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Conserved domains on  [gi|45549263|ref|NP_524834|]
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eukaryotic translation initiation factor 3 subunit h, isoform A [Drosophila melanogaster]

Protein Classification

eukaryotic translation initiation factor 3 subunit H( domain architecture ID 10169158)

eukaryotic translation initiation factor 3 subunit H is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
20-281 6.50e-128

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs.


:

Pssm-ID: 163696 [Multi-domain]  Cd Length: 266  Bit Score: 366.59  E-value: 6.50e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  20 NYVQCDGLAVMKMVKHCHEESSnmDLAQGALLGLVVDKCLEITNCFPFPKSGDE-----TMDEEMYQLTVMRRLRRVNVD 94
Cdd:cd08065   1 TSVQIDGLVVLKIIKHCKEELP--ELVQGQLLGLDVGGTLEVTNCFPFPKSEEDdsdraDEDIADYQLEMMRLLREVNVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  95 HLHVGWYQSSDVGNSLSMALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRTLKVG 174
Cdd:cd08065  79 HNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELYKEGKFSTESLREANLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263 175 YENLFAEIPIVIKNSPLTNIMMSELNELLP-EDKGHNFLDLGTATVLENQMRSLIERVDELYQEAVRYNKYQQVVFKQDT 253
Cdd:cd08065 159 FSNIFEEIPVVIRNSHLVNALLSELEEDSPsSQSDFDRLDLSTNSFLEKNLELLMESVDELSQEQGKFNYYQRNLARQQA 238
                       250       260
                ....*....|....*....|....*...
gi 45549263 254 EKHRALAKLAAENAVRTSKGEPTVPEEE 281
Cdd:cd08065 239 QIQQWLQKRKAENAQREARGEEPLPEED 266
 
Name Accession Description Interval E-value
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
20-281 6.50e-128

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs.


Pssm-ID: 163696 [Multi-domain]  Cd Length: 266  Bit Score: 366.59  E-value: 6.50e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  20 NYVQCDGLAVMKMVKHCHEESSnmDLAQGALLGLVVDKCLEITNCFPFPKSGDE-----TMDEEMYQLTVMRRLRRVNVD 94
Cdd:cd08065   1 TSVQIDGLVVLKIIKHCKEELP--ELVQGQLLGLDVGGTLEVTNCFPFPKSEEDdsdraDEDIADYQLEMMRLLREVNVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  95 HLHVGWYQSSDVGNSLSMALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRTLKVG 174
Cdd:cd08065  79 HNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELYKEGKFSTESLREANLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263 175 YENLFAEIPIVIKNSPLTNIMMSELNELLP-EDKGHNFLDLGTATVLENQMRSLIERVDELYQEAVRYNKYQQVVFKQDT 253
Cdd:cd08065 159 FSNIFEEIPVVIRNSHLVNALLSELEEDSPsSQSDFDRLDLSTNSFLEKNLELLMESVDELSQEQGKFNYYQRNLARQQA 238
                       250       260
                ....*....|....*....|....*...
gi 45549263 254 EKHRALAKLAAENAVRTSKGEPTVPEEE 281
Cdd:cd08065 239 QIQQWLQKRKAENAQREARGEEPLPEED 266
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
138-329 9.55e-75

C-terminal region of eIF3h; This entry represents a C-terminal helical region present in eukaryotic initiation factor 3 chain H. This protein is part of the eIF3 complex that is involved in eukaryotic translation initiation. eIF3 is a large and structurally complex molecular assembly that, in the majority of eukaryotes, consists of 11-13 subunits (eIF3a-IF3m) with a molecular weight of 600-800 kDa.


Pssm-ID: 466087  Cd Length: 196  Bit Score: 228.89  E-value: 9.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263   138 SSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRTLKVGYENLFAEIPIVIKNSPLTNIMMSELNELLPEDKGHNFLDLGTA 217
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELEEKSPVADKHQLLDLATS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263   218 TVLENQMRSLIERVDELYQEAVRYNKYQQVVFKQDTEKHRALAKLAAENAVRTSKGEPTVPEEEVIKQFRPMTAPNRLTA 297
Cdd:pfam19445  81 SVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDINKLFKPIQPPPRLDS 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 45549263   298 TITSGQINTHAQHIAQFCSQSLAKLFITESLQ 329
Cdd:pfam19445 161 LLIAGQINTYCQQVSEFTSQSLGKLFMAESLQ 192
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
21-152 1.84e-16

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 74.72  E-value: 1.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263     21 YVQCDGLAVMKMVKHCHEESSNMdlAQGALLGLVVDKCLEITNCFPFPKSGDETM---DEEMYQLTVMRRLRRVNVDHLH 97
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRDGPEE--VCGVLLGKSNKDRPEVKEVFAVPNEPQDDSvqeYDEDYSHLMDEELKKVNKDLEI 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 45549263     98 VGWYQS-SDVGNSLSMALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTP 152
Cdd:smart00232  79 VGWYHShPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLRAFRLTP 134
 
Name Accession Description Interval E-value
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
20-281 6.50e-128

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; Eukaryotic translation initiation factor 3 (eIF3) subunit h (eIF3h; eIF3 subunit 3; eIF3S3; eIF3-gamma; eIF3-p40) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.Together with eIF3e and eIF3f, eIF3h stabilizes the eIF3 complex. Results suggest that eIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells. For example, EIF3h gene amplification is common in late-stage prostate cancer suggesting that it may be functionally involved in the progression of the disease. It has been shown that coamplification of MYC, a well characterized oncogene involved in cell growth, differentiation, and apoptosis, and EIF3h in patients with non-small cell lung cancer (NSCLC) improves survival if treated with the Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor (EGFR-TKI), Gefitinib. Plant eIF3h is implicated in translation of specific mRNAs.


Pssm-ID: 163696 [Multi-domain]  Cd Length: 266  Bit Score: 366.59  E-value: 6.50e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  20 NYVQCDGLAVMKMVKHCHEESSnmDLAQGALLGLVVDKCLEITNCFPFPKSGDE-----TMDEEMYQLTVMRRLRRVNVD 94
Cdd:cd08065   1 TSVQIDGLVVLKIIKHCKEELP--ELVQGQLLGLDVGGTLEVTNCFPFPKSEEDdsdraDEDIADYQLEMMRLLREVNVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  95 HLHVGWYQSSDVGNSLSMALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRTLKVG 174
Cdd:cd08065  79 HNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELYKEGKFSTESLREANLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263 175 YENLFAEIPIVIKNSPLTNIMMSELNELLP-EDKGHNFLDLGTATVLENQMRSLIERVDELYQEAVRYNKYQQVVFKQDT 253
Cdd:cd08065 159 FSNIFEEIPVVIRNSHLVNALLSELEEDSPsSQSDFDRLDLSTNSFLEKNLELLMESVDELSQEQGKFNYYQRNLARQQA 238
                       250       260
                ....*....|....*....|....*...
gi 45549263 254 EKHRALAKLAAENAVRTSKGEPTVPEEE 281
Cdd:cd08065 239 QIQQWLQKRKAENAQREARGEEPLPEED 266
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
138-329 9.55e-75

C-terminal region of eIF3h; This entry represents a C-terminal helical region present in eukaryotic initiation factor 3 chain H. This protein is part of the eIF3 complex that is involved in eukaryotic translation initiation. eIF3 is a large and structurally complex molecular assembly that, in the majority of eukaryotes, consists of 11-13 subunits (eIF3a-IF3m) with a molecular weight of 600-800 kDa.


Pssm-ID: 466087  Cd Length: 196  Bit Score: 228.89  E-value: 9.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263   138 SSRGFLCLKAYRLTPQAIQMYKDGDFTPEAFRTLKVGYENLFAEIPIVIKNSPLTNIMMSELNELLPEDKGHNFLDLGTA 217
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELEEKSPVADKHQLLDLATS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263   218 TVLENQMRSLIERVDELYQEAVRYNKYQQVVFKQDTEKHRALAKLAAENAVRTSKGEPTVPEEEVIKQFRPMTAPNRLTA 297
Cdd:pfam19445  81 SVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDINKLFKPIQPPPRLDS 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 45549263   298 TITSGQINTHAQHIAQFCSQSLAKLFITESLQ 329
Cdd:pfam19445 161 LLIAGQINTYCQQVSEFTSQSLGKLFMAESLQ 192
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
21-152 1.84e-16

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 74.72  E-value: 1.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263     21 YVQCDGLAVMKMVKHCHEESSNMdlAQGALLGLVVDKCLEITNCFPFPKSGDETM---DEEMYQLTVMRRLRRVNVDHLH 97
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRDGPEE--VCGVLLGKSNKDRPEVKEVFAVPNEPQDDSvqeYDEDYSHLMDEELKKVNKDLEI 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 45549263     98 VGWYQS-SDVGNSLSMALLESQYHYQTSIEESVVVVYDTQKSSRGFLCLKAYRLTP 152
Cdd:smart00232  79 VGWYHShPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLRAFRLTP 134
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
22-127 1.76e-14

JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain and PAD-1-like domain, JABP1 domain or JAMM domain. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates.


Pssm-ID: 396120  Cd Length: 117  Bit Score: 68.91  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263    22 VQCDGLAVMKMVKHCHEESSNMDLAQGALLGLVV-DKCLEITNCFPFPKSGDETMDE-----EMYQLTVMRRLRRVNVDH 95
Cdd:pfam01398   6 VIIHPLVLLKILDHANRGGKIGEEVMGVLLGKLEgDGTIEITNSFALPQEETEDDVNavaldQEYMENMHEMLKKVNRKE 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 45549263    96 LHVGWYQSSDVGNSLSMALLESQYHYQTSIEE 127
Cdd:pfam01398  86 EVVGWYHTHPGLCWLSSVDVHTHALYQRMIPE 117
MPN_euk_non_mb cd08057
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non ...
22-139 1.23e-12

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non metal-binding); eukaryotic; This family contains MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains variants lacking key residues in the JAB1/MPN/Mov34 metalloenzyme (JAMM) motif and are unable to coordinate a metal ion. Comparisons of key catalytic and metal binding residues explain why the MPN-containing proteins Rpn7/PSMD7, Rpn8/PSMD8, CSN6, Prp8p, and the translation initiation factor 3 subunits f and h do not show catalytic isopeptidase activity. It has been proposed that the MPN domain in these proteins has a primarily structural function. Rpn7 is known to be critical for the integrity of the 26S proteasome complex by establishing a correct lid structure. It is necessary for the incorporation/anchoring of Rpn3 and Rpn12 to the lid and essential for viability and normal mitosis. CSN6 is a highly conserved protein complex with diverse functions, including several important intracellular pathways such as the ubiquitin/proteasome system, DNA repair, cell cycle, developmental changes, and some aspects of immune responses. It cleaves ubiquitin-like protein Nedd8 (neural precursor cell expressed, developmentally downregulated 8)) in the cullin 1 in cells. EIF3f s a potent inhibitor of HIV-1 replication as well as an important negative regulator of cell growth and proliferation. EIF3h regulates cell growth and viability, and that over-expression of the gene may provide growth advantage to prostate, breast, and liver cancer cells.


Pssm-ID: 163688 [Multi-domain]  Cd Length: 157  Bit Score: 64.77  E-value: 1.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  22 VQCDGLAVMKMVKHCHEESSNMDLAQGALLGLVVDKCLEITNCFPFPKSGDETMD-------EEMYQLtvmrrLRRVNVD 94
Cdd:cd08057   1 VQLHPLVLLNISDHYTRRKYGIKRVIGVLLGYVDGDKIEVTNSFELPFDEEEESIfidteylEKRYNL-----HKKVYPQ 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 45549263  95 HLHVGWYQSSDVGNSLSMAlLESQYHYQ---TSIEESVVVVYDTQKSS 139
Cdd:cd08057  76 EKIVGWYSIGSNNSNEISK-SDNSLHSQfslISEENPLILILDPSLQS 122
MPN_RPN11_CSN5 cd08069
Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit ...
27-266 2.34e-09

Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit CSN5; This family contains proteasomal regulatory protein Rpn11 (26S proteasome regulatory subunit rpn11; PAD1; POH1; RPN11; PSMD14; Rpn11 subunit of the 19S-proteasome; regulatory particle number 11) and signalosomal CSN5 (COP9 signalosome complex subunit 5; COP9 complex homolog subunit 5; c-Jun activation domain-binding protein-1; CSN5/JAB1; JAB1). COP9 signalosome (CSN) and the proteasome lid are paralogous complexes and their respective subunits CSN5 and Rpn11 are most closely related between the two complexes, both containing the conserved JAMM (JAB1/MPN/Mov34 metalloenzyme) motif involved in zinc ion coordination and providing the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology; mutations in Rpn11 cause cell cycle and mitochondrial defects, temperature sensitivity and sensitivity to DNA damaging reagents such as UV. It has been shown that the C-terminal region of Rpn11 is involved in the regulation of the mitochondrial fission and tubulation processes. CSN5, one of the eight subunits of CSN, is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Its MPN+ domain is critical for the physical interaction of RUNX3 and Jab1. It has been suggested that the direct interaction of CSN5/JAB1 with p27 provides p27 with a leucine-rich nuclear export signal (NES), which is required for binding to chromosomal region maintenance 1 (CRM1), and facilitates nuclear export. The over-expression of CSN5/JAB1 also has been implicated in cancer initiation and progression, including cancer of the lung, pancreas, mouth, thyroid, and breast, suggesting that the oncogenic activity of CSN5 is associated with the down-regulation of RUNX3.


Pssm-ID: 163700 [Multi-domain]  Cd Length: 268  Bit Score: 57.26  E-value: 2.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  27 LAVMKMVKHCHEESSN--MdlaqGALLGLVVDKCLEITNCFPFPKSGDET-------MDEEMYQLTVMRRLRRV-NVdhl 96
Cdd:cd08069  17 LALLKMLKHARAGGPIevM----GLMLGKVDDYTIIVVDVFALPVEGTETrvnaqdeFQEYMVQYEMLKQTGRPeNV--- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  97 hVGWYQS--------S--DVGNSLSMallesqyhyQTSIEESVVVVYD-TQKSSRGFLCLKAYRLTPQAiQMYKDGDFTP 165
Cdd:cd08069  90 -VGWYHShpgygcwlSgiDVNTQQLN---------QQLQDPFVAVVVDpIRSLVKGKVVIGAFRTIPPG-YKPLEPRQTT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263 166 EAFRTLKV-------GYENLFAEIPIVIKNSPL-TNIMMSELNELLPEDKGHNFLDLGTATVLENQMRSLIERVDELYQE 237
Cdd:cd08069 159 SNIGHLPKpkiedfgGHNKQYYSLPIEYFKSSLdRKLLLNLWNKYWVNTLSLSPLLENSNEYTIKQILDLAEKLEKAEQQ 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 45549263 238 AVRYNKYQQV---VFKQDteKHRALAKLAAEN 266
Cdd:cd08069 239 EERLTGEELDianVGKLD--KARDSSKIHLEE 268
MPN_eIF3f cd08064
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF3f; ...
48-231 1.38e-06

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF3f; Eukaryotic translation initiation factor 3 (eIF3) subunit F (eIF3F; EIF3S5; eIF3-p47; eukaryotic translation initiation factor 3, subunit 5 epsilon, 47kDa; Mov34/MPN/PAD-1 family protein) is an evolutionarily non-conserved subunit of the functional core that comprises eIF3a, eIF3b, eIF3c, eIF3e, eIF3f, and eIF3h, and contains the MPN domain. However, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity. It has been shown that eIF3f mRNA expression is significantly decreased in many human tumors including pancreatic cancer and melanoma. EIF3f is a potent inhibitor of HIV-1 replication; it mediates restriction of HIV-1 expression through several factors including the serine/arginine-rich (SR) protein 9G8, and cyclin-dependent kinase 11 (CDK11). EIF3f phosphorylation by CDK11 is important in regulating its function in translation and apoptosis. It enhances its association with the core eIF3 subunits during apoptosis, suggesting that eIF3f may inhibit translation by increasing the binding to the eIF3 complex during apoptosis. Thus, eIF3f may be an important negative regulator of cell growth and proliferation.


Pssm-ID: 163695 [Multi-domain]  Cd Length: 265  Bit Score: 49.13  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263  48 GALLGLVVDKCLEITNCF--PFPKSGDE-TMD----EEMYQLtvmrrLRRVNVDHLHVGWYQSSDVGNSLSmALLESQYH 120
Cdd:cd08064  27 GTLLGTRSEGEVEITNCFavPHNESEDQvAVDmeyhRTMYEL-----HQKVNPKEVIVGWYATGSEITEHS-ALIHDYYS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549263 121 YQTSIEESVVVVYDTQKSSrGFLCLKAYRLTPQAIqmykdgdfTPEAfrtlkvgYENLFAEIPIVIKNSPLTNIMMSELN 200
Cdd:cd08064 101 RECTSYNPIHLTVDTSLDD-GKMSIKAYVSSPLGV--------PGKT-------LGSMFVPIPLELLYSEAERVALDLLA 164
                       170       180       190
                ....*....|....*....|....*....|...
gi 45549263 201 ELLPEDKGHNFLDLGTATVLE--NQMRSLIERV 231
Cdd:cd08064 165 KTLASPSRSAPLTSDLEQLEAslEKLQEMLDRV 197
 
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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