NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1696019939|gb|TPX69578|]
View 

hypothetical protein SpCBS45565_g02295 [Spizellomyces sp. 'palustris']

Protein Classification

proteasome subunit alpha( domain architecture ID 10132902)

proteasome subunit alpha is a component of the proteasome complex that is involved in the proteolytic degradation of most intracellular proteins; similar to human proteasome subunit alpha type-7, -8 and fungal proteasome subunit alpha type-4

Gene Ontology:  GO:0051603|GO:0005839
PubMed:  7682410|7697118|1317508|8882582

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 2.90e-162

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: 447.58  E-value: 2.90e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIG 163
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1696019939 164 RSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQTGAKNIEIAVM 210
Cdd:cd03755   161 RNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
 
Name Accession Description Interval E-value
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 2.90e-162

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: 447.58  E-value: 2.90e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIG 163
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1696019939 164 RSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQTGAKNIEIAVM 210
Cdd:cd03755   161 RNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-233 2.67e-100

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 292.12  E-value: 2.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   1 MSGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTAD 80
Cdd:PRK03996    7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  81 ARVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKAA 160
Cdd:PRK03996   87 ARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKAT 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696019939 161 SIGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ--TGAKNIEIAVMGEDCilRTLEAAEVEEITSIIEK 233
Cdd:PRK03996  166 AIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEgkLDPENVEIAYIDVET--KKFRKLSVEEIEKYLEK 238
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 2-209 1.17e-91

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: 269.52  E-value: 1.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   2 SGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADA 81
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  82 RVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKAAS 161
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGALLEYKATA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696019939 162 IGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ--TGAKNIEIAV 209
Cdd:TIGR03633 160 IGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEdkLTPENVEVAY 209
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-213 2.25e-75

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 228.49  E-value: 2.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   1 MSGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVA-KLQDPRTVRKIAMLDDHICMTFAGLTA 79
Cdd:COG0638     6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  80 DARVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSgGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKA 159
Cdd:COG0638    86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1696019939 160 ASIGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ----TGaKNIEIAVMGED 213
Cdd:COG0638   164 VAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAErdsaSG-DGIDVAVITED 220
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-210 4.85e-72

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: 218.59  E-value: 4.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  27 VRKGTCAVGVRGKDVVVLGVEKKSVA--KLQDPRTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVS 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 105 VEyITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNRE 184
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 1696019939 185 DTIKLAIKSLLEVVQ---TGAKNIEIAVM 210
Cdd:pfam00227 160 EAVELAVKALKEAIDrdaLSGGNIEVAVI 188
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 4-26 7.21e-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: 58.28  E-value: 7.21e-12
                           10        20
                   ....*....|....*....|...
gi 1696019939    4 YDRALTVFSPDGHLFQVEYALEA 26
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 ...
 4-210 2.90e-162

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: 447.58  E-value: 2.90e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIG 163
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAIG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1696019939 164 RSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQTGAKNIEIAVM 210
Cdd:cd03755   161 RNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQSGSKNIELAVM 207
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 4.41e-123

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: 348.66  E-value: 4.41e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd01911     1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIG 163
Cdd:cd01911    81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAIG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1696019939 164 RSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQTG--AKNIEIAVM 210
Cdd:cd01911   161 KGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDkkAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-233 2.67e-100

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 292.12  E-value: 2.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   1 MSGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTAD 80
Cdd:PRK03996    7 QMGYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  81 ARVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKAA 160
Cdd:PRK03996   87 ARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYLEYKAT 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696019939 161 SIGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ--TGAKNIEIAVMGEDCilRTLEAAEVEEITSIIEK 233
Cdd:PRK03996  166 AIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEgkLDPENVEIAYIDVET--KKFRKLSVEEIEKYLEK 238
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 2-209 1.17e-91

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: 269.52  E-value: 1.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   2 SGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADA 81
Cdd:TIGR03633   1 MGYDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  82 RVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKAAS 161
Cdd:TIGR03633  81 RVLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGALLEYKATA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1696019939 162 IGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ--TGAKNIEIAV 209
Cdd:TIGR03633 160 IGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEdkLTPENVEVAY 209
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-209 5.59e-90

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: 264.96  E-value: 5.59e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   3 GYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADAR 82
Cdd:cd03756     1 GYDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  83 VLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKAASI 162
Cdd:cd03756    81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVD-DGGPRLFETDPSGAYNEYKATAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1696019939 163 GRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ--TGAKNIEIAV 209
Cdd:cd03756   160 GSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEenETPENVEIAY 208
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-226 1.02e-78

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: 236.83  E-value: 1.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd03750     1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKAASIG 163
Cdd:cd03750    81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWD-EGGPYLYQVDPSGSYFTWKATAIG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1696019939 164 RSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVV--QTGAKNIEIAVMGEDCILRTLEAAEVEE 226
Cdd:cd03750   160 KNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFegQMTEKNIEIGICGETKGFRLLTPAEIKD 224
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 1-213 2.25e-75

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 228.49  E-value: 2.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   1 MSGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVA-KLQDPRTVRKIAMLDDHICMTFAGLTA 79
Cdd:COG0638     6 QSSYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATMgNLIASKSIEKIFKIDDHIGVAIAGLVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  80 DARVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSgGVRPFGISTLLIGFDaDKVPKLYQTDPSGIYSEWKA 159
Cdd:COG0638    86 DARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQY-GVRPFGVALLIGGVD-DGGPRLFSTDPSGGLYEEKA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1696019939 160 ASIGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQ----TGaKNIEIAVMGED 213
Cdd:COG0638   164 VAIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAErdsaSG-DGIDVAVITED 220
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 27-210 4.85e-72

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: 218.59  E-value: 4.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  27 VRKGTCAVGVRGKDVVVLGVEKKSVA--KLQDPRTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVS 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRgsKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 105 VEyITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNRE 184
Cdd:pfam00227  81 VE-LAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDLTLE 159

                         170       180
                  ....*....|....*....|....*....
gi 1696019939 185 DTIKLAIKSLLEVVQ---TGAKNIEIAVM 210
Cdd:pfam00227 160 EAVELAVKALKEAIDrdaLSGGNIEVAVI 188
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 1.01e-69

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: 213.36  E-value: 1.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQD-PRTVRKIAMLDDHICMTFAGLTADAR 82
Cdd:cd03752     3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDqSFSSEKIYKIDDHIACAVAGITSDAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  83 VLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASI 162
Cdd:cd03752    83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKATAI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696019939 163 GRSSKTVREFLEKNYKEEMNREDTIKLAIKSL---LEVVQTGAKNIEIAVM 210
Cdd:cd03752   163 GNNNQAAQSLLKQDYKDDMTLEEALALAVKVLsktMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 4-242 7.58e-68

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 210.09  E-value: 7.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDP-RTVRKIAMLDDHICMTFAGLTADAR 82
Cdd:PTZ00246    5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPgKINEKIYKIDSHIFCAVAGLTADAN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  83 VLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASI 162
Cdd:PTZ00246   85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWKATAI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 163 GRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQT---GAKNIEIAVMGED-----CILRTLEAAEVEEITSIIEKE 234
Cdd:PTZ00246  165 GQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDStspKADKIEVGILSHGetdgePIQKMLSEKEIAELLKKVTQE 244


                  ....*...
gi 1696019939 235 NAAEAEKK 242
Cdd:PTZ00246  245 YAKENTNN 252
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-211 5.00e-65

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: 201.37  E-value: 5.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRtvRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQ--KKIFKVDDHIGIAIAGLTADARV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKvPKLYQTDPSGIYSEWKAASIG 163
Cdd:cd03749    79 LSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESG-PHLFQTCPSGNYFEYKATSIG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1696019939 164 RSSKTVREFLEKNYK--EEMNREDTIKLAIKSLLEVVQTG----AKNIEIAVMG 211
Cdd:cd03749   158 ARSQSARTYLERHFEefEDCSLEELIKHALRALRETLPGEqeltIKNVSIAIVG 211
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 31-210 6.33e-64

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: 197.72  E-value: 6.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  31 TCAVGVRGKDVVVLGVEKKSVAKLQD-PRTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSVEYIT 109
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 110 RYIAGVQQKYTQSggVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNREDTIKL 189
Cdd:cd01906    81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEAIEL 158

                         170       180
                  ....*....|....*....|....
gi 1696019939 190 AIKSLLEVVQTGA---KNIEIAVM 210
Cdd:cd01906   159 ALKALKSALERDLysgGNIEVAVI 182
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 4-210 2.32e-62

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: 194.86  E-value: 2.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADARV 83
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  84 LINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGV-----RPFGISTLLIGFDADKvPKLYQTDPSGIYSEWK 158
Cdd:cd03753    81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDDGkkamsRPFGVALLIAGVDENG-PQLFHTDPSGTFTRCD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1696019939 159 AASIGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEVVQT--GAKNIEIAVM 210
Cdd:cd03753   160 AKAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEklNSTNVELATV 213
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 2-197 1.98e-55

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: 177.09  E-value: 1.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   2 SGYDRALTVFSPDGHLFQVEYALEAVRKGTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHICMTFAGLTADA 81
Cdd:cd03751     2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  82 RVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKvPKLYQTDPSGIYSEWKAAS 161
Cdd:cd03751    82 RHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDG-PQLYMIEPSGVSYGYFGCA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1696019939 162 IGRSSKTVREFLEKNYKEEMNREDTIKLAIKSLLEV 197
Cdd:cd03751   161 IGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIV 196
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-209 1.61e-54

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: 174.73  E-value: 1.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   3 GYDRALTVFSPDGHLFQVEYALEAVRK-GTCAVGVRGKDVVVLGVEKKSVAKLQDPRTVRKIAMLDDHI--CMTfaGLTA 79
Cdd:cd03754     1 GFDRHITIFSPEGRLYQVEYAFKAVKNaGLTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIgcVMT--GMIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  80 DARVLINKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKA 159
Cdd:cd03754    79 DSRSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1696019939 160 ASIGRSSKTVREFLEKNYKEE----MNREDTIKLAIKSLLEVVQTG--AKNIEIAV 209
Cdd:cd03754   159 TAAGVKEQEATNFLEKKLKKKpdliESYEETVELAISCLQTVLSTDfkATEIEVGV 214
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 31-196 3.93e-45

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: 149.08  E-value: 3.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  31 TCAVGVRGKDVVVLGVEKKSVAKLQDP-RTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSVEYIT 109
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 110 RYIAGVQQKYTQsggVRPFGISTLLIGFDADKvPKLYQTDPSGIYSEW-KAASIGRSSKTVREFLEKNYKEEMNREDTIK 188
Cdd:cd01901    81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGG-GNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEAVE 156


                  ....*...
gi 1696019939 189 LAIKSLLE 196
Cdd:cd01901   157 LALKALKS 164
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 31-215 2.62e-23

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: 93.28  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  31 TCAVGVRGKDVVVLGVEKKS-----VAKlqdpRTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSV 105
Cdd:cd01912     1 TTIVGIKGKDGVVLAADTRAsagslVAS----RNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 106 EYITRYIAGVQQKYtQSGgvrPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNRED 185
Cdd:cd01912    77 KAAANLLSNILYSY-RGF---PYYVSLIVGGVDKGGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEE 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1696019939 186 TIKLAIKSLLEV----VQTGaKNIEIAVMGEDCI 215
Cdd:cd01912   153 AVELVKKAIDSAierdLSSG-GGVDVAVITKDGV 185
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-213 1.73e-22

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: 91.16  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  31 TCAVGVRGKDVVVLGVEKK-SVAKLQDPRTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSVEYIT 109
Cdd:cd03764     1 TTTVGIVCKDGVVLAADKRaSMGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 110 RYIAGVqqkyTQSGGVRPFGISTLLIGFDADKvPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNREDTIKL 189
Cdd:cd03764    81 TLLSNI----LNSSKYFPYIVQLLIGGVDEEG-PHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKKL 155

                         170       180
                  ....*....|....*....|....*...
gi 1696019939 190 AIKSLLEVVQ----TGaKNIEIAVMGED 213
Cdd:cd03764   156 AIRAIKSAIErdsaSG-DGIDVVVITKD 182
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 4-26 7.21e-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: 58.28  E-value: 7.21e-12
                           10        20
                   ....*....|....*....|...
gi 1696019939    4 YDRALTVFSPDGHLFQVEYALEA 26
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 4-26 1.47e-11

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: 57.36  E-value: 1.47e-11
                          10        20
                  ....*....|....*....|...
gi 1696019939   4 YDRALTVFSPDGHLFQVEYALEA 26
Cdd:pfam10584   1 YDRSITTFSPDGRLFQVEYAMKA 23
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-197 8.85e-09

proteasome beta type-2 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: 239727  Cd Length: 193  Bit Score: 53.74  E-value: 8.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  32 CAVGVRGKDVVVL---GVEKKSVAKLQDprTVRKIAMLDDHICMTFAGLTAD---------ARVLINKARiecqsHRLTV 99
Cdd:cd03758     3 TLIGIKGKDFVILaadTSAARSILVLKD--DEDKIYKLSDHKLMACSGEAGDrlqfaeyiqKNIQLYKMR-----NGYEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 100 EDPVSVEYITRYIAgvqqKYTQSGGvrPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKE 179
Cdd:cd03758    76 SPKAAANFTRRELA----ESLRSRT--PYQVNLLLAGYDKVEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKP 149

                         170
                  ....*....|....*...
gi 1696019939 180 EMNREDTIKLAIKSLLEV 197
Cdd:cd03758   150 DMTVEEALELMKKCIKEL 167
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-195 7.12e-08

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: 51.04  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  31 TCAVGVRGKDVVVLGVEKKSVaklQDP----RTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSVE 106
Cdd:cd03763     1 TTIVGVVFKDGVVLGADTRAT---EGPivadKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 107 YITRYIagvQQKYTQSGGvrpfGISTLLI--GFDAdKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNRE 184
Cdd:cd03763    78 TALTML---KQHLFRYQG----HIGAALVlgGVDY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEE 149

                         170
                  ....*....|.
gi 1696019939 185 DTIKLAIKSLL 195
Cdd:cd03763   150 EAKKLVCEAIE 160
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 6-194 3.60e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 46.91  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939   6 RALTVFSPDGHLfQVEYAleavrKGTCAVGVRGKDVVVLGVEKKSVA-KLQDPRTVRKIAMLDDHICMTFAGLTADARVL 84
Cdd:PTZ00488   21 AEYTFDHGDANK-AIEFA-----HGTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADCSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  85 INKARIECQSHRLTVEDPVSVEYITRYIAGVQQKYtqsggvRPFGIS--TLLIGFDaDKVPKLYQTDPSGIYSEWKAASI 162
Cdd:PTZ00488   95 ERELAMQCRLYELRNGELISVAAASKILANIVWNY------KGMGLSmgTMICGWD-KKGPGLFYVDNDGTRLHGNMFSC 167

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1696019939 163 GRSSKTVREFLEKNYKEEMNREDTIKLAIKSL 194
Cdd:PTZ00488  168 GSGSTYAYGVLDAGFKWDLNDEEAQDLGRRAI 199
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 31-194 8.46e-05

proteasome beta type-6 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: 239731  Cd Length: 188  Bit Score: 42.21  E-value: 8.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  31 TCAVGVRGKDVVVLGVEKKS-----VAKlqdpRTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSV 105
Cdd:cd03762     1 TTIIAVEYDGGVVLGADSRTstgsyVAN----RVTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 106 EYITRYIAGVQQKYTQSggvrpfgISTLLI--GFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNR 183
Cdd:cd03762    77 KTAASLFKNLCYNYKEM-------LSAGIIvaGWDEQNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTL 149

                         170
                  ....*....|.
gi 1696019939 184 EDTIKLAIKSL 194
Cdd:cd03762   150 EECIKFVKNAL 160
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 59-190 3.52e-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: 37.22  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  59 TVRKIAMLDDHICMTFAGLTADA----RVLinkaRIECQSHRLTVEDPVSVEYITRYIAGVQQKYtqsggvRPFGIS--T 132
Cdd:cd03761    30 TVKKVIEINPYLLGTMAGGAADCqyweRVL----GRECRLYELRNKERISVAAASKLLSNMLYQY------KGMGLSmgT 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1696019939 133 LLIGFDaDKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLEKNYKEEMNREDTIKLA 190
Cdd:cd03761   100 MICGWD-KTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLSVEEAYDLA 156
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-219 5.66e-03

proteasome beta type-1 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: 239726  Cd Length: 212  Bit Score: 36.85  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939  30 GTCaVGVRGKDVVVLGVEKKSVAKLQDP-RTVRKIAMLDDHICMTFAGLTADARVLINKARIECQSHRLTVEDPVSveyi 108
Cdd:cd03757     9 GTV-LAIAGNDFAVIAGDTRLSEGYSILsRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMS---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696019939 109 TRYIAGVQQKYTQSGGVRPFGISTLLIGFDADKVPKLYQTDPSGIYSEWKAASIGRSSKTVREFLE-----KNYK----E 179
Cdd:cd03757    84 TEAIAQLLSTILYSRRFFPYYVFNILAGIDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLLDnqvgrKNQNnverT 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1696019939 180 EMNREDTIKL---AIKSLLEV-VQTGaKNIEIAVMGEDCILRTL 219
Cdd:cd03757   164 PLSLEEAVSLvkdAFTSAAERdIYTG-DSLEIVIITKDGIEEET 206
 
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