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Conserved domains on  [gi|218364842|emb|CAR02534|]
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putative tail fiber component K of prophage [Escherichia coli S88]

Protein Classification

C40 family peptidase( domain architecture ID 10169217)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 3-108 3.31e-49

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: 157.07  E-value: 3.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   3 ETESAILAHARRCAPAESCGFVVRAPEGERYFPCVNISGEPEAYFRMAPEDWLQAEMQGEIVALVHSHPGGLPWLSEADR 82
Cdd:cd08073    1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                         90       100
                 ....*....|....*....|....*...
gi 218364842  83 RLQVQSDLPWWLVCR--GAIHKFRCVPH 108
Cdd:cd08073   81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
NLPC_P60 super family cl21534
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 111-224 5.75e-14

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


The actual alignment was detected with superfamily member pfam00877:

Pssm-ID: 473902 [Multi-domain]  Cd Length: 105  Bit Score: 65.77  E-value: 5.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842  111 GRRFEHG-----VTDCYTLFRDAYHLAGIEMPDFHREddWWRNGQNlyldnleatglyQVPLSAAQPGDVLLccFGS-SV 184
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--QYNAGKK------------TIPKSEPQRGDLVF--FGTgKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 218364842  185 PNHAAIYCGDGELLHHIP-EQLSKRERYTDKWQRRTHSLWR 224
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
 
Name Accession Description Interval E-value
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 3-108 3.31e-49

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: 157.07  E-value: 3.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   3 ETESAILAHARRCAPAESCGFVVRAPEGERYFPCVNISGEPEAYFRMAPEDWLQAEMQGEIVALVHSHPGGLPWLSEADR 82
Cdd:cd08073    1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                         90       100
                 ....*....|....*....|....*...
gi 218364842  83 RLQVQSDLPWWLVCR--GAIHKFRCVPH 108
Cdd:cd08073   81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 7-96 1.61e-26

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: 99.60  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   7 AILAHARRCAPAESCGFVVRAPEGE----RYFPCVNISGEPEAYFRMAPEDWLQA-----EMQGEIVALVHSHPGGLPWL 77
Cdd:COG1310   11 AILAHAEAAYPEECCGLLLGKGGGDkrvtRVYPARNVAESPETRFEIDPEDLLAAerearERGLEIVGIYHSHPDGPAYP 90

                         90
                 ....*....|....*....
gi 218364842  78 SEADRRLQVQSDLPWWLVC 96
Cdd:COG1310   91 SETDRAQAAWPGLPYLIVS 109
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 111-224 5.75e-14

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 65.77  E-value: 5.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842  111 GRRFEHG-----VTDCYTLFRDAYHLAGIEMPDFHREddWWRNGQNlyldnleatglyQVPLSAAQPGDVLLccFGS-SV 184
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--QYNAGKK------------TIPKSEPQRGDLVF--FGTgKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 218364842  185 PNHAAIYCGDGELLHHIP-EQLSKRERYTDKWQRRTHSLWR 224
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 7-92 8.15e-13

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: 63.55  E-value: 8.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842     7 AILAHARRCAPAESCGFVVRAPEGERYFPCVNI-----------SGEPEAYFRMAPEDWLQAEMQGEIVALVHSHPGGLP 75
Cdd:smart00232  11 NILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFavpnepqddsvQEYDEDYSHLMDEELKKVNKDLEIVGWYHSHPDESP 90

                           90
                   ....*....|....*..
gi 218364842    76 WLSEADRRLQVQSDLPW 92
Cdd:smart00232  91 FPSEVDVATHESYQAPW 107
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 3-106 1.77e-12

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: 62.14  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842    3 ETESAILAHARRCAPAESCGFVV-RAPEGERYFPCVNISgEPEAYFRMAPEDWLQ--AEM---QGEIVALVHSHPGGLPW 76
Cdd:pfam14464   3 PLLDAIVAHARAAHPLECCGILLgNELESQSVRVIPLVN-PMRNRFEIDPGDSLRrvKAArerGLELVGIYHSHPGGPAY 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 218364842   77 LSEADRRLqVQSDLPWWLVCRGAIHKFRCV 106
Cdd:pfam14464  82 PSETDRRD-AAGPLPSYVIGGRAPPEIRSW 110
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
120-199 2.50e-08

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


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 52.78  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842 120 DCYTLFRDAYHLAGIEMPdfHREDDWWRNGQnlyldnleatglyQVPLSAAQPGDVLLccFGSS--VPNHAAIYCGDGEL 197
Cdd:COG0791  126 DCSGLVQYVYRQAGISLP--RTSADQAAAGT-------------PVSRSELQPGDLVF--FRTGggGISHVGIYLGNGKF 188


                 ..
gi 218364842 198 LH 199
Cdd:COG0791  189 IH 190
 
Name Accession Description Interval E-value
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 3-108 3.31e-49

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: 157.07  E-value: 3.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   3 ETESAILAHARRCAPAESCGFVVRAPEGERYFPCVNISGEPEAYFRMAPEDWLQAEMQGEIVALVHSHPGGLPWLSEADR 82
Cdd:cd08073    1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                         90       100
                 ....*....|....*....|....*...
gi 218364842  83 RLQVQSDLPWWLVCR--GAIHKFRCVPH 108
Cdd:cd08073   81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 3-106 1.55e-38

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: 129.60  E-value: 1.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   3 ETESAILAHARRCAPAESCGFVVRAPEGeryfPCVNISGEPEAYFRMAPE-DWLQAEMQGEIVALVHSHPGGLPWLSEAD 81
Cdd:cd08059    1 DLLKTILVHAKDAHPDEFCGFLSGSKDN----VMDELIFLPFVSGSVSAViDLAALEIGMKVVGLVHSHPSGSCRPSEAD 76

                         90       100
                 ....*....|....*....|....*
gi 218364842  82 RRLQVQSDLPWWLVCRGAIHKFRCV 106
Cdd:cd08059   77 LSLFTRFGLYHVIVCYPYENSWKCY 101
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 7-96 1.61e-26

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: 99.60  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   7 AILAHARRCAPAESCGFVVRAPEGE----RYFPCVNISGEPEAYFRMAPEDWLQA-----EMQGEIVALVHSHPGGLPWL 77
Cdd:COG1310   11 AILAHAEAAYPEECCGLLLGKGGGDkrvtRVYPARNVAESPETRFEIDPEDLLAAerearERGLEIVGIYHSHPDGPAYP 90

                         90
                 ....*....|....*....
gi 218364842  78 SEADRRLQVQSDLPWWLVC 96
Cdd:COG1310   91 SETDRAQAAWPGLPYLIVS 109
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 7-105 1.57e-19

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: 81.53  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   7 AILAHARRCAPAESCGFVVRAPEG-----ERYFPCVNISGEPEAYFRMAPEDWLQAEMQG-----EIVALVHSHPGGLPW 76
Cdd:cd08070    6 AILAHAEAEYPEECCGLLLGKGGGvtaivTEVYPVRNVAESPRRRFEIDPAEQLAAQREArerglEVVGIYHSHPDGPAR 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 218364842  77 LSEADRRLQVQSDLPWWLVC-RGAIHKFRC 105
Cdd:cd08070   86 PSETDLRLAWPPGVSYLIVSlAGGAPELRA 115
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 111-224 5.75e-14

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 65.77  E-value: 5.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842  111 GRRFEHG-----VTDCYTLFRDAYHLAGIEMPDFHREddWWRNGQNlyldnleatglyQVPLSAAQPGDVLLccFGS-SV 184
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--QYNAGKK------------TIPKSEPQRGDLVF--FGTgKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 218364842  185 PNHAAIYCGDGELLHHIP-EQLSKRERYTDKWQRRTHSLWR 224
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 7-92 8.15e-13

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: 63.55  E-value: 8.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842     7 AILAHARRCAPAESCGFVVRAPEGERYFPCVNI-----------SGEPEAYFRMAPEDWLQAEMQGEIVALVHSHPGGLP 75
Cdd:smart00232  11 NILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFavpnepqddsvQEYDEDYSHLMDEELKKVNKDLEIVGWYHSHPDESP 90

                           90
                   ....*....|....*..
gi 218364842    76 WLSEADRRLQVQSDLPW 92
Cdd:smart00232  91 FPSEVDVATHESYQAPW 107
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 3-106 1.77e-12

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: 62.14  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842    3 ETESAILAHARRCAPAESCGFVV-RAPEGERYFPCVNISgEPEAYFRMAPEDWLQ--AEM---QGEIVALVHSHPGGLPW 76
Cdd:pfam14464   3 PLLDAIVAHARAAHPLECCGILLgNELESQSVRVIPLVN-PMRNRFEIDPGDSLRrvKAArerGLELVGIYHSHPGGPAY 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 218364842   77 LSEADRRLqVQSDLPWWLVCRGAIHKFRCV 106
Cdd:pfam14464  82 PSETDRRD-AAGPLPSYVIGGRAPPEIRSW 110
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
120-199 2.50e-08

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


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 52.78  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842 120 DCYTLFRDAYHLAGIEMPdfHREDDWWRNGQnlyldnleatglyQVPLSAAQPGDVLLccFGSS--VPNHAAIYCGDGEL 197
Cdd:COG0791  126 DCSGLVQYVYRQAGISLP--RTSADQAAAGT-------------PVSRSELQPGDLVF--FRTGggGISHVGIYLGNGKF 188


                 ..
gi 218364842 198 LH 199
Cdd:COG0791  189 IH 190
MPN_archaeal cd08072
Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only ...
 3-84 2.11e-03

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: 36.85  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218364842   3 ETESAILAHARRCAPAESCGFVvRAPEG---ERYFPCVNISGEPEAYFR--MAPEDWlqaemqgEIVALVHSHPGGLPWL 77
Cdd:cd08072    4 DLLDSILEAAKSSHPNEFAALL-RGKDGvitELLILPGTESGEVSAVFPllMLPLDM-------SIVGSVHSHPSGSPRP 75


                 ....*..
gi 218364842  78 SEADRRL 84
Cdd:cd08072   76 SDADLSF 82
 
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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