGEGVDELLDELIEALEEEPE 325
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
163-337 |
8.93e-11 |
|
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: 60.17 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLL-------SVITAAKPKigayhfTTIVPNLGmVRTKSGESFAVADLPGLIEGASQgvgLGTQFLRH 235
Cdd:cd04163 6 VAIIGRPNVGKSTLLnalvgqkISIVSPKPQ------TTRNRIRG-IYTDDDAQIIFVDTPGIHKPKKK---LGERMVKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 IERT----RVILHVLDmsASEGRDPYEDYVAinNELETYNlrlmeRPQIIVANKMDMPEAAENLEEFKKKLAANYDeFDE 311
Cdd:cd04163 76 AWSAlkdvDLVLFVVD--ASEWIGEGDEFIL--ELLKKSK-----TPVILVLNKIDLVKDKEDLLPLLEKLKELHP-FAE 145
|
170 180
....*....|....*....|....*.
gi 1929598373 312 lpqIFPISGIAHQGLENLLEATAELL 337
Cdd:cd04163 146 ---IFPISALKGENVDELLEYIVEYL 168
|
|
| FeoB |
cd01879 |
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ... |
165-339 |
1.21e-10 |
|
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: 59.78 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 165 LVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGL--IEGASQGVGLGTQFLRHiERTRVI 242
Cdd:cd01879 2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLG-GKEIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 243 LHVLDMSAsegrdpyedyvainneLETyNLRL------MERPQIIVANKMDmpEAAenleefKKKLAANYDEFDEL---P 313
Cdd:cd01879 80 VNVVDATN----------------LER-NLYLtlqlleLGLPVVVALNMID--EAE------KRGIKIDLDKLSELlgvP 134
|
170 180
....*....|....*....|....*.
gi 1929598373 314 qIFPISGIAHQGLENLLEATAELLEK 339
Cdd:cd01879 135 -VVPTSARKGEGIDELLDAIAKLAES 159
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
163-332 |
8.78e-10 |
|
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 460552 [Multi-domain] Cd Length: 156 Bit Score: 57.07 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGL--IEGASQGVGLGTQFLRHiERTR 240
Cdd:pfam02421 3 IALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYK-GYEIEIVDLPGIysLSPYSEEERVARDYLLN-EKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 241 VILHVLDMSASEgRDPYedyvainneLeTYNLRLMERPQIIVANKMDMPEAAE---NLEEFKKKLAanydefdeLPqIFP 317
Cdd:pfam02421 81 VIVNVVDATNLE-RNLY---------L-TLQLLELGLPVVLALNMMDEAEKKGikiDIKKLSELLG--------VP-VVP 140
|
170
....*....|....*
gi 1929598373 318 ISGIAHQGLENLLEA 332
Cdd:pfam02421 141 TSARKGEGIDELLDA 155
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
163-348 |
1.13e-09 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 59.29 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSV-------ITAAKPKigayhfTTIVPNLGmVRTKSGESFAVADLPGLiegasqgvglgtqflrH 235
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNAlvgqkisIVSPKPQ------TTRHRIRG-IVTEDDAQIIFVDTPGI----------------H 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 IERTR-----------------VILHVLDmsASEGRDPYEDYVainneLEtyNLRLMERPQIIVANKMDMPEAAENLEEF 298
Cdd:PRK00089 65 KPKRAlnramnkaawsslkdvdLVLFVVD--ADEKIGPGDEFI-----LE--KLKKVKTPVILVLNKIDLVKDKEELLPL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1929598373 299 KKKLAANYDeFDElpqIFPISGIAHQGLENLLEATAELLEKTPefLLYEE 348
Cdd:PRK00089 136 LEELSELMD-FAE---IVPISALKGDNVDELLDVIAKYLPEGP--PYYPE 179
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
163-329 |
1.67e-09 |
|
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: 56.61 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTT---IVPNLGMVRTKSGEsFAVADLPGLIEGASQGVGLGTQFLRHIERT 239
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTtrnYVTTVIEEDGKTYK-FNLLDTAGQEDYDAIRRLYYPQVERSLRVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 240 RVILHVLDMsaSEGrdPYEDYVAINNELEtynlrlMERPQIIVANKMDMPEAAEnLEEFKKKLAANYDEfdelpQIFPIS 319
Cdd:TIGR00231 83 DIVILVLDV--EEI--LEKQTKEIIHHAD------SGVPIILVGNKIDLKDADL-KTHVASEFAKLNGE-----PIIPLS 146
|
170
....*....|
gi 1929598373 320 GIAHQGLENL 329
Cdd:TIGR00231 147 AETGKNIDSA 156
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
163-337 |
5.50e-08 |
|
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: 52.85 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAA----KPKIgayhFTTIVPNLGMVRTKSGESFAVADLpgliegasqgVGlgtqFLRHI-- 236
Cdd:cd01878 44 VALVGYTNAGKSTLFNALTGAdvlaEDQL----FATLDPTTRRIKLPGGREVLLTDT----------VG----FIRDLph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 237 ----------ERTR---VILHVLDMSasegrDP-YEDYVAINNELetynLRLM---ERPQIIVANKMDMPEAAENLEEFK 299
Cdd:cd01878 106 qlveafrstlEEVAeadLLLHVVDAS-----DPdREEQIETVEEV----LKELgadDIPIILVLNKIDLLDDEELEERLR 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1929598373 300 kklaanydefDELPQIFPISGIAHQGLENLLEATAELL 337
Cdd:cd01878 177 ----------AGRPDAVFISAKTGEGLDLLKEAIEELL 204
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
163-337 |
1.36e-07 |
|
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: 50.97 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAK--PKIGAYHFTTIVPNLGMVrtksGESFAVADLPG----------------LIEgasq 224
Cdd:cd01876 2 VAFAGRSNVGKSSLINALTNRKklARTSKTPGRTQLINFFNV----GDKFRLVDLPGygyakvskevrekwgkLIE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 225 gvglgtQFLRHIERTRVILHVLDMSasegRDPYEDYVAINNELETYNLrlmerPQIIVANKMDM---PEAAENLEEFKKK 301
Cdd:cd01876 74 ------EYLENRENLKGVVLLIDAR----HGPTPIDLEMLEFLEELGI-----PFLIVLTKADKlkkSELAKVLKKIKEE 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 1929598373 302 LaanyDEFDELPQIFPISGIAHQGLENLLEATAELL 337
Cdd:cd01876 139 L----NLFNILPPVILFSSKKGTGIDELRALIAEWL 170
|
|
| FeoB |
COG0370 |
Fe2+ transporter FeoB [Inorganic ion transport and metabolism]; |
163-428 |
8.14e-07 |
|
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
Pssm-ID: 440139 [Multi-domain] Cd Length: 662 Bit Score: 51.27 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKsGESFAVADLPGL--IEGASQGVGLGTQFLRHiERTR 240
Cdd:COG0370 6 IALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLK-GKEIELVDLPGTysLSAYSPDEKVARDFLLE-EKPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 241 VILHVLDMSAsegrdpyedyvainneLETyNLRL------MERPQIIVANKMDmpEAAE-----NLEEFKKKLaanydef 309
Cdd:COG0370 84 VVVNVVDATN----------------LER-NLYLtlqlleLGIPVVLALNMMD--EAEKkgikiDVEKLSKLL------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 310 dELPqIFPISGIAHQGLENLLEATAELLEKTPEFLLYEESDFQEEEAyygFNPDEPEFDISRADDASWVlsgdkLEKLfi 389
Cdd:COG0370 138 -GVP-VVPTSARKGKGIDELKEAIIEAAEGKKPRPLRIDYPEEIEEA---IEELEELLEEDGPYPSRWL-----AIKL-- 205
|
250 260 270
....*....|....*....|....*....|....*....
gi 1929598373 390 mtnFDRDESVMKFARQLRGMgVDEALRARGAKDGDTVRI 428
Cdd:COG0370 206 ---LEGDEEVLELLSELLEL-LEEIREELEEELGEDLES 240
|
|
| PRK11058 |
PRK11058 |
GTPase HflX; Provisional |
163-337 |
7.77e-06 |
|
GTPase HflX; Provisional
Pssm-ID: 182934 [Multi-domain] Cd Length: 426 Bit Score: 47.79 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRTKSGESFAVADLPGLIEGASQgvGLGTQFLRHIERTR-- 240
Cdd:PRK11058 200 VSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPH--DLVAAFKATLQETRqa 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 241 -VILHVLDMSASEGRdpyEDYVAINNELETYNLRlmERPQIIVANKMDMpeaaenLEEFKKKLaaNYDEfDELPQIFPIS 319
Cdd:PRK11058 278 tLLLHVVDAADVRVQ---ENIEAVNTVLEEIDAH--EIPTLLVMNKIDM------LDDFEPRI--DRDE-ENKPIRVWLS 343
|
170
....*....|....*...
gi 1929598373 320 GIAHQGLENLLEATAELL 337
Cdd:PRK11058 344 AQTGAGIPLLFQALTERL 361
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
163-342 |
1.25e-05 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 47.33 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITaakpkigayhfttivpnlgmvrtksGESFA-VADLPGL----IEGASQ------------G 225
Cdd:COG1160 5 VAIVGRPNVGKSTLFNRLT-------------------------GRRDAiVDDTPGVtrdrIYGEAEwggreftlidtgG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 226 VGLGT----------QFLRHIERTRVILHVLDmsASEGRDPYEDYVAinneletYNLRLMERPQIIVANKMDMPEAAENL 295
Cdd:COG1160 60 IEPDDddgleaeireQAELAIEEADVILFVVD--GRAGLTPLDEEIA-------KLLRRSGKPVILVVNKVDGPKREADA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1929598373 296 EEFKKkLAanydeFDElpqIFPISGIAHQGLENLLEATAELLEKTPE 342
Cdd:COG1160 131 AEFYS-LG-----LGE---PIPISAEHGRGVGDLLDAVLELLPEEEE 168
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
236-338 |
1.84e-05 |
|
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: 44.79 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 IERTR-------VILHVLDmsASEGRDPyEDYVAINneletynlRLMERPQIIVANKMDMPEAAENLEEFKKKlaanyde 308
Cdd:cd04164 73 IERAReaieeadLVLLVVD--ASEGLDE-EDLEILE--------LPAKKPVIVVLNKSDLLSDAEGISELNGK------- 134
|
90 100 110
....*....|....*....|....*....|
gi 1929598373 309 fdelpQIFPISGIAHQGLENLLEATAELLE 338
Cdd:cd04164 135 -----PIIAISAKTGEGIDELKEALLELAG 159
|
|
| EngA1 |
cd01894 |
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ... |
165-337 |
3.68e-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: 43.58 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 165 LVGFPSVGKSTLLSVITaaKPKIgayhftTIVPNL-GMVR-TKSGE------SFAVADLPGLIEGASqgvGLGT----QF 232
Cdd:cd01894 2 IVGRPNVGKSTLFNRLT--GRRD------AIVSDTpGVTRdRKYGEaewggrEFILIDTGGIEPDDE---GISKeireQA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 233 LRHIERTRVILHVLDmsASEGRDPYEDYVAinneletYNLRLMERPQIIVANKMDMPEAAENLEEFkkklaanYdEFDeL 312
Cdd:cd01894 71 EIAIEEADVILFVVD--GREGLTPADEEIA-------KYLRKSKKPVILVVNKIDNIKEEEEAAEF-------Y-SLG-F 132
|
170 180
....*....|....*....|....*
gi 1929598373 313 PQIFPISGIAHQGLENLLEATAELL 337
Cdd:cd01894 133 GEPIPISAEHGRGIGDLLDAILELL 157
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
163-342 |
5.95e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 45.04 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITaakpkigayhfttivpnlgmvrtksGESFA-VADLPGL----IEGASQ------------G 225
Cdd:PRK00093 4 VAIVGRPNVGKSTLFNRLT-------------------------GKRDAiVADTPGVtrdrIYGEAEwlgrefilidtgG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 226 VGLGT---------QFLRHIERTRVILHVLDmsASEGRDPYEDYVAinneletYNLRLMERPQIIVANKMDmpeaaenle 296
Cdd:PRK00093 59 IEPDDdgfekqireQAELAIEEADVILFVVD--GRAGLTPADEEIA-------KILRKSNKPVILVVNKVD--------- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1929598373 297 efKKKLAANYDEFDEL--PQIFPISGIAHQGLENLLEATAELLEKTPE 342
Cdd:PRK00093 121 --GPDEEADAYEFYSLglGEPYPISAEHGRGIGDLLDAILEELPEEEE 166
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
163-336 |
8.19e-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: 43.19 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLS-------VITAAKPkiGayhfTTIVPNLGMVrTKSGESFAVADLPGLIEGASqgVGLGTQF--- 232
Cdd:cd01895 5 IAIIGRPNVGKSSLLNallgeerVIVSDIA--G----TTRDSIDVPF-EYDGQKYTLIDTAGIRKKGK--VTEGIEKysv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 233 ---LRHIERTRVILHVLDmsASEGrdpyedyvainneLETYNLRLME------RPQIIVANKMD-MPEAAENLEEFKKKL 302
Cdd:cd01895 76 lrtLKAIERADVVLLVLD--ASEG-------------ITEQDLRIAGlileegKALIIVVNKWDlVEKDEKTMKEFEKEL 140
|
170 180 190
....*....|....*....|....*....|....
gi 1929598373 303 AANYDEFDELPQIFpISGIAHQGLENLLEATAEL 336
Cdd:cd01895 141 RRKLPFLDYAPIVF-ISALTGQGVDKLFDAIKEV 173
|
|
| ARLTS1 |
cd04156 |
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ... |
163-336 |
1.10e-04 |
|
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: 42.40 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVITAAKPkigayhFTTIvPNLG----MVRTKSGESFAVADLPGliegasQGvGLGTQFLRHIER 238
Cdd:cd04156 2 VLLLGLDSAGKSTLLYKLKHAEL------VTTI-PTVGfnveMLQLEKHLSLTVWDVGG------QE-KMRTVWKCYLEN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 239 TRVILHVLDMSASEGRDpyEDYVAINNELETYNLRlmERPQIIVANKMDMPEAAeNLEE----FK-KKLAANYDEFdelp 313
Cdd:cd04156 68 TDGLVYVVDSSDEARLD--ESQKELKHILKNEHIK--GVPVVLLANKQDLPGAL-TAEEitrrFKlKKYCSDRDWY---- 138
|
170 180
....*....|....*....|...
gi 1929598373 314 qIFPISGIAHQGLENLLEATAEL 336
Cdd:cd04156 139 -VQPCSAVTGEGLAEAFRKLASF 160
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
236-339 |
1.19e-04 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 44.33 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 IERTR-------VILHVLDMSASEGRDPYEDYVAINNEletynlrlmerPQIIVANKMDMPEAAENLEEfkkklaanyde 308
Cdd:PRK05291 285 IERSReaieeadLVLLVLDASEPLTEEDDEILEELKDK-----------PVIVVLNKADLTGEIDLEEE----------- 342
|
90 100 110
....*....|....*....|....*....|.
gi 1929598373 309 fdELPQIFPISGIAHQGLENLLEATAELLEK 339
Cdd:PRK05291 343 --NGKPVIRISAKTGEGIDELREAIKELAFG 371
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
271-339 |
1.33e-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: 42.51 E-value: 1.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929598373 271 NLRLMER---PQIIVANKMDMPEAA---ENLEEFKKKLAANYDEFDELPQIFPISGIAHQGLENLLEATAELLEK 339
Cdd:pfam00009 113 HLRLARQlgvPIIVFINKMDRVDGAeleEVVEEVSRELLEKYGEDGEFVPVVPGSALKGEGVQTLLDALDEYLPS 187
|
|
| era |
TIGR00436 |
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
163-351 |
1.86e-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: 43.15 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLL-------SVITAAKPKigayhfTTIVPNLGMVRTKSGESFAVaDLPGLIEGASQGVGLGTQFLRH 235
Cdd:TIGR00436 3 VAILGRPNVGKSTLLnqlhgqkISITSPKAQ------TTRNRISGIHTTGASQIIFI-DTPGFHEKKHSLNRLMMKEARS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 -IERTRVILHVLDMSASEGRDPYedyvaINNELETynlrlMERPQIIVANKMDMPEAAENLEEFKKklAANYDEFDElpq 314
Cdd:TIGR00436 76 aIGGVDLILFVVDSDQWNGDGEF-----VLTKLQN-----LKRPVVLTRNKLDNKFKDKLLPLIDK--YAILEDFKD--- 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 1929598373 315 IFPISgiAHQGlENLLEATAELLEKTPEFLLYEESDF 351
Cdd:TIGR00436 141 IVPIS--ALTG-DNTSFLAAFIEVHLPEGPFRYPEDY 174
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
163-345 |
2.10e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 41.89 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 163 VGLVGFPSVGKSTLLSVI---TAAKPKIGAYHFTTIVPNLgmVRTKSGE-SFAVADLPGLIEGASqgvgLGTQFLRHIER 238
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLvgdIFSLEKYLSTNGVTIDKKE--LKLDGLDvDLVIWDTPGQDEFRE----TRQFYARQLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 239 TRVILHVLDmsaseGRDPyEDYVAINNELETYNLRLMERPQIIVANKMDMPEAAE--NLEEFKKKLAAnydefDELPQIF 316
Cdd:COG1100 80 ASLYLFVVD-----GTRE-ETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEieDEERLKEALSE-----DNIVEVV 148
|
170 180
....*....|....*....|....*....
gi 1929598373 317 PISGIAHQGLENLLEATAELLEKTPEFLL 345
Cdd:COG1100 149 ATSAKTGEGVEELFAALAEILRGEGDSLD 177
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
233-336 |
3.49e-04 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 42.73 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 233 LRHIERTRVILHVLDmsASEGrdpyedyvainneLETYNLRLME------RPQIIVANKMDMPEAAEnLEEFKKKLAANY 306
Cdd:PRK00093 250 LKAIERADVVLLVID--ATEG-------------ITEQDLRIAGlaleagRALVIVVNKWDLVDEKT-MEEFKKELRRRL 313
|
90 100 110
....*....|....*....|....*....|
gi 1929598373 307 DEFDELPQIFpISGIAHQGLENLLEATAEL 336
Cdd:PRK00093 314 PFLDYAPIVF-ISALTGQGVDKLLEAIDEA 342
|
|
| PRK04213 |
PRK04213 |
GTP-binding protein EngB; |
158-287 |
4.14e-04 |
|
GTP-binding protein EngB;
Pssm-ID: 179790 [Multi-domain] Cd Length: 201 Bit Score: 41.44 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 158 KVLADVGLVGFPSVGKSTLLSVITAAKPKIGAYHFTTIVPNLGMVRtksgeSFAVADLPGLieGASQGVGLGTQ------ 231
Cdd:PRK04213 7 DRKPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPNHYDWG-----DFILTDLPGF--GFMSGVPKEVQekikde 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929598373 232 FLRHIE----RTRVILHVLD-MSASEGRDPYEDYVAINNELETYN-LRLMERPQIIVANKMD 287
Cdd:PRK04213 80 IVRYIEdnadRILAAVLVVDgKSFIEIIERWEGRGEIPIDVEMFDfLRELGIPPIVAVNKMD 141
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
280-338 |
6.76e-04 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 41.92 E-value: 6.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 280 IIVA-NKMDMPEAaeNLEEFKKKLAanydEFDELP-------QIFPISGIAHQGLENLLEA---TAELLE 338
Cdd:COG0532 106 IIVAiNKIDKPGA--NPDRVKQELA----EHGLVPeewggdtIFVPVSAKTGEGIDELLEMillQAEVLE 169
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
233-338 |
9.00e-04 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.55 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 233 LRHIERTRVILHVLDmsASEGrdpyedyvainneLETYNLRLME------RPQIIVANKMD-MPEAAENLEEFKKKLAAN 305
Cdd:COG1160 252 LRAIERADVVLLVID--ATEG-------------ITEQDLKIAGlaleagKALVIVVNKWDlVEKDRKTREELEKEIRRR 316
|
90 100 110
....*....|....*....|....*....|...
gi 1929598373 306 YDEFDELPQIFpISGIAHQGLENLLEATAELLE 338
Cdd:COG1160 317 LPFLDYAPIVF-ISALTGQGVDKLLEAVDEVYE 348
|
|
| Arf_Arl |
cd00878 |
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
165-331 |
1.21e-03 |
|
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: 39.48 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 165 LVGFPSVGKSTLLSvitaakpKIGAYHFTTIVPNLG----MVRTKsGESFAVADlpgliegasqgVGlGTQFLRHI---- 236
Cdd:cd00878 4 MLGLDGAGKTTILY-------KLKLGEVVTTIPTIGfnveTVEYK-NVKFTVWD-----------VG-GQDKIRPLwkhy 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 237 -ERTRVILHVLDMSASEgR--DPYEDYVAINNELETYNLrlmerPQIIVANKMDMPEAAeNLEEFKKKLAANyDEFDELP 313
Cdd:cd00878 64 yENTDGLIFVVDSSDRE-RieEAKNELHKLLNEEELKGA-----PLLILANKQDLPGAL-TESELIELLGLE-SIKGRRW 135
|
170
....*....|....*...
gi 1929598373 314 QIFPISGIAHQGLENLLE 331
Cdd:cd00878 136 HIQPCSAVTGDGLDEGLD 153
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
172-339 |
2.13e-03 |
|
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: 38.61 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 172 GKSTLLSVIT----AAKP------KIGAYHFTTIV--PNLGMVRTKSGESF--------AVADLpgliegasqgvglgtq 231
Cdd:cd01887 12 GKTTLLDKIRktnvAAGEaggitqHIGAYQVPIDVkiPGITFIDTPGHEAFtnmrargaSVTDI---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 232 flrhiertrVILHVldmSASEGRDP--YEdyvAINNeLETYNLrlmerPQIIVANKMD-MPEAAENLEEFKKKLAANY-- 306
Cdd:cd01887 76 ---------AILVV---AADDGVMPqtIE---AINH-AKAANV-----PIIVAINKIDkPYGTEADPERVKNELSELGlv 134
|
170 180 190
....*....|....*....|....*....|....
gi 1929598373 307 -DEFDELPQIFPISGIAHQGLENLLEATAELLEK 339
Cdd:cd01887 135 gEEWGGDVSIVPISAKTGEGIDDLLEAILLLAEV 168
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
236-339 |
2.40e-03 |
|
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: 40.04 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 IERTR-------VILHVLDmsASEGRDPyEDYVAINneletynlRLMERPQIIVANKMDMPEAAEnleefkkklaANYDE 308
Cdd:COG0486 283 IERAReaieeadLVLLLLD--ASEPLTE-EDEEILE--------KLKDKPVIVVLNKIDLPSEAD----------GELKS 341
|
90 100 110
....*....|....*....|....*....|.
gi 1929598373 309 FDELPQIFpISGIAHQGLENLLEATAELLEK 339
Cdd:COG0486 342 LPGEPVIA-ISAKTGEGIDELKEAILELVGE 371
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
236-344 |
3.36e-03 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 38.07 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929598373 236 IERTRVILHVLDmsaseGRDPYEDYvaiNNELETYNLRlMERPQIIVANKMDM-PEaaENLEEFKKKLaanydEFDELPQ 314
Cdd:cd01859 9 IKEADVVLEVVD-----ARDPELTR---SRKLERMALE-LGKKLIIVLNKADLvPR--EVLEKWKEVF-----ESEGLPV 72
|
90 100 110
....*....|....*....|....*....|
gi 1929598373 315 IFpISGIAHQGLENLLEATAELLEKTPEFL 344
Cdd:cd01859 73 VY-VSARERLGTRILRRTIKELAIDGKPVI 101
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
272-342 |
7.21e-03 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 37.20 E-value: 7.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929598373 272 LRLMERPQIIVA-NKMDMPEAAEnLEEFKKKLAANYDE-FDELPQIFPISGIAHQGLENLLEATAELLEKTPE 342
Cdd:cd04171 98 LELLGIKKGLVVlTKADLVDEDR-LELVEEEILELLAGtFLADAPIFPVSSVTGEGIEELKNYLDELAEPQSK 169
|
|
| MMR_HSR1_C |
pfam08438 |
GTPase of unknown function C-terminal; This domain is found at the C-terminus of pfam01926 in ... |
282-332 |
7.88e-03 |
|
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: 35.97 E-value: 7.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1929598373 282 VANKMDMPEAAENLEEFKKKlaanydefDELPQIFPISGIAHQGLENLLEA 332
Cdd:pfam08438 1 AANKADLPAADENIEKLKEK--------YPDHIVVPTSAEAELALRKAAKA 43
|
|
| |
