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Conserved domains on  [gi|15928893|gb|AAH14912|]
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Eukaryotic translation initiation factor 3, subunit D [Homo sapiens]

Protein Classification

eukaryotic translation initiation factor 3 subunit D( domain architecture ID 10523878)

eukaryotic translation initiation factor 3 (eIF-3) subunit D is the mRNA cap-binding component of the eIF-3 complex, which is required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eIF-3_zeta pfam05091
Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of ...
4-521 0e+00

Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of eukaryotic translation initiation factor 3 subunit 7 (eIF-3 zeta/eIF3 p66/eIF3d). Eukaryotic initiation factor 3 is a multi-subunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. The gene coding for the protein has been implicated in cancer in mammals.


:

Pssm-ID: 461547  Cd Length: 521  Bit Score: 875.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893     4 FMTPVIQDNPSGWGPCA-VPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQ-FGGG--SQYAYFHEEDESS 79
Cdd:pfam05091   1 FELPELPDNPDGWGPPSsLPEEFKDIPYAPFSKSDKLGKIADWTSTMAKDGRQQRGRYQQyYGAGsaSAFAYQHAEDESS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893    80 FQLVDTARTQKT---AYQRNRMRFAQRNLRRDKDRRNMLQFNlqilpksakQKERERIRLQKKFQKQFGVRQKWDQKSQK 156
Cdd:pfam05091  81 FSLVDNSRAKKKrrgGRQRQRGRGRGGFQRRRGGQQAFNQKQ---------GGGRGASRGGRGGRGRRFGWKDWNDKPQR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   157 PRDSSVEVRSDWEVKEEMDFPQLMKMRyLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIR 236
Cdd:pfam05091 152 NREASVEVRPDWEVLEEIDFSRLSKLN-LEVPEPEDLDSYGTLYYYDKSYDRITVKNERPLQKLDRIFYNVTTSDDPVIQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   237 KLAK-TQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAME 315
Cdd:pfam05091 231 ELAKeNKANVFATDAILSTLMCATRSVYSWDIVVTKVGNKLFFDKRDGSPFDLLTVNETAADPPQDDEDSINSPSSLSLE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   316 ATYINHNFSQQCLRMG-KERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDD----IDLIVRCEHDGVMTGANGEVSF 390
Cdd:pfam05091 311 ATYINQNFSQQVLKEGeEEKVKFEEPNPFYNPDEETEPLASVAYRYRKFDLGDGedepINLIVRTEVDAVLKGTNGELQF 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   391 INIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQ 470
Cdd:pfam05091 391 LTIKALNEFDSKAQGAADWRTKLDSQRGAVLATELKNNSCKLAKWTVQALLAGADQMKLGYVSRANPRDNSNHVILGTQS 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15928893   471 FKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYS 521
Cdd:pfam05091 471 YKPRDFATQINLNLDNGWGIVRTIIDLCMKQPDGKYVLVKDPNKPVIRLYS 521
 
Name Accession Description Interval E-value
eIF-3_zeta pfam05091
Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of ...
4-521 0e+00

Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of eukaryotic translation initiation factor 3 subunit 7 (eIF-3 zeta/eIF3 p66/eIF3d). Eukaryotic initiation factor 3 is a multi-subunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. The gene coding for the protein has been implicated in cancer in mammals.


Pssm-ID: 461547  Cd Length: 521  Bit Score: 875.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893     4 FMTPVIQDNPSGWGPCA-VPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQ-FGGG--SQYAYFHEEDESS 79
Cdd:pfam05091   1 FELPELPDNPDGWGPPSsLPEEFKDIPYAPFSKSDKLGKIADWTSTMAKDGRQQRGRYQQyYGAGsaSAFAYQHAEDESS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893    80 FQLVDTARTQKT---AYQRNRMRFAQRNLRRDKDRRNMLQFNlqilpksakQKERERIRLQKKFQKQFGVRQKWDQKSQK 156
Cdd:pfam05091  81 FSLVDNSRAKKKrrgGRQRQRGRGRGGFQRRRGGQQAFNQKQ---------GGGRGASRGGRGGRGRRFGWKDWNDKPQR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   157 PRDSSVEVRSDWEVKEEMDFPQLMKMRyLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIR 236
Cdd:pfam05091 152 NREASVEVRPDWEVLEEIDFSRLSKLN-LEVPEPEDLDSYGTLYYYDKSYDRITVKNERPLQKLDRIFYNVTTSDDPVIQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   237 KLAK-TQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAME 315
Cdd:pfam05091 231 ELAKeNKANVFATDAILSTLMCATRSVYSWDIVVTKVGNKLFFDKRDGSPFDLLTVNETAADPPQDDEDSINSPSSLSLE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   316 ATYINHNFSQQCLRMG-KERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDD----IDLIVRCEHDGVMTGANGEVSF 390
Cdd:pfam05091 311 ATYINQNFSQQVLKEGeEEKVKFEEPNPFYNPDEETEPLASVAYRYRKFDLGDGedepINLIVRTEVDAVLKGTNGELQF 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   391 INIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQ 470
Cdd:pfam05091 391 LTIKALNEFDSKAQGAADWRTKLDSQRGAVLATELKNNSCKLAKWTVQALLAGADQMKLGYVSRANPRDNSNHVILGTQS 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15928893   471 FKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYS 521
Cdd:pfam05091 471 YKPRDFATQINLNLDNGWGIVRTIIDLCMKQPDGKYVLVKDPNKPVIRLYS 521
 
Name Accession Description Interval E-value
eIF-3_zeta pfam05091
Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of ...
4-521 0e+00

Eukaryotic translation initiation factor 3 subunit 7 (eIF-3); This family is made up of eukaryotic translation initiation factor 3 subunit 7 (eIF-3 zeta/eIF3 p66/eIF3d). Eukaryotic initiation factor 3 is a multi-subunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. The gene coding for the protein has been implicated in cancer in mammals.


Pssm-ID: 461547  Cd Length: 521  Bit Score: 875.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893     4 FMTPVIQDNPSGWGPCA-VPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQ-FGGG--SQYAYFHEEDESS 79
Cdd:pfam05091   1 FELPELPDNPDGWGPPSsLPEEFKDIPYAPFSKSDKLGKIADWTSTMAKDGRQQRGRYQQyYGAGsaSAFAYQHAEDESS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893    80 FQLVDTARTQKT---AYQRNRMRFAQRNLRRDKDRRNMLQFNlqilpksakQKERERIRLQKKFQKQFGVRQKWDQKSQK 156
Cdd:pfam05091  81 FSLVDNSRAKKKrrgGRQRQRGRGRGGFQRRRGGQQAFNQKQ---------GGGRGASRGGRGGRGRRFGWKDWNDKPQR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   157 PRDSSVEVRSDWEVKEEMDFPQLMKMRyLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIR 236
Cdd:pfam05091 152 NREASVEVRPDWEVLEEIDFSRLSKLN-LEVPEPEDLDSYGTLYYYDKSYDRITVKNERPLQKLDRIFYNVTTSDDPVIQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   237 KLAK-TQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAME 315
Cdd:pfam05091 231 ELAKeNKANVFATDAILSTLMCATRSVYSWDIVVTKVGNKLFFDKRDGSPFDLLTVNETAADPPQDDEDSINSPSSLSLE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   316 ATYINHNFSQQCLRMG-KERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDD----IDLIVRCEHDGVMTGANGEVSF 390
Cdd:pfam05091 311 ATYINQNFSQQVLKEGeEEKVKFEEPNPFYNPDEETEPLASVAYRYRKFDLGDGedepINLIVRTEVDAVLKGTNGELQF 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15928893   391 INIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQ 470
Cdd:pfam05091 391 LTIKALNEFDSKAQGAADWRTKLDSQRGAVLATELKNNSCKLAKWTVQALLAGADQMKLGYVSRANPRDNSNHVILGTQS 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15928893   471 FKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYS 521
Cdd:pfam05091 471 YKPRDFATQINLNLDNGWGIVRTIIDLCMKQPDGKYVLVKDPNKPVIRLYS 521
 
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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