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 1110278788   4 KTIDAIMAHAAAEYPRECCGVVAQKSRIERYFPCRNLATEPEGNFVLCPEDYAAAEDWGTVIAIAHSHPDATTQPSELDK 83
Cdd:cd08073     1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                          90       100
                  ....*....|....*....|....*...
gi 1110278788  84 AQCDGTLLPWHIVSWPEGDFRTIQPRGE 111
Cdd:cd08073    81 AQQEATGLPWIIVSWPEGDLRVFRPVGY 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 1110278788   4 KTIDAIMAHAAAEYPRECCGVVAQKSRIERYFPCRNLATEPEGNFVLCPEDYAAAEDWGTVIAIAHSHPDATTQPSELDK 83
Cdd:cd08073     1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                          90       100
                  ....*....|....*....|....*...
gi 1110278788  84 AQCDGTLLPWHIVSWPEGDFRTIQPRGE 111
Cdd:cd08073    81 AQQEATGLPWIIVSWPEGDLRVFRPVGY 108

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110278788    1 MRQKTIDAIMAHAAAEYPRECCGVVAQKSRIERYFPCRNLATEPEGN-----------FVLCPEDYAAAEDWGTVIAIAH 69
Cdd:smart00232   4 VHPLVPLNILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFAVPNEPQddsvqeydedySHLMDEELKKVNKDLEIVGWYH 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1110278788   70 SHPDATTQPSELDKAQCDGTLLPWHIVSWP-EGDFRTIQprgeLSLLERPFVLGHY 124
Cdd:smart00232  84 SHPDESPFPSEVDVATHESYQAPWPISVVLiVDPIKSFQ----GRLSLRAFRLTPE 135

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 1110278788   3 QKTIDAIMAHAAAEYPRECCGVVAQKSRI-ERYFPCRnLATEPEGNFVLCPEDY-----AAAEDWGTVIAIAHSHPDATT 76
Cdd:pfam14464   2 APLLDAIVAHARAAHPLECCGILLGNELEsQSVRVIP-LVNPMRNRFEIDPGDSlrrvkAARERGLELVGIYHSHPGGPA 80

                          90       100
                  ....*....|....*....|....*...
gi 1110278788  77 QPSELDKAQCDGTLLPWHIVSWPEGDFR 104
Cdd:pfam14464  81 YPSETDRRDAAGPLPSYVIGGRAPPEIR 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 1110278788   4 KTIDAIMAHAAAEYPRECCGVVAQKSRIERYFPCRNLATEPEGNFVLCPEDYAAAEDWGTVIAIAHSHPDATTQPSELDK 83
Cdd:cd08073     1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                          90       100
                  ....*....|....*....|....*...
gi 1110278788  84 AQCDGTLLPWHIVSWPEGDFRTIQPRGE 111
Cdd:cd08073    81 AQQEATGLPWIIVSWPEGDLRVFRPVGY 108

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110278788    1 MRQKTIDAIMAHAAAEYPRECCGVVAQKSRIERYFPCRNLATEPEGN-----------FVLCPEDYAAAEDWGTVIAIAH 69
Cdd:smart00232   4 VHPLVPLNILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFAVPNEPQddsvqeydedySHLMDEELKKVNKDLEIVGWYH 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1110278788   70 SHPDATTQPSELDKAQCDGTLLPWHIVSWP-EGDFRTIQprgeLSLLERPFVLGHY 124
Cdd:smart00232  84 SHPDESPFPSEVDVATHESYQAPWPISVVLiVDPIKSFQ----GRLSLRAFRLTPE 135

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 1110278788   6 IDAIMAHAAAEYPRECCGVVA-----QKSRIERYFPCRNLATEPEGNFVLCPEDYAAAEDWGT-----VIAIAHSHPDAT 75
Cdd:cd08070     4 LEAILAHAEAEYPEECCGLLLgkgggVTAIVTEVYPVRNVAESPRRRFEIDPAEQLAAQREARergleVVGIYHSHPDGP 83

                          90       100
                  ....*....|....*....|..
gi 1110278788  76 TQPSELDKAQCDGTLLPWHIVS 97
Cdd:cd08070    84 ARPSETDLRLAWPPGVSYLIVS 105

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110278788   5 TIDAIMAHAAAEYPRECCGVVAQKSRieryFPCRNLATEPEGNFVLCPE-DYAAAEDWGTVIAIAHSHPDATTQPSELDK 83
Cdd:cd08059     2 LLKTILVHAKDAHPDEFCGFLSGSKD----NVMDELIFLPFVSGSVSAViDLAALEIGMKVVGLVHSHPSGSCRPSEADL 77

                          90
                  ....*....|....*..
gi 1110278788  84 AQCDGTLLPWHIVSWPE 100
Cdd:cd08059    78 SLFTRFGLYHVIVCYPY 94