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Conserved domains on  [gi|2217373630|ref|XP_047278336|]
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eukaryotic translation initiation factor 3 subunit H isoform X1 [Homo sapiens]

Protein Classification

eukaryotic translation initiation factor 3 subunit H( domain architecture ID 17857898)

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
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
 170-365 4.62e-119

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: 342.53  E-value: 4.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 170 TAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASS 249
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELEEKSPVADKHQLLDLATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 250 NHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDS 329
Cdd:pfam19445  81 SVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDINKLFKPIQPPPRLDS 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217373630 330 LLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN 365
Cdd:pfam19445 161 LLIAGQINTYCQQVSEFTSQSLGKLFMAESLQEESK 196
MPN super family cl13996
Mpr1p, Pad1p N-terminal (MPN) domains; MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) ...
 100-185 1.11e-19

Mpr1p, Pad1p N-terminal (MPN) domains; MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains are found in the N-terminal termini of proteins with a variety of functions; they are components of the proteasome regulatory subunits, the signalosome (CSN), eukaryotic translation initiation factor 3 (eIF3) complexes, and regulators of transcription factors. These domains are isopeptidases that release ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. Catalytically active MPN domains contain a metalloprotease signature known as the JAB1/MPN/Mov34 metalloenzyme (JAMM) motif. For example, Rpn11 (also known as POH1 or PSMD14), a subunit of the 19S proteasome lid is involved in the ATP-dependent degradation of ubiquitinated proteins, contains the conserved JAMM motif involved in zinc ion coordination. Poh1 is a regulator of c-Jun, an important regulator of cell proliferation, differentiation, survival and death. JAB1 is a component of the COP9 signalosome (CSN), a regulatory particle of the ubiquitin (Ub)/26S proteasome system occurring in all eukaryotic cells; it cleaves the ubiquitin-like protein NEDD8 from the cullin subunit of the SCF (Skp1, Cullins, F-box proteins) family of E3 ubiquitin ligases. AMSH (associated molecule with the SH3 domain of STAM, also known as STAMBP), a member of JAMM/MPN+ deubiquitinases (DUBs), specifically cleaves Lys 63-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. Similarly, BRCC36, part of the nuclear complex that includes BRCA1 protein and is targeted to DNA damage foci after irradiation, specifically disassembles K63-linked polyUb. BRCC36 is aberrantly expressed in sporadic breast tumors, indicative of a potential role in the pathogenesis of the disease. Some variants of the JAB1/MPN domains lack key residues in their JAMM motif and are unable to coordinate a metal ion. Comparisons of key catalytic and metal binding residues explain why the MPN-containing proteins Mov34/PSMD7, Rpn8, CSN6, Prp8p, and the translation initiation factor 3 subunits f (p47) and h (p40) do not show catalytic isopeptidase activity. It has been proposed that the MPN domain in these proteins has a primarily structural function.


The actual alignment was detected with superfamily member smart00232:

Pssm-ID: 472685  Cd Length: 135  Bit Score: 83.96  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630  100 SREASADRWPFQYQMEMMRSLRHVNIDHLHVGWYQS-TYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLK 178
Cdd:smart00232  49 PQDDSVQEYDEDYSHLMDEELKKVNKDLEIVGWYHShPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLR 128


                   ....*..
gi 2217373630  179 AYRLTPK 185
Cdd:smart00232 129 AFRLTPE 135
 
Name Accession Description Interval E-value
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
 170-365 4.62e-119

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: 342.53  E-value: 4.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 170 TAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASS 249
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELEEKSPVADKHQLLDLATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 250 NHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDS 329
Cdd:pfam19445  81 SVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDINKLFKPIQPPPRLDS 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217373630 330 LLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN 365
Cdd:pfam19445 161 LLIAGQINTYCQQVSEFTSQSLGKLFMAESLQEESK 196
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
 111-313 1.53e-102

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: 303.03  E-value: 1.53e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 111 QYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVC 190
Cdd:cd08065    63 DYQLEMMRLLREVNVDHNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELY 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 191 KEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADK-HELLSLASSNHLGKNLQLLMDRVDEMSQD 269
Cdd:cd08065   143 KEGKFSTESLREANLTFSNIFEEIPVVIRNSHLVNALLSELEEDSPSSQSdFDRLDLSTNSFLEKNLELLMESVDELSQE 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217373630 270 IVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEED 313
Cdd:cd08065   223 QGKFNYYQRNLARQQAQIQQWLQKRKAENAQREARGEEPLPEED 266
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 100-185 1.11e-19

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: 83.96  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630  100 SREASADRWPFQYQMEMMRSLRHVNIDHLHVGWYQS-TYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLK 178
Cdd:smart00232  49 PQDDSVQEYDEDYSHLMDEELKKVNKDLEIVGWYHShPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLR 128


                   ....*..
gi 2217373630  179 AYRLTPK 185
Cdd:smart00232 129 AFRLTPE 135
MPN_euk_non_mb cd08057
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non ...
 110-217 9.29e-13

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: 65.54  E-value: 9.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 110 FQYQMEMMRSLRHVNIDHLHVGWYQSTYYGS---FVTRALLDSQFSYQHaIEESVVLIYDPIK-TAQGSLSLKAYRLTPK 185
Cdd:cd08057    59 TEYLEKRYNLHKKVYPQEKIVGWYSIGSNNSneiSKSDNSLHSQFSLIS-EENPLILILDPSLqSDSEKLEISTFTSAQR 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217373630 186 LMEVCKEKdfspealkkaniTFEYMFEEVPIV 217
Cdd:cd08057   138 EENGAEIT------------YEIGTEETERIA 157
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 110-159 2.11e-09

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: 54.66  E-value: 2.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217373630 110 FQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEE 159
Cdd:pfam01398  68 QEYMENMHEMLKKVNRKEEVVGWYHTHPGLCWLSSVDVHTHALYQRMIPE 117
 
Name Accession Description Interval E-value
eIF3h_C pfam19445
C-terminal region of eIF3h; This entry represents a C-terminal helical region present in ...
 170-365 4.62e-119

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: 342.53  E-value: 4.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 170 TAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASS 249
Cdd:pfam19445   1 TTQGFLSLKAYRLTPAMMEFYKEKDFSPESLKKANIGFENMFEEIPVVIKNSHLVNVLLCELEEKSPVADKHQLLDLATS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 250 NHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDS 329
Cdd:pfam19445  81 SVLEKNLQQLMECVDDMSQDTNKYINYQRQVSRQQQQKQQYLQKRQQENAQRQQRGEPPLPEEDINKLFKPIQPPPRLDS 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217373630 330 LLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN 365
Cdd:pfam19445 161 LLIAGQINTYCQQVSEFTSQSLGKLFMAESLQEESK 196
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
 111-313 1.53e-102

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: 303.03  E-value: 1.53e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 111 QYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVC 190
Cdd:cd08065    63 DYQLEMMRLLREVNVDHNHVGWYQSTYLGSFFTRDLIETQYNYQEAIEESVVLVYDPSKTSQGSLSLKAYRLSEKFMELY 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 191 KEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADK-HELLSLASSNHLGKNLQLLMDRVDEMSQD 269
Cdd:cd08065   143 KEGKFSTESLREANLTFSNIFEEIPVVIRNSHLVNALLSELEEDSPSSQSdFDRLDLSTNSFLEKNLELLMESVDELSQE 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217373630 270 IVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEED 313
Cdd:cd08065   223 QGKFNYYQRNLARQQAQIQQWLQKRKAENAQREARGEEPLPEED 266
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 100-185 1.11e-19

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: 83.96  E-value: 1.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630  100 SREASADRWPFQYQMEMMRSLRHVNIDHLHVGWYQS-TYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLK 178
Cdd:smart00232  49 PQDDSVQEYDEDYSHLMDEELKKVNKDLEIVGWYHShPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLR 128


                   ....*..
gi 2217373630  179 AYRLTPK 185
Cdd:smart00232 129 AFRLTPE 135
MPN_euk_non_mb cd08057
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non ...
 110-217 9.29e-13

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: 65.54  E-value: 9.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217373630 110 FQYQMEMMRSLRHVNIDHLHVGWYQSTYYGS---FVTRALLDSQFSYQHaIEESVVLIYDPIK-TAQGSLSLKAYRLTPK 185
Cdd:cd08057    59 TEYLEKRYNLHKKVYPQEKIVGWYSIGSNNSneiSKSDNSLHSQFSLIS-EENPLILILDPSLqSDSEKLEISTFTSAQR 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217373630 186 LMEVCKEKdfspealkkaniTFEYMFEEVPIV 217
Cdd:cd08057   138 EENGAEIT------------YEIGTEETERIA 157
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 110-159 2.11e-09

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: 54.66  E-value: 2.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217373630 110 FQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEE 159
Cdd:pfam01398  68 QEYMENMHEMLKKVNRKEEVVGWYHTHPGLCWLSSVDVHTHALYQRMIPE 117
 
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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