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Conserved domains on  [gi|283462287|gb|ADB22435|]
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GTP-binding protein 1 [Rattus norvegicus]

Protein Classification

GTPBP1 family GTP-binding protein( domain architecture ID 1000986)

GTPBP1 family GTP-binding protein binds GTP and has GTPase activity; similar to Homo sapiens GTP-binding protein 1 and 2

Gene Ontology:  GO:0003924|GO:0005525
PubMed:  11916378

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
GTPBP1 super family cl34959
GTPase [General function prediction only];
77-574 4.56e-162

GTPase [General function prediction only];


The actual alignment was detected with superfamily member COG5258:

Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 476.35  E-value: 4.56e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  77 SLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQ-ESGGRVRDYLVRKRvGD 155
Cdd:COG5258   39 SLAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAKIEDVETWEvGDGGLVGVVTIREG-KE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 156 NDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGnVVNKPDSHGGSl 235
Cdd:COG5258  118 KDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-PVRMKNPLRKT- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 236 EWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 315
Cdd:COG5258  196 DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 316 NILQETLKLLQRLLKSPGcrKIPVLVQSKDDViVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLsPRTSYREEEPA 395
Cdd:COG5258  276 ERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERL-PKRATDEDEPF 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 396 EFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRK 475
Cdd:COG5258  352 LMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELER 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 476 GMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQ 555
Cdd:COG5258  432 GMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRFKYRPYYVEEGQ 511

                        490
                 ....*....|....*....
gi 283462287 556 RLVFREGRTKAVGTITKLL 574
Cdd:COG5258  512 RFVFREGRSKGVGTVTDIL 530
 
Name Accession Description Interval E-value
GTPBP1 COG5258
GTPase [General function prediction only];
77-574 4.56e-162

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 476.35  E-value: 4.56e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  77 SLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQ-ESGGRVRDYLVRKRvGD 155
Cdd:COG5258   39 SLAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAKIEDVETWEvGDGGLVGVVTIREG-KE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 156 NDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGnVVNKPDSHGGSl 235
Cdd:COG5258  118 KDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-PVRMKNPLRKT- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 236 EWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 315
Cdd:COG5258  196 DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 316 NILQETLKLLQRLLKSPGcrKIPVLVQSKDDViVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLsPRTSYREEEPA 395
Cdd:COG5258  276 ERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERL-PKRATDEDEPF 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 396 EFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRK 475
Cdd:COG5258  352 LMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELER 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 476 GMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQ 555
Cdd:COG5258  432 GMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRFKYRPYYVEEGQ 511

                        490
                 ....*....|....*....
gi 283462287 556 RLVFREGRTKAVGTITKLL 574
Cdd:COG5258  512 RFVFREGRSKGVGTVTDIL 530
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 162-386 2.28e-154

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 444.43  E-value: 2.28e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 162 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEwTKIC 241
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELD-VEIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 242 EKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQET 321
Cdd:cd04165   80 EKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283462287 322 LKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPR 386
Cdd:cd04165  160 LKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNLSSGRVVPIFQVSNVTGEGLDLLRRFLNLLPPR 224
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 161-482 4.49e-28

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 119.21  E-value: 4.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  161 VRVAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfrHKHEiESGRTSSVGndiLGFDSegnvVNKPDshggslewtki 240
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAAD------------RLPE-EKKRGMTID---LGFAY----FPLPD----------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  241 cekssKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPANILQ 319
Cdd:TIGR00475  50 -----YRLGFIDVPGHEKFISNAIAGGGG--IDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIK 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  320 ETLKLLQRLLKSPGcrkipVLVQSKddvivtasnfssermcpIFQISNVTGENLDLLKMFL-NLLSPRTSYREEEPAEFQ 398
Cdd:TIGR00475 123 RTEMFMKQILNSYI-----FLKNAK-----------------IFKTSAKTGQGIGELKKELkNLLESLDIKRIQKPLRMA 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  399 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLgpDPLGNflSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 478
Cdd:TIGR00475 181 IDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL--LPINH--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLL 256


                  ....
gi 283462287  479 MVSP 482
Cdd:TIGR00475 257 ILTP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 161-385 4.60e-25

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: 102.60  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  161 VRVAVVGNVDAGKSTLLGVLTH--GELDNG---RGFARQKLFRHKHEIESGRTSSVGNDilgfdsegnvvnkpdshggSL 235
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYytGAISKRgevKGEGEAGLDNLPEERERGITIKSAAV-------------------SF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  236 EWTKicekssKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 315
Cdd:pfam00009  65 ETKD------YLINLIDTPGHVDFVKEVIRGLA--QADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 283462287  316 NILQETLKLLQRLLkspgcrkIPVLVQSKDDVivtasnfssermcPIFQISNVTGENLD-LLKMFLNLLSP 385
Cdd:pfam00009 137 AELEEVVEEVSREL-------LEKYGEDGEFV-------------PVVPGSALKGEGVQtLLDALDEYLPS 187
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 163-546 2.11e-20

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 94.22  E-value: 2.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 163 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEIESGRTSSVGNdiLGFDSEgnvv 225
Cdd:PRK12317   9 LAVIGHVDHGKSTLVGRLlyETGAIDehiieELREEAKEKgkesfkfawvMDRLKEERERGVTIDLAH--KKFETD---- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 226 nkpdshggslewtkiceksSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSN--AGIVGMTKEHLGLALALNVP- 302
Cdd:PRK12317  83 -------------------KYYFTIVDCPGHRDFVKNMITGASQ--ADAAVLVVAADdaGGVMPQTREHVFLARTLGINq 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 303 VFVVVTKIDMcpANILQ----ETLKLLQRLLKSPGCRK-----IPVLVQSKDDVIVtasnfSSERMcPIFqisnvTG--- 370
Cdd:PRK12317 142 LIVAINKMDA--VNYDEkryeEVKEEVSKLLKMVGYKPddipfIPVSAFEGDNVVK-----KSENM-PWY-----NGptl 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 371 -ENLDLLKMflnllSPRTSyreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGP-DPLGNflsiaVKSIHRK 448
Cdd:PRK12317 209 lEALDNLKP-----PEKPT---DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPaGVVGE-----VKSIEMH 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 449 RMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMD 528
Cdd:PRK12317 276 HEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELV 355

                        410       420       430
                 ....*....|....*....|....*....|..
gi 283462287 529 K--------------DCLRTGDKATVHFRFIK 546
Cdd:PRK12317 356 KkldprtgqvaeenpQFIKTGDAAIVKIKPTK 387
 
Name Accession Description Interval E-value
GTPBP1 COG5258
GTPase [General function prediction only];
77-574 4.56e-162

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 476.35  E-value: 4.56e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  77 SLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQ-ESGGRVRDYLVRKRvGD 155
Cdd:COG5258   39 SLAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAKIEDVETWEvGDGGLVGVVTIREG-KE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 156 NDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGnVVNKPDSHGGSl 235
Cdd:COG5258  118 KDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-PVRMKNPLRKT- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 236 EWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 315
Cdd:COG5258  196 DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 316 NILQETLKLLQRLLKSPGcrKIPVLVQSKDDViVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLsPRTSYREEEPA 395
Cdd:COG5258  276 ERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERL-PKRATDEDEPF 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 396 EFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRK 475
Cdd:COG5258  352 LMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELER 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 476 GMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQ 555
Cdd:COG5258  432 GMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRFKYRPYYVEEGQ 511

                        490
                 ....*....|....*....
gi 283462287 556 RLVFREGRTKAVGTITKLL 574
Cdd:COG5258  512 RFVFREGRSKGVGTVTDIL 530
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 162-386 2.28e-154

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 444.43  E-value: 2.28e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 162 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEwTKIC 241
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELD-VEIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 242 EKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQET 321
Cdd:cd04165   80 EKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283462287 322 LKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPR 386
Cdd:cd04165  160 LKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNLSSGRVVPIFQVSNVTGEGLDLLRRFLNLLPPR 224
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 487-573 4.64e-54

Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 179.64  E-value: 4.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 487 QASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQRLVFREGRTKA 566
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTKG 80


                 ....*..
gi 283462287 567 VGTITKL 573
Cdd:cd03708   81 IGTVTKV 87
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 162-386 3.14e-46

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 162.08  E-value: 3.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 162 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQ--KLFRHKHEIESGRTSSVGNDilgfdsegnvvnkpdshggSLEWTK 239
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKetFLDTLKEERERGITIKTGVV-------------------EFEWPK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 240 icekssKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQ 319
Cdd:cd00881   62 ------RRINFIDTPGHEDFSKETVRGLA--QADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFD 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 283462287 320 ETLKLLQRLLKSPGCRkipvlvqskddvivtasnFSSERMCPIFQISNVTGEN-LDLLKMFLNLLSPR 386
Cdd:cd00881  134 EVLREIKELLKLIGFT------------------FLKGKDVPIIPISALTGEGiEELLDAIVEHLPPP 183
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 395-481 9.47e-46

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 157.00  E-value: 9.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 395 AEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIR 474
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*..
gi 283462287 475 KGMVMVS 481
Cdd:cd03694   81 KGMVLVS 87
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 244-560 1.85e-30

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 126.95  E-value: 1.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 244 SSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIvgM--TKEHLG-LALaLNVPV-FVVVTKIDMCPANILQ 319
Cdd:COG3276   49 DGRRLGFVDVPGHEKFIKNMLAGAGG--IDLVLLVVAADEGV--MpqTREHLAiLDL-LGIKRgIVVLTKADLVDEEWLE 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 320 ETLKLLQRLLKSpgcrkipvlvqskddvivtaSNFSSermCPIFQISNVTGENLDLLKMFLNLLSPRTSYREEE-PAEFQ 398
Cdd:COG3276  124 LVEEEIRELLAG--------------------TFLED---APIVPVSAVTGEGIDELRAALDALAAAVPARDADgPFRLP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 399 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPlgnfLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 478
Cdd:COG3276  181 IDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDV 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 479 MVSPRLnPQASWEFEAEILVLHH-PTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFiKTPEYLHIDQRL 557
Cdd:COG3276  257 LAAPGA-LRPTDRIDVRLRLLPSaPRPLKHWQRVHLHHGTAEVLARVVLLDREELAPGEEALAQLRL-EEPLVAARGDRF 334


                 ...
gi 283462287 558 VFR 560
Cdd:COG3276  335 ILR 337
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 161-482 4.49e-28

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 119.21  E-value: 4.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  161 VRVAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfrHKHEiESGRTSSVGndiLGFDSegnvVNKPDshggslewtki 240
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAAD------------RLPE-EKKRGMTID---LGFAY----FPLPD----------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  241 cekssKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPANILQ 319
Cdd:TIGR00475  50 -----YRLGFIDVPGHEKFISNAIAGGGG--IDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIK 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  320 ETLKLLQRLLKSPGcrkipVLVQSKddvivtasnfssermcpIFQISNVTGENLDLLKMFL-NLLSPRTSYREEEPAEFQ 398
Cdd:TIGR00475 123 RTEMFMKQILNSYI-----FLKNAK-----------------IFKTSAKTGQGIGELKKELkNLLESLDIKRIQKPLRMA 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  399 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLgpDPLGNflSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 478
Cdd:TIGR00475 181 IDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL--LPINH--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLL 256


                  ....
gi 283462287  479 MVSP 482
Cdd:TIGR00475 257 ILTP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 161-385 4.60e-25

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: 102.60  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  161 VRVAVVGNVDAGKSTLLGVLTH--GELDNG---RGFARQKLFRHKHEIESGRTSSVGNDilgfdsegnvvnkpdshggSL 235
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYytGAISKRgevKGEGEAGLDNLPEERERGITIKSAAV-------------------SF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  236 EWTKicekssKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 315
Cdd:pfam00009  65 ETKD------YLINLIDTPGHVDFVKEVIRGLA--QADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 283462287  316 NILQETLKLLQRLLkspgcrkIPVLVQSKDDVivtasnfssermcPIFQISNVTGENLD-LLKMFLNLLSP 385
Cdd:pfam00009 137 AELEEVVEEVSREL-------LEKYGEDGEFV-------------PVVPGSALKGEGVQtLLDALDEYLPS 187
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 163-546 7.76e-23

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 101.55  E-value: 7.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 163 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEIESGRTSSVGNdiLGFDSEGNVv 225
Cdd:COG5256   10 LVVIGHVDHGKSTLVGRLlyETGAIDehiieKYEEEAEKKgkesfkfawvMDRLKEERERGVTIDLAH--KKFETDKYY- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 226 nkpdshggslewtkiceksskvITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VF 304
Cdd:COG5256   87 ----------------------FTIIDAPGHRDFVKNMITGASQ--ADAAILVVSAKDGVMGQTREHAFLARTLGINqLI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 305 VVVTKIDMcpANILQ----ETLKLLQRLLKSPGCR--KIPVLVQS--KDDVIVTASnfssERMcPIFqisnvTG----EN 372
Cdd:COG5256  143 VAVNKMDA--VNYSEkryeEVKEEVSKLLKMVGYKvdKIPFIPVSawKGDNVVKKS----DNM-PWY-----NGptllEA 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 373 LDLLKMflnllSPRTSyreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPdplgNFLSIAVKSIHRKRMPV 452
Cdd:COG5256  211 LDNLKE-----PEKPV---DKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMP----AGVVGEVKSIEMHHEEL 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 453 KEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDK--- 529
Cdd:COG5256  279 EQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSkld 358

                        410       420
                 ....*....|....*....|....*...
gi 283462287 530 -----------DCLRTGDKATVHFRFIK 546
Cdd:COG5256  359 prtgqvkeenpQFLKTGDAAIVKIKPTK 386
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 163-546 2.11e-20

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 94.22  E-value: 2.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 163 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEIESGRTSSVGNdiLGFDSEgnvv 225
Cdd:PRK12317   9 LAVIGHVDHGKSTLVGRLlyETGAIDehiieELREEAKEKgkesfkfawvMDRLKEERERGVTIDLAH--KKFETD---- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 226 nkpdshggslewtkiceksSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSN--AGIVGMTKEHLGLALALNVP- 302
Cdd:PRK12317  83 -------------------KYYFTIVDCPGHRDFVKNMITGASQ--ADAAVLVVAADdaGGVMPQTREHVFLARTLGINq 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 303 VFVVVTKIDMcpANILQ----ETLKLLQRLLKSPGCRK-----IPVLVQSKDDVIVtasnfSSERMcPIFqisnvTG--- 370
Cdd:PRK12317 142 LIVAINKMDA--VNYDEkryeEVKEEVSKLLKMVGYKPddipfIPVSAFEGDNVVK-----KSENM-PWY-----NGptl 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 371 -ENLDLLKMflnllSPRTSyreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGP-DPLGNflsiaVKSIHRK 448
Cdd:PRK12317 209 lEALDNLKP-----PEKPT---DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPaGVVGE-----VKSIEMH 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 449 RMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMD 528
Cdd:PRK12317 276 HEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELV 355

                        410       420       430
                 ....*....|....*....|....*....|..
gi 283462287 529 K--------------DCLRTGDKATVHFRFIK 546
Cdd:PRK12317 356 KkldprtgqvaeenpQFIKTGDAAIVKIKPTK 387
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 156-546 5.74e-18

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 87.11  E-value: 5.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 156 NDFLEVRVAVVGNVDAGKSTLLGVLTH--GELDngrgfarqklfrhKHEIESgrtssvgndilgFDSEGNVVNKpdshgG 233
Cdd:PTZ00141   3 KEKTHINLVVIGHVDSGKSTTTGHLIYkcGGID-------------KRTIEK------------FEKEAAEMGK-----G 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 234 SLEWTKICEK-------------------SSK-VITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIV------- 286
Cdd:PTZ00141  53 SFKYAWVLDKlkaerergitidialwkfeTPKyYFTIIDAPGHRDFIKNMITGTSQ--ADVAILVVASTAGEFeagiskd 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 287 GMTKEHLGLALALNVPVFVV-VTKIDMCPANILQ----ETLKLLQRLLKSPGcrkipvlvqskddvivtasnFSSERMcP 361
Cdd:PTZ00141 131 GQTREHALLAFTLGVKQMIVcINKMDDKTVNYSQerydEIKKEVSAYLKKVG--------------------YNPEKV-P 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 362 IFQISNVTGENL-------------DLLKMFLNLLSPRTSYreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLL 428
Cdd:PTZ00141 190 FIPISGWQGDNMieksdnmpwykgpTLLEALDTLEPPKRPV--DKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVT 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 429 LGPDPlgnfLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNP-QASWEFEAEILVLHHPTTISP 507
Cdd:PTZ00141 268 FAPSG----VTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPaKECADFTAQVIVLNHPGQIKN 343

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 283462287 508 RYQAMVHCGSIR---QTATILS-MDKdclRTGDKATVHFRFIK 546
Cdd:PTZ00141 344 GYTPVLDCHTAHiacKFAEIESkIDR---RSGKVLEENPKAIK 383
PLN03127 PLN03127
Elongation factor Tu; Provisional
 161-575 3.66e-15

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 78.33  E-value: 3.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 161 VRVAVVGNVDAGKSTLLGVLThgeldngrgfarqklfrhKHEIESGRTSSVGNDILGFDSE----GNVVNKpdSHggsLE 236
Cdd:PLN03127  62 VNVGTIGHVDHGKTTLTAAIT------------------KVLAEEGKAKAVAFDEIDKAPEekarGITIAT--AH---VE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 237 WtkicEKSSKVITFIDLAGHEKYLKTTVFG---MTGHLpdfcmLMVGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDM 312
Cdd:PLN03127 119 Y----ETAKRHYAHVDCPGHADYVKNMITGaaqMDGGI-----LVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDV 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 313 CPANILQETLKL-LQRLL---KSPGcRKIPVLVQSKddvivtasnfssermcpifqISNVTGENLDLLK-MFLNLLSPRT 387
Cdd:PLN03127 190 VDDEELLELVEMeLRELLsfyKFPG-DEIPIIRGSA--------------------LSALQGTNDEIGKnAILKLMDAVD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 388 SYREE------EPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGPDPLGNFLSIaVKSIHRKRMPVKEVRGGQT 460
Cdd:PLN03127 249 EYIPEpvrvldKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVeIVGLRPGGPLKTT-VTGVEMFKKILDQGQAGDN 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 461 ASFALKKIKRSSIRKGMVMVSPRlNPQASWEFEAEILVL-------HHPTTISPRYQAMVHCGSIRQTATiLSMDKDCLR 533
Cdd:PLN03127 328 VGLLLRGLKREDVQRGQVICKPG-SIKTYKKFEAEIYVLtkdeggrHTPFFSNYRPQFYLRTADVTGKVE-LPEGVKMVM 405

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 283462287 534 TGDKATVHFRFIkTPEYLHIDQRLVFRE-GRTKAVGTITKLLQ 575
Cdd:PLN03127 406 PGDNVTAVFELI-SPVPLEPGQRFALREgGRTVGAGVVSKVLS 447
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 163-388 6.08e-15

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 73.02  E-value: 6.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 163 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEIESGRTSSvgndiLGFdsegnvvnkpdshggslEWTKIce 242
Cdd:cd04171    2 IGTAGHIDHGKTTLIKALTGIETD-----------RLPEEKKRGITID-----LGF-----------------AYLDL-- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 243 KSSKVITFIDLAGHEKYLKTTVFGMTGHlpDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPanilQET 321
Cdd:cd04171   47 PDGKRLGFIDVPGHEKFVKNMLAGAGGI--DAVLLVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVD----EDR 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 283462287 322 LKLLqrllkspgcrkipvlvqsKDDVIVTASNFSSERMcPIFQISNVTGENLDLLKMFLNLLSPRTS 388
Cdd:cd04171  121 LELV------------------EEEILELLAGTFLADA-PIFPVSSVTGEGIEELKNYLDELAEPQS 168
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 163-476 1.96e-14

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 76.63  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 163 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEIESGRTSSVGNDILgfdsegnvvnkPDSHGgslewtkice 242
Cdd:PRK10512   3 IATAGHVDHGKTTLLQAITGVNAD-----------RLPEEKKRGMTIDLGYAYW-----------PQPDG---------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 243 kssKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLG-LALALNVPVFVVVTKIDMCPANILQET 321
Cdd:PRK10512  51 ---RVLGFIDVPGHEKFLSNMLAGVGG--IDHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 322 LKLLQRLLKSPGCRKIpvlvqskddvivtasnfssermcPIFQISNVTGENLDLLKMFLNLLSPRtsyreEEPAE--FQ- 398
Cdd:PRK10512 126 RRQVKAVLREYGFAEA-----------------------KLFVTAATEGRGIDALREHLLQLPER-----EHAAQhrFRl 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 399 -IDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGPDPlgnflSIAVKSIHRKRMPVKEVRGGQTASFALK-KIKRSSIRK 475
Cdd:PRK10512 178 aIDRAFTVKGAGLVVTGTALSGEVKVGDTLwLTGVNK-----PMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINR 252


                 .
gi 283462287 476 G 476
Cdd:PRK10512 253 G 253
tufA CHL00071
elongation factor Tu
 251-575 1.23e-12

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 69.99  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 251 IDLAGHEKYLKTTVFG---MTGhlpdfCMLMVGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDMCPANILQETLKL-L 325
Cdd:CHL00071  80 VDCPGHADYVKNMITGaaqMDG-----AILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVDDEELLELVELeV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 326 QRLLKS---PGcRKIPvlvqskddvIVTASNFSSerMCPIFQISNVT-GENLDLLKMFlNLLSPRTSY-----RE-EEPA 395
Cdd:CHL00071 155 RELLSKydfPG-DDIP---------IVSGSALLA--LEALTENPKIKrGENKWVDKIY-NLMDAVDSYiptpeRDtDKPF 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 396 EFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGpdpLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIR 474
Cdd:CHL00071 222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVeIVG---LRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 475 KGMVMVSPR-LNPQAswEFEAEILVL-------HHPTTISPRYQAMVH----CGSIRQTATILSMDKDCLRTGDKATVHF 542
Cdd:CHL00071 299 RGMVLAKPGtITPHT--KFEAQVYILtkeeggrHTPFFPGYRPQFYVRttdvTGKIESFTADDGSKTEMVMPGDRIKMTV 376

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 283462287 543 RFIKTpeyLHIDQRLVF--RE-GRTKAVGTITKLLQ 575
Cdd:CHL00071 377 ELIYP---IAIEKGMRFaiREgGRTVGAGVVSKILK 409
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 399-478 2.05e-11

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 60.23  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 399 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLgpDPLGnfLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 478
Cdd:cd03696    5 IDHVFSIKGAGTVVTGTVLSGKVKVGDELEI--PPLG--KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 159-515 2.14e-10

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 63.19  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 159 LEVRVAVVGNVDAGKSTLLGVLTH--GELDNgRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVnkpDSHGGSLE 236
Cdd:PLN00043   6 VHINIVVIGHVDSGKSTTTGHLIYklGGIDK-RVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITI---DIALWKFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 237 WTKIceksskVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMV-----GSNAGIV--GMTKEHLGLALALNVPVFVVV-T 308
Cdd:PLN00043  82 TTKY------YCTVIDAPGHRDFIKNMITGTSQ--ADCAVLIIdsttgGFEAGISkdGQTREHALLAFTLGVKQMICCcN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 309 KIDMCPAN--------ILQETLKLLQRLLKSPGcrKIPvlvqskddvIVTASNFSSERMcpifqISNVTgeNLD------ 374
Cdd:PLN00043 154 KMDATTPKyskarydeIVKEVSSYLKKVGYNPD--KIP---------FVPISGFEGDNM-----IERST--NLDwykgpt 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 375 LLKMFLNLLSPRTSyrEEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPdplgNFLSIAVKSIHRKRMPVKE 454
Cdd:PLN00043 216 LLEALDQINEPKRP--SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGP----TGLTTEVKSVEMHHESLQE 289

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 283462287 455 VRGGQTASFALKKIKRSSIRKGMVMVSPRLNP-QASWEFEAEILVLHHPTTISPRYQAMVHC 515
Cdd:PLN00043 290 ALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPaKEAANFTSQVIIMNHPGQIGNGYAPVLDC 351
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 487-570 4.37e-09

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 54.32  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 487 QASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDK------------DCLRTGDKATVHFRFIK-----TPE 549
Cdd:cd01513    1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSkedgktkekkppDSLQPGENGTVEVELQKpvvleRGK 80

                         90       100
                 ....*....|....*....|..
gi 283462287 550 YLHIDQRLVFRE-GRTKAVGTI 570
Cdd:cd01513   81 EFPTLGRFALRDgGRTVGAGLI 102
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 251-574 9.36e-09

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 57.85  E-value: 9.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 251 IDLAGHEKYLKTTVFG---MTGhlpdfCMLMVGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDMCPANILQE------ 320
Cdd:COG0050   80 VDCPGHADYVKNMITGaaqMDG-----AILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEELLElvemev 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 321 --------------------TLKLLQRLLKSPGCRKIPVLVQSKDDVIVTAsnfssERmcpifqisnvtgenlDLLKMFL 380
Cdd:COG0050  155 rellskygfpgddtpiirgsALKALEGDPDPEWEKKILELMDAVDSYIPEP-----ER---------------DTDKPFL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 381 nllsprtsyreeepaeFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGpdpLGNFLSIAVKSIHRKRMPVKEVRGGQ 459
Cdd:COG0050  215 ----------------MPVEDVFSITGRGTVVTGRVERGIIKVGDEVeIVG---IRDTQKTVVTGVEMFRKLLDEGEAGD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 460 TASFALKKIKRSSIRKGMVMVSPR-LNPQAswEFEAEILVL-------HHPttISPRYQAMVHCGSIRQTATI-LSMDKD 530
Cdd:COG0050  276 NVGLLLRGIKREDVERGQVLAKPGsITPHT--KFEAEVYVLskeeggrHTP--FFNGYRPQFYFRTTDVTGVItLPEGVE 351

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 283462287 531 CLRTGDKATVHFRFIkTPEYLHIDQRLVFREG-RTKAVGTITKLL 574
Cdd:COG0050  352 MVMPGDNVTMTVELI-TPIAMEEGLRFAIREGgRTVGAGVVTKII 395
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 491-573 1.76e-07

C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 49.86  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 491 EFEAEILVL-HHPTTISPRYQAMVHCGSIRQTATILS----MDKD----------CLRTGDKATVHFRFIKT---PEYLH 552
Cdd:cd03704    5 EFEAQIVILdLLKSIITAGYSAVLHIHTAVEEVTITKllatIDKKtgkkkkkkpkFVKSGQVVIARLETARPiclETFKD 84

                         90       100
                 ....*....|....*....|....
gi 283462287 553 IDQ--RLVFR-EGRTKAVGTITKL 573
Cdd:cd03704   85 FPQlgRFTLRdEGKTIAIGKVLKL 108
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 161-330 2.38e-07

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 51.60  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 161 VRVAVVGNVDAGKSTLLGVLTH----GELDngrgfarqklfRHKHEIESGRTSSvgndiLGFDSegNVVNKPDShggsLE 236
Cdd:cd01889    1 VNVGLLGHVDSGKTSLAKALSEiastAAFD-----------KNPQSQERGITLD-----LGFSS--FEVDKPKH----LE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 237 WTKICEKSSKVITFIDLAGHEKYLKTTVFGmtGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPAN 316
Cdd:cd01889   59 DNENPQIENYQITLVDCPGHASLIRTIIGG--AQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEE 136

                        170
                 ....*....|....*
gi 283462287 317 ILQETL-KLLQRLLK 330
Cdd:cd01889  137 ERKRKIeKMKKRLQK 151
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 399-479 4.63e-07

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 47.95  E-value: 4.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 399 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPdplgNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 478
Cdd:cd03693    9 IQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP----AGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGDV 84


                 .
gi 283462287 479 M 479
Cdd:cd03693   85 A 85
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 248-384 9.10e-07

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 49.39  E-value: 9.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 248 ITFIDLAGHEKYLKTTVFGmtGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDmcpanilqetlkllqr 327
Cdd:cd01887   51 ITFIDTPGHEAFTNMRARG--ASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKID---------------- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 328 llKSPGCRKIPVLVQSkddvIVTASNFSSERM---CPIFQISNVTGENLDLLKMFLNLLS 384
Cdd:cd01887  113 --KPYGTEADPERVKN----ELSELGLVGEEWggdVSIVPISAKTGEGIDDLLEAILLLA 166
infB CHL00189
translation initiation factor 2; Provisional
 163-430 4.40e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 49.83  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 163 VAVVGNVDAGKSTLLGVLTHGEldngrgfARQKlfrhkhEIeSGRTSSVGNDILGFDSEGNvvnkpdshggslewtkice 242
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRKTQ-------IAQK------EA-GGITQKIGAYEVEFEYKDE------------------- 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 243 ksSKVITFIDLAGHEKYLKTTVFGMtgHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANIlqetL 322
Cdd:CHL00189 294 --NQKIVFLDTPGHEAFSSMRSRGA--NVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANT----E 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 323 KLLQRLLKspgcrkipvlvqskddvivtaSNFSSERM---CPIFQISNVTGENLD-LLKMFLnLLSPRTSYR--EEEPAE 396
Cdd:CHL00189 366 RIKQQLAK---------------------YNLIPEKWggdTPMIPISASQGTNIDkLLETIL-LLAEIEDLKadPTQLAQ 423

                        250       260       270
                 ....*....|....*....|....*....|....
gi 283462287 397 FQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLG 430
Cdd:CHL00189 424 GIILEAHLDKTKGPVATILVQNGTLHIGDIIVIG 457
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
 246-324 8.39e-06

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 49.00  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  246 KVITFIDLAGHEKYlkTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPAN---ILQETL 322
Cdd:TIGR00487 135 KMITFLDTPGHEAF--TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANpdrVKQELS 212


                  ..
gi 283462287  323 KL 324
Cdd:TIGR00487 213 EY 214
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 397-478 3.15e-05

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 42.64  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 397 FQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGnflsIAVKSIHRKRMPVKEVRGGQTASFALKKIKrsSIRKG 476
Cdd:cd01342    3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGIT----GRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76


                 ..
gi 283462287 477 MV 478
Cdd:cd01342   77 DT 78
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 491-570 4.21e-04

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 40.25  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 491 EFEAEILVLHHPTTISPRYQAM--VHCGSI------------RQTATILSMDKDCLRTGDKATVHFRFIKtP-------E 549
Cdd:cd03705    5 SFTAQVIILNHPGQIKAGYTPVldCHTAHVackfaelkekidRRTGKKLEENPKFLKSGDAAIVKMVPTK-PlcvetfsE 83

                         90       100
                 ....*....|....*....|..
gi 283462287 550 YLHIDqRLVFREGR-TKAVGTI 570
Cdd:cd03705   84 YPPLG-RFAVRDMRqTVAVGVI 104
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 491-573 1.78e-03

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 38.40  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287  491 EFEAEILVLHH-----PTTISPRYQAMVHCGSIRQTATILSMDKDC-----------LRTGDKATVHFRFIKtPEYLHID 554
Cdd:pfam03143   7 KFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLdpggvsenpefVMPGDNVIVTVELIK-PIALEKG 85

                          90       100
                  ....*....|....*....|
gi 283462287  555 QRLVFRE-GRTKAVGTITKL 573
Cdd:pfam03143  86 QRFAIREgGRTVAAGVVTEI 105
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 293-388 1.82e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ 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. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 40.07  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 293 LGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLlkspgcrkipvlvqskddvivtasnfsserMCPIFQISNVTGEN 372
Cdd:cd01854   26 LVAAEASGIEPVIVLNKADLVDDEELEELLEIYEKL------------------------------GYPVLAVSAKTGEG 75

                         90
                 ....*....|....*.
gi 283462287 373 LDLLKmflNLLSPRTS 388
Cdd:cd01854   76 LDELR---ELLKGKTS 88
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 487-573 3.64e-03

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 37.52  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 487 QASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATIL----SMDKD----------CLRTGDKATVHFRFIKT---PE 549
Cdd:cd04093    3 ATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISklvsTLDKStgevikkkprCLGKNQSAVVEIELERPiplET 82

                         90       100
                 ....*....|....*....|....*..
gi 283462287 550 YLHIDQ--RLVFR-EGRTKAVGTITKL 573
Cdd:cd04093   83 FKDNKElgRFVLRrGGETIAAGIVTEI 109
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 293-381 6.48e-03

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: 37.88  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 293 LGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKipvlvqskddvivtasnfssermcPIFQISNVTGEN 372
Cdd:cd01876  103 LEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILP------------------------PVILFSSKKGTG 158


                 ....*....
gi 283462287 373 LDLLKMFLN 381
Cdd:cd01876  159 IDELRALIA 167
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 126-197 8.59e-03

50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 38.91  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283462287 126 QIEAD-------VILLRERQESGGRVRDyLVRKRVGDNDFleVRVAVVG--NvdAGKSTLLGVLTHGELdngrgFARQKL 196
Cdd:COG2262  161 QLETDrrlirdrIARLKRELEKVRKQRE-LQRKRRKRSGI--PTVALVGytN--AGKSTLFNRLTGADV-----LAEDKL 230


                 .
gi 283462287 197 F 197
Cdd:COG2262  231 F 231
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 126-197 9.35e-03

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 37.82  E-value: 9.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 283462287 126 QIEADVILLRER-------QESGGRVRDYLVRKRVGDNDFlevRVAVVGNVDAGKSTLLGVLTHGELdngrgFARQKLF 197
Cdd:cd01878    3 QLETDRRLIRERiaklrkeLEKVKKQRELQRARRKRSGVP---TVALVGYTNAGKSTLFNALTGADV-----LAEDQLF 73
 
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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