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Conserved domains on  [gi|488954368|ref|WP_002865443|]
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MULTISPECIES: ferrous iron transport protein B [Campylobacter]

Protein Classification

ferrous iron transporter B( domain architecture ID 11417566)

ferrous iron transporter B is part of an Fe(2+) uptake system that is probably driven by GTP hydrolysis

CATH:  1.10.287.1770
Gene Symbol:  feoB
Gene Ontology:  GO:0015093|GO:0005525|GO:0006826
PubMed:  12446835
SCOP:  4004042
TCDB:  9.A.8

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-612 0e+00

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


:

Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 785.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQN 80
Cdd:COG0370    1 MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDEKVARDFLLEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  81 DYDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKII 160
Cdd:COG0370   81 KPDVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAII 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 161 -ILFESKFIPRSQFYTP---------------------------LCEKSPEKEDLLY----------------------- 189
Cdd:COG0370  161 eAAEGKKPRPLRIDYPEeieeaieeleelleedgpypsrwlaikLLEGDEEVLELLSellelleeireeleeelgedles 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 190 --------FINELSKKIITHKKEER-NLTKKIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLGEFVK 260
Cdd:COG0370  241 iiadaryaFIERILKEVVTKPGEKKlTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGAPLMDLIDGGFGWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 261 NNISNTFIASALADGIIAGVGAVILFLPNIMILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLITGFGCSVPA 340
Cdd:COG0370  321 ALLPPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVPA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 341 FMATRTLKNKRDRLLTLFVINFMSCGARLPVYVLFIGAFFPsEKAGNYLFGIYILGAILGLCAAKFLRMTAFRGLDEPFV 420
Cdd:COG0370  401 IMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFP-DNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPFV 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 421 MEMPKYRMPNWHLVWFMVYNKAKMYLKKAGTFILLASLLIWFASNFPKSEENLNdfnaqeraIEQSYLGQFGKGIEPIFQ 500
Cdd:COG0370  480 MELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESED--------LENSYLGRIGKALEPVFA 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 501 PLELDWKLSVSLISGLAAKEVMISTMGVLYSLGkDVDETNNDLKGIIAKNIPIPSAVAFILFVMIYNPCFAATIVFSKES 580
Cdd:COG0370  552 PLGFDWQIGVALITGFAAKEVVVGTLGTLYGVG-EDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRET 630
                        650       660       670
                 ....*....|....*....|....*....|..
gi 488954368 581 GKLKYTLFLFLFTCTSAYIVAFIGLHIAKILL 612
Cdd:COG0370  631 GSWKWTLFAVGYMTVLAYLVAFLVYQIGRLLG 662
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-612 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 785.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQN 80
Cdd:COG0370    1 MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDEKVARDFLLEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  81 DYDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKII 160
Cdd:COG0370   81 KPDVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAII 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 161 -ILFESKFIPRSQFYTP---------------------------LCEKSPEKEDLLY----------------------- 189
Cdd:COG0370  161 eAAEGKKPRPLRIDYPEeieeaieeleelleedgpypsrwlaikLLEGDEEVLELLSellelleeireeleeelgedles 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 190 --------FINELSKKIITHKKEER-NLTKKIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLGEFVK 260
Cdd:COG0370  241 iiadaryaFIERILKEVVTKPGEKKlTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGAPLMDLIDGGFGWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 261 NNISNTFIASALADGIIAGVGAVILFLPNIMILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLITGFGCSVPA 340
Cdd:COG0370  321 ALLPPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVPA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 341 FMATRTLKNKRDRLLTLFVINFMSCGARLPVYVLFIGAFFPsEKAGNYLFGIYILGAILGLCAAKFLRMTAFRGLDEPFV 420
Cdd:COG0370  401 IMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFP-DNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPFV 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 421 MEMPKYRMPNWHLVWFMVYNKAKMYLKKAGTFILLASLLIWFASNFPKSEENLNdfnaqeraIEQSYLGQFGKGIEPIFQ 500
Cdd:COG0370  480 MELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESED--------LENSYLGRIGKALEPVFA 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 501 PLELDWKLSVSLISGLAAKEVMISTMGVLYSLGkDVDETNNDLKGIIAKNIPIPSAVAFILFVMIYNPCFAATIVFSKES 580
Cdd:COG0370  552 PLGFDWQIGVALITGFAAKEVVVGTLGTLYGVG-EDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRET 630
                        650       660       670
                 ....*....|....*....|....*....|..
gi 488954368 581 GKLKYTLFLFLFTCTSAYIVAFIGLHIAKILL 612
Cdd:COG0370  631 GSWKWTLFAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
10-579 0e+00

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


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 543.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   10 GQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQNDYDVIVNVL 89
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   90 DATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTK---ENLELLLQKIIILFES- 165
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGrgiERLKDAIRKAIGLKELk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  166 ----KFIPRSQFYTPLCEKSPE---------KEDLLYFINELSKKI---------ITHKKEERNLT-------------K 210
Cdd:TIGR00437 161 kraiEIVPEAYQVVEVVEGLIEiiysiskrgLEILLGLLEDLSLEIekiernlaeVVIKESPSNLSpteiadedrvlveK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  211 KIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLGEFVKNNISNTFIASALADGIIAGVGAVILFLPNI 290
Cdd:TIGR00437 241 SIGRKILDRFLGLPIFLFVMFILFLLTFLVGQPLVDLIETGFSFLSEAVKSFIGNYWLASLLGDGLIGGVGAVLSFVPLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  291 MILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLITGFGCSVPAFMATRTLKNKRDRLLTLFVINFMSCGARLP 370
Cdd:TIGR00437 321 AILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCSARLP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  371 VYVLFIGAFFPSEKAGNYLFGIYILGAILGLCAAKFLRMTAFRGLDEPFVMEMPKYRMPNWHLVWFMVYNKAKMYLKKAG 450
Cdd:TIGR00437 401 VIVLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFIKKAG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  451 TFILLASLLIWFASNFPKSEenlndfnaqeraIEQSYLGQFGKGIEPIFQPL--ELDWKLSVSLISGLAAKEVMISTMGV 528
Cdd:TIGR00437 481 TIIVIGSVLIWFLSSFPGGK------------ILESWLAAIGSIMAPLFVPLgkILDWFASVALIFGFVAKEVVVATLGV 548
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488954368  529 LYSLGkdvdetnNDLKGIIAKNIPIpSAVAFILFVMIYNPCFAATIVFSKE 579
Cdd:TIGR00437 549 LYGLG-------NILSSIGHAMVPV-EALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-601 1.14e-108

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 344.01  E-value: 1.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEE----EKITRHF 76
Cdd:PRK09554   1 MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQtsldEQIACHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  77 LNQNDYDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEI------------ 144
Cdd:PRK09554  81 ILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLvstrgrgiealk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 145 ----SAKTKENLEL------LLQKIIILFE--SKFIPRSQ-------------FYTPLCEKSPEKEDLL----------- 188
Cdd:PRK09554 161 laidRHQANENVELvhypqpLLNEADSLAKvmPSDIPLQQrrwlglqmlegdiYSRAYAGEASQHLDAAlarlrnemddp 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 189 --------Y-FINELSKKII-THKKEERNLTKKIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLgeF 258
Cdd:PRK09554 241 alhiadarYqCIAAICDAVSnTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVAI--F 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 259 VKNN--ISNTF-----IASALADGIIAGVGAVILFLPNIMILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLI 331
Cdd:PRK09554 319 IHGIqwLGYTLhfpdwLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLI 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 332 TGFGCSVPAFMATRTLKNKRDRLLTLFVINFMSCGARLPVYVLFIGAFFPSEKAGnYLFGIYILGAILGLCAAKFLRMTA 411
Cdd:PRK09554 399 VGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGAL-AVFSLYLLGIVMAILTGLMLKYTI 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 412 FRGLDEPFVMEMPKYRMPNWHLVWFMVYNKAKMYLKKAGTFILLASLLIWFASNFPKSEENLNDFNaqeraieQSYLGQF 491
Cdd:PRK09554 478 MRGEASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIVDNIN-------DSALASV 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 492 GKGIEPIFQPL---ELDWKLSVSLISGLAAKEVMISTMGVLYS-------------------LGKDVDETNNDLKGIIAK 549
Cdd:PRK09554 551 SRVITPVLKPIgvhEDNWQATVGLFTGAMAKEVVVGTLNTLYTaeniqdeefnpaefnlgdeLFGAVDETWQSLKDTFSL 630
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368 550 NI---PIP------------------------SAVAFILFVMIYNPCFAATIVFSKESGKlKYTLFLFLFTCTSAYIVA 601
Cdd:PRK09554 631 SVlanPIEaskgdgemgtgamgvmsqkfgsaaAAYSYLIFVLLYVPCISVMGAIARESSR-GWMGFSILWGLNIAYSLA 708
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
7-165 1.22e-78

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: 245.83  E-value: 1.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   7 ALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQNDYDVIV 86
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368  87 NVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKIIILFES 165
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIAKLAES 159
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
4-159 5.38e-74

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: 233.50  E-value: 5.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    4 IKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQNDYD 83
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488954368   84 VIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKI 159
Cdd:pfam02421  81 VIVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELLDAI 156
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-612 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 785.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQN 80
Cdd:COG0370    1 MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDEKVARDFLLEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  81 DYDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKII 160
Cdd:COG0370   81 KPDVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAII 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 161 -ILFESKFIPRSQFYTP---------------------------LCEKSPEKEDLLY----------------------- 189
Cdd:COG0370  161 eAAEGKKPRPLRIDYPEeieeaieeleelleedgpypsrwlaikLLEGDEEVLELLSellelleeireeleeelgedles 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 190 --------FINELSKKIITHKKEER-NLTKKIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLGEFVK 260
Cdd:COG0370  241 iiadaryaFIERILKEVVTKPGEKKlTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGAPLMDLIDGGFGWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 261 NNISNTFIASALADGIIAGVGAVILFLPNIMILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLITGFGCSVPA 340
Cdd:COG0370  321 ALLPPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVPA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 341 FMATRTLKNKRDRLLTLFVINFMSCGARLPVYVLFIGAFFPsEKAGNYLFGIYILGAILGLCAAKFLRMTAFRGLDEPFV 420
Cdd:COG0370  401 IMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFP-DNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPFV 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 421 MEMPKYRMPNWHLVWFMVYNKAKMYLKKAGTFILLASLLIWFASNFPKSEENLNdfnaqeraIEQSYLGQFGKGIEPIFQ 500
Cdd:COG0370  480 MELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESED--------LENSYLGRIGKALEPVFA 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 501 PLELDWKLSVSLISGLAAKEVMISTMGVLYSLGkDVDETNNDLKGIIAKNIPIPSAVAFILFVMIYNPCFAATIVFSKES 580
Cdd:COG0370  552 PLGFDWQIGVALITGFAAKEVVVGTLGTLYGVG-EDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRET 630
                        650       660       670
                 ....*....|....*....|....*....|..
gi 488954368 581 GKLKYTLFLFLFTCTSAYIVAFIGLHIAKILL 612
Cdd:COG0370  631 GSWKWTLFAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
10-579 0e+00

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


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 543.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   10 GQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQNDYDVIVNVL 89
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   90 DATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTK---ENLELLLQKIIILFES- 165
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGrgiERLKDAIRKAIGLKELk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  166 ----KFIPRSQFYTPLCEKSPE---------KEDLLYFINELSKKI---------ITHKKEERNLT-------------K 210
Cdd:TIGR00437 161 kraiEIVPEAYQVVEVVEGLIEiiysiskrgLEILLGLLEDLSLEIekiernlaeVVIKESPSNLSpteiadedrvlveK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  211 KIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLGEFVKNNISNTFIASALADGIIAGVGAVILFLPNI 290
Cdd:TIGR00437 241 SIGRKILDRFLGLPIFLFVMFILFLLTFLVGQPLVDLIETGFSFLSEAVKSFIGNYWLASLLGDGLIGGVGAVLSFVPLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  291 MILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLITGFGCSVPAFMATRTLKNKRDRLLTLFVINFMSCGARLP 370
Cdd:TIGR00437 321 AILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCSARLP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  371 VYVLFIGAFFPSEKAGNYLFGIYILGAILGLCAAKFLRMTAFRGLDEPFVMEMPKYRMPNWHLVWFMVYNKAKMYLKKAG 450
Cdd:TIGR00437 401 VIVLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFIKKAG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  451 TFILLASLLIWFASNFPKSEenlndfnaqeraIEQSYLGQFGKGIEPIFQPL--ELDWKLSVSLISGLAAKEVMISTMGV 528
Cdd:TIGR00437 481 TIIVIGSVLIWFLSSFPGGK------------ILESWLAAIGSIMAPLFVPLgkILDWFASVALIFGFVAKEVVVATLGV 548
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488954368  529 LYSLGkdvdetnNDLKGIIAKNIPIpSAVAFILFVMIYNPCFAATIVFSKE 579
Cdd:TIGR00437 549 LYGLG-------NILSSIGHAMVPV-EALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-601 1.14e-108

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 344.01  E-value: 1.14e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEE----EKITRHF 76
Cdd:PRK09554   1 MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQtsldEQIACHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  77 LNQNDYDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEI------------ 144
Cdd:PRK09554  81 ILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLvstrgrgiealk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 145 ----SAKTKENLEL------LLQKIIILFE--SKFIPRSQ-------------FYTPLCEKSPEKEDLL----------- 188
Cdd:PRK09554 161 laidRHQANENVELvhypqpLLNEADSLAKvmPSDIPLQQrrwlglqmlegdiYSRAYAGEASQHLDAAlarlrnemddp 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 189 --------Y-FINELSKKII-THKKEERNLTKKIDALLIHKFFGLPIFLFLMWLLFQLTFSLGQIPMDYIESGFNTLgeF 258
Cdd:PRK09554 241 alhiadarYqCIAAICDAVSnTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVAI--F 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 259 VKNN--ISNTF-----IASALADGIIAGVGAVILFLPNIMILFLGIALLETTGYMSRVAFLLDGILHKFGLHGKSFIPLI 331
Cdd:PRK09554 319 IHGIqwLGYTLhfpdwLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLI 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 332 TGFGCSVPAFMATRTLKNKRDRLLTLFVINFMSCGARLPVYVLFIGAFFPSEKAGnYLFGIYILGAILGLCAAKFLRMTA 411
Cdd:PRK09554 399 VGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGAL-AVFSLYLLGIVMAILTGLMLKYTI 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 412 FRGLDEPFVMEMPKYRMPNWHLVWFMVYNKAKMYLKKAGTFILLASLLIWFASNFPKSEENLNDFNaqeraieQSYLGQF 491
Cdd:PRK09554 478 MRGEASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIVDNIN-------DSALASV 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368 492 GKGIEPIFQPL---ELDWKLSVSLISGLAAKEVMISTMGVLYS-------------------LGKDVDETNNDLKGIIAK 549
Cdd:PRK09554 551 SRVITPVLKPIgvhEDNWQATVGLFTGAMAKEVVVGTLNTLYTaeniqdeefnpaefnlgdeLFGAVDETWQSLKDTFSL 630
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368 550 NI---PIP------------------------SAVAFILFVMIYNPCFAATIVFSKESGKlKYTLFLFLFTCTSAYIVA 601
Cdd:PRK09554 631 SVlanPIEaskgdgemgtgamgvmsqkfgsaaAAYSYLIFVLLYVPCISVMGAIARESSR-GWMGFSILWGLNIAYSLA 708
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
7-165 1.22e-78

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: 245.83  E-value: 1.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   7 ALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQNDYDVIV 86
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368  87 NVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKIIILFES 165
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIAKLAES 159
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
4-159 5.38e-74

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: 233.50  E-value: 5.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    4 IKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDGYSEEEKITRHFLNQNDYD 83
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488954368   84 VIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKI 159
Cdd:pfam02421  81 VIVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELLDAI 156
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
5-117 1.91e-24

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: 98.08  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    5 KIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYslDGYSEEEKITRHFLNQNDYDV 84
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLI--EGASEGEGLGRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488954368   85 IVNVLDATNLERNLILSAE--LLSLNKKMLLALNM 117
Cdd:pfam01926  79 ILFVVDSEEGITPLDEELLelLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
7-163 1.92e-23

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: 96.93  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   7 ALVGQPNVGKSLLINALCKANM-KVGNFSGVTIEKASAK-TFYKNYEFEVIDLPGTYSLDGYSEE--EKITRHFlnqNDY 82
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTRDPVRKEwELLPLGPVVLIDTPGLDEEGGLGRErvEEARQVA---DRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  83 DVIVNVLDATNLERNLILSAELLS-LNKKMLLALNMCD--EAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQKI 159
Cdd:cd00880   78 DLVLLVVDSDLTPVEEEAKLGLLReRGKPVLLVLNKIDlvPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKKI 157

                 ....
gi 488954368 160 IILF 163
Cdd:cd00880  158 AELL 161
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
7-160 3.86e-20

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: 87.51  E-value: 3.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   7 ALVGQPNVGKSLLINALCKAN-MKVGNFSGVT--IEKASAKTFYKNYEFEVIDLPGTYSLdGYSEEEKITRHFLNQndYD 83
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEvGEVSDVPGTTrdPDVYVKELDKGKVKLVLVDTPGLDEF-GGLGREELARLLLRG--AD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  84 VIVNVLDATNLE----RNLILSAELLSLNKKMLLALNMCD--EAKKEGIELDTSILSQEFQSQVVEISAKTKENLELLLQ 157
Cdd:cd00882   78 LILLVVDSTDREseedAKLLILRRLRKEGIPIILVGNKIDllEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDELFE 157

                 ...
gi 488954368 158 KII 160
Cdd:cd00882  158 KLI 160
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
1-159 5.98e-16

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 76.17  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNF---SGVTIEKASAKTFYKNYEFEVIDLPGTYsldgysEEEKITRHFL 77
Cdd:COG1100    1 MGEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYlstNGVTIDKKELKLDGLDVDLVIWDTPGQD------EFRETRQFYA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  78 NQ-NDYDVIVNVLDAT---NLERNLILSAELLSLNKK--MLLALNMCDEAKKEGIELDTSI---LSQEFQSQVVEISAKT 148
Cdd:COG1100   75 RQlTGASLYLFVVDGTreeTLQSLYELLESLRRLGKKspIILVLNKIDLYDEEEIEDEERLkeaLSEDNIVEVVATSAKT 154
                        170
                 ....*....|.
gi 488954368 149 KENLELLLQKI 159
Cdd:COG1100  155 GEGVEELFAAL 165
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
7-160 3.56e-15

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: 73.58  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   7 ALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNY-EFEVIDLPGTysLDGYSEE----EKITRHfLNQNd 81
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGvDIQIIDLPGL--LDGASEGrglgEQILAH-LYRS- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  82 yDVIVNVLDATNLERNLILSaELLSLN------------KKMLLALNMCDEAKKEGIELDTSILSQEfQSQVVEISAKTK 149
Cdd:cd01881   77 -DLILHVIDASEDCVGDPLE-DQKTLNeevsgsflflknKPEMIVANKIDMASENNLKRLKLDKLKR-GIPVVPTSALTR 153
                        170
                 ....*....|.
gi 488954368 150 ENLELLLQKII 160
Cdd:cd01881  154 LGLDRVIRTIR 164
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
283-376 6.83e-15

Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for determining nucleoside specificity in the human CNT1 and CNT2 proteins. In the FeoB proteins, which are believed to be Fe2+ transporters, it includes the membrane pore region, so the function of this region is likely to be more general than just nucleoside specificity. This family may represent the pore and gate, with a wide potential range of specificity. Hence its name 'Gate'.


Pssm-ID: 429586 [Multi-domain]  Cd Length: 101  Bit Score: 70.75  E-value: 6.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  283 VILFLPNIMILFLGIALLETTGYMSRVAFLLDGILHKFG---LHGKSFIPLITGFGC---SVPAFMATRTLKNKRDRLLT 356
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGLLDRIGKLLGPLMRPLGlfpLPGKAAIALLLGFGAkevGVPLLATPYGIDTPRERLAA 80
                          90       100
                  ....*....|....*....|.
gi 488954368  357 LFVINFMS-CGARLPVYVLFI 376
Cdd:pfam07670  81 LLFTSFSTpCGATLPVYAGEL 101
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
4-159 2.97e-13

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 67.90  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKanmkvgnfsgvtIEKASaktfyknyefeVIDLPGT--------YSLDGY--------- 66
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAG------------RDRAI-----------VSDIAGTtrdvieeeIDLGGIpvrlidtag 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  67 ---SEE--EKI----TRHFLNQNdyDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSilsqef 137
Cdd:cd04164   61 lreTEDeiEKIgierAREAIEEA--DLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISELN------ 132
                        170       180
                 ....*....|....*....|..
gi 488954368 138 QSQVVEISAKTKENLELLLQKI 159
Cdd:cd04164  133 GKPIIAISAKTGEGIDELKEAL 154
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
4-163 2.99e-12

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: 65.15  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKAN-MKVGNFSGVTIEKASAKTFYKNYEFEVIDLPG-------TYSLDGYSeeekITRH 75
Cdd:cd01895    3 IKIAIIGRPNVGKSSLLNALLGEErVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgkvTEGIEKYS----VLRT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  76 FLNQNDYDVIVNVLDATN--LERNLILSAELLSLNKKMLLALNMCD--EAKKEGIELDTSILSQEFQ----SQVVEISAK 147
Cdd:cd01895   79 LKAIERADVVLLVLDASEgiTEQDLRIAGLILEEGKALIIVVNKWDlvEKDEKTMKEFEKELRRKLPfldyAPIVFISAL 158
                        170
                 ....*....|....*.
gi 488954368 148 TKENLELLLQKIIILF 163
Cdd:cd01895  159 TGQGVDKLFDAIKEVY 174
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
7-163 7.35e-12

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: 63.61  E-value: 7.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   7 ALVGQPNVGKSLLINALCKANMK-VGNFSGVTIEKASAKTFYKNYEFEVIDLPGtysLDGYSE--EEKITRHFLNQ-NDY 82
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGG---IEPDDEgiSKEIREQAEIAiEEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  83 DVIVNVLDA----TNLERNLilsAELL-SLNKKMLLALNMCDEAKKEgieldtsILSQEFQS----QVVEISAKTKENLE 153
Cdd:cd01894   78 DVILFVVDGreglTPADEEI---AKYLrKSKKPVILVVNKIDNIKEE-------EEAAEFYSlgfgEPIPISAEHGRGIG 147
                        170
                 ....*....|
gi 488954368 154 LLLQKIIILF 163
Cdd:cd01894  148 DLLDAILELL 157
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
4-165 9.73e-12

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 67.38  E-value: 9.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKAN-MKVGNFSGVTIEKASAKTFYKNYEFEVIDLPG-------TYSLDGYSeeekITRH 75
Cdd:PRK00093 174 IKIAIIGRPNVGKSSLINALLGEErVIVSDIAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEGVEKYS----VIRT 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  76 FLNQNDYDVIVNVLDATN-LER------NLILSAellslNKKMLLALNMCDEAKKEGIELDTSILSQEFQ----SQVVEI 144
Cdd:PRK00093 250 LKAIERADVVLLVIDATEgITEqdlriaGLALEA-----GRALVIVVNKWDLVDEKTMEEFKKELRRRLPfldyAPIVFI 324
                        170       180
                 ....*....|....*....|.
gi 488954368 145 SAKTKENLELLLQKIIILFES 165
Cdd:PRK00093 325 SALTGQGVDKLLEAIDEAYEN 345
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
5-160 1.55e-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: 62.86  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   5 KIALVGQPNVGKSLLINALckanmkVGnfsgvtiEKASA---------------KTFyKNYEFEVIDLPgtysldGYSEE 69
Cdd:cd04163    5 FVAIIGRPNVGKSTLLNAL------VG-------QKISIvspkpqttrnrirgiYTD-DDAQIIFVDTP------GIHKP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  70 EKITRHFLNQN------DYDVIVNVLDATN-LERNLILSAELLS-LNKKMLLALNMCDEAKKEGIELD--TSILSQEFQS 139
Cdd:cd04163   65 KKKLGERMVKAawsalkDVDLVLFVVDASEwIGEGDEFILELLKkSKTPVILVLNKIDLVKDKEDLLPllEKLKELHPFA 144
                        170       180
                 ....*....|....*....|.
gi 488954368 140 QVVEISAKTKENLELLLQKII 160
Cdd:cd04163  145 EIFPISALKGENVDELLEYIV 165
obgE PRK12297
GTPase CgtA; Reviewed
6-205 4.27e-11

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 65.12  E-value: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANMKVGNFS--------GVTiekasakTFYKNYEFEVIDLPGTysLDGYSE--------- 68
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHfttlvpnlGVV-------ETDDGRSFVMADIPGL--IEGASEgvglghqfl 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  69 ---EEkiTRhflnqndydVIVNVLDATNLE-RN-----LILSAELLS-----LNKKMLLALNMCDEakkEGIELDTSILS 134
Cdd:PRK12297 232 rhiER--TR---------VIVHVIDMSGSEgRDpiedyEKINKELKLynprlLERPQIVVANKMDL---PEAEENLEEFK 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488954368 135 QEFQSQVVEISAKTKENLELLLQKIIILFESkfIPRSQFYTPlceksPEKEDLLYFINELSKKIITHKKEE 205
Cdd:PRK12297 298 EKLGPKVFPISALTGQGLDELLYAVAELLEE--TPEFPLEEE-----EVEEEVYYKFEEEEKDFTITRDED 361
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-166 1.34e-10

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 63.89  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIkIALVGQPNVGKSLLINALCKanmK----VGNFSGVT---IEkasAKTFYKNYEFEVIDLPGtysLDGYSEEEkIT 73
Cdd:COG1160    1 MSPV-VAIVGRPNVGKSTLFNRLTG---RrdaiVDDTPGVTrdrIY---GEAEWGGREFTLIDTGG---IEPDDDDG-LE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  74 RHFLNQ-----NDYDVIVNVLDA----TNLERNLilsAELL-SLNKKMLLALNmcdeaKKEGIELDTSILsqEFQS---- 139
Cdd:COG1160   70 AEIREQaelaiEEADVILFVVDGraglTPLDEEI---AKLLrRSGKPVILVVN-----KVDGPKREADAA--EFYSlglg 139
                        170       180
                 ....*....|....*....|....*..
gi 488954368 140 QVVEISAKTKENLELLLQKIIILFESK 166
Cdd:COG1160  140 EPIPISAEHGRGVGDLLDAVLELLPEE 166
FeoB_C pfam07664
Ferrous iron transport protein B C terminus; Escherichia coli has an iron(II) transport system ...
389-438 1.39e-10

Ferrous iron transport protein B C terminus; 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 has been previously erroneously described as being ATP-binding. Recent work shows that it is similar to eukaryotic G-proteins and that it is a GTPase.


Pssm-ID: 462224 [Multi-domain]  Cd Length: 51  Bit Score: 56.65  E-value: 1.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488954368  389 LFGIYILGAILGLCAAKFL-RMTAFRGLDEPFVMEMPKYRMPNWHLVWFMV 438
Cdd:pfam07664   1 LFSLYLLGILVALLVALLLkKTTLLKGEPSPFVMELPPYRLPTLKNVLRKT 51
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
5-166 1.56e-10

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 63.53  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   5 KIALVGQPNVGKSLLINALCKANMK-VGNFSGVT---IEkasAKTFYKNYEFEVIDLPGtysLDGysEEEKITRHFLNQ- 79
Cdd:PRK00093   3 VVAIVGRPNVGKSTLFNRLTGKRDAiVADTPGVTrdrIY---GEAEWLGREFILIDTGG---IEP--DDDGFEKQIREQa 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  80 ----NDYDVIVNVLDAtnleRNLILSA------ELLSLNKKMLLALNmcdeaKKEGIELDTSILsqEFQS----QVVEIS 145
Cdd:PRK00093  75 elaiEEADVILFVVDG----RAGLTPAdeeiakILRKSNKPVILVVN-----KVDGPDEEADAY--EFYSlglgEPYPIS 143
                        170       180
                 ....*....|....*....|.
gi 488954368 146 AKTKENLELLLQKIIILFESK 166
Cdd:PRK00093 144 AEHGRGIGDLLDAILEELPEE 164
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
6-159 1.60e-10

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: 60.13  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNY-EFEVIDLPGTysLDGYSEE--------EKITR-- 74
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGrSFVIADIPGL--IEGASEGkglghrflRHIERtr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  75 ---HFLNQNDYDVIVNVLDATNLErnLIL-SAELLslNKKMLLALNMCD-EAKKEGIELDTSILSQEFQSQVVEISAKTK 149
Cdd:cd01898   81 vllHVIDLSGEDDPVEDYETIRNE--LEAyNPGLA--EKPRIVVLNKIDlLDAEERFEKLKELLKELKGKKVFPISALTG 156
                        170
                 ....*....|
gi 488954368 150 ENLELLLQKI 159
Cdd:cd01898  157 EGLDELLKKL 166
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
4-169 3.73e-10

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 62.44  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKAnmkvgnfsgvtiEKASaktfyknyefeVIDLPGT--------YSLDGY--------- 66
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGE------------ERAI-----------VTDIAGTtrdvieehINLDGIplrlidtag 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  67 ---SEE--EKI----TRHFLNQNdyDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSilsqef 137
Cdd:PRK05291 273 ireTDDevEKIgierSREAIEEA--DLVLLVLDASEPLTEEDDEILEELKDKPVIVVLNKADLTGEIDLEEENG------ 344
                        170       180       190
                 ....*....|....*....|....*....|..
gi 488954368 138 qSQVVEISAKTKENLELLLQKIIILFESKFIP 169
Cdd:PRK05291 345 -KPVIRISAKTGEGIDELREAIKELAFGGFGG 375
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
6-160 5.61e-10

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: 58.34  E-value: 5.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTysLDGYSEE----EK--IT--RHFl 77
Cdd:cd01897    3 LVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI--LDRPLEErntiEMqaITalAHL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  78 nqndYDVIVNVLDATN-----LERNLILSAELLSL-NKKMLLALNMCDEAKKEGIELDTSILSQEFQsQVVEISAKTKEN 151
Cdd:cd01897   80 ----RAAVLFFIDPSEtcgysIEEQLSLFKEIKPLfNKPVIVVLNKIDLLTEEDLSEIEKELEKEGE-EVIKISTLTEEG 154

                 ....*....
gi 488954368 152 LELLLQKII 160
Cdd:cd01897  155 VDELKNKAC 163
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
6-160 6.03e-10

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 60.77  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKAnmKVG-----------NFSGVTIEKasaktfykNYEFEVIDLPG----TYSLDgyseee 70
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQ--KVSivspkpqttrhRIRGIVTRE--------DAQIVFVDTPGihkpKRKLG------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  71 kitrHFLNQ------NDYDVIVNVLDAT---NLERNLILsAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQ-SQ 140
Cdd:COG1159   70 ----RRMNKaawsalEDVDVILFVVDATekiGEGDEFIL-ELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDfAE 144
                        170       180
                 ....*....|....*....|
gi 488954368 141 VVEISAKTKENLELLLQKII 160
Cdd:COG1159  145 IVPISALKGDNVDELLDEIA 164
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
4-205 1.02e-09

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: 59.71  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    4 IKIALVGQPNVGKSLLINALC---------KANMKVGNFSGVTIEKASAKTFyknyefevIDLPgtysldGYSEEEKITR 74
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHgqkisitspKAQTTRNRISGIHTTGASQIIF--------IDTP------GFHEKKHSLN 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   75 HFLNQN------DYDVIVNVLDAT--NLERNLILSaELLSLNKKMLLALNMCD-EAKKEGIELDTSILSQEFQSQVVEIS 145
Cdd:TIGR00436  67 RLMMKEarsaigGVDLILFVVDSDqwNGDGEFVLT-KLQNLKRPVVLTRNKLDnKFKDKLLPLIDKYAILEDFKDIVPIS 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488954368  146 AKTKENLELLLQKIiilfESKFIPRSQFYTP-LCEKSPEKEDLLYFINElskKIITHKKEE 205
Cdd:TIGR00436 146 ALTGDNTSFLAAFI----EVHLPEGPFRYPEdYVTDQPDRFKISEIIRE---KIIRYTKEE 199
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
4-163 1.05e-09

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


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 60.19  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    4 IKIALVGQPNVGKSLLINALCKAnmkvgnfsgvtiEKAsaktfyknyefevI--DLPGT--------YSLDGY------- 66
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGE------------ERA-------------IvtDIPGTtrdvieetINIGGIplrlidt 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   67 -----SEE--EKI----TRHFLNQNdyDVIVNVLDATN-LERNLILSAELLSLNKKMLLALNMCDEAKKEgieldtSILS 134
Cdd:pfam12631 150 agireTDDevEKIgierAREAIEEA--DLVLLVLDASRpLDEEDLEILELLKDKKPIIVVLNKSDLLGEI------DELE 221
                         170       180
                  ....*....|....*....|....*....
gi 488954368  135 QEFQSQVVEISAKTKENLELLLQKIIILF 163
Cdd:pfam12631 222 ELKGKPVLAISAKTGEGLDELEEAIKELF 250
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
4-165 2.67e-09

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 59.65  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKAN-MKVGNFSGVT-------IEkasaktfYKNYEFEVIDLPG-------TYSLDGYSe 68
Cdd:COG1160  176 IKIAIVGRPNVGKSSLINALLGEErVIVSDIAGTTrdsidtpFE-------RDGKKYTLIDTAGirrkgkvDEGIEKYS- 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  69 eekITRHFLNQNDYDVIVNVLDAT-NLER------NLILSAellslNKKMLLALNMCDEAKKEGIELD--TSILSQEFQ- 138
Cdd:COG1160  248 ---VLRTLRAIERADVVLLVIDATeGITEqdlkiaGLALEA-----GKALVIVVNKWDLVEKDRKTREelEKEIRRRLPf 319
                        170       180       190
                 ....*....|....*....|....*....|
gi 488954368 139 ---SQVVEISAKTKENLELLLQKIIILFES 165
Cdd:COG1160  320 ldyAPIVFISALTGQGVDKLLEAVDEVYES 349
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
4-159 3.02e-09

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: 59.30  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKAnmkvgnfsgvtiEKAsaktfyknyefevI--DLPGT--------YSLDGY------- 66
Cdd:COG0486  214 IKVVIVGRPNVGKSSLLNALLGE------------ERA-------------IvtDIAGTtrdvieerINIGGIpvrlidt 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  67 -----SEE--EKI----TRHFLNQNdyDVIVNVLDATNLERNLILSAELLSLNKKMLLALNMCDEAKKEGIEldtsiLSQ 135
Cdd:COG0486  269 aglreTEDevEKIgierAREAIEEA--DLVLLLLDASEPLTEEDEEILEKLKDKPVIVVLNKIDLPSEADGE-----LKS 341
                        170       180
                 ....*....|....*....|....
gi 488954368 136 EFQSQVVEISAKTKENLELLLQKI 159
Cdd:COG0486  342 LPGEPVIAISAKTGEGIDELKEAI 365
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
446-579 3.22e-09

Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for determining nucleoside specificity in the human CNT1 and CNT2 proteins. In the FeoB proteins, which are believed to be Fe2+ transporters, it includes the membrane pore region, so the function of this region is likely to be more general than just nucleoside specificity. This family may represent the pore and gate, with a wide potential range of specificity. Hence its name 'Gate'.


Pssm-ID: 429586 [Multi-domain]  Cd Length: 101  Bit Score: 54.57  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  446 LKKAGTFILLASLLIWFASNFpkseenlndfnaqeraieqSYLGQFGKGIEPIFQPL---ELDWKLSVSLISGLAAKEVM 522
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYS-------------------GLLDRIGKLLGPLMRPLglfPLPGKAAIALLLGFGAKEVG 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488954368  523 ISTMGVLYSLGKDVdetnndlkgiiaknipipSAVAFILFVMIYNPCFAATIVFSKE 579
Cdd:pfam07670  62 VPLLATPYGIDTPR------------------ERLAALLFTSFSTPCGATLPVYAGE 100
YeeP COG3596
Predicted GTPase [General function prediction only];
6-160 1.14e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 57.08  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKAN-MKVGNFSGVTIEkasaktfYKNYEFE--------VIDLPGTYSLDGYSEEEKITRHF 76
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEvAEVGVGRPCTRE-------IQRYRLEsdglpglvLLDTPGLGEVNERDREYRELREL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  77 LNQndYDVIVNVLDATN----LERNLILSAELLSLNKKMLLALNMCDEAkkEGIELDTSILSQEFQSQVVEISAKT---K 149
Cdd:COG3596  115 LPE--ADLILWVVKADDralaTDEEFLQALRAQYPDPPVLVVLTQVDRL--EPEREWDPPYNWPSPPKEQNIRRALeaiA 190
                        170
                 ....*....|.
gi 488954368 150 ENLELLLQKII 160
Cdd:COG3596  191 EQLGVPIDRVI 201
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
4-159 8.62e-08

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: 51.99  E-value: 8.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    4 IKIALVGQPNVGKSLLINALCK---ANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYSLDgyseeeKITRHFLNQN 80
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGnkgSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYD------AIRRLYYPQV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   81 D-----YDVIVNVLDATN-LERNLILSAELLSLNKKMLLALNMCDeakKEGIELDT---SILSQEFQSQVVEISAKTKEN 151
Cdd:TIGR00231  76 ErslrvFDIVILVLDVEEiLEKQTKEIIHHADSGVPIILVGNKID---LKDADLKThvaSEFAKLNGEPIIPLSAETGKN 152

                  ....*...
gi 488954368  152 LELLLQKI 159
Cdd:TIGR00231 153 IDSAFKIV 160
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
6-110 1.24e-07

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 54.03  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTysLDGYSEEEKITRHFLNQ-NDYDV 84
Cdd:COG1163   66 VVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGL--IEGAASGKGRGKEVLSVvRNADL 143
                         90       100       110
                 ....*....|....*....|....*....|
gi 488954368  85 IVNVLDATNLERNLILSAEL----LSLNKK 110
Cdd:COG1163  144 ILIVLDVFELEQYDVLKEELydagIRLNKP 173
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
6-159 1.78e-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: 51.36  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANM--KVGNFSGVTiekasaKT--FYK-NYEFEVIDLPGtYsldGY---SEEEK-----I 72
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRKKlaRTSKTPGRT------QLinFFNvGDKFRLVDLPG-Y---GYakvSKEVRekwgkL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  73 TRHFLNQNDYDVIVNVL-DA----TNLERNLIlsAELLSLNKKMLLALNMCD-----EAKKEGIELDTSILSQEFQSQVV 142
Cdd:cd01876   72 IEEYLENRENLKGVVLLiDArhgpTPIDLEML--EFLEELGIPFLIVLTKADklkksELAKVLKKIKEELNLFNILPPVI 149
                        170
                 ....*....|....*..
gi 488954368 143 EISAKTKENLELLLQKI 159
Cdd:cd01876  150 LFSSKKGTGIDELRALI 166
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
10-166 2.68e-07

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 52.91  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  10 GQPNVGKSLLINALCKANMKVGNF----SGVTIekasAKTFYKNYEFEVIDLPGTysLD-GYSEEEKITRH------FLN 78
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYpfttKGIIV----GHFERGHGRYQVIDTPGL--LDrPLSERNEIERQailalkHLA 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  79 qndyDVIVNVLDATN-----LERNLILSAELLSL-NKKMLLALNMCDEAKKEGIELDTSIlsqefqsQVVEISAKTKENL 152
Cdd:COG1084  241 ----DVILFLFDPSEtcgysLEEQLNLLEEIRSLfDVPVIVVINKIDLSDEEELKEAEEE-------ADIKISALTGEGV 309
                        170
                 ....*....|....
gi 488954368 153 ELLLQKIIILFESK 166
Cdd:COG1084  310 DELLDELIEALEEE 323
PRK04213 PRK04213
GTP-binding protein EngB;
1-91 5.16e-07

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 50.69  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEkasaKTFYKNYEFEVIDLPGTYSLDGYSEE--EKITR---H 75
Cdd:PRK04213   7 DRKPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRK----PNHYDWGDFILTDLPGFGFMSGVPKEvqEKIKDeivR 82
                         90
                 ....*....|....*...
gi 488954368  76 FL--NQNDYDVIVNVLDA 91
Cdd:PRK04213  83 YIedNADRILAAVLVVDG 100
era PRK00089
GTPase Era; Reviewed
6-160 1.53e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 50.05  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANmkvgnfsgVTIekASAK------------TFyKNYEFEVIDLPGTysldgYSEEEKIT 73
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQK--------ISI--VSPKpqttrhrirgivTE-DDAQIIFVDTPGI-----HKPKRALN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  74 RhFLNQN------DYDVIVNVLDATNL---ERNLILSaELLSLNKKMLLALNMCDEAKKEGI--ELDTSILSQEFQSQVV 142
Cdd:PRK00089  72 R-AMNKAawsslkDVDLVLFVVDADEKigpGDEFILE-KLKKVKTPVILVLNKIDLVKDKEEllPLLEELSELMDFAEIV 149
                        170
                 ....*....|....*...
gi 488954368 143 EISAKTKENLELLLQKII 160
Cdd:PRK00089 150 PISALKGDNVDELLDVIA 167
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
5-167 1.58e-06

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 48.70  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   5 KIALVGQPNVGKSLLINALCKANMKVgnfSGVTIEkaSAKTFYKNYEF----EVIDLPGTYSLDgySEEEKITRHFLnqN 80
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLGEEVLP---TGVTPT--TAVITVLRYGLlkgvVLVDTPGLNSTI--EHHTEITESFL--P 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  81 DYDVIVNVLDA----TNLERNLILSAeLLSLNKKMLLALNMCDEAKKEGIELDTSILSQEFQ--------SQVVEISAK- 147
Cdd:cd09912   73 RADAVIFVLSAdqplTESEREFLKEI-LKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGvlelgggePRIFPVSAKe 151
                        170       180
                 ....*....|....*....|....*
gi 488954368 148 -----TKENLELLLQKIIILFESKF 167
Cdd:cd09912  152 alearLQGDEELLEQSGFEELEEHL 176
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
1-59 1.73e-06

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 48.29  E-value: 1.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   1 MKKIKIALVGQPNVGKSLLINALC-KANMKVGNFSGVTieKASaKTFYKNYEFEVIDLPG 59
Cdd:cd01856  113 PRPLRAMVVGIPNVGKSTLINRLRgKKVAKVGNKPGVT--RGQ-QWIRIGPNIELLDTPG 169
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
6-97 1.75e-06

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: 50.30  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNY----EFEVIDLPGTYS-LDGYseeekitRH----- 75
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVGYVRVEcpckELGVSCNPRYGKcIDGK-------RYvpvel 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488954368  76 -------------------FLNQ-NDYDVIVNVLDA---TNLERN 97
Cdd:cd01899   74 idvaglvpgahegkglgnqFLDDlRDADVLIHVVDAsggTDAEGN 118
PTZ00258 PTZ00258
GTP-binding protein; Provisional
5-44 3.26e-06

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 49.56  E-value: 3.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488954368   5 KIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAK 44
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTAR 62
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
2-37 5.32e-06

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 48.57  E-value: 5.32e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 488954368   2 KKIKIALVGQPNVGKSLLINALCKANM-KVGNFSGVT 37
Cdd:COG1161  112 RPIRVMIVGIPNVGKSTLINRLAGKKVaKTGNKPGVT 148
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
2-59 2.76e-05

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 46.35  E-value: 2.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368    2 KKIKIALVGQPNVGKSLLINALCKANM-KVGNFSGVTieKASAKTFYKNyEFEVIDLPG 59
Cdd:TIGR03596 117 RPIRAMIVGIPNVGKSTLINRLAGKKVaKVGNRPGVT--KGQQWIKLSD-NLELLDTPG 172
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
5-39 2.93e-05

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 46.55  E-value: 2.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 488954368   5 KIALVGQPNVGKSLLINALCKANMKVGNFSGVTIE 39
Cdd:COG0012    2 KCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIE 36
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
4-110 4.27e-05

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: 45.23  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   4 IKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDLPGTYslDGYSEEEKITRHFL----NQ 79
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGII--EGASDGKGRGRQVIavarTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488954368  80 ndyDVIVNVLDATNLERNL-ILSAEL----LSLNKK 110
Cdd:cd01896   79 ---DLILIVLDATKPEGQReILERELegvgIRLNKK 111
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
5-160 4.99e-05

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: 43.72  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   5 KIALVGQPNVGKSLLINALckanmKVGNFS------GVTIEKASaktfYKNYEFEVIDLPGtysldgyseeEKITRHFLN 78
Cdd:cd00878    1 RILMLGLDGAGKTTILYKL-----KLGEVVttiptiGFNVETVE----YKNVKFTVWDVGG----------QDKIRPLWK 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  79 Q--NDYDVIVNVLDATNLER--------NLILSAELLS-------LNKKMLLALNMCDEAKKEgIELdTSILSQEFqsQV 141
Cdd:cd00878   62 HyyENTDGLIFVVDSSDRERieeaknelHKLLNEEELKgapllilANKQDLPGALTESELIEL-LGL-ESIKGRRW--HI 137
                        170
                 ....*....|....*....
gi 488954368 142 VEISAKTKENLELLLQKII 160
Cdd:cd00878  138 QPCSAVTGDGLDEGLDWLI 156
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
35-165 5.45e-05

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 44.44  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   35 GVTIEKASAKTFYKNYEFEVIDLPGtySLDgYSEEekiTRHFLNQNDYdVIVnVLDAT-----NLERNLILsaeLLSLNK 109
Cdd:pfam00009  54 GITIKSAAVSFETKDYLINLIDTPG--HVD-FVKE---VIRGLAQADG-AIL-VVDAVegvmpQTREHLRL---ARQLGV 122
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488954368  110 KMLLALNMCDEAKKEGIELDTSILSQEFQSQ---------VVEISAKTKENLELLLQKIIILFES 165
Cdd:pfam00009 123 PIIVFINKMDRVDGAELEEVVEEVSRELLEKygedgefvpVVPGSALKGEGVQTLLDALDEYLPS 187
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
2-59 1.03e-04

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 42.76  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368   2 KKIKIALVGQPNVGKSLLINALCKA-NMKVGNFSGVTiekASAKTFYKNYEFEVIDLPG 59
Cdd:cd01849   90 KGIRVGVVGLPNVGKSSFINALLNKfKLKVGSIPGTT---KLQQDVKLDKEIYLYDTPG 145
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
6-153 1.22e-04

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 43.23  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    6 IALVGQPNVGKSLLINALC--KANMKVGNFSGvtiekasaKT----FYK-NYEFEVIDLPGtYsldGY---SEEEKI--- 72
Cdd:TIGR03598  21 IAFAGRSNVGKSSLINALTnrKKLARTSKTPG--------RTqlinFFEvNDGFRLVDLPG-Y---GYakvSKEEKEkwq 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   73 --TRHFLN--QNDYDVIVnVLDA----TNLERNLIlsAELLSLNKKMLLALNMCD-----EAKKEGIELDTSILSQEFQS 139
Cdd:TIGR03598  89 klIEEYLEkrENLKGVVL-LMDIrhplKELDLEMI--EWLRERGIPVLIVLTKADklkksELNKQLKKIKKALKKDADDP 165
                         170
                  ....*....|....
gi 488954368  140 QVVEISAKTKENLE 153
Cdd:TIGR03598 166 SVQLFSSLKKTGID 179
PRK09602 PRK09602
translation-associated GTPase; Reviewed
4-39 2.24e-04

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 44.03  E-value: 2.24e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 488954368   4 IKIALVGQPNVGKSLLINALCKANMKVGNFSGVTIE 39
Cdd:PRK09602   2 ITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTID 37
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
2-37 2.61e-04

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 42.18  E-value: 2.61e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 488954368   2 KKIKIALVGQPNVGKSLLINALCKANM-KVGNFSGVT 37
Cdd:cd04178  115 TSITVGVVGYPNVGKSSVINSLKRSRAcNVGATPGVT 151
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
5-164 2.88e-04

Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) subfamily. Rheb was initially identified in rat brain, where its expression is elevated by seizures or by long-term potentiation. It is expressed ubiquitously, with elevated levels in muscle and brain. Rheb functions as an important mediator between the tuberous sclerosis complex proteins, TSC1 and TSC2, and the mammalian target of rapamycin (TOR) kinase to stimulate cell growth. TOR kinase regulates cell growth by controlling nutrient availability, growth factors, and the energy status of the cell. TSC1 and TSC2 form a dimeric complex that has tumor suppressor activity, and TSC2 is a GTPase activating protein (GAP) for Rheb. The TSC1/TSC2 complex inhibits the activation of TOR kinase through Rheb. Rheb has also been shown to induce the formation of large cytoplasmic vacuoles in a process that is dependent on the GTPase cycle of Rheb, but independent of the TOR kinase, suggesting Rheb plays a role in endocytic trafficking that leads to cell growth and cell-cycle progression. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 206709 [Multi-domain]  Cd Length: 180  Bit Score: 42.23  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   5 KIALVGQPNVGKSLLINALCKanmkvGNFSGV---TIEKASAKTF-YKN--YEFEVID---------LPGTYSLD--GYS 67
Cdd:cd04137    3 KIAVLGSRSVGKSSLTVQFVE-----GHFVESyypTIENTFSKIItYKGqeYHLEIVDtagqdeysiLPQKYSIGihGYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  68 EEEKIT-RHFLN--QNDYDVIVNVLDATNLERNLIlsaellsLNKKmllALNMCDE-AKKEGIEldtsiLSQEFQSQVVE 143
Cdd:cd04137   78 LVYSVTsRKSFEvvKVIYDKILDMLGKESVPIVLV-------GNKS---DLHMERQvSAEEGKK-----LAESWGAAFLE 142
                        170       180
                 ....*....|....*....|.
gi 488954368 144 ISAKTKENLELLLQKIIILFE 164
Cdd:cd04137  143 SSAKENENVEEAFELLIEEIE 163
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
6-125 3.41e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 43.63  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINA-LCKANMKVGNFSGVTIEKASAKTFYKNYEFEVIDlPGTYSLDGYSEEEKITRHF-LNQNDYD 83
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRiLGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVD-TGGWEADVEGIDSAIASQAqIAVSLAD 356
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488954368  84 VIVNVLDATN--LERNLILSAELLSLNKKMLLALNMCDEAKKEG 125
Cdd:PRK09518 357 AVVFVVDGQVglTSTDERIVRMLRRAGKPVVLAVNKIDDQASEY 400
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
6-39 8.63e-04

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: 41.68  E-value: 8.63e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488954368   6 IALVGQPNVGKSLLINALCKANMKVGNFSGVTIE 39
Cdd:cd01900    1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIE 34
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
6-159 1.44e-03

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 40.06  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368   6 IALVGQPNVGKSLLINALC--KANMKVGNFSGvtiekasaKT----FYK-NYEFEVIDLPGtYsldGY---SEEEK---- 71
Cdd:COG0218   26 IAFAGRSNVGKSSLINALTnrKKLARTSKTPG--------KTqlinFFLiNDKFYLVDLPG-Y---GYakvSKAEKekwq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368  72 --IT------------------RHFLNQNDYDVIvNVLDATNLERNLILS-AELLSLNKKMLLALNMCDEAKKEGIEldt 130
Cdd:COG0218   94 klIEdylegrenlkgvvllidiRHPPKELDLEML-EWLDEAGIPFLIVLTkADKLKKSELAKQLKAIKKALGKDPAA--- 169
                        170       180
                 ....*....|....*....|....*....
gi 488954368 131 silsqefqSQVVEISAKTKENLELLLQKI 159
Cdd:COG0218  170 --------PEVILFSSLKKEGIDELRAAI 190
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
6-24 1.77e-03

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 39.14  E-value: 1.77e-03
                         10
                 ....*....|....*....
gi 488954368   6 IALVGQPNVGKSLLINALC 24
Cdd:cd01857   85 IGLVGYPNVGKSSLINALV 103
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
3-123 4.48e-03

Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a role in in intracellular defence. IIGP is predominantly associated with the Golgi apparatus and also localizes to the endoplasmic reticulum and exerts a distinct role in IFN-induced intracellular membrane trafficking or processing.


Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 39.77  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488954368    3 KIKIALVGQPNVGKSLLINAL------CKANMKVGnfsgvTIEKASAKTFYKNYEF---EVIDLPGT----YSLDGYSEE 69
Cdd:pfam05049  35 PLKIAVTGDSGNGKSSFINALrgigheEDGSAPTG-----VVETTMKRTPYSHPHFpnvVLWDLPGLgatnFTVESYLEE 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488954368   70 EKITrhflnqnDYDVIVnvldatnlernlILSAELLSLNkKMLLALNMCDEAKK 123
Cdd:pfam05049 110 MKFS-------EYDFFI------------IISSERFSLN-DVKLAKAIQRMGKR 143
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
83-159 8.67e-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: 37.30  E-value: 8.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488954368  83 DVIVNVLDATN--LERNLILSAELLSLNKKMLLALNMCDEAKKEGIELDTSILSQEfQSQVVEISAKTKENLELLLQKI 159
Cdd:cd01859   13 DVVLEVVDARDpeLTRSRKLERMALELGKKLIIVLNKADLVPREVLEKWKEVFESE-GLPVVYVSARERLGTRILRRTI 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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