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Conserved domains on  [gi|1120208808|ref|WP_073076187|]
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M67 family metallopeptidase [Sporobacter termitidis]

Protein Classification

M67 family metallopeptidase( domain architecture ID 10169184)

M67 family metallopeptidase similar to isopeptidases that release ubiquitin from ubiquitinated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 7-133 5.22e-58

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: 175.91  E-value: 5.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808   7 RSDYDAIIAHAKAGLPNEACGLIAGTIDGGVKTIEKVYLLKNIDESPE-HFSIDPREQLAAVKDMRALGLSPLGNFHSHP 85
Cdd:cd08070     1 RELLEAILAHAEAEYPEECCGLLLGKGGGVTAIVTEVYPVRNVAESPRrRFEIDPAEQLAAQREARERGLEVVGIYHSHP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1120208808  86 ETPARPSAEDIRLAYDPKASYLILSLAGEAPDLKAFEIESGAATRQTL 133
Cdd:cd08070    81 DGPARPSETDLRLAWPPGVSYLIVSLAGGAPELRAWRLEGGQFEEEEV 128
 
Name Accession Description Interval E-value
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 7-133 5.22e-58

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: 175.91  E-value: 5.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808   7 RSDYDAIIAHAKAGLPNEACGLIAGTIDGGVKTIEKVYLLKNIDESPE-HFSIDPREQLAAVKDMRALGLSPLGNFHSHP 85
Cdd:cd08070     1 RELLEAILAHAEAEYPEECCGLLLGKGGGVTAIVTEVYPVRNVAESPRrRFEIDPAEQLAAQREARERGLEVVGIYHSHP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1120208808  86 ETPARPSAEDIRLAYDPKASYLILSLAGEAPDLKAFEIESGAATRQTL 133
Cdd:cd08070    81 DGPARPSETDLRLAWPPGVSYLIVSLAGGAPELRAWRLEGGQFEEEEV 128
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 2-126 6.05e-53

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: 163.16  E-value: 6.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808   2 TVKLKRSDYDAIIAHAKAGLPNEACGLIAGTIDGGvKTIEKVYLLKNIDESPE-HFSIDPREQLAAVKDMRALGLSPLGN 80
Cdd:COG1310     1 MLVLPRELLDAILAHAEAAYPEECCGLLLGKGGGD-KRVTRVYPARNVAESPEtRFEIDPEDLLAAEREARERGLEIVGI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1120208808  81 FHSHPETPARPSAEDIRLAYDPKASYLILSLAGEAPDLKAFEIESG 126
Cdd:COG1310    80 YHSHPDGPAYPSETDRAQAAWPGLPYLIVSLPDGGPELRAWRLRDG 125
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 10-123 4.83e-31

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: 107.21  E-value: 4.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808  10 YDAIIAHAKAGLPNEACGLIAGTIDGGVKTIekvyLLKNIDESPEHFSIDPREQLAAVKDMRALGLSPLGNFHSHPETPA 89
Cdd:pfam14464   5 LDAIVAHARAAHPLECCGILLGNELESQSVR----VIPLVNPMRNRFEIDPGDSLRRVKAARERGLELVGIYHSHPGGPA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1120208808  90 RPSAEDIRLAYDPKASYLILSlaGEAPDLKAFEI 123
Cdd:pfam14464  81 YPSETDRRDAAGPLPSYVIGG--RAPPEIRSWRL 112
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 2-116 1.19e-14

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: 65.86  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808    2 TVKLKRSDYDAIIAHAKAGLPNEACGLIAGTIDGGVKTIEKVYLLKN------IDESPEHFSIDPREQLAAVKDmralGL 75
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFAVPNepqddsVQEYDEDYSHLMDEELKKVNK----DL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1120208808   76 SPLGNFHSHPETPARPSAEDIRLAYDPKASYLILSLAGEAP 116
Cdd:smart00232  77 EIVGWYHSHPDESPFPSEVDVATHESYQAPWPISVVLIVDP 117
 
Name Accession Description Interval E-value
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 7-133 5.22e-58

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: 175.91  E-value: 5.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808   7 RSDYDAIIAHAKAGLPNEACGLIAGTIDGGVKTIEKVYLLKNIDESPE-HFSIDPREQLAAVKDMRALGLSPLGNFHSHP 85
Cdd:cd08070     1 RELLEAILAHAEAEYPEECCGLLLGKGGGVTAIVTEVYPVRNVAESPRrRFEIDPAEQLAAQREARERGLEVVGIYHSHP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1120208808  86 ETPARPSAEDIRLAYDPKASYLILSLAGEAPDLKAFEIESGAATRQTL 133
Cdd:cd08070    81 DGPARPSETDLRLAWPPGVSYLIVSLAGGAPELRAWRLEGGQFEEEEV 128
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 2-126 6.05e-53

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: 163.16  E-value: 6.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808   2 TVKLKRSDYDAIIAHAKAGLPNEACGLIAGTIDGGvKTIEKVYLLKNIDESPE-HFSIDPREQLAAVKDMRALGLSPLGN 80
Cdd:COG1310     1 MLVLPRELLDAILAHAEAAYPEECCGLLLGKGGGD-KRVTRVYPARNVAESPEtRFEIDPEDLLAAEREARERGLEIVGI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1120208808  81 FHSHPETPARPSAEDIRLAYDPKASYLILSLAGEAPDLKAFEIESG 126
Cdd:COG1310    80 YHSHPDGPAYPSETDRAQAAWPGLPYLIVSLPDGGPELRAWRLRDG 125
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 10-123 4.83e-31

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: 107.21  E-value: 4.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808  10 YDAIIAHAKAGLPNEACGLIAGTIDGGVKTIekvyLLKNIDESPEHFSIDPREQLAAVKDMRALGLSPLGNFHSHPETPA 89
Cdd:pfam14464   5 LDAIVAHARAAHPLECCGILLGNELESQSVR----VIPLVNPMRNRFEIDPGDSLRRVKAARERGLELVGIYHSHPGGPA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1120208808  90 RPSAEDIRLAYDPKASYLILSlaGEAPDLKAFEI 123
Cdd:pfam14464  81 YPSETDRRDAAGPLPSYVIGG--RAPPEIRSWRL 112
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 2-116 1.19e-14

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: 65.86  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808    2 TVKLKRSDYDAIIAHAKAGLPNEACGLIAGTIDGGVKTIEKVYLLKN------IDESPEHFSIDPREQLAAVKDmralGL 75
Cdd:smart00232   1 EVKVHPLVPLNILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFAVPNepqddsVQEYDEDYSHLMDEELKKVNK----DL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1120208808   76 SPLGNFHSHPETPARPSAEDIRLAYDPKASYLILSLAGEAP 116
Cdd:smart00232  77 EIVGWYHSHPDESPFPSEVDVATHESYQAPWPISVVLIVDP 117
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 10-110 2.48e-14

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: 64.24  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808  10 YDAIIAHAKAGLPNEACGLIAgtidggVKTIEKVYL-LKNIDESP-EHFSIDPREQLAAvkdmRALGlSPLGNFHSHPET 87
Cdd:cd08073     3 EDAILAHAKAEYPREACGLVV------RKGRKLRYIpCRNIAADPeEHFEISPEDYAAA----EDEG-EIVAVVHSHPDG 71

                          90       100
                  ....*....|....*....|...
gi 1120208808  88 PARPSAEDIRLAYDPKASYLILS 110
Cdd:cd08073    72 SPAPSEADRAQQEATGLPWIIVS 94
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 11-121 9.11e-11

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: 54.88  E-value: 9.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808  11 DAIIAHAKAGLPNEACGLIAGTIDGGVKTIEKvyllknidESPEHFSIDPREQLAAVKdmraLGLSPLGNFHSHPETPAR 90
Cdd:cd08059     4 KTILVHAKDAHPDEFCGFLSGSKDNVMDELIF--------LPFVSGSVSAVIDLAALE----IGMKVVGLVHSHPSGSCR 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1120208808  91 PSAEDIRLAYDPKASYLILSLaGEAPDLKAF 121
Cdd:cd08059    72 PSEADLSLFTRFGLYHVIVCY-PYENSWKCY 101
MPN_euk_mb cd08058
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 16-123 5.82e-08

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); eukaryotic; This family contains eukaryotic MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains found in proteins with a variety of functions, including AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM), H2A-DUB (histone H2A deubiquitinase), BRCC36 (BRCA1/BRCA2-containing complex subunit 36), as well as Rpn11 (regulatory particle number 11) and CSN5 (COP9 signalosome complex subunit 5). 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. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology. CSN5 is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Over-expression of CSN5 has been implicated in cancer initiation and progression. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. It is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity; it is targeted to DNA damage foci after irradiation. 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. It is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene and serves as a marker in prostate tumors.


Pssm-ID: 163689  Cd Length: 119  Bit Score: 47.96  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808  16 HAKAGLPNEACGLIAGTIDGGVKTIEKVYLlknIDESPEHFSIDPREQLAAVKDMRALGLSPLGNFHSHPETPARPSAED 95
Cdd:cd08058     9 HAESNTGIEVMGLLCGELTHNEFTDKHVIV---PKQSAGPDSCTGENVEELFNVQTGRPLLVVGWYHSHPTFTAWLSSVD 85

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1120208808  96 IRL-----AYDPKASYLILSLAGEAPDLKAFEI 123
Cdd:cd08058    86 IHTqasyqLMLPEAIAIVVSPKHRNKDTGIFRL 118
MPN cd07767
Mpr1p, Pad1p N-terminal (MPN) domains; MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) ...
 13-96 2.33e-06

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: 43.65  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808  13 IIAHAKAGLPNEACGLIAGTIDGGVKTIEKVYLLKNiDESPEHFSIDPREQLAAVKDMRalGLSPLGNFHSHPETPARPS 92
Cdd:cd07767     4 FLDAAKSINGKEVIGLLYGSKTKKVLDVDEVIAVPF-DEGDKDDNVWFLMYLDFKKLNA--GLRIVGWYHTHPKPSCFLS 80


                  ....
gi 1120208808  93 AEDI 96
Cdd:cd07767    81 PNDL 84
MPN_archaeal cd08072
Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only ...
 5-98 2.94e-05

Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only archaeal 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: 163703  Cd Length: 117  Bit Score: 40.70  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120208808   5 LKRSDYDAIIAHAKAGLPNEACGLIAGTIdggvKTIEKVYLLKNiDESPEHFSIDPreqlaavKDMRALGLSPLGNFHSH 84
Cdd:cd08072     1 ISRDLLDSILEAAKSSHPNEFAALLRGKD----GVITELLILPG-TESGEVSAVFP-------LLMLPLDMSIVGSVHSH 68

                          90
                  ....*....|....
gi 1120208808  85 PETPARPSAEDIRL 98
Cdd:cd08072    69 PSGSPRPSDADLSF 82
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 23-96 1.91e-04

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: 39.17  E-value: 1.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1120208808  23 NEACGLIAGTIDGGVK--TIEKVYLLKNIdESPEHFSIDPREQLAAVKDMRALGLSPLGNFHSHPETPARPSAEDI 96
Cdd:cd08067    26 SEVIGYLGGTWDPNTQnlTILQAFPCRSR-LTGLDCEMDPVSETEIRESLESRGLSVVGWYHSHPTFPPNPSLRDI 100
 
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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