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Conserved domains on  [gi|768026532|ref|XP_011528839|]
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GTP-binding protein 1 isoform X2 [Homo sapiens]

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];
77-582 1.01e-159

GTPase [General function prediction only];


The actual alignment was detected with superfamily member COG5258:

Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 471.34  E-value: 1.01e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  77 SLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVillRERQEAGGRVRDYLVRKRVGDn 156
Cdd:COG5258   39 SLAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAKI---EDVETWEVGDGGLVGVVTIRE- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 157 dflevrcmGSSTRR----VAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGnV 232
Cdd:COG5258  115 --------GKEKDPehivVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-P 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 233 VNKPDSHGGSlEWTKICEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVF 312
Cdd:COG5258  186 VRMKNPLRKT-DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVI 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 313 VVVTKIDMCPANILQETLKLLQRLLKSPGcrKIPVLVQSKDDViVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLs 392
Cdd:COG5258  265 VAITKIDKVDDERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERL- 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 393 PRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFA 472
Cdd:COG5258  341 PKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIA 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 473 LKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRF 552
Cdd:COG5258  421 LKGVEEEELERGMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRF 500

                        490       500       510
                 ....*....|....*....|....*....|
gi 768026532 553 IKTPEYLHIDQRLVFREGRTKAVGTITKLL 582
Cdd:COG5258  501 KYRPYYVEEGQRFVFREGRSKGVGTVTDIL 530
 
Name Accession Description Interval E-value
GTPBP1 COG5258
GTPase [General function prediction only];
77-582 1.01e-159

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 471.34  E-value: 1.01e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  77 SLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVillRERQEAGGRVRDYLVRKRVGDn 156
Cdd:COG5258   39 SLAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAKI---EDVETWEVGDGGLVGVVTIRE- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 157 dflevrcmGSSTRR----VAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGnV 232
Cdd:COG5258  115 --------GKEKDPehivVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-P 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 233 VNKPDSHGGSlEWTKICEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVF 312
Cdd:COG5258  186 VRMKNPLRKT-DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVI 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 313 VVVTKIDMCPANILQETLKLLQRLLKSPGcrKIPVLVQSKDDViVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLs 392
Cdd:COG5258  265 VAITKIDKVDDERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERL- 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 393 PRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFA 472
Cdd:COG5258  341 PKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIA 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 473 LKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRF 552
Cdd:COG5258  421 LKGVEEEELERGMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRF 500

                        490       500       510
                 ....*....|....*....|....*....|
gi 768026532 553 IKTPEYLHIDQRLVFREGRTKAVGTITKLL 582
Cdd:COG5258  501 KYRPYYVEEGQRFVFREGRSKGVGTVTDIL 530
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 170-394 8.20e-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: 8.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 170 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEwTKIC 249
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELD-VEIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 250 EKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQET 329
Cdd:cd04165   80 EKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768026532 330 LKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPR 394
Cdd:cd04165  160 LKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNLSSGRVVPIFQVSNVTGEGLDLLRRFLNLLPPR 224
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 171-490 5.68e-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: 5.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  171 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfrHKHEiESGRTSSVGndiLGFDSegnvVNKPDshggslewtkice 250
Cdd:TIGR00475   3 IATAGHVDHGKTTLLKALTGIAAD------------RLPE-EKKRGMTID---LGFAY----FPLPD------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  251 kstKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPANILQET 329
Cdd:TIGR00475  50 ---YRLGFIDVPGHEKFISNAIAGGGG--IDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIKRT 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  330 LKLLQRLLKSPGcrkipVLVQSKddvivtasnfssermcpIFQISNVTGENLDLLKMFL-NLLSPRTSYREEEPAEFQID 408
Cdd:TIGR00475 125 EMFMKQILNSYI-----FLKNAK-----------------IFKTSAKTGQGIGELKKELkNLLESLDIKRIQKPLRMAID 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  409 DTYSVPGVGTVVSGTTLRGLIKLNDTLLLgpDPLGNflSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMV 488
Cdd:TIGR00475 183 RAFKVKGAGTVVTGTAFSGEVKVGDNLRL--LPINH--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLIL 258


                  ..
gi 768026532  489 SP 490
Cdd:TIGR00475 259 TP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 169-393 8.82e-26

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: 104.91  E-value: 8.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  169 RRVAVVGNVDAGKSTLLGVLTH--GELDNG---RGFARQKLFRHKHEIESGRTSSVGNDilgfdsegnvvnkpdshggSL 243
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYytGAISKRgevKGEGEAGLDNLPEERERGITIKSAAV-------------------SF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  244 EWTKicekstKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 323
Cdd:pfam00009  65 ETKD------YLINLIDTPGHVDFVKEVIRGLA--QADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768026532  324 NILQETLKLLQRLLkspgcrkIPVLVQSKDDVivtasnfssermcPIFQISNVTGENLD-LLKMFLNLLSP 393
Cdd:pfam00009 137 AELEEVVEEVSREL-------LEKYGEDGEFV-------------PVVPGSALKGEGVQtLLDALDEYLPS 187
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 171-554 1.31e-20

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 94.99  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 171 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEIESGRTSSVGNdiLGFDSEgnvv 233
Cdd:PRK12317   9 LAVIGHVDHGKSTLVGRLlyETGAIDehiieELREEAKEKgkesfkfawvMDRLKEERERGVTIDLAH--KKFETD---- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 234 nkpdshggslewtkiceksTKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSN--AGIVGMTKEHLGLALALNVP- 310
Cdd:PRK12317  83 -------------------KYYFTIVDCPGHRDFVKNMITGASQ--ADAAVLVVAADdaGGVMPQTREHVFLARTLGINq 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 311 VFVVVTKIDMcpANILQ----ETLKLLQRLLKSPGCRK-----IPVLVQSKDDVIVtasnfSSERMcPIFqisnvTG--- 378
Cdd:PRK12317 142 LIVAINKMDA--VNYDEkryeEVKEEVSKLLKMVGYKPddipfIPVSAFEGDNVVK-----KSENM-PWY-----NGptl 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 379 -ENLDLLKMflnllSPRTSyreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGP-DPLGNflsiaVKSIHRK 456
Cdd:PRK12317 209 lEALDNLKP-----PEKPT---DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPaGVVGE-----VKSIEMH 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 457 RMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMD 536
Cdd:PRK12317 276 HEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELV 355

                        410       420       430
                 ....*....|....*....|....*....|..
gi 768026532 537 K--------------DCLRTGDKATVHFRFIK 554
Cdd:PRK12317 356 KkldprtgqvaeenpQFIKTGDAAIVKIKPTK 387
 
Name Accession Description Interval E-value
GTPBP1 COG5258
GTPase [General function prediction only];
77-582 1.01e-159

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 471.34  E-value: 1.01e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  77 SLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVillRERQEAGGRVRDYLVRKRVGDn 156
Cdd:COG5258   39 SLAAQMKYRLESGDGEATYVIGVTDDGEIAGISPDEFSESMDVLSLLAEEIGAKI---EDVETWEVGDGGLVGVVTIRE- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 157 dflevrcmGSSTRR----VAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGnV 232
Cdd:COG5258  115 --------GKEKDPehivVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSFLDVQPHEVERGLSADLSYAVYGFDDDG-P 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 233 VNKPDSHGGSlEWTKICEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVF 312
Cdd:COG5258  186 VRMKNPLRKT-DRARVVEESDKLVSFVDTVGHEPWLRTTIRGLVGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVI 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 313 VVVTKIDMCPANILQETLKLLQRLLKSPGcrKIPVLVQSKDDViVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLs 392
Cdd:COG5258  265 VAITKIDKVDDERVEEVEREIENLLRIVG--RTPLEVESRHDV-DAAIEEINGRVVPILKTSAVTGEGLDLLDELFERL- 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 393 PRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFA 472
Cdd:COG5258  341 PKRATDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIA 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 473 LKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRF 552
Cdd:COG5258  421 LKGVEEEELERGMVLLPRDADPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEPIDKGYLLPGDSGRVRLRF 500

                        490       500       510
                 ....*....|....*....|....*....|
gi 768026532 553 IKTPEYLHIDQRLVFREGRTKAVGTITKLL 582
Cdd:COG5258  501 KYRPYYVEEGQRFVFREGRSKGVGTVTDIL 530
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 170-394 8.20e-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: 8.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 170 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEwTKIC 249
Cdd:cd04165    1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELD-VEIC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 250 EKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQET 329
Cdd:cd04165   80 EKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768026532 330 LKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPR 394
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 ...
 495-581 6.89e-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: 6.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 495 QASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQRLVFREGRTKA 574
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTKG 80


                 ....*..
gi 768026532 575 VGTITKL 581
Cdd:cd03708   81 IGTVTKV 87
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 170-394 1.30e-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: 163.23  E-value: 1.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 170 RVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQ--KLFRHKHEIESGRTSSVGNDilgfdsegnvvnkpdshggSLEWTK 247
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKetFLDTLKEERERGITIKTGVV-------------------EFEWPK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 248 icekstKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQ 327
Cdd:cd00881   62 ------RRINFIDTPGHEDFSKETVRGLA--QADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFD 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768026532 328 ETLKLLQRLLKSPGCRkipvlvqskddvivtasnFSSERMCPIFQISNVTGEN-LDLLKMFLNLLSPR 394
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 ...
 403-489 8.45e-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: 157.38  E-value: 8.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 403 AEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIR 482
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*..
gi 768026532 483 KGMVMVS 489
Cdd:cd03694   81 KGMVLVS 87
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 254-568 2.55e-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: 2.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 254 KVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIvgM--TKEHLG-LALaLNVPV-FVVVTKIDMCPANILQET 329
Cdd:COG3276   51 RRLGFVDVPGHEKFIKNMLAGAGG--IDLVLLVVAADEGV--MpqTREHLAiLDL-LGIKRgIVVLTKADLVDEEWLELV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 330 LKLLQRLLKSpgcrkipvlvqskddvivtaSNFSSermCPIFQISNVTGENLDLLKMFLNLLSPRTSYREEE-PAEFQID 408
Cdd:COG3276  126 EEEIRELLAG--------------------TFLED---APIVPVSAVTGEGIDELRAALDALAAAVPARDADgPFRLPID 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 409 DTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPlgnfLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMV 488
Cdd:COG3276  183 RVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLA 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 489 SPRLnPQASWEFEAEILVLHH-PTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFiKTPEYLHIDQRLVF 567
Cdd:COG3276  259 APGA-LRPTDRIDVRLRLLPSaPRPLKHWQRVHLHHGTAEVLARVVLLDREELAPGEEALAQLRL-EEPLVAARGDRFIL 336


                 .
gi 768026532 568 R 568
Cdd:COG3276  337 R 337
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 171-490 5.68e-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: 5.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  171 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfrHKHEiESGRTSSVGndiLGFDSegnvVNKPDshggslewtkice 250
Cdd:TIGR00475   3 IATAGHVDHGKTTLLKALTGIAAD------------RLPE-EKKRGMTID---LGFAY----FPLPD------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  251 kstKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPANILQET 329
Cdd:TIGR00475  50 ---YRLGFIDVPGHEKFISNAIAGGGG--IDAALLVVDADEGVMTQTGEHLAVLDLLGIPhTIVVITKADRVNEEEIKRT 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  330 LKLLQRLLKSPGcrkipVLVQSKddvivtasnfssermcpIFQISNVTGENLDLLKMFL-NLLSPRTSYREEEPAEFQID 408
Cdd:TIGR00475 125 EMFMKQILNSYI-----FLKNAK-----------------IFKTSAKTGQGIGELKKELkNLLESLDIKRIQKPLRMAID 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  409 DTYSVPGVGTVVSGTTLRGLIKLNDTLLLgpDPLGNflSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMV 488
Cdd:TIGR00475 183 RAFKVKGAGTVVTGTAFSGEVKVGDNLRL--LPINH--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLIL 258


                  ..
gi 768026532  489 SP 490
Cdd:TIGR00475 259 TP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 169-393 8.82e-26

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: 104.91  E-value: 8.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  169 RRVAVVGNVDAGKSTLLGVLTH--GELDNG---RGFARQKLFRHKHEIESGRTSSVGNDilgfdsegnvvnkpdshggSL 243
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLLYytGAISKRgevKGEGEAGLDNLPEERERGITIKSAAV-------------------SF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  244 EWTKicekstKVITFIDLAGHEKYLKTTVFGMTghLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPA 323
Cdd:pfam00009  65 ETKD------YLINLIDTPGHVDFVKEVIRGLA--QADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768026532  324 NILQETLKLLQRLLkspgcrkIPVLVQSKDDVivtasnfssermcPIFQISNVTGENLD-LLKMFLNLLSP 393
Cdd:pfam00009 137 AELEEVVEEVSREL-------LEKYGEDGEFV-------------PVVPGSALKGEGVQtLLDALDEYLPS 187
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 171-554 3.29e-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: 102.70  E-value: 3.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 171 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEIESGRTSSVGNdiLGFDSEgnvv 233
Cdd:COG5256   10 LVVIGHVDHGKSTLVGRLlyETGAIDehiieKYEEEAEKKgkesfkfawvMDRLKEERERGVTIDLAH--KKFETD---- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 234 nkpdshggslewtkiceksTKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VF 312
Cdd:COG5256   84 -------------------KYYFTIIDAPGHRDFVKNMITGASQ--ADAAILVVSAKDGVMGQTREHAFLARTLGINqLI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 313 VVVTKIDMcpANILQ----ETLKLLQRLLKSPGCR--KIPVLVQS--KDDVIVTASnfssERMcPIFqisnvTG----EN 380
Cdd:COG5256  143 VAVNKMDA--VNYSEkryeEVKEEVSKLLKMVGYKvdKIPFIPVSawKGDNVVKKS----DNM-PWY-----NGptllEA 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 381 LDLLKMflnllSPRTSyreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPdplgNFLSIAVKSIHRKRMPV 460
Cdd:COG5256  211 LDNLKE-----PEKPV---DKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMP----AGVVGEVKSIEMHHEEL 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 461 KEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDK--- 537
Cdd:COG5256  279 EQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSkld 358

                        410       420
                 ....*....|....*....|....*...
gi 768026532 538 -----------DCLRTGDKATVHFRFIK 554
Cdd:COG5256  359 prtgqvkeenpQFLKTGDAAIVKIKPTK 386
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 171-554 1.31e-20

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 94.99  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 171 VAVVGNVDAGKSTLLGVL--THGELD-----NGRGFARQK----------LFRHKHEIESGRTSSVGNdiLGFDSEgnvv 233
Cdd:PRK12317   9 LAVIGHVDHGKSTLVGRLlyETGAIDehiieELREEAKEKgkesfkfawvMDRLKEERERGVTIDLAH--KKFETD---- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 234 nkpdshggslewtkiceksTKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSN--AGIVGMTKEHLGLALALNVP- 310
Cdd:PRK12317  83 -------------------KYYFTIVDCPGHRDFVKNMITGASQ--ADAAVLVVAADdaGGVMPQTREHVFLARTLGINq 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 311 VFVVVTKIDMcpANILQ----ETLKLLQRLLKSPGCRK-----IPVLVQSKDDVIVtasnfSSERMcPIFqisnvTG--- 378
Cdd:PRK12317 142 LIVAINKMDA--VNYDEkryeEVKEEVSKLLKMVGYKPddipfIPVSAFEGDNVVK-----KSENM-PWY-----NGptl 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 379 -ENLDLLKMflnllSPRTSyreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGP-DPLGNflsiaVKSIHRK 456
Cdd:PRK12317 209 lEALDNLKP-----PEKPT---DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPaGVVGE-----VKSIEMH 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 457 RMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMD 536
Cdd:PRK12317 276 HEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELV 355

                        410       420       430
                 ....*....|....*....|....*....|..
gi 768026532 537 K--------------DCLRTGDKATVHFRFIK 554
Cdd:PRK12317 356 KkldprtgqvaeenpQFIKTGDAAIVKIKPTK 387
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 173-554 1.55e-17

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 85.95  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 173 VVGNVDAGKSTLLGVLTH--GELDngrgfarqklfrhKHEIESgrtssvgndilgFDSEGNVVNKpdshgGSLEWTKICE 250
Cdd:PTZ00141  12 VIGHVDSGKSTTTGHLIYkcGGID-------------KRTIEK------------FEKEAAEMGK-----GSFKYAWVLD 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 251 K-------------------STK-VITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIV-------GMTKEHLGL 303
Cdd:PTZ00141  62 KlkaerergitidialwkfeTPKyYFTIIDAPGHRDFIKNMITGTSQ--ADVAILVVASTAGEFeagiskdGQTREHALL 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 304 ALALNVPVFVV-VTKIDMCPANILQ----ETLKLLQRLLKSPGcrkipvlvqskddvivtasnFSSERMcPIFQISNVTG 378
Cdd:PTZ00141 140 AFTLGVKQMIVcINKMDDKTVNYSQerydEIKKEVSAYLKKVG--------------------YNPEKV-PFIPISGWQG 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 379 ENL-------------DLLKMFLNLLSPRTSYreEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPlgnf 445
Cdd:PTZ00141 199 DNMieksdnmpwykgpTLLEALDTLEPPKRPV--DKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSG---- 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 446 LSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNP-QASWEFEAEILVLHHPTTISPRYQAMVHCG 524
Cdd:PTZ00141 273 VTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPaKECADFTAQVIVLNHPGQIKNGYTPVLDCH 352

                        410       420       430
                 ....*....|....*....|....*....|....
gi 768026532 525 SIR---QTATILS-MDKdclRTGDKATVHFRFIK 554
Cdd:PTZ00141 353 TAHiacKFAEIESkIDR---RSGKVLEENPKAIK 383
PLN03127 PLN03127
Elongation factor Tu; Provisional
 162-583 3.30e-16

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 81.79  E-value: 3.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 162 RCMGSSTR-----RVAVVGNVDAGKSTLLGVLThgeldngrgfarqklfrhKHEIESGRTSSVGNDILGFDSE----GNV 232
Cdd:PLN03127  50 RSMATFTRtkphvNVGTIGHVDHGKTTLTAAIT------------------KVLAEEGKAKAVAFDEIDKAPEekarGIT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 233 VNKpdSHggsLEWtkicEKSTKVITFIDLAGHEKYLKTTVFG---MTGHLpdfcmLMVGSNAGIVGMTKEHLGLALALNV 309
Cdd:PLN03127 112 IAT--AH---VEY----ETAKRHYAHVDCPGHADYVKNMITGaaqMDGGI-----LVVSAPDGPMPQTKEHILLARQVGV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 310 PVFVV-VTKIDMCPANILQETLKL-LQRLL---KSPGcRKIPVLVQSKddvivtasnfssermcpifqISNVTGENLDLL 384
Cdd:PLN03127 178 PSLVVfLNKVDVVDDEELLELVEMeLRELLsfyKFPG-DEIPIIRGSA--------------------LSALQGTNDEIG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 385 K-MFLNLLSPRTSYREE------EPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGPDPLGNFLSIaVKSIHRK 456
Cdd:PLN03127 237 KnAILKLMDAVDEYIPEpvrvldKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVeIVGLRPGGPLKTT-VTGVEMF 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 457 RMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRlNPQASWEFEAEILVL-------HHPTTISPRYQAMVHCGSIRQT 529
Cdd:PLN03127 316 KKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPG-SIKTYKKFEAEIYVLtkdeggrHTPFFSNYRPQFYLRTADVTGK 394

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768026532 530 ATiLSMDKDCLRTGDKATVHFRFIkTPEYLHIDQRLVFRE-GRTKAVGTITKLLQ 583
Cdd:PLN03127 395 VE-LPEGVKMVMPGDNVTAVFELI-SPVPLEPGQRFALREgGRTVGAGVVSKVLS 447
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 171-396 4.78e-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: 73.41  E-value: 4.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 171 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEIESGRTSSvgndiLGFdsegnvVNKPDSHGgslewtkice 250
Cdd:cd04171    2 IGTAGHIDHGKTTLIKALTGIETD-----------RLPEEKKRGITID-----LGF------AYLDLPDG---------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 251 kstKVITFIDLAGHEKYLKTTVFGMTGHlpDFCMLMVGSNAGIVGMTKEHLGLALALNVP-VFVVVTKIDMCPanilQET 329
Cdd:cd04171   50 ---KRLGFIDVPGHEKFVKNMLAGAGGI--DAVLLVVAADEGIMPQTREHLEILELLGIKkGLVVLTKADLVD----EDR 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768026532 330 LKLLqrllkspgcrkipvlvqsKDDVIVTASNFSSERMcPIFQISNVTGENLDLLKMFLNLLSPRTS 396
Cdd:cd04171  121 LELV------------------EEEILELLAGTFLADA-PIFPVSSVTGEGIEELKNYLDELAEPQS 168
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 171-484 2.14e-14

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 76.63  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 171 VAVVGNVDAGKSTLLGVLTHGELDngrgfarqklfRHKHEIESGRTSSVGNDILgfdsegnvvnkPDSHGgslewtkice 250
Cdd:PRK10512   3 IATAGHVDHGKTTLLQAITGVNAD-----------RLPEEKKRGMTIDLGYAYW-----------PQPDG---------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 251 kstKVITFIDLAGHEKYLKTTVFGMTGhlPDFCMLMVGSNAGIVGMTKEHLG-LALALNVPVFVVVTKIDMCPANILQET 329
Cdd:PRK10512  51 ---RVLGFIDVPGHEKFLSNMLAGVGG--IDHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 330 LKLLQRLLKSPGCRKIpvlvqskddvivtasnfssermcPIFQISNVTGENLDLLKMFLNLLSPRtsyreEEPAE--FQ- 406
Cdd:PRK10512 126 RRQVKAVLREYGFAEA-----------------------KLFVTAATEGRGIDALREHLLQLPER-----EHAAQhrFRl 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 407 -IDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGPDPlgnflSIAVKSIHRKRMPVKEVRGGQTASFALK-KIKRSSIRK 483
Cdd:PRK10512 178 aIDRAFTVKGAGLVVTGTALSGEVKVGDTLwLTGVNK-----PMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINR 252


                 .
gi 768026532 484 G 484
Cdd:PRK10512 253 G 253
tufA CHL00071
elongation factor Tu
 259-583 7.14e-13

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 71.14  E-value: 7.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 259 IDLAGHEKYLKTTVFG---MTGhlpdfCMLMVGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDMCPANILQETLKL-L 333
Cdd:CHL00071  80 VDCPGHADYVKNMITGaaqMDG-----AILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVDDEELLELVELeV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 334 QRLLKS---PGcRKIPvlvqskddvIVTASNFSSerMCPIFQISNVT-GENLDLLKMFlNLLSPRTSY-----RE-EEPA 403
Cdd:CHL00071 155 RELLSKydfPG-DDIP---------IVSGSALLA--LEALTENPKIKrGENKWVDKIY-NLMDAVDSYiptpeRDtDKPF 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 404 EFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGpdpLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIR 482
Cdd:CHL00071 222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVeIVG---LRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIE 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 483 KGMVMVSPR-LNPQAswEFEAEILVL-------HHPTTISPRYQAMVH----CGSIRQTATILSMDKDCLRTGDKATVHF 550
Cdd:CHL00071 299 RGMVLAKPGtITPHT--KFEAQVYILtkeeggrHTPFFPGYRPQFYVRttdvTGKIESFTADDGSKTEMVMPGDRIKMTV 376

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 768026532 551 RFIKTpeyLHIDQRLVF--RE-GRTKAVGTITKLLQ 583
Cdd:CHL00071 377 ELIYP---IAIEKGMRFaiREgGRTVGAGVVSKILK 409
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 407-486 1.71e-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: 60.62  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 407 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLgpDPLGnfLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 486
Cdd:cd03696    5 IDHVFSIKGAGTVVTGTVLSGKVKVGDELEI--PPLG--KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 257-523 2.57e-10

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 63.19  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 257 TFIDLAGHEKYLKTTVFGMTGhlPDFCMLMV-----GSNAGIV--GMTKEHLGLALALNVPVFVVV-TKIDMCPAN---- 324
Cdd:PLN00043  88 TVIDAPGHRDFIKNMITGTSQ--ADCAVLIIdsttgGFEAGISkdGQTREHALLAFTLGVKQMICCcNKMDATTPKyska 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 325 ----ILQETLKLLQRLLKSPGcrKIPvlvqskddvIVTASNFSSERMcpifqISNVTgeNLD------LLKMFLNLLSPR 394
Cdd:PLN00043 166 rydeIVKEVSSYLKKVGYNPD--KIP---------FVPISGFEGDNM-----IERST--NLDwykgptLLEALDQINEPK 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 395 TSyrEEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPdplgNFLSIAVKSIHRKRMPVKEVRGGQTASFALK 474
Cdd:PLN00043 228 RP--SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGP----TGLTTEVKSVEMHHESLQEALPGDNVGFNVK 301

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768026532 475 KIKRSSIRKGMVMVSPRLNP-QASWEFEAEILVLHHPTTISPRYQAMVHC 523
Cdd:PLN00043 302 NVAVKDLKRGYVASNSKDDPaKEAANFTSQVIIMNHPGQIGNGYAPVLDC 351
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 495-578 3.83e-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: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 495 QASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDK------------DCLRTGDKATVHFRFIK-----TPE 557
Cdd:cd01513    1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSkedgktkekkppDSLQPGENGTVEVELQKpvvleRGK 80

                         90       100
                 ....*....|....*....|..
gi 768026532 558 YLHIDQRLVFRE-GRTKAVGTI 578
Cdd:cd01513   81 EFPTLGRFALRDgGRTVGAGLI 102
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 259-582 7.58e-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: 58.24  E-value: 7.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 259 IDLAGHEKYLKTTVFG---MTGhlpdfCMLMVGSNAGIVGMTKEHLGLALALNVPVFVV-VTKIDMCPANILQE------ 328
Cdd:COG0050   80 VDCPGHADYVKNMITGaaqMDG-----AILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDDEELLElvemev 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 329 --------------------TLKLLQRLLKSPGCRKIPVLVQSKDDVIVTAsnfssERmcpifqisnvtgenlDLLKMFL 388
Cdd:COG0050  155 rellskygfpgddtpiirgsALKALEGDPDPEWEKKILELMDAVDSYIPEP-----ER---------------DTDKPFL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 389 nllsprtsyreeepaeFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTL-LLGpdpLGNFLSIAVKSIHRKRMPVKEVRGGQ 467
Cdd:COG0050  215 ----------------MPVEDVFSITGRGTVVTGRVERGIIKVGDEVeIVG---IRDTQKTVVTGVEMFRKLLDEGEAGD 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 468 TASFALKKIKRSSIRKGMVMVSPR-LNPQAswEFEAEILVL-------HHPttISPRYQAMVHCGSIRQTATI-LSMDKD 538
Cdd:COG0050  276 NVGLLLRGIKREDVERGQVLAKPGsITPHT--KFEAEVYVLskeeggrHTP--FFNGYRPQFYFRTTDVTGVItLPEGVE 351

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 768026532 539 CLRTGDKATVHFRFIkTPEYLHIDQRLVFREG-RTKAVGTITKLL 582
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, ...
 499-581 1.50e-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: 50.25  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 499 EFEAEILVL-HHPTTISPRYQAMVHCGSIRQTATILS----MDKD----------CLRTGDKATVHFRFIKT---PEYLH 560
Cdd:cd03704    5 EFEAQIVILdLLKSIITAGYSAVLHIHTAVEEVTITKllatIDKKtgkkkkkkpkFVKSGQVVIARLETARPiclETFKD 84

                         90       100
                 ....*....|....*....|....
gi 768026532 561 IDQ--RLVFR-EGRTKAVGTITKL 581
Cdd:cd03704   85 FPQlgRFTLRdEGKTIAIGKVLKL 108
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 407-487 4.22e-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: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 407 IDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPdplgNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMV 486
Cdd:cd03693    9 IQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP----AGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGDV 84


                 .
gi 768026532 487 M 487
Cdd:cd03693   85 A 85
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 171-338 5.83e-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: 50.44  E-value: 5.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 171 VAVVGNVDAGKSTLLGVLTH----GELDngrgfarqklfRHKHEIESGRTSSvgndiLGFDSegNVVNKPDShggsLEWT 246
Cdd:cd01889    3 VGLLGHVDSGKTSLAKALSEiastAAFD-----------KNPQSQERGITLD-----LGFSS--FEVDKPKH----LEDN 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 247 KICEKSTKVITFIDLAGHEKYLKTTVFGmtGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANIL 326
Cdd:cd01889   61 ENPQIENYQITLVDCPGHASLIRTIIGG--AQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEER 138

                        170
                 ....*....|...
gi 768026532 327 QETL-KLLQRLLK 338
Cdd:cd01889  139 KRKIeKMKKRLQK 151
infB CHL00189
translation initiation factor 2; Provisional
 165-438 7.47e-07

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 52.53  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 165 GSSTRR---VAVVGNVDAGKSTLLGVLTHGEldngrgfARQKlfrhkhEIeSGRTSSVGNDILGFDSEGNvvnkpdshgg 241
Cdd:CHL00189 238 ENSINRppiVTILGHVDHGKTTLLDKIRKTQ-------IAQK------EA-GGITQKIGAYEVEFEYKDE---------- 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 242 slewtkiceksTKVITFIDLAGHEKYLKTTVFGMtgHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMC 321
Cdd:CHL00189 294 -----------NQKIVFLDTPGHEAFSSMRSRGA--NVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKA 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 322 PANIlqetLKLLQRLLKspgcrkipvlvqskddvivtaSNFSSERM---CPIFQISNVTGENLD-LLKMFLnLLSPRTSY 397
Cdd:CHL00189 361 NANT----ERIKQQLAK---------------------YNLIPEKWggdTPMIPISASQGTNIDkLLETIL-LLAEIEDL 414

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768026532 398 R--EEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLG 438
Cdd:CHL00189 415 KadPTQLAQGIILEAHLDKTKGPVATILVQNGTLHIGDIIVIG 457
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 256-392 7.82e-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: 49.78  E-value: 7.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 256 ITFIDLAGHEKYLKTTVFGmtGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDmcpanilqetlkllqr 335
Cdd:cd01887   51 ITFIDTPGHEAFTNMRARG--ASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKID---------------- 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 336 llKSPGCRKIPVLVQSkddvIVTASNFSSERM---CPIFQISNVTGENLDLLKMFLNLLS 392
Cdd:cd01887  113 --KPYGTEADPERVKN----ELSELGLVGEEWggdVSIVPISAKTGEGIDDLLEAILLLA 166
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
 254-332 7.62e-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: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  254 KVITFIDLAGHEKYlkTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPAN---ILQETL 330
Cdd:TIGR00487 135 KMITFLDTPGHEAF--TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDKPEANpdrVKQELS 212


                  ..
gi 768026532  331 KL 332
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 ...
 405-486 2.45e-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: 43.02  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 405 FQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGnflsIAVKSIHRKRMPVKEVRGGQTASFALKKIKrsSIRKG 484
Cdd:cd01342    3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGIT----GRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76


                 ..
gi 768026532 485 MV 486
Cdd:cd01342   77 DT 78
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 499-578 4.53e-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: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 499 EFEAEILVLHHPTTISPRYQAM--VHCGSI------------RQTATILSMDKDCLRTGDKATVHFRFIKtP-------E 557
Cdd:cd03705    5 SFTAQVIILNHPGQIKAGYTPVldCHTAHVackfaelkekidRRTGKKLEENPKFLKSGDAAIVKMVPTK-PlcvetfsE 83

                         90       100
                 ....*....|....*....|..
gi 768026532 558 YLHIDqRLVFREGR-TKAVGTI 578
Cdd:cd03705   84 YPPLG-RFAVRDMRqTVAVGVI 104
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 499-581 1.44e-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: 38.78  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532  499 EFEAEILVLHH-----PTTISPRYQAMVHCGSIRQTATILSMDKDC-----------LRTGDKATVHFRFIKtPEYLHID 562
Cdd:pfam03143   7 KFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLdpggvsenpefVMPGDNVIVTVELIK-PIALEKG 85

                          90       100
                  ....*....|....*....|
gi 768026532  563 QRLVFRE-GRTKAVGTITKL 581
Cdd:pfam03143  86 QRFAIREgGRTVAAGVVTEI 105
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 301-396 1.93e-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: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 301 LGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLlkspgcrkipvlvqskddvivtasnfsserMCPIFQISNVTGEN 380
Cdd:cd01854   26 LVAAEASGIEPVIVLNKADLVDDEELEELLEIYEKL------------------------------GYPVLAVSAKTGEG 75

                         90
                 ....*....|....*.
gi 768026532 381 LDLLKmflNLLSPRTS 396
Cdd:cd01854   76 LDELR---ELLKGKTS 88
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 495-581 3.49e-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: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 495 QASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATIL----SMDKD----------CLRTGDKATVHFRFIKT---PE 557
Cdd:cd04093    3 ATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISklvsTLDKStgevikkkprCLGKNQSAVVEIELERPiplET 82

                         90       100
                 ....*....|....*....|....*..
gi 768026532 558 YLHIDQ--RLVFR-EGRTKAVGTITKL 581
Cdd:cd04093   83 FKDNKElgRFVLRrGGETIAAGIVTEI 109
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 301-389 6.86e-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: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768026532 301 LGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKipvlvqskddvivtasnfssermcPIFQISNVTGEN 380
Cdd:cd01876  103 LEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILP------------------------PVILFSSKKGTG 158


                 ....*....
gi 768026532 381 LDLLKMFLN 389
Cdd:cd01876  159 IDELRALIA 167
 
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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