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Conserved domains on  [gi|159895342|gb|ABX09955|]
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translation elongation factor 1-alpha, partial [[Candida] sp. NRRL Y-679]

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 ...
 1-311 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: 583.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--SVQWNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:PTZ00141 109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRV 158
Cdd:PTZ00141 189 PFIPISGWQGDNMIEKSDNMPWYKG-------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 159 ETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLVDGgVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAASFNAQVII 238
Cdd:PTZ00141 256 ETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEA-VPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIV 334

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159895342 239 LNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:PTZ00141 335 LNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYP 407
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-311 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 583.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--SVQWNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:PTZ00141 109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRV 158
Cdd:PTZ00141 189 PFIPISGWQGDNMIEKSDNMPWYKG-------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 159 ETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLVDGgVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAASFNAQVII 238
Cdd:PTZ00141 256 ETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEA-VPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIV 334

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159895342 239 LNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:PTZ00141 335 LNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYP 407
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-311 1.99e-168

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: 474.35  E-value: 1.99e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342    1 ADCAVLIIAGGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPKNVPF 80
Cdd:TIGR00483 109 ADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPF 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   81 VPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:TIGR00483 185 IPISAWNGDNVIKKSENTPWYKG-------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVET 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  161 G*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAASFNAQVIILN 240
Cdd:TIGR00483 252 GVLKPGDKVVFEPAGVSGEVKSIEMHHEQI-EQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQ 329

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159895342  241 HPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:TIGR00483 330 HPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIP 400
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-311 1.00e-154

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: 439.37  E-value: 1.00e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPKNVPF 80
Cdd:COG5256  109 ADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  81 VPISGWNGDNMIEPSANCPWYkgwtketkasgvvKGKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:COG5256  182 IPVSAWKGDNVVKKSDNMPWY-------------NGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVET 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 161 G*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAASFNAQVIILN 240
Cdd:COG5256  249 GVLKVGDKVVFMPAGVVGEVKSIEMHHEEL-EQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQ 326

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159895342 241 HPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:COG5256  327 HPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFP 397
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-129 1.09e-70

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: 218.13  E-value: 1.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSV--QWNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:cd01883  101 ADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDV 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYKGWtketkasgvvkgkTLLEAIDAIEPP 129
Cdd:cd01883  181 PFIPISGFTGDNLIEKSENMPWYKGP-------------TLLEALDSLEPP 218
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 225-310 1.43e-28

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: 105.81  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  225 PPKGAASFNAQVIILNH-----PGQISAGYSPVLDCHTAHIACRFDELIEKIDrrTGKAVEaSPKFVKSGDAAMVRLIPT 299
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77

                          90
                  ....*....|.
gi 159895342  300 KPMCVESFTEY 310
Cdd:pfam03143  78 KPIALEKGQRF 88
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-311 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 583.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--SVQWNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:PTZ00141 109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRV 158
Cdd:PTZ00141 189 PFIPISGWQGDNMIEKSDNMPWYKG-------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 159 ETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLVDGgVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAASFNAQVII 238
Cdd:PTZ00141 256 ETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEA-VPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIV 334

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159895342 239 LNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:PTZ00141 335 LNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYP 407
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-311 1.99e-168

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: 474.35  E-value: 1.99e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342    1 ADCAVLIIAGGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPKNVPF 80
Cdd:TIGR00483 109 ADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPF 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   81 VPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:TIGR00483 185 IPISAWNGDNVIKKSENTPWYKG-------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVET 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  161 G*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAASFNAQVIILN 240
Cdd:TIGR00483 252 GVLKPGDKVVFEPAGVSGEVKSIEMHHEQI-EQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQ 329

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159895342  241 HPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:TIGR00483 330 HPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIP 400
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-311 2.09e-155

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 442.22  E-value: 2.09e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSV--QWNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:PLN00043 109 ADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKI 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRV 158
Cdd:PLN00043 189 PFVPISGFEGDNMIERSTNLDWYKG-------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRV 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 159 ETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLVDGgVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAASFNAQVII 238
Cdd:PLN00043 256 ETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEA-LPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVII 334

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159895342 239 LNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:PLN00043 335 MNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYP 407
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-311 1.00e-154

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: 439.37  E-value: 1.00e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPKNVPF 80
Cdd:COG5256  109 ADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  81 VPISGWNGDNMIEPSANCPWYkgwtketkasgvvKGKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:COG5256  182 IPVSAWKGDNVVKKSDNMPWY-------------NGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVET 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 161 G*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNdPPKGAASFNAQVIILN 240
Cdd:COG5256  249 GVLKVGDKVVFMPAGVVGEVKSIEMHHEEL-EQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQ 326

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159895342 241 HPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:COG5256  327 HPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFP 397
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-311 1.50e-150

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 428.96  E-value: 1.50e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPKNVPF 80
Cdd:PRK12317 108 ADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPF 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  81 VPISGWNGDNMIEPSANCPWYKGwtketkasgvvkgKTLLEAIDAIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:PRK12317 183 IPVSAFEGDNVVKKSENMPWYNG-------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVET 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 161 G*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAGdSKNDPPKGAASFNAQVIILN 240
Cdd:PRK12317 250 GVLKVGDKVVFMPAGVVGEVKSIEMHHEEL-PQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQ 327

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159895342 241 HPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEYP 311
Cdd:PRK12317 328 HPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVKEIP 398
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-129 1.09e-70

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: 218.13  E-value: 1.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSV--QWNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:cd01883  101 ADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDV 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYKGWtketkasgvvkgkTLLEAIDAIEPP 129
Cdd:cd01883  181 PFIPISGFTGDNLIEKSENMPWYKGP-------------TLLEALDSLEPP 218
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 133-224 1.56e-57

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: 180.08  E-value: 1.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 133 TDKPLRLPLQDVYKIGGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEI 212
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPL-EEAIPGDNVGFNVKGVSVKDI 79

                         90
                 ....*....|..
gi 159895342 213 RRGNVAGDSKND 224
Cdd:cd03693   80 KRGDVAGDSKND 91
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 227-311 1.40e-54

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: 173.15  E-value: 1.40e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 227 KGAASFNAQVIILNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVES 306
Cdd:cd03705    1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80


                 ....*
gi 159895342 307 FTEYP 311
Cdd:cd03705   81 FSEYP 85
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-311 5.15e-53

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: 179.13  E-value: 5.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIaggtgefEA--GISKdgQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYnpKNV 78
Cdd:COG2895  119 ADLAILLI-------DArkGVLE--QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGL--EDI 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  79 PFVPISGWNGDNMIEPSANCPWYkgwtketkasgvvKGKTLLEAIDAIEPPARPTDKPLRLPLQDVYKiggigtvP---- 154
Cdd:COG2895  188 TFIPISALKGDNVVERSENMPWY-------------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------Pnldf 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 155 ---VGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVK---NVSvkeirRGNVAGDSkNDPPKG 228
Cdd:COG2895  248 rgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDL-EEAFAGQSVTLTLEdeiDIS-----RGDVIVAA-DAPPEV 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 229 AASFNAQVIILN-HPGQISAGYspVLDCHTAHIACRFDELIEKIDRRTGKAVEASPkfVKSGDAAMVRLIPTKPMCVESF 307
Cdd:COG2895  321 ADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHEAADS--LELNDIGRVTLRLAEPIAFDPY 396


                 ....
gi 159895342 308 TEYP 311
Cdd:COG2895  397 ADNR 400
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-282 8.77e-35

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: 130.19  E-value: 8.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342    1 ADCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGynPKNVPF 80
Cdd:TIGR02034 104 ADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   81 VPISGWNGDNMIEPSANCPWYkgwtketkasgvvKGKTLLEAIDAIEPPARPTDKPLRLPLQDVYKI-----GGIGTVPV 155
Cdd:TIGR02034 175 IPLSALKGDNVVSRSESMPWY-------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIAS 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  156 GRVETG*ikagmIVTFAPAGVTTEVKSVeMHHEQLVDGGVPGDNVGFNVKNVSvkEIRRGN--VAGDSkndPPKGAASFN 233
Cdd:TIGR02034 242 GSVHVGD-----EVVVLPSGRSSRVARI-VTFDGDLEQARAGQAVTLTLDDEI--DISRGDllAAADS---APEVADQFA 310

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 159895342  234 AQVIIL-NHPgqISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEAS 282
Cdd:TIGR02034 311 ATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAAK 358
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-183 5.40e-32

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 123.87  E-value: 5.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPkNVPF 80
Cdd:PRK05124 131 CDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL-DIRF 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  81 VPISGWNGDNMIEPSANCPWYkgwtketkasgvvKGKTLLEAIDAIEPPARPTDKPLRLPLQDVYKI-----GGIGTvpv 155
Cdd:PRK05124 203 VPLSALEGDNVVSQSESMPWY-------------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT--- 266

                        170       180
                 ....*....|....*....|....*...
gi 159895342 156 grVETG*IKAGMIVTFAPAGVTTEVKSV 183
Cdd:PRK05124 267 --LASGVVKVGDRVKVLPSGKESNVARI 292
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 24-237 5.79e-31

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 122.35  E-value: 5.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  24 QTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNpkNVPFVPISGWNGDNMIEPSANCPWYkg 103
Cdd:PRK05506 144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY-- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 104 wtketkasgvvKGKTLLEAIDAIEPPARPTDKPLRLPLQDVYKI-----GGIGTvpvgrVETG*IKAGMIVTFAPAGVTT 178
Cdd:PRK05506 220 -----------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTS 283

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159895342 179 EVKSVEMhHEQLVDGGVPGDNVgfnvkNVSVK---EIRRGNVAGDSkNDPPKGAASFNAQVI 237
Cdd:PRK05506 284 RVKRIVT-PDGDLDEAFAGQAV-----TLTLAdeiDISRGDMLARA-DNRPEVADQFDATVV 338
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-130 2.07e-29

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: 111.51  E-value: 2.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQWNEQRFEEIIKETSNFIKKVGYNPknVPF 80
Cdd:cd04166  102 ADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITF 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 159895342  81 VPISGWNGDNMIEPSANCPWYkgwtketkasgvvKGKTLLEAIDAIEPPA 130
Cdd:cd04166  173 IPISALEGDNVVSRSENMPWY-------------KGPTLLEHLETVEIAS 209
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 225-310 1.43e-28

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: 105.81  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  225 PPKGAASFNAQVIILNH-----PGQISAGYSPVLDCHTAHIACRFDELIEKIDrrTGKAVEaSPKFVKSGDAAMVRLIPT 299
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77

                          90
                  ....*....|.
gi 159895342  300 KPMCVESFTEY 310
Cdd:pfam03143  78 KPIALEKGQRF 88
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 22-217 7.07e-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: 111.40  E-value: 7.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  22 DG---QTREHALLAFTLGVRQLIVAVNKMDSVQwneqrFEEIIK----ETSNFIKKVGYNPKNVPFVPISGW---NGDnm 91
Cdd:COG0050  110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD-----DEELLElvemEVRELLSKYGFPGDDTPIIRGSALkalEGD-- 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  92 iepsANCPWYKgwtketkasgvvKGKTLLEAIDA-IEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETG*IKAG---M 167
Cdd:COG0050  183 ----PDPEWEK------------KILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevE 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 159895342 168 IVTFAPAgVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:COG0050  247 IVGIRDT-QKTVVTGVEMFRKLL-DEGEAGDNVGLLLRGIKREDVERGQV 294
PRK00049 PRK00049
elongation factor Tu; Reviewed
 22-217 5.04e-27

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 109.12  E-value: 5.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  22 DG---QTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNVPFVPISGWNGdnmIEPSANC 98
Cdd:PRK00049 110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDE 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  99 PWYKgwtketkasgvvKGKTLLEAIDA-IEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETG*IKAG---MIVTFAPA 174
Cdd:PRK00049 186 EWEK------------KILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDT 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 159895342 175 GVTTeVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:PRK00049 254 QKTT-VTGVEMFRKLL-DEGQAGDNVGALLRGIKREDVERGQV 294
tufA CHL00071
elongation factor Tu
 2-240 6.15e-27

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 108.89  E-value: 6.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNVPFV 81
Cdd:CHL00071 100 DGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD-DEELLELVELEVRELLSKYDFPGDDIPIV 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  82 PISGWNG-DNMIEPSANCPWYKGWtketkasgVVKGKTLLEAIDA-IEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVE 159
Cdd:CHL00071 172 SGSALLAlEALTENPKIKRGENKW--------VDKIYNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIE 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 160 TG*IKAG---MIVTFAPAGVTTeVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKgaASFNAQV 236
Cdd:CHL00071 244 RGTVKVGdtvEIVGLRETKTTT-VTGLEMFQKTL-DEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPH--TKFEAQV 319


                 ....
gi 159895342 237 IILN 240
Cdd:CHL00071 320 YILT 323
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-217 4.52e-26

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 106.18  E-value: 4.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNV 78
Cdd:PRK12736 100 DGAILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVDLVD-DEELLELVEMEVRELLSEYDFPGDDI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  79 PFVPISGW---NGDNmiepsancPWYKgwtketkasgvvKGKTLLEAIDA-IEPPARPTDKPLRLPLQDVYKIGGIGTVP 154
Cdd:PRK12736 169 PVIRGSALkalEGDP--------KWED------------AIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVV 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 159895342 155 VGRVETG*IKAG---MIVTFAPAgVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:PRK12736 229 TGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLL-DEGQAGDNVGVLLRGVDRDEVERGQV 292
PRK12735 PRK12735
elongation factor Tu; Reviewed
 22-239 1.90e-25

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 104.54  E-value: 1.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  22 DG---QTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNVPFVPISGWNGdnmIEPSANC 98
Cdd:PRK12735 110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDE 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  99 PWYKgwtketkasgvvKGKTLLEAIDA-IEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETG*IKAG---MIVTFAPA 174
Cdd:PRK12735 186 EWEA------------KILELMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKET 253

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 159895342 175 GVTTeVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAASFNAQVIIL 239
Cdd:PRK12735 254 QKTT-VTGVEMFRKLL-DEGQAGDNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
PLN03127 PLN03127
Elongation factor Tu; Provisional
 11-240 2.77e-25

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 104.91  E-value: 2.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  11 GTGEFEAGI----SKDG---QTREHALLAFTLGVRQLIVAVNKMDSVQWNE--QRFEEIIKETSNFIKKVGYNpknvpfV 81
Cdd:PLN03127 144 GAAQMDGGIlvvsAPDGpmpQTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYKFPGDE------I 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  82 PIsgwngdnmIEPSANCPwYKGWTKETKASGVVKgktLLEAIDAIEP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:PLN03127 218 PI--------IRGSALSA-LQGTNDEIGKNAILK---LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQ 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 161 G*IKAG---MIVTFAPAG-VTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAASFNAQV 236
Cdd:PLN03127 286 GTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKIL-DQGQAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEI 362


                 ....
gi 159895342 237 IILN 240
Cdd:PLN03127 363 YVLT 366
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-217 1.35e-23

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: 100.76  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMDSVqwNEQRFEEIIKETSNFIKkvGYNPKN 77
Cdd:COG3276   76 DLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLED 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  78 VPFVPISGWNGDNmIEpsancpwykgwtketkasgvvkgkTLLEAIDAI--EPPARPTDKPLRLPLQDVYKIGGIGTVPV 155
Cdd:COG3276  141 APIVPVSAVTGEG-ID------------------------ELRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVT 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159895342 156 GRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQlVDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:COG3276  196 GTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQP-VEEAYAGQRVALNLAGVEKEEIERGDV 256
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 2-217 2.19e-23

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: 99.08  E-value: 2.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342    2 DCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNVPFV 81
Cdd:TIGR00485 100 DGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD-DEELLELVEMEVRELLSQYDFPGDDTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   82 PISGWNgdnmiepsancpwykgwTKETKASGVVKGKTLLEAIDA-IEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:TIGR00485 172 RGSALK-----------------ALEGDAEWEAKILELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVER 234

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  161 G*IKAG---MIVTFAPAGVTTeVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:TIGR00485 235 GIIKVGeevEIVGLKDTRKTT-VTGVEMFRKEL-DEGRAGDNVGLLLRGIKREEIERGMV 292
PLN03126 PLN03126
Elongation factor Tu; Provisional
 2-305 2.58e-23

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 99.69  E-value: 2.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNVPFV 81
Cdd:PLN03126 169 DGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPII 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  82 PISGWNGDNMIEPSANcpwykgwTKETKASGVVKGKTLLEAIDAIEP-PARPTDKPLRLPLQDVYKIGGIGTVPVGRVET 160
Cdd:PLN03126 241 SGSALLALEALMENPN-------IKRGDNKWVDKIYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVER 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 161 G*IKAGMIVTFAPAGVT--TEVKSVEMhHEQLVDGGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGAASFNAQVII 238
Cdd:PLN03126 314 GTVKVGETVDIVGLRETrsTTVTGVEM-FQKILDEALAGDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYV 390

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159895342 239 LNHP--GQIS---AGYSPVLDCHTAHIACRFDELIEKIDRRTgkaveaspKFVKSGDAAMVRLIPTKPMCVE 305
Cdd:PLN03126 391 LKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------KMVMPGDRVKMVVELIVPVACE 454
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-129 8.45e-23

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: 92.97  E-value: 8.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342    1 ADCAVLIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDSVqwNEQRFEEIIKETSN-FIKKVGYNPKNVP 79
Cdd:pfam00009  93 ADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVP 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 159895342   80 FVPISGWNGDNMiepsancpwykgwtketkasgvvkgKTLLEAIDAIEPP 129
Cdd:pfam00009 163 VVPGSALKGEGV-------------------------QTLLDALDEYLPS 187
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 227-311 2.08e-22

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: 89.37  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 227 KGAASFNAQVIILNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKavEASPKFVKSGDAAMVRLIPTKPMCVES 306
Cdd:cd01513    1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLER 78


                 ....*
gi 159895342 307 FTEYP 311
Cdd:cd01513   79 GKEFP 83
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 232-311 6.20e-20

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: 82.99  E-value: 6.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 232 FNAQVIILNHPGQI-SAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCVESFTEY 310
Cdd:cd03704    6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85


                 .
gi 159895342 311 P 311
Cdd:cd03704   86 P 86
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-295 1.03e-17

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: 83.38  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342    1 ADCAVLIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDSVqwNEQRFEEIIKETSNFIKKVGYNpKN 77
Cdd:TIGR00475  74 IDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFL-KN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   78 VPFVPISGWNGDNMiepsancpwykgwtKETKASgvvkGKTLLEAIDaieppARPTDKPLRLPLQDVYKIGGIGTVPVGR 157
Cdd:TIGR00475 141 AKIFKTSAKTGQGI--------------GELKKE----LKNLLESLD-----IKRIQKPLRMAIDRAFKVKGAGTVVTGT 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  158 VETG*IKAGMIVTFAPAGVTTEVKSVEmHHEQLVDGGVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGAASFNAQVI 237
Cdd:TIGR00475 198 AFSGEVKVGDNLRLLPINHEVRVKAIQ-AQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVP 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 159895342  238 ILnhPGQIsagyspvldCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVR 295
Cdd:TIGR00475 277 LL--ELQP---------YHIAHGMSVTTGKISLLDKGIALLTLDAPLILAKGDKLVLR 323
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 137-217 3.17e-16

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: 72.30  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 137 LRLPLQDVYKIGGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQlVDGGVPGDNVGFNVKNvsVKEIRRGN 216
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEE-VDEAKAGDIVGIGILG--VKDILTGD 77


                 .
gi 159895342 217 V 217
Cdd:cd01342   78 T 78
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-129 1.41e-15

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: 73.48  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDSVqwNEQRFEEIIKETSNFIKKVGY---NPKN 77
Cdd:cd00881   86 ADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV--GEEDFDEVLREIKELLKLIGFtflKGKD 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 159895342  78 VPFVPISGWNGDNMiepsancpwykgwtketkasgvvkgKTLLEAIDAIEPP 129
Cdd:cd00881  156 VPIIPISALTGEGI-------------------------EELLDAIVEHLPP 182
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 137-217 1.35e-14

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: 67.94  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 137 LRLPLQDVYKIGGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQlVDGGVPGDNVGFNVKNVSVKEIRRGN 216
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKP-VEEAKAGDRVALNLTGVDAKELERGF 79


                 .
gi 159895342 217 V 217
Cdd:cd03696   80 V 80
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 139-217 6.99e-14

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: 66.00  E-value: 6.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 139 LPLQDVYKIGGIGTVPVGRVETG*IKAGM---IVTFAPaGVTTEVKSVEMHHEQLvDGGVPGDNVGFNVKNVSVKEIRRG 215
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKE-TLKTTVTGIEMFRKTL-DEAEAGDNVGVLLRGVKKEDVERG 80


                 ..
gi 159895342 216 NV 217
Cdd:cd03697   81 MV 82
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 225-311 7.61e-13

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: 63.72  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 225 PPKGAASFNAQVIILNHPGQISAGYSPVLDCHTAHIACRFDELIEKIDRRTGKAVEASPKFVKSGDAAMVRLIPTKPMCV 304
Cdd:cd04093    1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80


                 ....*..
gi 159895342 305 ESFTEYP 311
Cdd:cd04093   81 ETFKDNK 87
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 136-220 1.11e-12

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: 62.53  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 136 PLRLPLQDVYKIGGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQlVDGGVPGDNVGFNVKNVSVKEIRRG 215
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEP-VDWAVAGDNVTLTLTGIDPNHLRVG 79


                 ....*
gi 159895342 216 NVAGD 220
Cdd:cd16267   80 SILCD 84
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 151-217 1.66e-12

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: 61.90  E-value: 1.66e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159895342  151 GTVPVGRVETG*IKAGMIVTFAPAGV-----TTEVKSVEMHHEQlVDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAP-LREAVAGDNAGLILAGVGLEDIRVGDT 71
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 136-217 8.08e-10

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: 54.41  E-value: 8.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 136 PLRLPLQDVYKigGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQlVDGGVPGDNVGFNVKNVSVKEIRRG 215
Cdd:cd04089    1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEE-VDSAKPGENVKLKLKGVEEEDISPG 77


                 ..
gi 159895342 216 NV 217
Cdd:cd04089   78 FV 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 143-217 1.38e-09

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: 54.15  E-value: 1.38e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159895342 143 DVYKIGGIGTVPVGRVETG*IKAGMIVTFAPAG----VTTEVKSVEMHHeQLVDGGVPGDNVGFNVKNVSVKEIRRGNV 217
Cdd:cd03694    7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNR-QPVDRARAGQSASFALKKIKRESLRKGMV 84
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 136-220 1.45e-09

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: 54.04  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342 136 PLRLPLQDVYKiGGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLVDGGVPGDNVGFNVKNVSVKEIRRG 215
Cdd:cd03698    1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                 ....*
gi 159895342 216 NVAGD 220
Cdd:cd03698   80 DILSS 84
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 2-81 2.42e-07

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: 50.27  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDSVQwNEQRFEEIIKETSNFIKKVGYNPKNVPFV 81
Cdd:cd01884   90 DGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD-DEELLELVEMEVRELLSKYGFDGDDTPIV 161
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-89 2.45e-06

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: 46.83  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAGgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDSVqwNEQRFEEIIKETSNFIKKVGYnpKNVPFV 81
Cdd:cd04171   75 DAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL--ADAPIF 143


                 ....*...
gi 159895342  82 PISGWNGD 89
Cdd:cd04171  144 PVSSVTGE 151
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 137-202 5.95e-06

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: 43.71  E-value: 5.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 159895342 137 LRLPLQDVYKIGGIGTVPVGRVETG*IKAGMIVTFAPAGVTTEVKSVEMHHEQLvDGGVPGDNVGF 202
Cdd:cd03695    1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGEL-DSAGAGEAVTL 65
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 232-287 6.99e-06

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: 43.66  E-value: 6.99e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 159895342 232 FNAQVIILNHPGQISAGYSPVLDCHTAHIACRfdelIEKIDR---RTGKAVEASPKFVK 287
Cdd:cd03708    6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTAR----IISIDKevlRTGDRALVRFRFLY 60
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 24-139 6.31e-05

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 44.07  E-value: 6.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342  24 QTREHaLLAFT-LGVRQLIVAVNKMDSVqwNEQRFEEIIKETSNFIKkvGYNPKNVPFVPISGWNGDNMiepsancpwyk 102
Cdd:PRK04000 126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNI----------- 189

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 159895342 103 gwtketkasgvvkgKTLLEAIDA-IEPPARPTDKPLRL 139
Cdd:PRK04000 190 --------------DALIEAIEEeIPTPERDLDKPPRM 213
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 1-91 3.99e-04

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: 40.53  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   1 ADCAVLIIAGGTGeFEAgiskdgQTRE---HALLAFTlgvrQLIVAVNKMD---SVQWNEQRFEEIIKETSNFIKKVGyn 74
Cdd:cd01887   73 TDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKIDkpyGTEADPERVKNELSELGLVGEEWG-- 139

                         90
                 ....*....|....*..
gi 159895342  75 pKNVPFVPISGWNGDNM 91
Cdd:cd01887  140 -GDVSIVPISAKTGEGI 155
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 2-84 5.82e-03

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 38.06  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159895342   2 DCAVLIIAGGTGefeagiSKDGQTREHALLAFTLGVRQLIVAVNKMDSVQwnEQRFEEIIKETSNFIKkvGYNPKNVPFV 81
Cdd:PTZ00327 142 DAALLLIAANES------CPQPQTSEHLAAVEIMKLKHIIILQNKIDLVK--EAQAQDQYEEIRNFVK--GTIADNAPII 211


                 ...
gi 159895342  82 PIS 84
Cdd:PTZ00327 212 PIS 214
 
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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