NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528474296|ref|XP_005164058|]
View 

GTP-binding protein 1 isoform X2 [Danio rerio]

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GTPBP1 super family cl34959
GTPase [General function prediction only];
77-571 1.97e-156

GTPase [General function prediction only];


The actual alignment was detected with superfamily member COG5258:

Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 460.94  E-value: 1.97e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  77 LLRQLRERMDEGCGETIYVLGVGSDGGDYGLNESDMQASVATVRSMCEQIEADlILLRERTEA--GGQVRDYLIRRRvGE 154
Cdd:COG5258   40 LAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAK-IEDVETWEVgdGGLVGVVTIREG-KE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 155 ADFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEMESGRTSSVGNDILGFDQEGqVVNKPDSHGGSl 234
Cdd:COG5258  118 KDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-PVRMKNPLRKT- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 235 DWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 314
Cdd:COG5258  196 DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 315 NILQETLKLLQKILKSPGcrKIPVLVQNKDDViVTASNFSSERICPIFQISNVTGENMDLLKMFLNLLSSRSSfKDHEPA 394
Cdd:COG5258  276 ERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERLPKRAT-DEDEPF 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 395 EFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPLGAFLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRK 474
Cdd:COG5258  352 LMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELER 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 475 GMVMVSPRLNPQAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTRDCLRTGDKATVHFRFIKTPEYLHTDQ 554
Cdd:COG5258  432 GMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRFKYRPYYVEEGQ 511

                        490
                 ....*....|....*..
gi 528474296 555 RLVFREGRTKAVGTITK 571
Cdd:COG5258  512 RFVFREGRSKGVGTVTD 528
 
Name Accession Description Interval E-value
GTPBP1 COG5258
GTPase [General function prediction only];
77-571 1.97e-156

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 460.94  E-value: 1.97e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  77 LLRQLRERMDEGCGETIYVLGVGSDGGDYGLNESDMQASVATVRSMCEQIEADlILLRERTEA--GGQVRDYLIRRRvGE 154
Cdd:COG5258   40 LAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAK-IEDVETWEVgdGGLVGVVTIREG-KE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 155 ADFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEMESGRTSSVGNDILGFDQEGqVVNKPDSHGGSl 234
Cdd:COG5258  118 KDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-PVRMKNPLRKT- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 235 DWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 314
Cdd:COG5258  196 DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 315 NILQETLKLLQKILKSPGcrKIPVLVQNKDDViVTASNFSSERICPIFQISNVTGENMDLLKMFLNLLSSRSSfKDHEPA 394
Cdd:COG5258  276 ERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERLPKRAT-DEDEPF 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 395 EFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPLGAFLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRK 474
Cdd:COG5258  352 LMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELER 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 475 GMVMVSPRLNPQAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTRDCLRTGDKATVHFRFIKTPEYLHTDQ 554
Cdd:COG5258  432 GMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRFKYRPYYVEEGQ 511

                        490
                 ....*....|....*..
gi 528474296 555 RLVFREGRTKAVGTITK 571
Cdd:COG5258  512 RFVFREGRSKGVGTVTD 528
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 161-385 2.59e-153

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: 441.34  E-value: 2.59e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 161 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEMESGRTSSVGNDILGFDQEGQVVNKPDSHGGSLDwTKIC 240
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELD-VEIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 241 EKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQET 320
Cdd:cd04165   80 EKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528474296 321 LKLLQKILKSPGCRKIPVLVQNKDDVIVTASNFSSERICPIFQISNVTGENMDLLKMFLNLLSSR 385
Cdd:cd04165  160 LKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNLSSGRVVPIFQVSNVTGEGLDLLRRFLNLLPPR 224
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 160-481 9.54e-29

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: 121.13  E-value: 9.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  160 VRVAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEMESGRTSSVGNDILGFDQegqvvnkpdshggsldwtki 239
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAAD-----------RLPEEKKRGMTIDLGFAYFPLPD-------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  240 cekssKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPANILQ 318
Cdd:TIGR00475  50 -----YRLGFIDVPGHEKFISNAIAGGGG--IDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIK 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  319 ETLKLLQKILKSpgcrkipvlvqnkddvivTASNFSSEricpIFQISNVTGENMDLLKMFL-NLLSSRSSFKDHEPAEFQ 397
Cdd:TIGR00475 123 RTEMFMKQILNS------------------YIFLKNAK----IFKTSAKTGQGIGELKKELkNLLESLDIKRIQKPLRMA 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  398 IDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLgpDPLGAflSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 477
Cdd:TIGR00475 181 IDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL--LPINH--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLL 256


                  ....
gi 528474296  478 MVSP 481
Cdd:TIGR00475 257 ILTP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 160-384 1.06e-22

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: 95.67  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  160 VRVAVVGNVDAGKSTLLGVLTH--GELDNG---RGFARQKLFRHKHEMESGRTSSVGNDilgfdqegqvvnkpdshggSL 234
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYytGAISKRgevKGEGEAGLDNLPEERERGITIKSAAV-------------------SF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  235 DWTKicekssKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 314
Cdd:pfam00009  65 ETKD------YLINLIDTPGHVDFVKEVIRGLA--QADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528474296  315 NILQETLKLLQKILkspgcrkIPVLVQNKDDVivtasnfssericPIFQISNVTGENMD-LLKMFLNLLSS 384
Cdd:pfam00009 137 AELEEVVEEVSREL-------LEKYGEDGEFV-------------PVVPGSALKGEGVQtLLDALDEYLPS 187
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 162-545 2.28e-18

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 88.06  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 162 VAVVGNVDAGKSTLLGVL--THGELDngrgfaRQKLFRHKHEMES-GRTS---SVGNDILGFDQEgqvvnkpdsHGGSLD 235
Cdd:PRK12317   9 LAVIGHVDHGKSTLVGRLlyETGAID------EHIIEELREEAKEkGKESfkfAWVMDRLKEERE---------RGVTID 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 236 WT-KICEKSSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSN--AGIVGMTKEHLGLALALNVP-VFVVVTKIDM 311
Cdd:PRK12317  74 LAhKKFETDKYYFTIVDCPGHRDFVKNMITGASQ--ADAAVLVVAADdaGGVMPQTREHVFLARTLGINqLIVAINKMDA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 312 cpANILQ----ETLKLLQKILKSPGcrkipvlvQNKDDVivtasnfssericPIFQISNVTGENmdLLKMFLN------- 380
Cdd:PRK12317 152 --VNYDEkryeEVKEEVSKLLKMVG--------YKPDDI-------------PFIPVSAFEGDN--VVKKSENmpwyngp 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 381 -LLSSRSSFKDHE-----PAEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPdplgAFLSITVKSIHRKRMPVKEV 454
Cdd:PRK12317 207 tLLEALDNLKPPEkptdkPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMP----AGVVGEVKSIEMHHEELPQA 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 455 RGGQTASFALKKIKRSSIRKGMVMVSPRLNPQAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTR------ 528
Cdd:PRK12317 283 EPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKkldprt 362

                        410       420
                 ....*....|....*....|....*
gi 528474296 529 --------DCLRTGDKATVHFRFIK 545
Cdd:PRK12317 363 gqvaeenpQFIKTGDAAIVKIKPTK 387
 
Name Accession Description Interval E-value
GTPBP1 COG5258
GTPase [General function prediction only];
77-571 1.97e-156

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 460.94  E-value: 1.97e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  77 LLRQLRERMDEGCGETIYVLGVGSDGGDYGLNESDMQASVATVRSMCEQIEADlILLRERTEA--GGQVRDYLIRRRvGE 154
Cdd:COG5258   40 LAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAK-IEDVETWEVgdGGLVGVVTIREG-KE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 155 ADFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEMESGRTSSVGNDILGFDQEGqVVNKPDSHGGSl 234
Cdd:COG5258  118 KDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-PVRMKNPLRKT- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 235 DWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 314
Cdd:COG5258  196 DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVAITKIDKVDD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 315 NILQETLKLLQKILKSPGcrKIPVLVQNKDDViVTASNFSSERICPIFQISNVTGENMDLLKMFLNLLSSRSSfKDHEPA 394
Cdd:COG5258  276 ERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERLPKRAT-DEDEPF 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 395 EFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPLGAFLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRK 474
Cdd:COG5258  352 LMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELER 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 475 GMVMVSPRLNPQAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTRDCLRTGDKATVHFRFIKTPEYLHTDQ 554
Cdd:COG5258  432 GMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRFKYRPYYVEEGQ 511

                        490
                 ....*....|....*..
gi 528474296 555 RLVFREGRTKAVGTITK 571
Cdd:COG5258  512 RFVFREGRSKGVGTVTD 528
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 161-385 2.59e-153

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: 441.34  E-value: 2.59e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 161 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEMESGRTSSVGNDILGFDQEGQVVNKPDSHGGSLDwTKIC 240
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELD-VEIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 241 EKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQET 320
Cdd:cd04165   80 EKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528474296 321 LKLLQKILKSPGCRKIPVLVQNKDDVIVTASNFSSERICPIFQISNVTGENMDLLKMFLNLLSSR 385
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 ...
 486-571 1.15e-51

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: 172.70  E-value: 1.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 486 QAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTRDCLRTGDKATVHFRFIKTPEYLHTDQRLVFREGRTKA 565
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTKG 80


                 ....*.
gi 528474296 566 VGTITK 571
Cdd:cd03708   81 IGTVTK 86
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 394-480 8.72e-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: 8.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 394 AEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPLGAFLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIR 473
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*..
gi 528474296 474 KGMVMVS 480
Cdd:cd03694   81 KGMVLVS 87
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 161-385 3.81e-45

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: 158.61  E-value: 3.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 161 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQ--KLFRHKHEMESGRTSSVGNDilgfdqegqvvnkpdshggSLDWTK 238
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKetFLDTLKEERERGITIKTGVV-------------------EFEWPK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 239 icekssKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQ 318
Cdd:cd00881   62 ------RRINFIDTPGHEDFSKETVRGLA--QADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFD 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528474296 319 ETLKLLQKILKSPGCRkipvlvqnkddvivtasnFSSERICPIFQISNVTGENMD-LLKMFLNLLSSR 385
Cdd:cd00881  134 EVLREIKELLKLIGFT------------------FLKGKDVPIIPISALTGEGIEeLLDAIVEHLPPP 183
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 243-559 5.99e-29

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: 122.33  E-value: 5.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 243 SSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIvgM--TKEHLGLALALNVPV-FVVVTKIDMCPAnilqE 319
Cdd:COG3276   49 DGRRLGFVDVPGHEKFIKNMLAGAGG--IDLVLLVVAADEGV--MpqTREHLAILDLLGIKRgIVVLTKADLVDE----E 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 320 TLKLLqkilkspgcrkipvlvqnKDDV--IVTASNFsseRICPIFQISNVTGENMDLLKMFLNLLSSRSSFKDHE-PAEF 396
Cdd:COG3276  121 WLELV------------------EEEIreLLAGTFL---EDAPIVPVSAVTGEGIDELRAALDALAAAVPARDADgPFRL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 397 QIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPlgafLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGM 476
Cdd:COG3276  180 PIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGD 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 477 VMVSPRLNPQAYWeFEAEILVLHH-PTTISPRYQAMVHCGSIRQTATILSMTRDCLRTGDKATVHFRFiKTPEYLHTDQR 555
Cdd:COG3276  256 VLAAPGALRPTDR-IDVRLRLLPSaPRPLKHWQRVHLHHGTAEVLARVVLLDREELAPGEEALAQLRL-EEPLVAARGDR 333


                 ....
gi 528474296 556 LVFR 559
Cdd:COG3276  334 FILR 337
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 160-481 9.54e-29

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: 121.13  E-value: 9.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  160 VRVAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEMESGRTSSVGNDILGFDQegqvvnkpdshggsldwtki 239
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAAD-----------RLPEEKKRGMTIDLGFAYFPLPD-------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  240 cekssKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPANILQ 318
Cdd:TIGR00475  50 -----YRLGFIDVPGHEKFISNAIAGGGG--IDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIK 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  319 ETLKLLQKILKSpgcrkipvlvqnkddvivTASNFSSEricpIFQISNVTGENMDLLKMFL-NLLSSRSSFKDHEPAEFQ 397
Cdd:TIGR00475 123 RTEMFMKQILNS------------------YIFLKNAK----IFKTSAKTGQGIGELKKELkNLLESLDIKRIQKPLRMA 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  398 IDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLgpDPLGAflSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 477
Cdd:TIGR00475 181 IDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL--LPINH--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLL 256


                  ....
gi 528474296  478 MVSP 481
Cdd:TIGR00475 257 ILTP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 160-384 1.06e-22

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: 95.67  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  160 VRVAVVGNVDAGKSTLLGVLTH--GELDNG---RGFARQKLFRHKHEMESGRTSSVGNDilgfdqegqvvnkpdshggSL 234
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYytGAISKRgevKGEGEAGLDNLPEERERGITIKSAAV-------------------SF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  235 DWTKicekssKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 314
Cdd:pfam00009  65 ETKD------YLINLIDTPGHVDFVKEVIRGLA--QADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528474296  315 NILQETLKLLQKILkspgcrkIPVLVQNKDDVivtasnfssericPIFQISNVTGENMD-LLKMFLNLLSS 384
Cdd:pfam00009 137 AELEEVVEEVSREL-------LEKYGEDGEFV-------------PVVPGSALKGEGVQtLLDALDEYLPS 187
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 162-545 4.30e-21

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: 96.16  E-value: 4.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 162 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEMESGRTSSVgndilgfdqegqvv 224
Cdd:COG5256   10 LVVIGHVDHGKSTLVGRLlyETGAIDehiieKYEEEAEKKgkesfkfawvMDRLKEERERGVTIDL-------------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 225 nkpdSHggsldwtKICEKSSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIVGMTKEHLGLALALNVP-VF 303
Cdd:COG5256   76 ----AH-------KKFETDKYYFTIIDAPGHRDFVKNMITGASQ--ADAAILVVSAKDGVMGQTREHAFLARTLGINqLI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 304 VVVTKIDMcpANILQ----ETLKLLQKILKSPGCR--KIPVlvqnkddviVTASNFSSEricpifqisNVT--GENMDLL 375
Cdd:COG5256  143 VAVNKMDA--VNYSEkryeEVKEEVSKLLKMVGYKvdKIPF---------IPVSAWKGD---------NVVkkSDNMPWY 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 376 KMfLNLLSSRSSFKDHE-----PAEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPdplgAFLSITVKSIHRKRMP 450
Cdd:COG5256  203 NG-PTLLEALDNLKEPEkpvdkPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMP----AGVVGEVKSIEMHHEE 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 451 VKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTR-- 528
Cdd:COG5256  278 LEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSkl 357

                        410       420
                 ....*....|....*....|....*....
gi 528474296 529 ------------DCLRTGDKATVHFRFIK 545
Cdd:COG5256  358 dprtgqvkeenpQFLKTGDAAIVKIKPTK 386
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 162-545 2.28e-18

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 88.06  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 162 VAVVGNVDAGKSTLLGVL--THGELDngrgfaRQKLFRHKHEMES-GRTS---SVGNDILGFDQEgqvvnkpdsHGGSLD 235
Cdd:PRK12317   9 LAVIGHVDHGKSTLVGRLlyETGAID------EHIIEELREEAKEkGKESfkfAWVMDRLKEERE---------RGVTID 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 236 WT-KICEKSSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSN--AGIVGMTKEHLGLALALNVP-VFVVVTKIDM 311
Cdd:PRK12317  74 LAhKKFETDKYYFTIVDCPGHRDFVKNMITGASQ--ADAAVLVVAADdaGGVMPQTREHVFLARTLGINqLIVAINKMDA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 312 cpANILQ----ETLKLLQKILKSPGcrkipvlvQNKDDVivtasnfssericPIFQISNVTGENmdLLKMFLN------- 380
Cdd:PRK12317 152 --VNYDEkryeEVKEEVSKLLKMVG--------YKPDDI-------------PFIPVSAFEGDN--VVKKSENmpwyngp 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 381 -LLSSRSSFKDHE-----PAEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPdplgAFLSITVKSIHRKRMPVKEV 454
Cdd:PRK12317 207 tLLEALDNLKPPEkptdkPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMP----AGVVGEVKSIEMHHEELPQA 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 455 RGGQTASFALKKIKRSSIRKGMVMVSPRLNPQAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTR------ 528
Cdd:PRK12317 283 EPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKkldprt 362

                        410       420
                 ....*....|....*....|....*
gi 528474296 529 --------DCLRTGDKATVHFRFIK 545
Cdd:PRK12317 363 gqvaeenpQFIKTGDAAIVKIKPTK 387
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 160-539 2.11e-16

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 82.10  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 160 VRVAVVGNVDAGKSTLLGVLTH--GELDngrgfarqKLFRHKHEMESgrtSSVGN---------DILGFDQEgqvvnkpd 228
Cdd:PTZ00141   8 INLVVIGHVDSGKSTTTGHLIYkcGGID--------KRTIEKFEKEA---AEMGKgsfkyawvlDKLKAERE-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 229 sHGGSLD---WTkiCEKSSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIV-------GMTKEHLGLALAL 298
Cdd:PTZ00141  69 -RGITIDialWK--FETPKYYFTIIDAPGHRDFIKNMITGTSQ--ADVAILVVASTAGEFeagiskdGQTREHALLAFTL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 299 NVPVFVV-VTKIDMCPANILQ----ETLKLLQKILKSPGcrkipvlvQNKDDVivtasnfssericPIFQISNVTGENM- 372
Cdd:PTZ00141 144 GVKQMIVcINKMDDKTVNYSQerydEIKKEVSAYLKKVG--------YNPEKV-------------PFIPISGWQGDNMi 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 373 ---DLL-----KMFLNLLSSRSSFKDH--EPAEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPlgafLSITVK 442
Cdd:PTZ00141 203 eksDNMpwykgPTLLEALDTLEPPKRPvdKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSG----VTTEVK 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 443 SIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNP-QAYWEFEAEILVLHHPTTISPRYQAMVHCGSI---- 517
Cdd:PTZ00141 279 SVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPaKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAhiac 358

                        410       420       430
                 ....*....|....*....|....*....|..
gi 528474296 518 ----------RQTATILSMTRDCLRTGDKATV 539
Cdd:PTZ00141 359 kfaeieskidRRSGKVLEENPKAIKSGDAAIV 390
PLN03127 PLN03127
Elongation factor Tu; Provisional
 160-574 4.78e-15

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 77.94  E-value: 4.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 160 VRVAVVGNVDAGKSTLLGVLThgeldngrgfarqklfrhKHEMESGRTSSVGNDilgfdqegQVVNKPD--SHGGSLDWT 237
Cdd:PLN03127  62 VNVGTIGHVDHGKTTLTAAIT------------------KVLAEEGKAKAVAFD--------EIDKAPEekARGITIATA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 238 KI-CEKSSKVITFIDLAGHEKYLKTTVFG---MTGHLpdfcmLMIGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDMC 312
Cdd:PLN03127 116 HVeYETAKRHYAHVDCPGHADYVKNMITGaaqMDGGI-----LVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 313 PANILQETLKL-LQKIL---KSPGcRKIPVL-------VQNKDDVIVTASnfssericpIFQISNVTGENMDLLKMFLNl 381
Cdd:PLN03127 191 DDEELLELVEMeLRELLsfyKFPG-DEIPIIrgsalsaLQGTNDEIGKNA---------ILKLMDAVDEYIPEPVRVLD- 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 382 lssrssfkdhEPAEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTL-LLGPDPLGAfLSITVKSIHRKRMPVKEVRGGQTA 460
Cdd:PLN03127 260 ----------KPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVeIVGLRPGGP-LKTTVTGVEMFKKILDQGQAGDNV 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 461 SFALKKIKRSSIRKGMVMVSPRlNPQAYWEFEAEILVL-------HHPTTISPRYQAMVHCGSIRQTATILSMTrDCLRT 533
Cdd:PLN03127 329 GLLLRGLKREDVQRGQVICKPG-SIKTYKKFEAEIYVLtkdeggrHTPFFSNYRPQFYLRTADVTGKVELPEGV-KMVMP 406

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 528474296 534 GDKATVHFRFIkTPEYLHTDQRLVFRE-GRTKAVGTITKMQS 574
Cdd:PLN03127 407 GDNVTAVFELI-SPVPLEPGQRFALREgGRTVGAGVVSKVLS 447
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 162-475 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 528474296 162 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEMESGRTSSVGNDILgfdqegqvvnkPDSHGgsldwtkice 241
Cdd:PRK10512   3 IATAGHVDHGKTTLLQAITGVNAD-----------RLPEEKKRGMTIDLGYAYW-----------PQPDG---------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 242 kssKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIVGMTKEHLG-LALALNVPVFVVVTKIDMCPANILQET 320
Cdd:PRK10512  51 ---RVLGFIDVPGHEKFLSNMLAGVGG--IDHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 321 LKLLQKILKSPGcrkipvlvqnkddvivtasnFSserICPIFQISNVTGENMDLLKMFLNLLSSRSSFKDHepaEFQ--I 398
Cdd:PRK10512 126 RRQVKAVLREYG--------------------FA---EAKLFVTAATEGRGIDALREHLLQLPEREHAAQH---RFRlaI 179

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528474296 399 DDTYSVPGVGTVVSGTTLRGLIRLNDTLLLgpdpLGAFLSITVKSIHRKRMPVKEVRGGQTASFALK-KIKRSSIRKG 475
Cdd:PRK10512 180 DRAFTVKGAGLVVTGTALSGEVKVGDTLWL----TGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINRG 253
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 162-389 3.14e-14

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: 71.10  E-value: 3.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 162 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEMESGRTSSvgndiLGFdqegqvvnkpdshgGSLDWtkice 241
Cdd:cd04171    2 IGTAGHIDHGKTTLIKALTGIETD-----------RLPEEKKRGITID-----LGF--------------AYLDL----- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 242 KSSKVITFIDLAGHEKYLKTTVFGMTGHlpDFCMLMIGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPanilQET 320
Cdd:cd04171   47 PDGKRLGFIDVPGHEKFVKNMLAGAGGI--DAVLLVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVD----EDR 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528474296 321 LKLLqkilkspgcrkipvlvqnKDDVIVTASNfSSERICPIFQISNVTGENMDLLKMFLNLLSSRSSFK 389
Cdd:cd04171  121 LELV------------------EEEILELLAG-TFLADAPIFPVSSVTGEGIEELKNYLDELAEPQSKD 170
tufA CHL00071
elongation factor Tu
 250-571 6.99e-11

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 64.59  E-value: 6.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 250 IDLAGHEKYLKTTVFG---MTGhlpdfCMLMIGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDMCPANILQETLKL-L 324
Cdd:CHL00071  80 VDCPGHADYVKNMITGaaqMDG-----AILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVDDEELLELVELeV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 325 QKILKS---PGcRKIPV-----------LVQNKDdvIVTASNfssERICPIFQISNVTGENM-----DLLKMFLnllssr 385
Cdd:CHL00071 155 RELLSKydfPG-DDIPIvsgsallaleaLTENPK--IKRGEN---KWVDKIYNLMDAVDSYIptperDTDKPFL------ 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 386 ssfkdhepaeFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTL-LLGpdpLGAFLSITVKSIHRKRMPVKEVRGGQTASFAL 464
Cdd:CHL00071 223 ----------MAIEDVFSITGRGTVATGRIERGTVKVGDTVeIVG---LRETKTTTVTGLEMFQKTLDEGLAGDNVGILL 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 465 KKIKRSSIRKGMVMVSPR-LNPqaYWEFEAEILVL-------HHPTTISPRYQAMVHCGSIrqTATILSMTRD------C 530
Cdd:CHL00071 290 RGIQKEDIERGMVLAKPGtITP--HTKFEAQVYILtkeeggrHTPFFPGYRPQFYVRTTDV--TGKIESFTADdgskteM 365

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 528474296 531 LRTGDKATVHFRFIKtPEYLHTDQRLVFRE-GRTKAVGTITK 571
Cdd:CHL00071 366 VMPGDRIKMTVELIY-PIAIEKGMRFAIREgGRTVGAGVVSK 406
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 398-477 1.21e-10

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: 57.92  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 398 IDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLgpDPLGafLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 477
Cdd:cd03696    5 IDHVFSIKGAGTVVTGTVLSGKVKVGDELEI--PPLG--KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 158-514 8.37e-10

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 61.26  E-value: 8.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 158 LEVRVAVVGNVDAGKSTLLGVLTHgeldNGRGFARQKLFRHKHEMESGRTSSVgndilgfdQEGQVVNKPDSH---GGSL 234
Cdd:PLN00043   6 VHINIVVIGHVDSGKSTTTGHLIY----KLGGIDKRVIERFEKEAAEMNKRSF--------KYAWVLDKLKAErerGITI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 235 D---WTkiCEKSSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMI-----GSNAGIV--GMTKEHLGLALALNVPVFV 304
Cdd:PLN00043  74 DialWK--FETTKYYCTVIDAPGHRDFIKNMITGTSQ--ADCAVLIIdsttgGFEAGISkdGQTREHALLAFTLGVKQMI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 305 VV-TKIDMCPAN--------ILQETLKLLQKILKSPGcrKIPvlvqnkddvIVTASNFSSERIcpIFQISNVTGENMDLL 375
Cdd:PLN00043 150 CCcNKMDATTPKyskarydeIVKEVSSYLKKVGYNPD--KIP---------FVPISGFEGDNM--IERSTNLDWYKGPTL 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 376 KMFLNLLSSRSSFKDhEPAEFQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPdplgAFLSITVKSIHRKRMPVKEVR 455
Cdd:PLN00043 217 LEALDQINEPKRPSD-KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGP----TGLTTEVKSVEMHHESLQEAL 291

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 456 GGQTASFALKKIKRSSIRKGMVMVSPRLNP-QAYWEFEAEILVLHHPTTISPRYQAMVHC 514
Cdd:PLN00043 292 PGDNVGFNVKNVAVKDLKRGYVASNSKDDPaKEAANFTSQVIIMNHPGQIGNGYAPVLDC 351
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 486-569 2.56e-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: 54.71  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 486 QAYWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMTR------------DCLRTGDKATVHFRFIK-----TPE 548
Cdd:cd01513    1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSkedgktkekkppDSLQPGENGTVEVELQKpvvleRGK 80

                         90       100
                 ....*....|....*....|..
gi 528474296 549 YLHTDQRLVFRE-GRTKAVGTI 569
Cdd:cd01513   81 EFPTLGRFALRDgGRTVGAGLI 102
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 398-571 1.79e-07

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: 54.00  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 398 IDDTYSVPGVGTVVSGTTLRGLIRLNDTL-LLGpdpLGAFLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGM 476
Cdd:COG0050  217 VEDVFSITGRGTVVTGRVERGIIKVGDEVeIVG---IRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 477 VMVSPR-LNPqaYWEFEAEILVL-------HHPttISPRYQAMVHCGSIRQTATI-LSMTRDCLRTGDKATVHFRFIkTP 547
Cdd:COG0050  294 VLAKPGsITP--HTKFEAEVYVLskeeggrHTP--FFNGYRPQFYFRTTDVTGVItLPEGVEMVMPGDNVTMTVELI-TP 368

                        170       180
                 ....*....|....*....|....*
gi 528474296 548 EYLHTDQRLVFREG-RTKAVGTITK 571
Cdd:COG0050  369 IAMEEGLRFAIREGgRTVGAGVVTK 393
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 162-385 2.31e-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: 50.93  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 162 VAVVGNVDAGKSTLLGVLthgeldngRGFARQklfrhkhEMESGR-TSSVGndilGFdqegqVVNKPDSHGGsldwtkic 240
Cdd:cd01887    3 VTVMGHVDHGKTTLLDKI--------RKTNVA-------AGEAGGiTQHIG----AY-----QVPIDVKIPG-------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 241 eksskvITFIDLAGHEKYLKTTVFGmtGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDmcpanilqet 320
Cdd:cd01887   51 ------ITFIDTPGHEAFTNMRARG--ASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKID---------- 112

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528474296 321 lkllqkilKSPGCRKIPVLVQNkddvIVTASNFSSE---RICPIFQISNVTGENMDLLKMFLNLLSSR 385
Cdd:cd01887  113 --------KPYGTEADPERVKN----ELSELGLVGEewgGDVSIVPISAKTGEGIDDLLEAILLLAEV 168
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 160-330 3.08e-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: 51.21  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 160 VRVAVVGNVDAGKSTLLGVLTH----GELDngrgfarqklfRHKHEMESGRTSSvgndiLGFdqEGQVVNKPDSHGGSLD 235
Cdd:cd01889    1 VNVGLLGHVDSGKTSLAKALSEiastAAFD-----------KNPQSQERGITLD-----LGF--SSFEVDKPKHLEDNEN 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 236 wtkiCEKSSKVITFIDLAGHEKYLKTTVFGmtGHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPAN 315
Cdd:cd01889   63 ----PQIENYQITLVDCPGHASLIRTIIGG--AQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEE 136

                        170
                 ....*....|....*
gi 528474296 316 ILQETLKLLQKILKS 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 ...
 398-478 3.60e-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: 48.34  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 398 IDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPdplgAFLSITVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 477
Cdd:cd03693    9 IQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP----AGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGDV 84


                 .
gi 528474296 478 M 478
Cdd:cd03693   85 A 85
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
 118-323 4.66e-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: 49.77  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  118 TVRSMCEQIEADLILLR--ERTEAGGQVRDYLirrrvgeaDFLEVRVAVV---GNVDAGKSTLLGVL-----THGELdng 187
Cdd:TIGR00487  49 TAELVAEEFGVKVEVRVtlEETEAEEQDEDSG--------DLLVERPPVVtimGHVDHGKTSLLDSIrktkvAQGEA--- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  188 rGFARQKLFRHKHEMESGrtssvgndilgfdqegqvvnkpdshggsldwtkicekssKVITFIDLAGHEKYlkTTVFGMT 267
Cdd:TIGR00487 118 -GGITQHIGAYHVENEDG---------------------------------------KMITFLDTPGHEAF--TSMRARG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528474296  268 GHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPAN---ILQETLKL 323
Cdd:TIGR00487 156 AKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANpdrVKQELSEY 214
infB CHL00189
translation initiation factor 2; Provisional
 243-429 1.25e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 48.29  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 243 SSKVITFIDLAGHEKYLKTTVFGMtgHLPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANI--LQET 320
Cdd:CHL00189 293 ENQKIVFLDTPGHEAFSSMRSRGA--NVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTerIKQQ 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 321 LkllqkilkspgcrkipvlvqnkddvivTASNFSSERI---CPIFQISNVTGENMDLLkmfLNLLSSRSSFKDhepaeFQ 397
Cdd:CHL00189 371 L---------------------------AKYNLIPEKWggdTPMIPISASQGTNIDKL---LETILLLAEIED-----LK 415

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528474296 398 IDDTYSVPGV----------GTVVSGTTLRGLIRLNDTLLLG 429
Cdd:CHL00189 416 ADPTQLAQGIileahldktkGPVATILVQNGTLHIGDIIVIG 457
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 490-571 3.20e-05

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: 43.31  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 490 EFEAEILVL-HHPTTISPRYQAMVHCGSIRQTATILSM-------TRD-------CLRTGDKATVHFRFIKT---PEYLH 551
Cdd:cd03704    5 EFEAQIVILdLLKSIITAGYSAVLHIHTAVEEVTITKLlatidkkTGKkkkkkpkFVKSGQVVIARLETARPiclETFKD 84

                         90       100
                 ....*....|....*....|...
gi 528474296 552 TDQ--RLVFR-EGRTKAVGTITK 571
Cdd:cd03704   85 FPQlgRFTLRdEGKTIAIGKVLK 107
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 396-477 8.00e-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: 41.48  E-value: 8.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 396 FQIDDTYSVPGVGTVVSGTTLRGLIRLNDTLLLGPDPLGAflsiTVKSIHRKRMPVKEVRGGQTASFALKKIKrsSIRKG 475
Cdd:cd01342    3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITG----RVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76


                 ..
gi 528474296 476 MV 477
Cdd:cd01342   77 DT 78
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 490-569 1.69e-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: 41.02  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 490 EFEAEILVLHHPTTISPRYQAM--VHCGSI------------RQTATILSMTRDCLRTGDKATVHFRFIKtPEYLHTDQ- 554
Cdd:cd03705    5 SFTAQVIILNHPGQIKAGYTPVldCHTAHVackfaelkekidRRTGKKLEENPKFLKSGDAAIVKMVPTK-PLCVETFSe 83

                         90       100
                 ....*....|....*....|.
gi 528474296 555 -----RLVFREGR-TKAVGTI 569
Cdd:cd03705   84 ypplgRFAVRDMRqTVAVGVI 104
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 162-331 1.31e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 41.04  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 162 VAVVGNVDAGKSTLLGVLthgeldngrgfarqkLFRhkhemeSGRTS---SV--GNDILGFDQEGQvvnkpdSHGGSLDW 236
Cdd:cd04170    2 IALVGHSGSGKTTLAEAL---------------LYA------TGAIDrlgRVedGNTVSDYDPEEK------KRKMSIET 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 237 TKI-CEKSSKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPAN 315
Cdd:cd04170   55 SVApLEWNGHKINLIDTPGYADFVGETLSALRA--VDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARAD 132

                        170
                 ....*....|....*.
gi 528474296 316 iLQETLKLLQKILKSP 331
Cdd:cd04170  133 -FDKTLAALREAFGRP 147
PRK00049 PRK00049
elongation factor Tu; Reviewed
 398-498 1.47e-03

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 41.33  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 398 IDDTYSVPGVGTVVSGTTLRGLIRLNDTL-LLGpdplgafLSITVKSI------HRKRMpvKEVRGGQTASFALKKIKRS 470
Cdd:PRK00049 217 IEDVFSISGRGTVVTGRVERGIIKVGEEVeIVG-------IRDTQKTTvtgvemFRKLL--DEGQAGDNVGALLRGIKRE 287

                         90       100
                 ....*....|....*....|....*....
gi 528474296 471 SIRKGMVMVSP-RLNPqaYWEFEAEILVL 498
Cdd:PRK00049 288 DVERGQVLAKPgSITP--HTKFEAEVYVL 314
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 490-571 1.75e-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: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296  490 EFEAEILVLHH-----PTTISPRYQAMVHCGSIRQTATILSMTRDC-----------LRTGDKATVHFRFIKtPEYLHTD 553
Cdd:pfam03143   7 KFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLdpggvsenpefVMPGDNVIVTVELIK-PIALEKG 85

                          90
                  ....*....|....*....
gi 528474296  554 QRLVFRE-GRTKAVGTITK 571
Cdd:pfam03143  86 QRFAIREgGRTVAAGVVTE 104
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 276-380 3.80e-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: 38.65  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528474296 276 LMIGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQETLKLLQKILKSPGCRKipvlvqnkddvivtasnfss 355
Cdd:cd01876   87 LLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILP-------------------- 146

                         90       100
                 ....*....|....*....|....*
gi 528474296 356 ericPIFQISNVTGENMDLLKMFLN 380
Cdd:cd01876  147 ----PVILFSSKKGTGIDELRALIA 167
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 125-196 6.41e-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: 38.59  E-value: 6.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528474296 125 QIEADLILLRERT-------EAGGQVRDYLIRRRVGEADFlevRVAVVGNVDAGKSTLLGVLTHGELdngrgFARQKLF 196
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH