NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1738373874|emb|VAN13445|]
View 

Mov34/MPN/PAD-1 family protein [Klebsiella variicola]

Protein Classification

Rri1 family protein( domain architecture ID 10003476)

Rri1 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 1-130 4.70e-36

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440921  Cd Length: 127  Bit Score: 120.40  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   1 MIELTREIARQIGAEGEKTYPNECCGALFGHlsAQGDGRVTAIFPIVNARESEEqyHRFVITADDALRAERAALAEGVDV 80
Cdd:COG1310     1 MLVLPRELLDAILAHAEAAYPEECCGLLLGK--GGGDKRVTRVYPARNVAESPE--TRFEIDPEDLLAAEREARERGLEI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1738373874  81 IGYYHSHPDHPAIPSEFDREHAL-PFYAYIIVAVAQRQaGALTSWRLTQDR 130
Cdd:COG1310    77 VGIYHSHPDGPAYPSETDRAQAAwPGLPYLIVSLPDGG-PELRAWRLRDGR 126
 
Name Accession Description Interval E-value
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 1-130 4.70e-36

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 120.40  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   1 MIELTREIARQIGAEGEKTYPNECCGALFGHlsAQGDGRVTAIFPIVNARESEEqyHRFVITADDALRAERAALAEGVDV 80
Cdd:COG1310     1 MLVLPRELLDAILAHAEAAYPEECCGLLLGK--GGGDKRVTRVYPARNVAESPE--TRFEIDPEDLLAAEREARERGLEI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1738373874  81 IGYYHSHPDHPAIPSEFDREHAL-PFYAYIIVAVAQRQaGALTSWRLTQDR 130
Cdd:COG1310    77 VGIYHSHPDGPAYPSETDRAQAAwPGLPYLIVSLPDGG-PELRAWRLRDGR 126
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 6-138 2.21e-33

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); This family contains archaeal and bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163701  Cd Length: 128  Bit Score: 113.51  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   6 REIARQIGAEGEKTYPNECCGALFGHLSAQGDGrVTAIFPIVNARESEEqyHRFVITADDALRAERAALAEGVDVIGYYH 85
Cdd:cd08070     1 RELLEAILAHAEAEYPEECCGLLLGKGGGVTAI-VTEVYPVRNVAESPR--RRFEIDPAEQLAAQREARERGLEVVGIYH 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1738373874  86 SHPDHPAIPSEFDREHALPF-YAYIIVAVAQRqAGALTSWRLTQDrlRFLQEEV 138
Cdd:cd08070    78 SHPDGPARPSETDLRLAWPPgVSYLIVSLAGG-APELRAWRLEGG--QFEEEEV 128
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 5-126 5.54e-19

Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism.


Pssm-ID: 464179  Cd Length: 113  Bit Score: 76.39  E-value: 5.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   5 TREIARQIGAEGEKTYPNECCGALFGHLSAQGDGRVTAIFPIVNareseeqyHRFVITADDALRAERAALAEGVDVIGYY 84
Cdd:pfam14464   1 PAPLLDAIVAHARAAHPLECCGILLGNELESQSVRVIPLVNPMR--------NRFEIDPGDSLRRVKAARERGLELVGIY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1738373874  85 HSHPDHPAIPSEFDREHAL-PFYAYIIVAvaqRQAGALTSWRL 126
Cdd:pfam14464  73 HSHPGGPAYPSETDRRDAAgPLPSYVIGG---RAPPEIRSWRL 112
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 1-114 5.47e-11

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: 56.23  E-value: 5.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874    1 MIELTREIARQIGAEGEKTYPNECCGALFGhlSAQGDG-RVTAIFPIVNARESEEQyHRFVITADDALRAERAALAEGVD 79
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRDGPEEVCGVLLG--KSNKDRpEVKEVFAVPNEPQDDSV-QEYDEDYSHLMDEELKKVNKDLE 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1738373874   80 VIGYYHSHPDHPAIPSEFDREHALPFYAYIIVAVA 114
Cdd:smart00232  78 IVGWYHSHPDESPFPSEVDVATHESYQAPWPISVV 112
 
Name Accession Description Interval E-value
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 1-130 4.70e-36

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 120.40  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   1 MIELTREIARQIGAEGEKTYPNECCGALFGHlsAQGDGRVTAIFPIVNARESEEqyHRFVITADDALRAERAALAEGVDV 80
Cdd:COG1310     1 MLVLPRELLDAILAHAEAAYPEECCGLLLGK--GGGDKRVTRVYPARNVAESPE--TRFEIDPEDLLAAEREARERGLEI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1738373874  81 IGYYHSHPDHPAIPSEFDREHAL-PFYAYIIVAVAQRQaGALTSWRLTQDR 130
Cdd:COG1310    77 VGIYHSHPDGPAYPSETDRAQAAwPGLPYLIVSLPDGG-PELRAWRLRDGR 126
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 6-138 2.21e-33

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); This family contains archaeal and bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163701  Cd Length: 128  Bit Score: 113.51  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   6 REIARQIGAEGEKTYPNECCGALFGHLSAQGDGrVTAIFPIVNARESEEqyHRFVITADDALRAERAALAEGVDVIGYYH 85
Cdd:cd08070     1 RELLEAILAHAEAEYPEECCGLLLGKGGGVTAI-VTEVYPVRNVAESPR--RRFEIDPAEQLAAQREARERGLEVVGIYH 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1738373874  86 SHPDHPAIPSEFDREHALPF-YAYIIVAVAQRqAGALTSWRLTQDrlRFLQEEV 138
Cdd:cd08070    78 SHPDGPARPSETDLRLAWPPgVSYLIVSLAGG-APELRAWRLEGG--QFEEEEV 128
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 5-126 5.54e-19

Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism.


Pssm-ID: 464179  Cd Length: 113  Bit Score: 76.39  E-value: 5.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   5 TREIARQIGAEGEKTYPNECCGALFGHLSAQGDGRVTAIFPIVNareseeqyHRFVITADDALRAERAALAEGVDVIGYY 84
Cdd:pfam14464   1 PAPLLDAIVAHARAAHPLECCGILLGNELESQSVRVIPLVNPMR--------NRFEIDPGDSLRRVKAARERGLELVGIY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1738373874  85 HSHPDHPAIPSEFDREHAL-PFYAYIIVAvaqRQAGALTSWRL 126
Cdd:pfam14464  73 HSHPGGPAYPSETDRRDAAgPLPSYVIGG---RAPPEIRSWRL 112
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 1-114 5.47e-11

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: 56.23  E-value: 5.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874    1 MIELTREIARQIGAEGEKTYPNECCGALFGhlSAQGDG-RVTAIFPIVNARESEEQyHRFVITADDALRAERAALAEGVD 79
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRDGPEEVCGVLLG--KSNKDRpEVKEVFAVPNEPQDDSV-QEYDEDYSHLMDEELKKVNKDLE 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1738373874   80 VIGYYHSHPDHPAIPSEFDREHALPFYAYIIVAVA 114
Cdd:smart00232  78 IVGWYHSHPDESPFPSEVDVATHESYQAPWPISVV 112
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 3-113 4.94e-10

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) found in proteins also containing NlpC/P60 domains; This family contains bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains at the N-terminus of NlpC/P60 phage tail protein domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163704  Cd Length: 108  Bit Score: 53.07  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   3 ELTREIARQIgaegEKTYPNECCGALFGhlsaqgDGRVTAIFPIVN-ARESEEQyhrFVITADDALRAERAAlaegvDVI 81
Cdd:cd08073     1 KLEDAILAHA----KAEYPREACGLVVR------KGRKLRYIPCRNiAADPEEH---FEISPEDYAAAEDEG-----EIV 62

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1738373874  82 GYYHSHPDHPAIPSEFDR----EHALPfyaYIIVAV 113
Cdd:cd08073    63 AVVHSHPDGSPAPSEADRaqqeATGLP---WIIVSW 95
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 7-124 2.24e-07

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); prokaryotic; This family contains bacterial and archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These catalytically active domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163690  Cd Length: 101  Bit Score: 46.02  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373874   7 EIARQIGAEGEKTYPNECCGALFGHLsaqgDGRVTAIFPIVNARESEEQYHrfvitaddalraERAALAEGVDVIGYYHS 86
Cdd:cd08059     1 DLLKTILVHAKDAHPDEFCGFLSGSK----DNVMDELIFLPFVSGSVSAVI------------DLAALEIGMKVVGLVHS 64

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1738373874  87 HPDHPAIPSEFDREHA-LPFYAYIIVAVaqRQAGALTSW 124
Cdd:cd08059    65 HPSGSCRPSEADLSLFtRFGLYHVIVCY--PYENSWKCY 101
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 77-95 3.40e-03

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 35.71  E-value: 3.40e-03
                          10
                  ....*....|....*....
gi 1738373874  77 GVDVIGYYHSHPDHPAIPS 95
Cdd:cd08067    78 GLSVVGWYHSHPTFPPNPS 96
 
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