NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|922581324|ref|NP_001300232|]
View 

GTP_EFTU_D3 domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 50-136 2.70e-51

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


:

Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 159.99  E-value: 2.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  50 VASMVFEAEILVLHHPTTIKPNYQAMLHIGSVRQTATLVSMGKEVLRTGDRDKVQFKFIRQPEYIRPGTKMVFREGRTKA 129
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTKG 80


                 ....*..
gi 922581324 130 VGTVSSV 136
Cdd:cd03708   81 IGTVTKV 87
Translation_Factor_II_like super family cl02787
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 1-44 1.73e-19

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.


The actual alignment was detected with superfamily member cd03694:

Pssm-ID: 445922 [Multi-domain]  Cd Length: 87  Bit Score: 78.80  E-value: 1.73e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 922581324   1 MPIPIKSIHRKRMPVGIVKCGQSASFALKKIPKKDVRKGMVLVD 44
Cdd:cd03694   44 RPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMVLVS 87
 
Name Accession Description Interval E-value
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 50-136 2.70e-51

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


Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 159.99  E-value: 2.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  50 VASMVFEAEILVLHHPTTIKPNYQAMLHIGSVRQTATLVSMGKEVLRTGDRDKVQFKFIRQPEYIRPGTKMVFREGRTKA 129
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTKG 80


                 ....*..
gi 922581324 130 VGTVSSV 136
Cdd:cd03708   81 IGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 1-44 1.73e-19

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: 78.80  E-value: 1.73e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 922581324   1 MPIPIKSIHRKRMPVGIVKCGQSASFALKKIPKKDVRKGMVLVD 44
Cdd:cd03694   44 RPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMVLVS 87
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 5-140 6.43e-08

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: 51.47  E-value: 6.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324   5 IKSI--HRKRMPVGIVkcGQSASFALKKIPKKDVRKGMVLVDPKVKPVASMVFEAEILVLHHPTTIKPNYQAMLHIGSVR 82
Cdd:COG5256  268 VKSIemHHEELEQAEP--GDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQ 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  83 QTATLVSM--------GKEV------LRTGDRDKVQFKFIRqPEYIRPgtkmvFRE------------GRTKAVGTVSSV 136
Cdd:COG5256  346 VACTFVELvskldprtGQVKeenpqfLKTGDAAIVKIKPTK-PLVIEK-----FKEfpqlgrfairdmGQTVAAGVVLDV 419


                 ....
gi 922581324 137 VPQE 140
Cdd:COG5256  420 KPKK 423
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 5-140 4.52e-07

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 49.15  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324   5 IKSIHRKRMPVGIVKCGQSASFALKKIPKKDVRKGMVLVDPKVKPVASMVFEAEILVLHHPTTIKPNYQAMLHIGSVRQT 84
Cdd:PRK12317 269 VKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVA 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  85 ATLVSMGKEV--------------LRTGDRDKVQFKFIRqPEYIRPgtkmvFRE------------GRTKAVGTVSSVVP 138
Cdd:PRK12317 349 CTFEELVKKLdprtgqvaeenpqfIKTGDAAIVKIKPTK-PLVIEK-----VKEipqlgrfairdmGQTIAAGMVIDVKP 422


                 ..
gi 922581324 139 QE 140
Cdd:PRK12317 423 AK 424
 
Name Accession Description Interval E-value
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 50-136 2.70e-51

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


Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 159.99  E-value: 2.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  50 VASMVFEAEILVLHHPTTIKPNYQAMLHIGSVRQTATLVSMGKEVLRTGDRDKVQFKFIRQPEYIRPGTKMVFREGRTKA 129
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTKG 80


                 ....*..
gi 922581324 130 VGTVSSV 136
Cdd:cd03708   81 IGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 1-44 1.73e-19

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: 78.80  E-value: 1.73e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 922581324   1 MPIPIKSIHRKRMPVGIVKCGQSASFALKKIPKKDVRKGMVLVD 44
Cdd:cd03694   44 RPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMVLVS 87
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 5-140 6.43e-08

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: 51.47  E-value: 6.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324   5 IKSI--HRKRMPVGIVkcGQSASFALKKIPKKDVRKGMVLVDPKVKPVASMVFEAEILVLHHPTTIKPNYQAMLHIGSVR 82
Cdd:COG5256  268 VKSIemHHEELEQAEP--GDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQ 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  83 QTATLVSM--------GKEV------LRTGDRDKVQFKFIRqPEYIRPgtkmvFRE------------GRTKAVGTVSSV 136
Cdd:COG5256  346 VACTFVELvskldprtGQVKeenpqfLKTGDAAIVKIKPTK-PLVIEK-----FKEfpqlgrfairdmGQTVAAGVVLDV 419


                 ....
gi 922581324 137 VPQE 140
Cdd:COG5256  420 KPKK 423
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 5-140 4.52e-07

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 49.15  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324   5 IKSIHRKRMPVGIVKCGQSASFALKKIPKKDVRKGMVLVDPKVKPVASMVFEAEILVLHHPTTIKPNYQAMLHIGSVRQT 84
Cdd:PRK12317 269 VKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVA 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  85 ATLVSMGKEV--------------LRTGDRDKVQFKFIRqPEYIRPgtkmvFRE------------GRTKAVGTVSSVVP 138
Cdd:PRK12317 349 CTFEELVKKLdprtgqvaeenpqfIKTGDAAIVKIKPTK-PLVIEK-----VKEipqlgrfairdmGQTIAAGMVIDVKP 422


                 ..
gi 922581324 139 QE 140
Cdd:PRK12317 423 AK 424
PRK12736 PRK12736
elongation factor Tu; Reviewed
 21-137 1.76e-05

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 44.16  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  21 GQSASFALKKIPKKDVRKGMVLVDPK-VKPvaSMVFEAEILVL-------HHP--TTIKPnyQAMLHIGSVRQTATLVSm 90
Cdd:PRK12736 272 GDNVGVLLRGVDRDEVERGQVLAKPGsIKP--HTKFKAEVYILtkeeggrHTPffNNYRP--QFYFRTTDVTGSIELPE- 346

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 922581324  91 GKEVLRTGDRDKVQFKFIRqPEYIRPGTKMVFREG-RTKAVGTVSSVV 137
Cdd:PRK12736 347 GTEMVMPGDNVTITVELIH-PIAMEQGLKFAIREGgRTVGAGTVTEIL 393
tufA CHL00071
elongation factor Tu
 28-137 1.82e-05

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 44.18  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  28 LKKIPKKDVRKGMVLVDPK-VKPVASmvFEAEILVL-------HHPttIKPNYQAMLHI------GSVRQTATLVSMGKE 93
Cdd:CHL00071 289 LRGIQKEDIERGMVLAKPGtITPHTK--FEAQVYILtkeeggrHTP--FFPGYRPQFYVrttdvtGKIESFTADDGSKTE 364

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 922581324  94 VLRTGDRDKVQFKFIrQPEYIRPGTKMVFRE-GRTKAVGTVSSVV 137
Cdd:CHL00071 365 MVMPGDRIKMTVELI-YPIAIEKGMRFAIREgGRTVGAGVVSKIL 408
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 5-150 3.21e-05

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 43.58  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324   5 IKSI--HRKRMPVGIVkcGQSASFALKKIPKKDVRKGMVLVDPKVKP-VASMVFEAEILVLHHPTTIKPNYQAMLHIgsv 81
Cdd:PTZ00141 277 VKSVemHHEQLAEAVP--GDNVGFNVKNVSVKDIKRGYVASDSKNDPaKECADFTAQVIVLNHPGQIKNGYTPVLDC--- 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  82 rQTATLVSMGKEVLRTGDR--DKVQFKfirQPEYIRPG----TKMV---------FRE----GR--------TKAVGTVS 134
Cdd:PTZ00141 352 -HTAHIACKFAEIESKIDRrsGKVLEE---NPKAIKSGdaaiVKMVptkpmcvevFNEypplGRfavrdmkqTVAVGVIK 427

                        170
                 ....*....|....*.
gi 922581324 135 SVVPQESLAQQRAKQK 150
Cdd:PTZ00141 428 SVEKKEGSGTKAAAKA 443
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 55-133 8.29e-04

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: 37.37  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581324  55 FEAEILVLHHPTTIKPNYQAMLHIGSVRQTATLVSMGKEVLRT------------GDRDKVQFKFIRQ------PEYIRP 116
Cdd:cd01513    6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKtkekkppdslqpGENGTVEVELQKPvvlergKEFPTL 85

                         90
                 ....*....|....*..
gi 922581324 117 GTKMVFREGRTKAVGTV 133
Cdd:cd01513   86 GRFALRDGGRTVGAGLI 102
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 54-110 5.91e-03

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: 35.22  E-value: 5.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 922581324  54 VFEAEILVL-HHPTTIKPNYQAMLHIGSVRQTATLVSMGKEV-LRTGDRDKVQFKFIRQ 110
Cdd:cd03704    5 EFEAQIVILdLLKSIITAGYSAVLHIHTAVEEVTITKLLATIdKKTGKKKKKKPKFVKS 63
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 5-46 6.32e-03

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: 34.47  E-value: 6.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 922581324   5 IKSI--HRKRMPVGIvkCGQSASFALKKIPKKDVRKGMVLVDPK 46
Cdd:cd03693   48 VKSVemHHEPLEEAI--PGDNVGFNVKGVSVKDIKRGDVAGDSK 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH