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Conserved domains on  [gi|145348207|ref|XP_001418547|]
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predicted protein [Ostreococcus lucimarinus CCE9901]

Protein Classification

PLN03246 family protein( domain architecture ID 11477601)

PLN03246 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03246 PLN03246
26S proteasome regulatory subunit; Provisional
 24-318 0e+00

26S proteasome regulatory subunit; Provisional


:

Pssm-ID: 215645 [Multi-domain]  Cd Length: 303  Bit Score: 547.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  24 EVVVHPLVLLSVVDHFRRCDEN--KRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAK 101
Cdd:PLN03246   7 KVVVHPLVLLSIVDHYNRVAKDtrKRVVGVLLGSSFRGRVDVTNSFAVPFEEDDKDPSIWFLDHNYLESMFGMFKRINAK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 102 EKIVGWYSTGPKLRESDIDIHELFYAYTPEPVLVIVDVRAENANIPTSAFAAQIEVKEDGTEKQQKTFVHVPNSIEAFEA 181
Cdd:PLN03246  87 EHVVGWYSTGPKLRENDLDIHELFNDYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQKVFVHVPSEIGAHEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 182 EEIGVEHLLRDVKDNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPNLNLEDYVK 261
Cdd:PLN03246 167 EEIGVEHLLRDVKDTTVSTLATEVTGKLTALKGLDARLREIRSYLDLVVEGKLPLNHEILYHLQDVFNLLPNLNVEELVK 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145348207 262 GFNVSTNDAMLVVYLSSLIRSVIALHDLINNKATNKERERALDAPGASDAEKDTDKE 318
Cdd:PLN03246 247 AFAVKTNDMMLVIYLSSLIRSVIALHNLINNKILNKEHEKAEDAKPAAKPAKKGSGK 303
 
Name Accession Description Interval E-value
PLN03246 PLN03246
26S proteasome regulatory subunit; Provisional
 24-318 0e+00

26S proteasome regulatory subunit; Provisional


Pssm-ID: 215645 [Multi-domain]  Cd Length: 303  Bit Score: 547.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  24 EVVVHPLVLLSVVDHFRRCDEN--KRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAK 101
Cdd:PLN03246   7 KVVVHPLVLLSIVDHYNRVAKDtrKRVVGVLLGSSFRGRVDVTNSFAVPFEEDDKDPSIWFLDHNYLESMFGMFKRINAK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 102 EKIVGWYSTGPKLRESDIDIHELFYAYTPEPVLVIVDVRAENANIPTSAFAAQIEVKEDGTEKQQKTFVHVPNSIEAFEA 181
Cdd:PLN03246  87 EHVVGWYSTGPKLRENDLDIHELFNDYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQKVFVHVPSEIGAHEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 182 EEIGVEHLLRDVKDNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPNLNLEDYVK 261
Cdd:PLN03246 167 EEIGVEHLLRDVKDTTVSTLATEVTGKLTALKGLDARLREIRSYLDLVVEGKLPLNHEILYHLQDVFNLLPNLNVEELVK 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145348207 262 GFNVSTNDAMLVVYLSSLIRSVIALHDLINNKATNKERERALDAPGASDAEKDTDKE 318
Cdd:PLN03246 247 AFAVKTNDMMLVIYLSSLIRSVIALHNLINNKILNKEHEKAEDAKPAAKPAKKGSGK 303
MPN_RPN7_8 cd08062
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in 19S ...
 24-301 4.89e-174

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in 19S proteasomal subunits Rpn7 and Rpn8; This family includes lid subunits of the 26 S proteasome regulatory particles, Rpn7 (PSMD7; proteasome 26S non-ATPase subunit 7; p44), and Rpn8 (PSMD8; proteasome 26S non-ATPase subunit 8; p40; Mov34). Rpn7 is known to be critical for the integrity of the 26 S 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. Rpn7 and Rpn8 are ATP-independent components of the 19S regulator subunit, and contain the MPN structural motif on its N-terminal region. However, while they show a typical MPN metalloprotease fold, they lack the canonical JAMM motif, and therefore do not show catalytic isopeptidase activity. It is suggested that Rpn7 function is primarily structural.


Pssm-ID: 163693 [Multi-domain]  Cd Length: 280  Bit Score: 483.62  E-value: 4.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  24 EVVVHPLVLLSVVDHFRRC--DENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAK 101
Cdd:cd08062    2 KVVVHPLVLLSVVDHYNRVakGTSKRVVGVLLGSWKKGVLDVTNSFAVPFEEDEKDPSVWFLDHNYLENMYGMFKKVNAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 102 EKIVGWYSTGPKLRESDIDIHELFYAYTPEPVLVIVDVRAENANIPTSAFAAQIEVKEDGTEkQQKTFVHVPNSIEAFEA 181
Cdd:cd08062   82 EKIVGWYSTGPKLRPNDLDINELFRRYCPNPVLVIIDVRPKDLGLPTEAYIAVEEVHDDGTP-TSKTFVHVPSEIGAEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 182 EEIGVEHLLRDVKDNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPNLNLEDYVK 261
Cdd:cd08062  161 EEVGVEHLLRDIKDVTVSTLSTRVTNKLNSLKGLQSKLKEIKDYLQLVVEGKLPINHQIIYNLQDIFNLLPNLNLPELVK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 145348207 262 GFNVSTNDAMLVVYLSSLIRSVIALHDLINNKATNKERER 301
Cdd:cd08062  241 AFAVKTNDQMLVIYLSSLIRSVIALHNLINNKIANKEAEK 280
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 25-131 5.80e-39

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: 134.01  E-value: 5.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207   25 VVVHPLVLLSVVDHF-RRCDENKRVVGVLLGEQRK-GRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAKE 102
Cdd:pfam01398   6 VIIHPLVLLKILDHAnRGGKIGEEVMGVLLGKLEGdGTIEITNSFALPQEETEDDVNAVALDQEYMENMHEMLKKVNRKE 85

                          90       100       110
                  ....*....|....*....|....*....|..
gi 145348207  103 KIVGWYSTGPK---LRESDIDIHELFYAYTPE 131
Cdd:pfam01398  86 EVVGWYHTHPGlcwLSSVDVHTHALYQRMIPE 117
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 24-151 5.54e-31

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: 113.62  E-value: 5.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207    24 EVVVHPLVLLSVVDHFRRCdENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNgiWFLDHSYLENMYRMSKKISAKEK 103
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRD-GPEEVCGVLLGKSNKDRPEVKEVFAVPNEPQDDSV--QEYDEDYSHLMDEELKKVNKDLE 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145348207   104 IVGWYSTGP----KLRESDIDIHELFYAYTPEPVLVIVDVRAENAN-IPTSAF 151
Cdd:smart00232  78 IVGWYHSHPdespFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGrLSLRAF 130
 
Name Accession Description Interval E-value
PLN03246 PLN03246
26S proteasome regulatory subunit; Provisional
 24-318 0e+00

26S proteasome regulatory subunit; Provisional


Pssm-ID: 215645 [Multi-domain]  Cd Length: 303  Bit Score: 547.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  24 EVVVHPLVLLSVVDHFRRCDEN--KRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAK 101
Cdd:PLN03246   7 KVVVHPLVLLSIVDHYNRVAKDtrKRVVGVLLGSSFRGRVDVTNSFAVPFEEDDKDPSIWFLDHNYLESMFGMFKRINAK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 102 EKIVGWYSTGPKLRESDIDIHELFYAYTPEPVLVIVDVRAENANIPTSAFAAQIEVKEDGTEKQQKTFVHVPNSIEAFEA 181
Cdd:PLN03246  87 EHVVGWYSTGPKLRENDLDIHELFNDYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQKVFVHVPSEIGAHEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 182 EEIGVEHLLRDVKDNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPNLNLEDYVK 261
Cdd:PLN03246 167 EEIGVEHLLRDVKDTTVSTLATEVTGKLTALKGLDARLREIRSYLDLVVEGKLPLNHEILYHLQDVFNLLPNLNVEELVK 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145348207 262 GFNVSTNDAMLVVYLSSLIRSVIALHDLINNKATNKERERALDAPGASDAEKDTDKE 318
Cdd:PLN03246 247 AFAVKTNDMMLVIYLSSLIRSVIALHNLINNKILNKEHEKAEDAKPAAKPAKKGSGK 303
MPN_RPN7_8 cd08062
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in 19S ...
 24-301 4.89e-174

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in 19S proteasomal subunits Rpn7 and Rpn8; This family includes lid subunits of the 26 S proteasome regulatory particles, Rpn7 (PSMD7; proteasome 26S non-ATPase subunit 7; p44), and Rpn8 (PSMD8; proteasome 26S non-ATPase subunit 8; p40; Mov34). Rpn7 is known to be critical for the integrity of the 26 S 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. Rpn7 and Rpn8 are ATP-independent components of the 19S regulator subunit, and contain the MPN structural motif on its N-terminal region. However, while they show a typical MPN metalloprotease fold, they lack the canonical JAMM motif, and therefore do not show catalytic isopeptidase activity. It is suggested that Rpn7 function is primarily structural.


Pssm-ID: 163693 [Multi-domain]  Cd Length: 280  Bit Score: 483.62  E-value: 4.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  24 EVVVHPLVLLSVVDHFRRC--DENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAK 101
Cdd:cd08062    2 KVVVHPLVLLSVVDHYNRVakGTSKRVVGVLLGSWKKGVLDVTNSFAVPFEEDEKDPSVWFLDHNYLENMYGMFKKVNAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 102 EKIVGWYSTGPKLRESDIDIHELFYAYTPEPVLVIVDVRAENANIPTSAFAAQIEVKEDGTEkQQKTFVHVPNSIEAFEA 181
Cdd:cd08062   82 EKIVGWYSTGPKLRPNDLDINELFRRYCPNPVLVIIDVRPKDLGLPTEAYIAVEEVHDDGTP-TSKTFVHVPSEIGAEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 182 EEIGVEHLLRDVKDNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPNLNLEDYVK 261
Cdd:cd08062  161 EEVGVEHLLRDIKDVTVSTLSTRVTNKLNSLKGLQSKLKEIKDYLQLVVEGKLPINHQIIYNLQDIFNLLPNLNLPELVK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 145348207 262 GFNVSTNDAMLVVYLSSLIRSVIALHDLINNKATNKERER 301
Cdd:cd08062  241 AFAVKTNDQMLVIYLSSLIRSVIALHNLINNKIANKEAEK 280
MPN_eIF3f cd08064
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF3f; ...
 25-288 8.85e-58

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: 187.41  E-value: 8.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  25 VVVHPLVLLSVVDHF-RRCDENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIwflDHSYLENMYRMSKKISAKEK 103
Cdd:cd08064    1 VRVHPVVLFSILDSYeRRNEGQERVIGTLLGTRSEGEVEITNCFAVPHNESEDQVAV---DMEYHRTMYELHQKVNPKEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 104 IVGWYSTGPKLRESDIDIHELFY--AYTPEPVLVIVDVRAENANIPTSAF-AAQIEVKeDGTEKQQktFVHVPNSIEAFE 180
Cdd:cd08064   78 IVGWYATGSEITEHSALIHDYYSreCTSYNPIHLTVDTSLDDGKMSIKAYvSSPLGVP-GKTLGSM--FVPIPLELLYSE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 181 AEEIGVEHLLRDVKDNTVS-TLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPNLNLEDY 259
Cdd:cd08064  155 AERVALDLLAKTLASPSRSaPLTSDLEQLEASLEKLQEMLDRVLRYVEDVLAGKVKADNAIGRYLMDALTSVPKLDPEEF 234

                        250       260
                 ....*....|....*....|....*....
gi 145348207 260 VKGFNVSTNDAMLVVYLSSLIRSVIALHD 288
Cdd:cd08064  235 EKMFNSSLQDLLMVTYLSNLTKTQLALAE 263
MPN_CSN6 cd08063
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in COP9 ...
 24-302 5.49e-42

Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in COP9 signalosome complex subunit 6; CSN6 (COP9 signalosome subunit 6; COP9 subunit 6; MOV34 homolog, 34 kD) is one of the eight subunits of COP9 signalosome, 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. CSN6 is an MPN-domain protein that directly interacts with the MPN+-domain subunit CSN5. It is cleaved during apoptosis by activated caspases. CSN6 processing occurs in CSN/CRL (cullin-RING Ub ligase) complexes and is followed by the cleavage of Rbx1, the direct interaction partner of CSN6. CSN6 cleavage enhances CSN-mediated deneddylating activity (i.e. cleavage of ubiquitin-like protein Nedd8 (neural precursor cell expressed, developmentally downregulated 8)) in the cullin 1 in cells. The cleavage of Rbx1 and increased deneddylation of cullins inactivate CRLs and presumably stabilize pro-apoptotic factors for final apoptotic steps. While CSN6 shows a typical MPN metalloprotease fold, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.


Pssm-ID: 163694 [Multi-domain]  Cd Length: 288  Bit Score: 147.40  E-value: 5.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  24 EVVVHPLVLLSVVDHFRRC-----DENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIwfLDHSYLENMYRMSKKI 98
Cdd:cd08063    2 SVKLHPLVILNISDHITRHraqsqSEPPRVVGALLGQQDGREIEIENSFELKYDTNEDGEIV--LDKEFLETRLEQFKQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  99 SAKEKIVGWYSTGPKL-RESDIDIHELFYAYTPEPVLVIVD--VRAENANIPTSAFAAQIEVkeDGTEKQQKtFVHVPNS 175
Cdd:cd08063   80 FKDLDFVGWYTTGPGGpTESDLPIHKQILEINESPVLLLLDpeANASGKDLPVTIYESVLEL--VDGEATLR-FRELPYT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 176 IEAFEAEEIGVEHLLR--DVKDNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNLLPN 253
Cdd:cd08063  157 IETGEAERIGVDHVARggASGSSEKSTVAAHLQAQHNAIKMLNSRVELILEYLKAVPVGEVPPDHSILRSISALCSRLPV 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 145348207 254 LNLEDYVKGFNVSTNDAMLVVYLSSLIRSVIALHDLINNKATNKERERA 302
Cdd:cd08063  237 LKSEAFREELLAEYNDVLLVAYLATLTKGCNTLNELVDKFNVVYDRKGS 285
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 25-131 5.80e-39

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: 134.01  E-value: 5.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207   25 VVVHPLVLLSVVDHF-RRCDENKRVVGVLLGEQRK-GRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAKE 102
Cdd:pfam01398   6 VIIHPLVLLKILDHAnRGGKIGEEVMGVLLGKLEGdGTIEITNSFALPQEETEDDVNAVALDQEYMENMHEMLKKVNRKE 85

                          90       100       110
                  ....*....|....*....|....*....|..
gi 145348207  103 KIVGWYSTGPK---LRESDIDIHELFYAYTPE 131
Cdd:pfam01398  86 EVVGWYHTHPGlcwLSSVDVHTHALYQRMIPE 117
MPN_euk_non_mb cd08057
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity (non ...
 25-185 2.24e-33

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: 120.63  E-value: 2.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  25 VVVHPLVLLSVVDHF-RRCDENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDngiWFLDHSYLENMYRMSKKISAKEK 103
Cdd:cd08057    1 VQLHPLVLLNISDHYtRRKYGIKRVIGVLLGYVDGDKIEVTNSFELPFDEEEES---IFIDTEYLEKRYNLHKKVYPQEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207 104 IVGWYSTGPKLR----ESDIDIHELFYAYT-PEPVLVIVDVRAENAN--IPTSAFAAQIEVKEdgtekqqktFVHVPNSI 176
Cdd:cd08057   78 IVGWYSIGSNNSneisKSDNSLHSQFSLISeENPLILILDPSLQSDSekLEISTFTSAQREEN---------GAEITYEI 148


                 ....*....
gi 145348207 177 EAFEAEEIG 185
Cdd:cd08057  149 GTEETERIA 157
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 24-151 5.54e-31

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: 113.62  E-value: 5.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207    24 EVVVHPLVLLSVVDHFRRCdENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNgiWFLDHSYLENMYRMSKKISAKEK 103
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRD-GPEEVCGVLLGKSNKDRPEVKEVFAVPNEPQDDSV--QEYDEDYSHLMDEELKKVNKDLE 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145348207   104 IVGWYSTGP----KLRESDIDIHELFYAYTPEPVLVIVDVRAENAN-IPTSAF 151
Cdd:smart00232  78 IVGWYHSHPdespFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGrLSLRAF 130
MitMem_reg pfam13012
Maintenance of mitochondrial structure and function; This is C-terminal to the Mov24 region of ...
 180-250 1.25e-18

Maintenance of mitochondrial structure and function; This is C-terminal to the Mov24 region of the yeast proteasomal subunit Rpn11 and seems likely to regulate the mitochondrial fission and tubulation processes, ie the outer mitochondrial membrane proteins. This function appears to be unrelated to the proteasome activity of the N-terminal region.


Pssm-ID: 463772 [Multi-domain]  Cd Length: 72  Bit Score: 78.69  E-value: 1.25e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145348207  180 EAEEIGVEHLLRdvkdNTVSTLSTKVSEKVQSLRGLKARLEEIKSYMDKVVDGSLPMNHEIMGHLQDAFNL 250
Cdd:pfam13012   1 EAERIGVDHLAR----PDIKSLSSDLERQYYSLKMLQDRLDLILKYVEDVLDGELPPDHAIGRYLQDLLAL 67
MPN cd07767
Mpr1p, Pad1p N-terminal (MPN) domains; MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) ...
 32-151 2.68e-18

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.


Pssm-ID: 163686 [Multi-domain]  Cd Length: 116  Bit Score: 79.48  E-value: 2.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  32 LLSVVDHFRRcDENKRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLdhsylenMYRMSKKISAKEKIVGWYSTG 111
Cdd:cd07767    1 LKMFLDAAKS-INGKEVIGLLYGSKTKKVLDVDEVIAVPFDEGDKDDNVWFL-------MYLDFKKLNAGLRIVGWYHTH 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 145348207 112 PK----LRESDIDIHELFYAYTPEPVLVIVDVRAENANIPTSAF 151
Cdd:cd07767   73 PKpscfLSPNDLATHELFQRYFPEKVMIIVDVKPKDLGNSWKCY 116
MPN_eIF3h cd08065
Mpr1p, Pad1p N-terminal (MPN) domains without catalytic isopeptidase activity, found in eIF2h; ...
 25-151 7.75e-09

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: 55.74  E-value: 7.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145348207  25 VVVHPLVLLSVVDHfrrCDEN--KRVVGVLLGEQRKGRLDVTSSFAVPFEEDDGDNGIWFLDHSYLENMYRMSKKISAKE 102
Cdd:cd08065    3 VQIDGLVVLKIIKH---CKEElpELVQGQLLGLDVGGTLEVTNCFPFPKSEEDDSDRADEDIADYQLEMMRLLREVNVDH 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145348207 103 KIVGWYSTGPKLRESDIDIHELFYAYT---PEPVLVIVD-VRAENANIPTSAF 151
Cdd:cd08065   80 NHVGWYQSTYLGSFFTRDLIETQYNYQeaiEESVVLVYDpSKTSQGSLSLKAY 132
 
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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