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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991  12 DIMQEIYLTAIKRYPNEACGFLVRTtGEKYRFMEARNVSENPENTFVMHADDIIAAEDAGDVVAIWHSHTDESADASDAD 91
Cdd:cd08073    1 KLEDAILAHAKAEYPREACGLVVRK-GRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 805410991  92 RAGCEATEVPWLILAVRknvEGDapfhfseMNVITPDGF 130
Cdd:cd08073   80 RAQQEATGLPWIIVSWP---EGD-------LRVFRPVGY 108

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991  12 DIMQEIYLTAIKRYPNEACGFLVRTtGEKYRFMEARNVSENPENTFVMHADDIIAAEDAGDVVAIWHSHTDESADASDAD 91
Cdd:cd08073    1 KLEDAILAHAKAEYPREACGLVVRK-GRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 805410991  92 RAGCEATEVPWLILAVRknvEGDapfhfseMNVITPDGF 130
Cdd:cd08073   80 RAQQEATGLPWIIVSWP---EGD-------LRVFRPVGY 108

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991   9 LGSDIMQEIYLTAIKRYPNEACGFLVRTTGEK---YRFMEARNVSENPENTFVMHADDIIAAEDA-----GDVVAIWHSH 80
Cdd:COG1310    4 LPRELLDAILAHAEAAYPEECCGLLLGKGGGDkrvTRVYPARNVAESPETRFEIDPEDLLAAEREarergLEIVGIYHSH 83

                         90       100
                 ....*....|....*....|....*....
gi 805410991  81 TDESADASDADRAGCEATEVPWLILAVRK 109
Cdd:COG1310   84 PDGPAYPSETDRAQAAWPGLPYLIVSLPD 112

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991   11 SDIMQEIYLTAIKRYPNEACGFLV--RTTGEKYRFMEarnVSENPENTFVMHADDIIAAEDA-----GDVVAIWHSHTDE 83
Cdd:pfam14464   2 APLLDAIVAHARAAHPLECCGILLgnELESQSVRVIP---LVNPMRNRFEIDPGDSLRRVKAarergLELVGIYHSHPGG 78

                          90       100
                  ....*....|....*....|....*....
gi 805410991   84 SADASDADRAGCEAtEVPWLILAVRKNVE 112
Cdd:pfam14464  79 PAYPSETDRRDAAG-PLPSYVIGGRAPPE 106

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991  12 DIMQEIYLTAIKRYPNEACGFLVRTtGEKYRFMEARNVSENPENTFVMHADDIIAAEDAGDVVAIWHSHTDESADASDAD 91
Cdd:cd08073    1 KLEDAILAHAKAEYPREACGLVVRK-GRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 805410991  92 RAGCEATEVPWLILAVRknvEGDapfhfseMNVITPDGF 130
Cdd:cd08073   80 RAQQEATGLPWIIVSWP---EGD-------LRVFRPVGY 108

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991   9 LGSDIMQEIYLTAIKRYPNEACGFLVRTTGEK---YRFMEARNVSENPENTFVMHADDIIAAEDA-----GDVVAIWHSH 80
Cdd:COG1310    4 LPRELLDAILAHAEAAYPEECCGLLLGKGGGDkrvTRVYPARNVAESPETRFEIDPEDLLAAEREarergLEIVGIYHSH 83

                         90       100
                 ....*....|....*....|....*....
gi 805410991  81 TDESADASDADRAGCEATEVPWLILAVRK 109
Cdd:COG1310   84 PDGPAYPSETDRAQAAWPGLPYLIVSLPD 112

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991  12 DIMQEIYLTAIKRYPNEACGFL------VRTTGEKYRFMeaRNVSENPENTFVMHADDIIAAEDAG-----DVVAIWHSH 80
Cdd:cd08070    2 ELLEAILAHAEAEYPEECCGLLlgkgggVTAIVTEVYPV--RNVAESPRRRFEIDPAEQLAAQREArerglEVVGIYHSH 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 805410991  81 TDESADASDADRAGCEATEVPWLILAVRKNVE 112
Cdd:cd08070   80 PDGPARPSETDLRLAWPPGVSYLIVSLAGGAP 111

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 805410991 134 YLGRPYVFG-----VFDCWMLCRdYLKREFNVELnpnPHlhipswytgDTDilDQnYRNEGLVRLApgtEPQRGD-VFFI 207
Cdd:COG0791  110 YLGTPYVWGgtspsGFDCSGLVQ-YVYRQAGISL---PR---------TSA--DQ-AAAGTPVSRS---ELQPGDlVFFR 170

                         90       100
                 ....*....|....*....|
gi 805410991 208 QYGKMPDHCAVYIGDGMILH 227
Cdd:COG0791  171 TGGGGISHVGIYLGNGKFIH 190