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Conserved domains on  [gi|1957425414|gb|QQQ16476|]
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translation elongation factor 1-alpha, partial [Paramonodictys solitarius]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-316 0e+00

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 605.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSESRFEEIIKETSSFIKKVGYNPKHVPF 78
Cdd:PTZ00141  111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  79 VPISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGT 158
Cdd:PTZ00141  191 IPISGWQGDNMIEKSDNMPWYKG-----------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGI 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 159 IKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAESFNAQVIVLNHPG 238
Cdd:PTZ00141  260 LKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPG 339

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 239 QVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:PTZ00141  340 QIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-316 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 605.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSESRFEEIIKETSSFIKKVGYNPKHVPF 78
Cdd:PTZ00141  111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  79 VPISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGT 158
Cdd:PTZ00141  191 IPISGWQGDNMIEKSDNMPWYKG-----------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGI 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 159 IKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAESFNAQVIVLNHPG 238
Cdd:PTZ00141  260 LKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPG 339

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 239 QVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:PTZ00141  340 QIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-316 1.16e-173

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 487.83  E-value: 1.16e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEagisKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHVPFVP 80
Cdd:TIGR00483 111 AAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIP 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  81 ISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIK 160
Cdd:TIGR00483 187 ISAWNGDNVIKKSENTPWYKG-----------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLK 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 161 AGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAESFNAQVIVLNHPGQV 240
Cdd:TIGR00483 256 PGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAI 334

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957425414 241 GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:TIGR00483 335 TVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDM 410
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-316 1.69e-161

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: 456.70  E-value: 1.69e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEfeagiskDGQTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHVPFVP 80
Cdd:COG5256   111 AAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIP 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  81 ISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIK 160
Cdd:COG5256   184 VSAWKGDNVVKKSDNMPWYNG-----------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLK 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 161 AGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAESFNAQVIVLNHPGQV 240
Cdd:COG5256   253 VGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAI 331

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957425414 241 GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:COG5256   332 TVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDM 407
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-125 2.57e-66

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 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 subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 207.34  E-value: 2.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSESRFEEIIKETSSFIKKVGYNPKHVPF 78
Cdd:cd01883   103 VAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPF 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1957425414  79 VPISGFNGDNMIEVSTNAPWYKGWqketkakvtgkTLLEAIDAIDPP 125
Cdd:cd01883   183 IPISGFTGDNLIEKSENMPWYKGP-----------TLLEALDSLEPP 218
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 220-316 3.54e-30

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: 110.05  E-value: 3.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 220 PPKGAESFNAQVIVLNH-----PGQVGAGYAPVLDCHTAHIACKFSELLEKIDrrTGKSVENsPKFIKSGDAAIVKMIPS 294
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|..
gi 1957425414 295 KPMCVEAFTeypplgRFAVRDM 316
Cdd:pfam03143  78 KPIALEKGQ------RFAIREG 93
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-316 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 605.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMD--TTKWSESRFEEIIKETSSFIKKVGYNPKHVPF 78
Cdd:PTZ00141  111 VAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  79 VPISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGT 158
Cdd:PTZ00141  191 IPISGWQGDNMIEKSDNMPWYKG-----------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGI 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 159 IKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAESFNAQVIVLNHPG 238
Cdd:PTZ00141  260 LKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPG 339

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 239 QVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:PTZ00141  340 QIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-316 1.16e-173

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 487.83  E-value: 1.16e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEagisKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHVPFVP 80
Cdd:TIGR00483 111 AAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIP 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  81 ISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIK 160
Cdd:TIGR00483 187 ISAWNGDNVIKKSENTPWYKG-----------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLK 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 161 AGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAESFNAQVIVLNHPGQV 240
Cdd:TIGR00483 256 PGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAI 334

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957425414 241 GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:TIGR00483 335 TVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDM 410
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-316 1.99e-168

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 475.35  E-value: 1.99e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSESRFEEIIKETSSFIKKVGYNPKHVPF 78
Cdd:PLN00043  111 CAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPF 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  79 VPISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGT 158
Cdd:PLN00043  191 VPISGFEGDNMIERSTNLDWYKG-----------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGV 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 159 IKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAESFNAQVIVLNHPG 238
Cdd:PLN00043  260 IKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPG 339

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 239 QVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:PLN00043  340 QIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYPPLGRFAVRDM 417
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-316 1.69e-161

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: 456.70  E-value: 1.69e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEfeagiskDGQTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHVPFVP 80
Cdd:COG5256   111 AAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIP 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  81 ISGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIK 160
Cdd:COG5256   184 VSAWKGDNVVKKSDNMPWYNG-----------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLK 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 161 AGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAESFNAQVIVLNHPGQV 240
Cdd:COG5256   253 VGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAI 331

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957425414 241 GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:COG5256   332 TVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDM 407
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-316 2.33e-159

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 451.30  E-value: 2.33e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   2 AIFIIAAgtgefEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHVPFVPI 81
Cdd:PRK12317  111 AVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  82 SGFNGDNMIEVSTNAPWYKGwqketkakvtgKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKA 161
Cdd:PRK12317  186 SAFEGDNVVKKSENMPWYNG-----------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKV 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 162 GMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGdSKNDPPKGAESFNAQVIVLNHPGQVG 241
Cdd:PRK12317  255 GDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAIT 333

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957425414 242 AGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRDM 316
Cdd:PRK12317  334 VGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVKEIPQLGRFAIRDM 408
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-125 2.57e-66

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 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 subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 207.34  E-value: 2.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAINKMDTT--KWSESRFEEIIKETSSFIKKVGYNPKHVPF 78
Cdd:cd01883   103 VAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPF 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1957425414  79 VPISGFNGDNMIEVSTNAPWYKGWqketkakvtgkTLLEAIDAIDPP 125
Cdd:cd01883   183 IPISGFTGDNLIEKSENMPWYKGP-----------TLLEALDSLEPP 218
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 222-316 4.21e-65

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: 200.11  E-value: 4.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 222 KGAESFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEA 301
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                          90
                  ....*....|....*
gi 1957425414 302 FTEYPPLGRFAVRDM 316
Cdd:cd03705    81 FSEYPPLGRFAVRDM 95
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 129-219 1.21e-60

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: 188.17  E-value: 1.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 129 SDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIR 208
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1957425414 209 RGNVAGDSKND 219
Cdd:cd03693    81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 22-311 1.27e-59

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 196.46  E-value: 1.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHvpFVPISGFNGDNMIEVSTNAPWYKg 101
Cdd:COG2895   135 QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWYD- 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 102 wqketkakvtGKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKiggigtvP-------VGRVETGTIKAGMIVTFAPAGVTT 174
Cdd:COG2895   212 ----------GPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTS 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 175 EVKSVEMHHEQLTEGVPGDNVGFNVK---NVSvkeirRGNVAGDSkNDPPKGAESFNAQVIVLN-HPGQVGAGYapVLDC 250
Cdd:COG2895   275 TVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS-----RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKH 346

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957425414 251 HTAHIACKFSELLEKIDRRTGKSVEnsPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRF 311
Cdd:COG2895   347 GTRTVRATVTAIKYRIDVNTLEHEA--ADSLELNDIGRVTLRLAEPIAFDPYADNRATGSF 405
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 22-315 1.92e-36

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 134.81  E-value: 1.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHvpFVPISGFNGDNMIEVSTNAPWYkg 101
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLGFRDVT--FIPLSALKGDNVVSRSESMPWY-- 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 102 wqketkakvTGKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKI-----GGIGTVPVGRVETGTikagmIVTFAPAGVTTEV 176
Cdd:TIGR02034 196 ---------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVGD-----EVVVLPSGRSSRV 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 177 KSVEMHHEQLTEGVPGDNVGFNVKNVSvkEIRRGN--VAGDSkndPPKGAESFNAQVIVL-NHPGQVGAGYapVLDCHTA 253
Cdd:TIGR02034 262 ARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDllAAADS---APEVADQFAATLVWMaEEPLLPGRSY--DLKLGTR 334

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957425414 254 HIACKFSELLEKIDRRTGKsvENSPKFIKSGDAAIVKMIPSKPMCVEAFTEYPPLGRFAVRD 315
Cdd:TIGR02034 335 KVRASVAAIKHKVDVNTLE--KGAAKSLELNEIGRVNLSLDEPIAFDPYAENRTTGAFILID 394
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-232 1.63e-32

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 125.41  E-value: 1.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   2 AIFIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPkHVPFVPI 81
Cdd:PRK05124  134 AILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL-DIRFVPL 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  82 SGFNGDNMIEVSTNAPWYKgwqketkakvtGKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVET 156
Cdd:PRK05124  206 SALEGDNVVSQSESMPWYS-----------GPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LAS 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 157 GTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNvsvkE--IRRGNVAGDSKNDPPKGaESFNAQVI 232
Cdd:PRK05124  270 GVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLED----EidISRGDLLVAADEALQAV-QHASADVV 342
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 22-232 3.16e-32

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 126.20  E-value: 3.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNpkHVPFVPISGFNGDNMIEVSTNAPWYkg 101
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY-- 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 102 wqketkakvTGKTLLEAIDAIDPPSRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGTIKAGMIVTFAPAGVTTEV 176
Cdd:PRK05506  220 ---------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRV 285

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1957425414 177 KSVEMHHEQLTEGVPGDNVgfnvkNVSVK---EIRRGNVAGDSkNDPPKGAESFNAQVI 232
Cdd:PRK05506  286 KRIVTPDGDLDEAFAGQAV-----TLTLAdeiDISRGDMLARA-DNRPEVADQFDATVV 338
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 220-316 3.54e-30

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: 110.05  E-value: 3.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 220 PPKGAESFNAQVIVLNH-----PGQVGAGYAPVLDCHTAHIACKFSELLEKIDrrTGKSVENsPKFIKSGDAAIVKMIPS 294
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|..
gi 1957425414 295 KPMCVEAFTeypplgRFAVRDM 316
Cdd:pfam03143  78 KPIALEKGQ------RFAIREG 93
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 22-126 6.42e-30

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 112.66  E-value: 6.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTKWSESRFEEIIKETSSFIKKVGYNPKHvpFVPISGFNGDNMIEVSTNAPWYKg 101
Cdd:cd04166   118 QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWYK- 194

                          90       100
                  ....*....|....*....|....*
gi 1957425414 102 wqketkakvtGKTLLEAIDAIDPPS 126
Cdd:cd04166   195 ----------GPTLLEHLETVEIAS 209
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 20-212 3.09e-28

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: 112.55  E-value: 3.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  20 DG---QTREHALLAYTLGVKQLIVAINKMDTTKwsesrFEEIIK----ETSSFIKKVGYNPKHVPFVPISGFNGdnmIEV 92
Cdd:COG0050   110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD-----DEELLElvemEVRELLSKYGFPGDDTPIIRGSALKA---LEG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  93 STNAPWYKGWQKetkakvtgktLLEAIDA-IDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MIVTFA 168
Cdd:COG0050   182 DPDPEWEKKILE----------LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIR 251

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1957425414 169 PAgVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNV 212
Cdd:COG0050   252 DT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQV 294
PRK00049 PRK00049
elongation factor Tu; Reviewed
 20-234 4.78e-27

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 109.12  E-value: 4.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  20 DG---QTREHALLAYTLGVKQLIVAINKMDTTKwsesrFEEIIK----ETSSFIKKVGYNPKHVPFVPISGFNGdnmIEV 92
Cdd:PRK00049  110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD-----DEELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  93 STNAPWYKGWQKetkakvtgktLLEAIDA-IDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MIVTFA 168
Cdd:PRK00049  182 DDDEEWEKKILE----------LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIR 251

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957425414 169 PAGVTTeVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESFNAQVIVL 234
Cdd:PRK00049  252 DTQKTT-VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-212 6.13e-27

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 108.88  E-value: 6.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   2 AIFIIAAgtgefeagisKDG---QTREHALLAYTLGVKQLIVAINKMDTTKwsesrFEEIIK----ETSSFIKKVGYNPK 74
Cdd:PRK12736  102 AILVVAA----------TDGpmpQTREHILLARQVGVPYLVVFLNKVDLVD-----DEELLElvemEVRELLSEYDFPGD 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  75 HVPFVPISGF---NGDnmievstnAPWYKGWQKetkakvtgktLLEAIDA-IDPPSRPSDKPLRLPLQDVYKIGGIGTVP 150
Cdd:PRK12736  167 DIPVIRGSALkalEGD--------PKWEDAIME----------LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVV 228

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957425414 151 VGRVETGTIKAG---MIVTFAPAgVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNV 212
Cdd:PRK12736  229 TGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQV 292
PLN03127 PLN03127
Elongation factor Tu; Provisional
 9-235 8.25e-27

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 109.14  E-value: 8.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   9 GTGEFEAGI----SKDG---QTREHALLAYTLGVKQLIVAINKMDTTKWSE--SRFEEIIKETSSFIKkvgynpkhvpfv 79
Cdd:PLN03127  144 GAAQMDGGIlvvsAPDGpmpQTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYK------------ 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  80 pisgFNGDNMIEVSTNA-PWYKGWQKETKAKVTGKtLLEAIDAIDP-PSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 157
Cdd:PLN03127  212 ----FPGDEIPIIRGSAlSALQGTNDEIGKNAILK-LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQG 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 158 TIKAG---MIVTFAPAG-VTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESFNAQVIV 233
Cdd:PLN03127  287 TIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYV 364


                  ..
gi 1957425414 234 LN 235
Cdd:PLN03127  365 LT 366
tufA CHL00071
elongation factor Tu
 20-235 8.69e-27

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 108.51  E-value: 8.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  20 DG---QTREHALLAYTLGVKQLIVAINKMDttKWSESRFEEIIK-ETSSFIKKVGYNPKHVPFVPISGFNG-DNMIEVST 94
Cdd:CHL00071  110 DGpmpQTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVSGSALLAlEALTENPK 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  95 NAPWYKGWQKetkaKVtgKTLLEAIDA-IDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MIVTFAPA 170
Cdd:CHL00071  188 IKRGENKWVD----KI--YNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRET 261

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957425414 171 GVTTeVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKgaESFNAQVIVLN 235
Cdd:CHL00071  262 KTTT-VTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPH--TKFEAQVYILT 323
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 222-316 1.80e-26

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: 100.55  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 222 KGAESFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKsvENSPKFIKSGDAAIVKMIPSKPMCVEA 301
Cdd:cd01513     1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLER 78

                          90
                  ....*....|....*
gi 1957425414 302 FTEYPPLGRFAVRDM 316
Cdd:cd01513    79 GKEFPTLGRFALRDG 93
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-236 4.12e-25

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: 105.38  E-value: 4.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   2 AIFIIAAgtgefeagisKDG---QTREH-ALLAyTLGVKQLIVAINKMDTTkwSESRFEEIIKETSSFIKkvGYNPKHVP 77
Cdd:COG3276    78 VLLVVAA----------DEGvmpQTREHlAILD-LLGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLEDAP 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  78 FVPISGfngdnmievstnapwykgwqketkakVTGK---TLLEAIDAI--DPPSRPSDKPLRLPLQDVYKIGGIGTVPVG 152
Cdd:COG3276   143 IVPVSA--------------------------VTGEgidELRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 153 RVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESFNAQVI 232
Cdd:COG3276   197 TLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVL--AAPGALRPTDRIDVRLR 274


                  ....
gi 1957425414 233 VLNH 236
Cdd:COG3276   275 LLPS 278
PRK12735 PRK12735
elongation factor Tu; Reviewed
 20-234 2.09e-24

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 101.84  E-value: 2.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  20 DG---QTREHALLAYTLGVKQLIVAINKMDTTKwSESRFEEIIKETSSFIKKVGYNPKHVPFVPISGFNGdnmIEVSTNA 96
Cdd:PRK12735  110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDE 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  97 PWYKGWQKetkakvtgktLLEAIDA-IDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MIVTFAPAGV 172
Cdd:PRK12735  186 EWEAKILE----------LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQK 255

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957425414 173 TTeVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESFNAQVIVL 234
Cdd:PRK12735  256 TT-VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 2-234 4.71e-24

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 101.01  E-value: 4.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   2 AIFIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKwSESRFEEIIKETSSFIKKVGYNPKHVPFV-- 79
Cdd:TIGR00485 102 AILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELLSQYDFPGDDTPIIrg 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  80 -PISGFNGDNmievstnapwykgwqkETKAKVtgKTLLEAIDA-IDPPSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 157
Cdd:TIGR00485 174 sALKALEGDA----------------EWEAKI--LELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERG 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 158 TIKAG---MIVTFAPAGVTTeVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESFNAQVIVL 234
Cdd:TIGR00485 236 IIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVL 312
PLN03126 PLN03126
Elongation factor Tu; Provisional
 22-315 8.04e-24

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 101.23  E-value: 8.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTKwSESRFEEIIKETSSFIKKVGYNPKHVPFVPISGFNGdnmIEVSTNAPWYKG 101
Cdd:PLN03126  184 QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPIISGSALLA---LEALMENPNIKR 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 102 WQKETKAKVTgkTLLEAIDAIDP-PSRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVT--TEVKS 178
Cdd:PLN03126  260 GDNKWVDKIY--ELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTG 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 179 VEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESFNAQVIVLNHP-----GQVGAGYAPVLDCHTA 253
Cdd:PLN03126  338 VEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMRTT 415

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957425414 254 HIACKFSELLEKIDRRTgksvenspKFIKSGDAaiVKMIPS--KPMCVEAFTeypplgRFAVRD 315
Cdd:PLN03126  416 DVTGKVTSIMNDKDEES--------KMVMPGDR--VKMVVEliVPVACEQGM------RFAIRE 463
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 224-315 1.91e-23

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: 92.62  E-value: 1.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 224 AESFNAQVIVLNHPGQV-GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCVEAF 302
Cdd:cd03704     3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETF 82

                          90
                  ....*....|...
gi 1957425414 303 TEYPPLGRFAVRD 315
Cdd:cd03704    83 KDFPQLGRFTLRD 95
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-92 1.87e-20

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: 86.81  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGefeagisKDGQTREHALLAYTLGVKqLIVAINKMDTTkwSESRFEEIIKETSS-FIKKVGYNPKHVPFV 79
Cdd:pfam00009  95 GAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVV 164

                          90
                  ....*....|...
gi 1957425414  80 PISGFNGDNMIEV 92
Cdd:pfam00009 165 PGSALKGEGVQTL 177
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 133-212 1.09e-18

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: 78.85  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 133 LRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNvsVKEIRRGNV 212
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 22-290 2.17e-18

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: 85.70  E-value: 2.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTKwsesrfEEIIKETSSFIKKV---GYNPKHVPFVPISGFNGDNMIEVstnapw 98
Cdd:TIGR00475  90 QTGEHLAVLDLLGIPHTIVVITKADRVN------EEEIKRTEMFMKQIlnsYIFLKNAKIFKTSAKTGQGIGEL------ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  99 ykgwqketkaKVTGKTLLEAIDAidppsRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKS 178
Cdd:TIGR00475 158 ----------KKELKNLLESLDI-----KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKA 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 179 VEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAESfnaqVIVLNHpgqvgagyAPVLDCHTAHIACK 258
Cdd:TIGR00475 223 IQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI--LTPEDPKLRVV----VKFIAE--------VPLLELQPYHIAHG 288

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1957425414 259 FSELLEKI---DRRTGKSVENSPKFIKSGDAAIVK 290
Cdd:TIGR00475 289 MSVTTGKIsllDKGIALLTLDAPLILAKGDKLVLR 323
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 220-315 5.20e-17

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: 75.27  E-value: 5.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 220 PPKGAESFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENSPKFIKSGDAAIVKMIPSKPMCV 299
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80

                          90
                  ....*....|....*.
gi 1957425414 300 EAFTEYPPLGRFAVRD 315
Cdd:cd04093    81 ETFKDNKELGRFVLRR 96
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 133-212 9.08e-17

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: 73.71  E-value: 9.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 133 LRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNV 212
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 135-212 2.30e-16

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 72.94  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 135 LPLQDVYKIGGIGTVPVGRVETGTIKAGM---IVTFAPaGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGN 211
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81


                  .
gi 1957425414 212 V 212
Cdd:cd03697    82 V 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 147-212 5.84e-16

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 71.14  E-value: 5.84e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957425414 147 GTVPVGRVETGTIKAGMIVTFAPAGV-----TTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNV 212
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 132-215 6.00e-14

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 66.00  E-value: 6.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 132 PLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGN 211
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80


                  ....
gi 1957425414 212 VAGD 215
Cdd:cd16267    81 ILCD 84
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-126 4.35e-12

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: 63.85  E-value: 4.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAGTGEfeagiskDGQTREHALLAyTLGVKQLIVAINKMDTTKwsESRFEEIIKETSSFIKKVGY---NPKHVP 77
Cdd:cd00881    88 GALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVP 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1957425414  78 FVPISGFNGDNMievstnapwykgwqketkakvtgKTLLEAIDAIDPPS 126
Cdd:cd00881   158 IIPISALTGEGI-----------------------EELLDAIVEHLPPP 183
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 132-212 3.12e-11

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. 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: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 58.65  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 132 PLRLPLQDVYKigGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGN 211
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 1957425414 212 V 212
Cdd:cd04089    79 V 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 139-212 1.33e-10

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: 56.84  E-value: 1.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 139 DVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAG----VTTEVKSVEMHHEQLTEGVPGDNVGFNVKNVSVKEIRRGNV 212
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 132-215 5.69e-10

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. 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. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 55.20  E-value: 5.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 132 PLRLPLQDVYKiGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMH-HEQLTEGVPGDNVGFNVKNVSVKEIRRG 210
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 1957425414 211 NVAGD 215
Cdd:cd03698    80 DILSS 84
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 133-197 1.39e-08

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 51.03  E-value: 1.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957425414 133 LRLPLQDVYKIGGIGTVPVGRVETGTIKAGMIVTFAPAGVTTEVKSVEMHHEQLTEGVPGDNVGF 197
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 2-125 9.47e-08

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 51.43  E-value: 9.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   2 AIFIIAAGTGEFEagiskdgQTREHALLAYTLGVKQLIVAINKMDTTKwSESRFEEIIKETSSFIKKVGYNPKHVPFVPI 81
Cdd:cd01884    92 AILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLELVEMEVRELLSKYGFDGDDTPIVRG 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1957425414  82 SGFNGdnmIEVSTNAPWYKGWQKetkakvtgktLLEAIDAIDPP 125
Cdd:cd01884   164 SALKA---LEGDDPNKWVDKILE----------LLDALDSYIPT 194
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-87 1.83e-05

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: 44.52  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414   1 CAIFIIAAgtgefEAGISKdgQTREHALLAYTLGVKQLIVAINKMDTTkwSESRFEEIIKETSSFIKKVGYNPkhVPFVP 80
Cdd:cd04171    76 AVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFLAD--APIFP 144


                  ....*..
gi 1957425414  81 ISGFNGD 87
Cdd:cd04171   145 VSSVTGE 151
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 227-285 3.27e-04

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: 39.04  E-value: 3.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425414 227 FNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFsellEKIDR---RTGKSVE------NSPKFIKSGD 285
Cdd:cd03708     6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDKevlRTGDRALvrfrflYRPEYLREGQ 69
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 22-221 4.00e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 41.76  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414  22 QTREHALLAYTLGVKQLIVAINKMDTTkwSESRFEEIIKETSSFIKkvGYNPKHVPFVPISGFNGDNmIEVstnapwykg 101
Cdd:PRK04000  126 QTKEHLMALDIIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVN-IDA--------- 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 102 wqketkakvtgktLLEAIDA-IDPPSRPSDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---TIKAGMI 164
Cdd:PRK04000  192 -------------LIEAIEEeIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIK 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957425414 165 VTFAPAG----VTTEVKSVEMHHEQLTEGVPGDNVGFNVK---NVSVKEIRRGNVAGDSKNDPP 221
Cdd:PRK04000  259 VEEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPP 322
PRK13351 PRK13351
elongation factor G-like protein;
115-219 4.09e-03

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 38.78  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425414 115 LLEAIDAIDP---------PSRPSDKPLRLPLQD-------VYKI---GGIGTVPVGRVETGTIKAGMIVTFAPAGVTTE 175
Cdd:PRK13351  269 LLDAVVDYLPsplevppprGSKDNGKPVKVDPDPekpllalVFKVqydPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREK 348

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1957425414 176 V-KSVEMH---HEQLTEGVPGDNVGFnvknVSVKEIRRGNVAGDSKND 219
Cdd:PRK13351  349 VgRLFRLQgnkREEVDRAKAGDIVAV----AGLKELETGDTLHDSADP 392
 
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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