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Conserved domains on  [gi|2507698956|ref|XP_056078901|]
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uncharacterized protein SMKI_13G4330 [Saccharomyces mikatae IFO 1815]

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

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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 ...
 6-217 4.70e-111

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 cd03749:

Pssm-ID: 469781 [Multi-domain]  Cd Length: 211  Bit Score: 317.31  E-value: 4.70e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDDHMGLSLAGLAPDARVLS 85
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  86 NYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIGARS 165
Cdd:cd03749    81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507698956 166 QGAKTYLERTLDTFikIDGNPDELIKAGIEAISQSLRDES-LTVDNLSIAIVG 217
Cdd:cd03749   161 QSARTYLERHFEEF--EDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
 
Name Accession Description Interval E-value
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-217 4.70e-111

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: 317.31  E-value: 4.70e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDDHMGLSLAGLAPDARVLS 85
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  86 NYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIGARS 165
Cdd:cd03749    81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507698956 166 QGAKTYLERTLDTFikIDGNPDELIKAGIEAISQSLRDES-LTVDNLSIAIVG 217
Cdd:cd03749   161 QSARTYLERHFEEF--EDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-234 4.92e-54

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 173.48  E-value: 4.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL---SSYQKkIIKCDDHMGLSLAGLAPDAR 82
Cdd:PRK03996   10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiepSSIEK-IFKIDDHIGAASAGLVADAR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  83 VLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIG 162
Cdd:PRK03996   89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIG 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507698956 163 ARSQGAKTYLERTLDTfikiDGNPDELIKAGIEAISQSLrDESLTVDNLSIAIVG-ENMPFTIYDGEAVAKYI 234
Cdd:PRK03996  169 AGRDTVMEFLEKNYKE----DLSLEEAIELALKALAKAN-EGKLDPENVEIAYIDvETKKFRKLSVEEIEKYL 236
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-216 1.40e-49

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: 160.43  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  29 IKQGSVTVGLRSNTHAVLVALKRN---ADELSSYQ-KKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLA 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrgSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 105 VEKAGYlLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGA-HLLEFQPSGNVMELYGTAIGARSQGAKTYLERtldtFIKID 183
Cdd:pfam00227  81 VELAAR-IADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK----LYRPD 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2507698956 184 GNPDELIKAGIEAISQSLRDESLTVDNLSIAIV 216
Cdd:pfam00227 156 LTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-219 1.95e-44

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 148.75  E-value: 1.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNAdeLSSYQ-----KKIIKCDDHMGLSLAGLAPD 80
Cdd:COG0638     9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAT--MGNLIasksiEKIFKIDDHIGVAIAGLVAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  81 ARVLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQsYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTA 160
Cdd:COG0638    87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVA 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2507698956 161 IGARSQGAKTYLERTLDTfikiDGNPDELIKAGIEAISQSLRDESLTVDNLSIAIVGEN 219
Cdd:COG0638   166 IGSGSPFARGVLEKEYRE----DLSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 6-28 8.31e-09

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: 49.80  E-value: 8.31e-09
                           10        20
                   ....*....|....*....|...
gi 2507698956    6 YDGDTVTFSPTGRLFQVEYALEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-217 4.70e-111

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: 317.31  E-value: 4.70e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDDHMGLSLAGLAPDARVLS 85
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  86 NYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIGARS 165
Cdd:cd03749    81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2507698956 166 QGAKTYLERTLDTFikIDGNPDELIKAGIEAISQSLRDES-LTVDNLSIAIVG 217
Cdd:cd03749   161 QSARTYLERHFEEF--EDCSLEELIKHALRALRETLPGEQeLTIKNVSIAIVG 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 1.67e-80

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: 239.65  E-value: 1.67e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDDHMGLSLAGLAPDARV 83
Cdd:cd01911     1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLldPSSVEKIFKIDDHIGCAVAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  84 LSNYLRQQCNYSSLVFNRKLAVEkagYL---LCDKAQKNTQSYGGRPYGVGLLIIGYDKS-GAHLLEFQPSGNVMELYGT 159
Cdd:cd01911    81 LVNRARVEAQNYRYTYGEPIPVE---VLvkrIADLAQVYTQYGGVRPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYKAT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2507698956 160 AIGARSQGAKTYLERTLDTFIkidgNPDELIKAGIEAISQSLrDESLTVDNLSIAIV 216
Cdd:cd01911   158 AIGKGSQEAKTFLEKRYKKDL----TLEEAIKLALKALKEVL-EEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
6-234 4.92e-54

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 173.48  E-value: 4.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL---SSYQKkIIKCDDHMGLSLAGLAPDAR 82
Cdd:PRK03996   10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiepSSIEK-IFKIDDHIGAASAGLVADAR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  83 VLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIG 162
Cdd:PRK03996   89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLEYKATAIG 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507698956 163 ARSQGAKTYLERTLDTfikiDGNPDELIKAGIEAISQSLrDESLTVDNLSIAIVG-ENMPFTIYDGEAVAKYI 234
Cdd:PRK03996  169 AGRDTVMEFLEKNYKE----DLSLEEAIELALKALAKAN-EGKLDPENVEIAYIDvETKKFRKLSVEEIEKYL 236
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 1.15e-49

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: 161.34  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL---SSYQKkIIKCDDHMGLSLAGLAPDAR 82
Cdd:cd03756     2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLvepESIEK-IYKIDDHVGAATSGLVADAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  83 VLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIG 162
Cdd:cd03756    81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2507698956 163 ARSQGAKTYLERTLdtfiKIDGNPDELIKAGIEAISQSLRDEsLTVDNLSIAIV 216
Cdd:cd03756   161 SGRQAVTEFLEKEY----KEDMSLEEAIELALKALYAALEEN-ETPENVEIAYV 209
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 29-216 1.40e-49

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: 160.43  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  29 IKQGSVTVGLRSNTHAVLVALKRN---ADELSSYQ-KKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLA 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRAtrgSKLLSKDTvEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 105 VEKAGYlLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGA-HLLEFQPSGNVMELYGTAIGARSQGAKTYLERtldtFIKID 183
Cdd:pfam00227  81 VELAAR-IADLLQAYTQYSGRRPFGVSLLIAGYDEDGGpHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEK----LYRPD 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2507698956 184 GNPDELIKAGIEAISQSLRDESLTVDNLSIAIV 216
Cdd:pfam00227 156 LTLEEAVELAVKALKEAIDRDALSGGNIEVAVI 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 4.07e-45

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: 149.81  E-value: 4.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQK---KIIKCDDHMGLSLAGLAPDAR 82
Cdd:cd03752     3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFsseKIYKIDDHIACAVAGITSDAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  83 VLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQsYGG-RPYGVGLLIIGYDKS-GAHLLEFQPSGNVMELYGTA 160
Cdd:cd03752    83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQ-YGGlRPFGVSFLYAGWDKHyGFQLYQSDPSGNYSGWKATA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2507698956 161 IGARSQGAKTYLERTldtfIKIDGNPDELIKAGIEAISQSLRDESLTVDNLSIAIV 216
Cdd:cd03752   162 IGNNNQAAQSLLKQD----YKDDMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 6-219 1.95e-44

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 148.75  E-value: 1.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNAdeLSSYQ-----KKIIKCDDHMGLSLAGLAPD 80
Cdd:COG0638     9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRAT--MGNLIasksiEKIFKIDDHIGVAIAGLVAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  81 ARVLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQsYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTA 160
Cdd:COG0638    87 ARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQ-YGVRPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAVA 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2507698956 161 IGARSQGAKTYLERTLDTfikiDGNPDELIKAGIEAISQSLRDESLTVDNLSIAIVGEN 219
Cdd:COG0638   166 IGSGSPFARGVLEKEYRE----DLSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 3.63e-43

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: 144.79  E-value: 3.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDDHMGLSLAGLAPDARV 83
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLmePSSVEKIMEIDDHIGCAMSGLIADART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  84 LSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKA-----QKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYG 158
Cdd:cd03753    81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLAlqfgeGDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507698956 159 TAIGARSQGAKTYLErtlDTFikidgNPDELIKAGIEAISQSLRD---ESLTVDNLSIAIV 216
Cdd:cd03753   161 KAIGSGSEGAQSSLQ---EKY-----HKDMTLEEAEKLALSILKQvmeEKLNSTNVELATV 213
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 35-216 8.09e-40

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: 135.32  E-value: 8.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  35 TVGLRSNTHAVLVALKRNA---DELSSYQKKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVEKAGYL 111
Cdd:cd01906     3 IVGIKGKDGVVLAADKRVTsglLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 112 LCDKAQKNTQSYggRPYGVGLLIIGYDK-SGAHLLEFQPSGNVMELYGTAIGARSQGAKTYLERtldtFIKIDGNPDELI 190
Cdd:cd01906    83 LANLLYEYTQSL--RPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEK----LYKPDMTLEEAI 156

                         170       180
                  ....*....|....*....|....*.
gi 2507698956 191 KAGIEAISQSLRDESLTVDNLSIAIV 216
Cdd:cd01906   157 ELALKALKSALERDLYSGGNIEVAVI 182
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 12-234 1.01e-39

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: 136.30  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  12 TFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSY--QKKIIKCDDHMGLSLAGLAPDARVLSNYLR 89
Cdd:cd03750     7 TFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDEssVHKVEQITPHIGMVYSGMGPDFRVLVKKAR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  90 QQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIGARSQGAK 169
Cdd:cd03750    87 KIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGKNYSNAK 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507698956 170 TYLERTLDTFIKIDGNpdelIKAGIEAISQSLrDESLTVDNLSIAIVGENMPFTIYDGEAVAKYI 234
Cdd:cd03750   167 TFLEKRYNEDLELEDA----IHTAILTLKEGF-EGQMTEKNIEIGICGETKGFRLLTPAEIKDYL 226
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-216 2.15e-38

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: 132.49  E-value: 2.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDDHMGLSLAGLAPDARV 83
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLqdPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  84 LSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSG-AHLLEFQPSGNVMELYGTAIG 162
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2507698956 163 ARSQGAKTYLERTLdtfiKIDGNPDELIKAGIEAISQSLRDESltvDNLSIAIV 216
Cdd:cd03755   161 RNSKTVREFLEKNY----KEEMTRDDTIKLAIKALLEVVQSGS---KNIELAVM 207
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 6-234 4.13e-36

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 128.05  E-value: 4.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQK---KIIKCDDHMGLSLAGLAPDAR 82
Cdd:PTZ00246    5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGKineKIYKIDSHIFCAVAGLTADAN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  83 VLSNYLR---QQCNYSslvFNRKLAVEKAGYLLCDKAQKNTQSYGGRPYGVGLLIIGYD-KSGAHLLEFQPSGNVMELYG 158
Cdd:PTZ00246   85 ILINQCRlyaQRYRYT---YGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDeNLGYQLYHTDPSGNYSGWKA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2507698956 159 TAIGARSQGAKTYLERTLdtfiKIDGNPDELIKAGIEAISQSLRDESLTVDNLSIAIVGENMPftiyDGEAVAKYI 234
Cdd:PTZ00246  162 TAIGQNNQTAQSILKQEW----KEDLTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHGET----DGEPIQKML 229
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 6-204 3.75e-33

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: 118.92  E-value: 3.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDDHMGLSLAGLAPDARV 83
Cdd:cd03751     4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLyePGSNKRIFNVDRHIGIAVAGLLADGRH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  84 LSNYLRQQC-----NYSSLVFNRKLAVEKAGYLlcdkaQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYG 158
Cdd:cd03751    84 LVSRAREEAenyrdNYGTPIPVKVLADRVAMYM-----HAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2507698956 159 TAIGARSQGAKTYLErtldtfiKIDGN---PDELIKAGIEAIsQSLRDE 204
Cdd:cd03751   159 CAIGKGKQAAKTELE-------KLKFSeltCREAVKEAAKII-YIVHDE 199
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 13-216 2.61e-31

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: 114.25  E-value: 2.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  13 FSPTGRLFQVEYALEAIKQGSVT-VGLRSNTHAVLVALKRNADEL--SSYQKKIIKCDDHMGLSLAGLAPDARVLSnylr 89
Cdd:cd03754     9 FSPEGRLYQVEYAFKAVKNAGLTsVAVRGKDCAVVVTQKKVPDKLidPSTVTHLFRITDEIGCVMTGMIADSRSQV---- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  90 QQCNYSSLVFNRKLAVEKAGYLLC----DKAQKNTQSYGGRPYGVGLLIIGYD-KSGAHLLEFQPSGNVMELYGTAIGAR 164
Cdd:cd03754    85 QRARYEAAEFKYKYGYEMPVDVLAkriaDINQVYTQHAYMRPLGVSMILIGIDeELGPQLYKCDPAGYFAGYKATAAGVK 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2507698956 165 SQGAKTYLERTLDTFIKIDGNPDELIKAGIEAISQSLrDESLTVDNLSIAIV 216
Cdd:cd03754   165 EQEATNFLEKKLKKKPDLIESYEETVELAISCLQTVL-STDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 35-198 1.56e-27

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: 102.86  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  35 TVGLRSNTHAVLVALKRNADEL---SSYQKKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVEKAGYL 111
Cdd:cd01901     3 SVAIKGKGGVVLAADKRLSSGLpvaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 112 LCDKAQKNTQsygGRPYGVGLLIIGYDKSGAHLLEFQPSGNVME-LYGTAIGARSQGAKTYLERTldtfIKIDGNPDELI 190
Cdd:cd01901    83 LAKLLQVYTQ---GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIEnPGAVATGSRSQRAKSLLEKL----YKPDMTLEEAV 155


                  ....*...
gi 2507698956 191 KAGIEAIS 198
Cdd:cd01901   156 ELALKALK 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 35-219 9.28e-17

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: 75.37  E-value: 9.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  35 TVGLRSNTHAVLVALKRNADE---LSSYQKKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVEKAGYL 111
Cdd:cd03764     3 TVGIVCKDGVVLAADKRASMGnfiASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 112 LCDKaqknTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIGARSQGAKTYLERTLDTFIKIdgnpDELIK 191
Cdd:cd03764    83 LSNI----LNSSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTV----EEAKK 154

                         170       180
                  ....*....|....*....|....*...
gi 2507698956 192 AGIEAISQSLRDESLTVDNLSIAIVGEN 219
Cdd:cd03764   155 LAIRAIKSAIERDSASGDGIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 35-219 5.55e-11

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: 59.38  E-value: 5.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  35 TVGLRSNTHAVLVALKR---NADELSSYQKKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVEKAGYL 111
Cdd:cd01912     3 IVGIKGKDGVVLAADTRasaGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 112 LcdkaqKNTQ-SYGGRPYGVGLLIIGYDK-SGAHLLEFQPSGNVMELYGTAIGARSQGAKTYLERtldtFIKIDGNPDEL 189
Cdd:cd01912    83 L-----SNILySYRGFPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDR----GYKPDMTLEEA 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 2507698956 190 IKAGIEAISQSLRDESLTVDNLSIAIVGEN 219
Cdd:cd01912   154 VELVKKAIDSAIERDLSSGGGVDVAVITKD 183
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 6-28 3.51e-09

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: 50.81  E-value: 3.51e-09
                          10        20
                  ....*....|....*....|...
gi 2507698956   6 YDGDTVTFSPTGRLFQVEYALEA 28
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 ...
 6-28 8.31e-09

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: 49.80  E-value: 8.31e-09
                           10        20
                   ....*....|....*....|...
gi 2507698956    6 YDGDTVTFSPTGRLFQVEYALEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 29-197 3.55e-05

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 43.82  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  29 IKQGSVTVGLRSNThAVLVALKRNADE----LSSYQKKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLA 104
Cdd:PTZ00488   36 FAHGTTTLAFKYGG-GIIIAVDSKATAgpyiASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELIS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956 105 VEKAGYLLCDKaqknTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVMELYGTAIGARSqgakTYLERTLDTFIKIDG 184
Cdd:PTZ00488  115 VAAASKILANI----VWNYKGMGLSMGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGS----TYAYGVLDAGFKWDL 186

                         170
                  ....*....|...
gi 2507698956 185 NPDELIKAGIEAI 197
Cdd:PTZ00488  187 NDEEAQDLGRRAI 199
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-174 1.22e-04

proteasome beta type-7 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: 239732  Cd Length: 189  Bit Score: 41.41  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  61 KKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKAQKntqsYGGRpYGVGLLIIGYDKS 140
Cdd:cd03763    32 EKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALTMLKQHLFR----YQGH-IGAALVLGGVDYT 106

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2507698956 141 GAHLLEFQPSGNVMELYGTAIGARSQGAKTYLER 174
Cdd:cd03763   107 GPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLED 140
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 61-203 1.61e-03

proteasome beta type-5 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: 239730  Cd Length: 188  Bit Score: 38.38  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507698956  61 KKIIKCDDHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVEKAGYLLCDKaqknTQSYGGRPYGVGLLIIGYDKS 140
Cdd:cd03761    32 KKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVAAASKLLSNM----LYQYKGMGLSMGTMICGWDKT 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507698956 141 GAHLLEFQPSGNVMELYGTAIGARSqgakTYLERTLDTFIKIDGNPDELIKAGIEAISQ-SLRD 203
Cdd:cd03761   108 GPGLYYVDSDGTRLKGDLFSVGSGS----TYAYGVLDSGYRYDLSVEEAYDLARRAIYHaTHRD 167
 
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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