NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119595806|gb|EAW75400|]
View 

hCG41772, isoform CRA_c [Homo sapiens]

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 3-155 3.62e-88

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


The actual alignment was detected with superfamily member cd03755:

Pssm-ID: 469781 [Multi-domain]  Cd Length: 207  Bit Score: 256.52  E-value: 3.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAGqsrLRHGGSCHV----TSALYAEQWAQ 153
Cdd:cd03755   81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRytqsgGVRPFGISTLIVG---FDPDGTPRLyqtdPSGTYSAWKAN 157


                 ..
gi 119595806 154 AV 155
Cdd:cd03755  158 AI 159
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-155 3.62e-88

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 256.52  E-value: 3.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAGqsrLRHGGSCHV----TSALYAEQWAQ 153
Cdd:cd03755   81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRytqsgGVRPFGISTLIVG---FDPDGTPRLyqtdPSGTYSAWKAN 157


                 ..
gi 119595806 154 AV 155
Cdd:cd03755  158 AI 159
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-116 5.30e-56

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 175.79  E-value: 5.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:PRK03996   8 MGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADA 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119595806  81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQ 116
Cdd:PRK03996  88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQ 123
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 1-130 1.86e-54

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 171.29  E-value: 1.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806    1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119595806   81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQytqhgGVRPFGVALLIAG 135
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-130 2.05e-44

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 146.06  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVA-KLQDERTVRKICALDDNVCMAFAGLTAD 79
Cdd:COG0638    7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119595806  80 ARIVINRARVECQSHRLTVEDPVTVEYITRYIASLK----QVGACPLACSPLAAG 130
Cdd:COG0638   87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLqgytQYGVRPFGVALLIGG 141
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 26-130 4.23e-34

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 118.44  E-value: 4.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   26 VKKGSTAVGVRGRDIVVLGVEKKSVA--KLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVT 103
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 119595806  104 VEyITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:pfam00227  81 VE-LAARIADLLQAytqysGRRPFGVSLLIAG 111
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 3-25 2.21e-12

Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 57.89  E-value: 2.21e-12
                           10        20
                   ....*....|....*....|...
gi 119595806     3 YDRAITVFSPDGHLFQVEYAQEA 25
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-155 3.62e-88

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 256.52  E-value: 3.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAGqsrLRHGGSCHV----TSALYAEQWAQ 153
Cdd:cd03755   81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRytqsgGVRPFGISTLIVG---FDPDGTPRLyqtdPSGTYSAWKAN 157


                 ..
gi 119595806 154 AV 155
Cdd:cd03755  158 AI 159
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-130 5.46e-70

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 210.38  E-value: 5.46e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:cd01911   81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVytqygGVRPFGVSLLIAG 133
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-116 5.30e-56

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 175.79  E-value: 5.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:PRK03996   8 MGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADA 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119595806  81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQ 116
Cdd:PRK03996  88 RVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQ 123
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 1-130 1.86e-54

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 171.29  E-value: 1.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806    1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADA 80
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119595806   81 RIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQytqhgGVRPFGVALLIAG 135
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-130 6.00e-53

proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 167.12  E-value: 6.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:cd03756   82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQytqhgGVRPFGVALLIAG 134
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-130 2.05e-44

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 146.06  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   1 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVA-KLQDERTVRKICALDDNVCMAFAGLTAD 79
Cdd:COG0638    7 SSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVAD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119595806  80 ARIVINRARVECQSHRLTVEDPVTVEYITRYIASLK----QVGACPLACSPLAAG 130
Cdd:COG0638   87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLqgytQYGVRPFGVALLIGG 141
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-114 7.27e-42

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 139.01  E-value: 7.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASL 114
Cdd:cd03753   81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDL 112
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-130 1.62e-35

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 122.84  E-value: 1.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQD-ERTVRKICALDDNVCMAFAGLTADAR 81
Cdd:cd03752    3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDqSFSSEKIYKIDDHIACAVAGITSDAN 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119595806  82 IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:cd03752   83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGytqygGLRPFGVSFLYAG 136
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-155 2.02e-35

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 122.39  E-value: 2.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03751    4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADGRH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQVGAC-----PLACSPLAAGQSrlRHGGSCHVT--SALYAEQWAQAV 155
Cdd:cd03751   84 LVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLyssvrPFGCSVLLGGYD--SDGPQLYMIepSGVSYGYFGCAI 161
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-133 2.20e-34

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 120.12  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03750    1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAGQSR 133
Cdd:cd03750   81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEytqsgGVRPFGVSLLIAGWDE 136
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 26-130 4.23e-34

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 118.44  E-value: 4.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   26 VKKGSTAVGVRGRDIVVLGVEKKSVA--KLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVT 103
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 119595806  104 VEyITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:pfam00227  81 VE-LAARIADLLQAytqysGRRPFGVSLLIAG 111
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-117 3.53e-32

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 113.92  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERtvRKICALDDNVCMAFAGLTADARI 82
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQ--KKIFKVDDHIGIAIAGLTADARV 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 119595806  83 VINRARVECQSHRLTVEDPVTVEYITRYIASLKQV 117
Cdd:cd03749   79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQI 113
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-130 4.61e-30

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 108.86  E-value: 4.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGS-TAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADAR 81
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119595806  82 IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVytqhaYMRPLGVSMILIG 135
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 30-155 2.96e-29

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 105.65  E-value: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  30 STAVGVRGRDIVVLGVEKKSVAKLQD-ERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYIT 108
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119595806 109 RYIASLKQV---GACPLACSPLAAGQSRLRHGGSCHVT-SALYAEQWAQAV 155
Cdd:cd01906   81 KLLANLLYEytqSLRPLGVSLLVAGVDEEGGPQLYSVDpSGSYIEYKATAI 131
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 3-130 1.10e-27

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 103.78  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806   3 YDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDE-RTVRKICALDDNVCMAFAGLTADAR 81
Cdd:PTZ00246   5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLTADAN 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119595806  82 IVINRARVECQSHRLTVEDPVTVEYITRYIASLKQV-----GACPLACSPLAAG 130
Cdd:PTZ00246  85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSytqfgGLRPFGVSFLFAG 138
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 30-157 2.31e-22

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 87.45  E-value: 2.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  30 STAVGVRGRDIVVLGVEKKSVAKLQD-ERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYIT 108
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLPVaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119595806 109 RYIASLKQV--GACPLACSPLAAGQSRlRHGGSCHVTSALYAEQWAQAVWH 157
Cdd:cd01901   81 KELAKLLQVytQGRPFGVNLIVAGVDE-GGGNLYYIDPSGPVIENPGAVAT 130
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 3-25 6.97e-13

Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 463156 [Multi-domain]  Cd Length: 23  Bit Score: 59.29  E-value: 6.97e-13
                          10        20
                  ....*....|....*....|...
gi 119595806    3 YDRAITVFSPDGHLFQVEYAQEA 25
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 3-25 2.21e-12

Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A subunits of the proteasome complex proteins.


Pssm-ID: 198016 [Multi-domain]  Cd Length: 23  Bit Score: 57.89  E-value: 2.21e-12
                           10        20
                   ....*....|....*....|...
gi 119595806     3 YDRAITVFSPDGHLFQVEYAQEA 25
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-131 2.22e-09

proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 238893  Cd Length: 189  Bit Score: 53.60  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  31 TAVGVRGRDIVVLGVEKKSVA-KLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITR 109
Cdd:cd01912    2 TIVGIKGKDGVVLAADTRASAgSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                         90       100
                 ....*....|....*....|...
gi 119595806 110 YIAS-LKQVGACPLACSPLAAGQ 131
Cdd:cd01912   82 LLSNiLYSYRGFPYYVSLIVGGV 104
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-114 6.73e-08

Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme for non-lysosomal protein degradation in both the cytosol and the nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are both members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239733  Cd Length: 188  Bit Score: 49.56  E-value: 6.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595806  31 TAVGVRGRDIVVLGVEKK-SVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITR 109
Cdd:cd03764    2 TTVGIVCKDGVVLAADKRaSMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81


                 ....*
gi 119595806 110 YIASL 114
Cdd:cd03764   82 LLSNI 86
 
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