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Conserved domains on  [gi|665407395|ref|NP_001285798|]
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proteasome alpha6 subunit, isoform B [Drosophila melanogaster]

Protein Classification

proteasome subunit alpha( domain architecture ID 10132875)

proteasome subunit alpha is a component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins; similar to Homo sapiens proteasome subunit alpha type-1 and Schizosaccharomyces pombe proteasome subunit alpha type-6

CATH:  3.60.20.10
Gene Ontology:  GO:0051603|GO:0005839

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-219 2.25e-136

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: 383.18  E-value: 2.25e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSDTQRKIIPIDDHLGISIAGLTADARVLS 85
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  86 RYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRS 165
Cdd:cd03749   81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665407395 166 QSARTYLEKNLNKFLDSSKDEIIRHGIRAILGTLPTDEqgkDAGQYDITVAIVG 219
Cdd:cd03749  161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQ---ELTIKNVSIAIVG 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 ...
6-219 2.25e-136

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: 383.18  E-value: 2.25e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSDTQRKIIPIDDHLGISIAGLTADARVLS 85
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  86 RYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRS 165
Cdd:cd03749   81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665407395 166 QSARTYLEKNLNKFLDSSKDEIIRHGIRAILGTLPTDEqgkDAGQYDITVAIVG 219
Cdd:cd03749  161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQ---ELTIKNVSIAIVG 211
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-241 3.62e-60

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 190.82  E-value: 3.62e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   1 MFRNQ---YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSEL--SDTQRKIIPIDDHLGISIA 75
Cdd:PRK03996   2 MMQPQqmgYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiePSSIEKIFKIDDHIGAASA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  76 GLTADARVLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFN 155
Cdd:PRK03996  82 GLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 156 CKANSIGSRSQSARTYLEKNLNKflDSSKDEIIRHGIRAILGtlpTDEQGKDAGQYDITVAIVgKDQPFTILSNKDSAKH 235
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAK---ANEGKLDPENVEIAYIDV-ETKKFRKLSVEEIEKY 235

                 ....*.
gi 665407395 236 VAIAKE 241
Cdd:PRK03996 236 LEKLLK 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
29-218 3.79e-60

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: 188.93  E-value: 3.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   29 VKLGTATVGLKNKDYAVLVALCKPTSE----LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYP 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGskllSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  105 VsRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERG-PHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSS 183
Cdd:pfam00227  81 V-ELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLT 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 665407395  184 KDEIIRHGIRAILGTLPTDEqgkdAGQYDITVAIV 218
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDA----LSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
1-231 3.13e-50

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 164.93  E-value: 3.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   1 MFRNQ---YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPT-SEL--SDTQRKIIPIDDHLGISI 74
Cdd:COG0638    1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLiaSKSIEKIFKIDDHIGVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  75 AGLTADARVLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQ-RYdrRPYGVGLLVAGYDERGPHIYQVTPSATF 153
Cdd:COG0638   81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQyGV--RPFGVALLIGGVDDGGPRLFSTDPSGGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 154 FNCKANSIGSRSQSARTYLEKNLNKflDSSKDEIIRHGIRAIlgtlptdeqgKDAGQYD------ITVAIVGKDQpFTIL 227
Cdd:COG0638  159 YEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRAL----------YSAAERDsasgdgIDVAVITEDG-FREL 225

                 ....
gi 665407395 228 SNKD 231
Cdd:COG0638  226 SEEE 229
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
32-221 8.21e-21

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 87.26  E-value: 8.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   32 GTATVGLKNKDYAVLVALCKPTSE---LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRL 108
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGnfvASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  109 ITNLGNKMQTTtqRYdrRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSSKDEII 188
Cdd:TIGR03634  81 ATLLSNILNSN--RF--FPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYRE--DMSVEEAK 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 665407395  189 RHGIRAIlgtlptdeqgKDAGQYD------ITVAIVGKD 221
Cdd:TIGR03634 155 KLAVRAI----------KSAIERDvasgngIDVAVITKD 183
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
6-28 1.16e-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: 52.50  E-value: 1.16e-09
                           10        20
                   ....*....|....*....|...
gi 665407395     6 YDSDVTVWSPQGRLHQVEYAMEA 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 ...
6-219 2.25e-136

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: 383.18  E-value: 2.25e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSDTQRKIIPIDDHLGISIAGLTADARVLS 85
Cdd:cd03749    1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSELSSYQKKIFKVDDHIGIAIAGLTADARVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  86 RYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRS 165
Cdd:cd03749   81 RYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKATSIGARS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665407395 166 QSARTYLEKNLNKFLDSSKDEIIRHGIRAILGTLPTDEqgkDAGQYDITVAIVG 219
Cdd:cd03749  161 QSARTYLERHFEEFEDCSLEELIKHALRALRETLPGEQ---ELTIKNVSIAIVG 211
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-218 2.92e-98

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: 286.65  E-value: 2.92e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSD--TQRKIIPIDDHLGISIAGLTADARV 83
Cdd:cd01911    1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDpsSVEKIFKIDDHIGCAVAGLTADARV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  84 LSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDE-RGPHIYQVTPSATFFNCKANSIG 162
Cdd:cd01911   81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEeGGPQLYQTDPSGTYFGYKATAIG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665407395 163 SRSQSARTYLEKNLNKFLdsSKDEIIRHGIRAILGTLPTDEQGKdagqyDITVAIV 218
Cdd:cd01911  161 KGSQEAKTFLEKRYKKDL--TLEEAIKLALKALKEVLEEDKKAK-----NIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
1-241 3.62e-60

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 190.82  E-value: 3.62e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   1 MFRNQ---YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSEL--SDTQRKIIPIDDHLGISIA 75
Cdd:PRK03996   2 MMQPQqmgYDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLiePSSIEKIFKIDDHIGAASA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  76 GLTADARVLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFN 155
Cdd:PRK03996  82 GLVADARVLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 156 CKANSIGSRSQSARTYLEKNLNKflDSSKDEIIRHGIRAILGtlpTDEQGKDAGQYDITVAIVgKDQPFTILSNKDSAKH 235
Cdd:PRK03996 162 YKATAIGAGRDTVMEFLEKNYKE--DLSLEEAIELALKALAK---ANEGKLDPENVEIAYIDV-ETKKFRKLSVEEIEKY 235

                 ....*.
gi 665407395 236 VAIAKE 241
Cdd:PRK03996 236 LEKLLK 241
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
29-218 3.79e-60

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: 188.93  E-value: 3.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   29 VKLGTATVGLKNKDYAVLVALCKPTSE----LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYP 104
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATRGskllSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  105 VsRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERG-PHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSS 183
Cdd:pfam00227  81 V-ELAARIADLLQAYTQYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP--DLT 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 665407395  184 KDEIIRHGIRAILGTLPTDEqgkdAGQYDITVAIV 218
Cdd:pfam00227 158 LEEAVELAVKALKEAIDRDA----LSGGNIEVAVI 188
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-218 1.52e-55

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: 177.94  E-value: 1.52e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSD--TQRKIIPIDDHLGISIAGLTADARV 83
Cdd:cd03755    1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDprTVRKICMLDDHVCLAFAGLTADARV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  84 LSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERG-PHIYQVTPSATFFNCKANSIG 162
Cdd:cd03755   81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKANAIG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665407395 163 SRSQSARTYLEKNLNKflDSSKDEIIRHGIRAILGTLPTdeqgkdaGQYDITVAIV 218
Cdd:cd03755  161 RNSKTVREFLEKNYKE--EMTRDDTIKLAIKALLEVVQS-------GSKNIELAVM 207
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-228 2.64e-53

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: 172.89  E-value: 2.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSD--TQRKIIPIDDHLGISIAGLTADARV 83
Cdd:cd03750    1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDesSVHKVEQITPHIGMVYSGMGPDFRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  84 LSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGS 163
Cdd:cd03750   81 LVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATAIGK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665407395 164 RSQSARTYLEKNLNKflDSSKDEIIRHGIRAILGTLPTDEQGKdagqyDITVAIVGKDQPFTILS 228
Cdd:cd03750  161 NYSNAKTFLEKRYNE--DLELEDAIHTAILTLKEGFEGQMTEK-----NIEIGICGETKGFRLLT 218
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-218 5.55e-52

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: 169.05  E-value: 5.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSEL--SDTQRKIIPIDDHLGISIAGLTADARV 83
Cdd:cd03756    2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLvePESIEKIYKIDDHVGAATSGLVADARV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  84 LSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGS 163
Cdd:cd03756   82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDGGPRLFETDPSGAYNEYKATAIGS 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665407395 164 RSQSARTYLEKNLNKflDSSKDEIIRHGIRAILGTLptdEQGKDAGQYDITVAIV 218
Cdd:cd03756  162 GRQAVTEFLEKEYKE--DMSLEEAIELALKALYAAL---EENETPENVEIAYVTV 211
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
1-231 3.13e-50

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 164.93  E-value: 3.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   1 MFRNQ---YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPT-SEL--SDTQRKIIPIDDHLGISI 74
Cdd:COG0638    1 MQPSQqssYDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLiaSKSIEKIFKIDDHIGVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  75 AGLTADARVLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQ-RYdrRPYGVGLLVAGYDERGPHIYQVTPSATF 153
Cdd:COG0638   81 AGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQyGV--RPFGVALLIGGVDDGGPRLFSTDPSGGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 154 FNCKANSIGSRSQSARTYLEKNLNKflDSSKDEIIRHGIRAIlgtlptdeqgKDAGQYD------ITVAIVGKDQpFTIL 227
Cdd:COG0638  159 YEEKAVAIGSGSPFARGVLEKEYRE--DLSLDEAVELALRAL----------YSAAERDsasgdgIDVAVITEDG-FREL 225

                 ....
gi 665407395 228 SNKD 231
Cdd:COG0638  226 SEEE 229
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
33-218 1.98e-49

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: 161.51  E-value: 1.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  33 TATVGLKNKDYAVLVALCKPTSEL---SDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRLI 109
Cdd:cd01906    1 TTIVGIKGKDGVVLAADKRVTSGLlvaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 110 TNLGNKMQTTTQRydRRPYGVGLLVAGYDE-RGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSSKDEII 188
Cdd:cd01906   81 KLLANLLYEYTQS--LRPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKP--DMTLEEAI 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 665407395 189 RHGIRAILGTLPTDeqgKDAGqYDITVAIV 218
Cdd:cd01906  157 ELALKALKSALERD---LYSG-GNIEVAVI 182
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-178 7.71e-49

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: 160.97  E-value: 7.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSEL--SDTQRKIIPIDDHLGISIAGLTADARV 83
Cdd:cd03753    1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLmePSSVEKIMEIDDHIGCAMSGLIADART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  84 LSRYLRSECLNYKHSYD-------TTYPVSRLITNLGNkmQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNC 156
Cdd:cd03753   81 LIDHARVEAQNHRFTYNepmtvesVTQAVSDLALQFGE--GDDGKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRC 158
                        170       180
                 ....*....|....*....|..
gi 665407395 157 KANSIGSRSQSARTYLEKNLNK 178
Cdd:cd03753  159 DAKAIGSGSEGAQSSLQEKYHK 180
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-178 9.69e-47

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: 155.58  E-value: 9.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSDTQR---KIIPIDDHLGISIAGLTADAR 82
Cdd:cd03752    3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSFsseKIYKIDDHIACAVAGITSDAN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  83 VLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDE-RGPHIYQVTPSATFFNCKANSI 161
Cdd:cd03752   83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKhYGFQLYQSDPSGNYSGWKATAI 162
                        170
                 ....*....|....*..
gi 665407395 162 GSRSQSARTYLEKNLNK 178
Cdd:cd03752  163 GNNNQAAQSLLKQDYKD 179
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-174 6.15e-44

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: 148.20  E-value: 6.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDyAVLVALCK-PTSEL--SDTQRKIIPIDDHLGISIAGLTADAR 82
Cdd:cd03751    4 YDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKD-GVVLAVEKlVTSKLyePGSNKRIFNVDRHIGIAVAGLLADGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  83 VLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIG 162
Cdd:cd03751   83 HLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSYGYFGCAIG 162
                        170
                 ....*....|..
gi 665407395 163 SRSQSARTYLEK 174
Cdd:cd03751  163 KGKQAAKTELEK 174
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
6-218 8.19e-43

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: 145.45  E-value: 8.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   6 YDSDVTVWSPQGRLHQVEYAMEAVKL-GTATVGLKNKDYAVLVALCKPTSEL--SDTQRKIIPIDDHLGISIAGLTADAR 82
Cdd:cd03754    2 FDRHITIFSPEGRLYQVEYAFKAVKNaGLTSVAVRGKDCAVVVTQKKVPDKLidPSTVTHLFRITDEIGCVMTGMIADSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  83 VLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYD-ERGPHIYQVTPSATFFNCKANSI 161
Cdd:cd03754   82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDeELGPQLYKCDPAGYFAGYKATAA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665407395 162 GSRSQSARTYLEKNLNKFLD--SSKDEIIRHGIRAILGTLPTDEQGKdagqyDITVAIV 218
Cdd:cd03754  162 GVKEQEATNFLEKKLKKKPDliESYEETVELAISCLQTVLSTDFKAT-----EIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
33-196 1.12e-37

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: 130.59  E-value: 1.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  33 TATVGLKNKDYAVLVALCKPTSEL---SDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRLI 109
Cdd:cd01901    1 STSVAIKGKGGVVLAADKRLSSGLpvaGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 110 TNLGNKMQTTTQrydRRPYGVGLLVAGYDERGPHIYQVTPSATFF-NCKANSIGSRSQSARTYLEKNLNKflDSSKDEII 188
Cdd:cd01901   81 KELAKLLQVYTQ---GRPFGVNLIVAGVDEGGGNLYYIDPSGPVIeNPGAVATGSRSQRAKSLLEKLYKP--DMTLEEAV 155

                 ....*...
gi 665407395 189 RHGIRAIL 196
Cdd:cd01901  156 ELALKALK 163
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
5-201 2.00e-37

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 132.67  E-value: 2.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   5 QYDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSD---TQRKIIPIDDHLGISIAGLTADA 81
Cdd:PTZ00246   4 RYDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDpgkINEKIYKIDSHIFCAVAGLTADA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  82 RVLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDER-GPHIYQVTPSATFFNCKANS 160
Cdd:PTZ00246  84 NILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENlGYQLYHTDPSGNYSGWKATA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 665407395 161 IGSRSQSARTYLEKNLNKflDSSKDEIIRHGIRAILGTLPT 201
Cdd:PTZ00246 164 IGQNNQTAQSILKQEWKE--DLTLEQGLLLAAKVLTKSMDS 202
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
33-221 5.71e-21

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: 87.50  E-value: 5.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  33 TATVGLKNKDYAVLVALCKpTSE----LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSrl 108
Cdd:cd01912    1 TTIVGIKGKDGVVLAADTR-ASAgslvASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVK-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 109 itNLGNKMQTTTQRYDRRPYGVGLLVAGYDE-RGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSSKDEI 187
Cdd:cd01912   78 --AAANLLSNILYSYRGFPYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKP--DMTLEEA 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665407395 188 IRHGIRAILGTLptdeqGKDAGQYD-ITVAIVGKD 221
Cdd:cd01912  154 VELVKKAIDSAI-----ERDLSSGGgVDVAVITKD 183
arc_protsome_B TIGR03634
proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the ...
32-221 8.21e-21

proteasome endopeptidase complex, archaeal, beta subunit; This protein family describes the archaeal proteasome beta subunit, homologous to both the alpha 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: 274690  Cd Length: 185  Bit Score: 87.26  E-value: 8.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395   32 GTATVGLKNKDYAVLVALCKPTSE---LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRL 108
Cdd:TIGR03634   1 GTTTVGIKCKDGVVLAADKRASMGnfvASKNAKKVFQIDDYIAMTIAGSVGDAQSLVRILKAEAKLYELRRGRPMSVKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  109 ITNLGNKMQTTtqRYdrRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSSKDEII 188
Cdd:TIGR03634  81 ATLLSNILNSN--RF--FPFIVQLLVGGVDEEGPHLYSLDPAGGIIEDDYTATGSGSPVAYGVLEDEYRE--DMSVEEAK 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 665407395  189 RHGIRAIlgtlptdeqgKDAGQYD------ITVAIVGKD 221
Cdd:TIGR03634 155 KLAVRAI----------KSAIERDvasgngIDVAVITKD 183
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
33-221 2.40e-20

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: 85.77  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  33 TATVGLKNKDYAVLVALCKPTSE---LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRLI 109
Cdd:cd03764    1 TTTVGIVCKDGVVLAADKRASMGnfiASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 110 TNLGNKMQTTtqRYdrRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKflDSSKDEIIR 189
Cdd:cd03764   81 TLLSNILNSS--KY--FPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKE--DMTVEEAKK 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 665407395 190 HGIRAIlgtlptdeqgKDAGQYD------ITVAIVGKD 221
Cdd:cd03764  155 LAIRAI----------KSAIERDsasgdgIDVVVITKD 182
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
6-28 2.73e-10

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: 54.28  E-value: 2.73e-10
                          10        20
                  ....*....|....*....|...
gi 665407395    6 YDSDVTVWSPQGRLHQVEYAMEA 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 1.16e-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: 52.50  E-value: 1.16e-09
                           10        20
                   ....*....|....*....|...
gi 665407395     6 YDSDVTVWSPQGRLHQVEYAMEA 28
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
57-195 1.98e-09

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: 55.71  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  57 SDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPV---SRLITNLgnkmqtttqRYDRRPYG--VG 131
Cdd:cd03761   28 SQTVKKVIEINPYLLGTMAGGAADCQYWERVLGRECRLYELRNKERISVaaaSKLLSNM---------LYQYKGMGlsMG 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665407395 132 LLVAGYDERGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKFLdsSKDEIIRHGIRAI 195
Cdd:cd03761   99 TMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDL--SVEEAYDLARRAI 160
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
32-179 5.43e-07

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: 49.18  E-value: 5.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  32 GTATVGLKNKDYAVLVA---LCKPTSELSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSyDTTYPVSRL 108
Cdd:cd03757    8 GGTVLAIAGNDFAVIAGdtrLSEGYSILSRDSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYS-HNKEMSTEA 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665407395 109 ITNLgnkmqTTTQRYDRR--PYGVGLLVAGYDERG-PHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKF 179
Cdd:cd03757   87 IAQL-----LSTILYSRRffPYYVFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIQPLLDNQVGRK 155
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
32-195 1.01e-06

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 48.83  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  32 GTATVGLKNKDYAVLVALCKPTSE---LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRL 108
Cdd:PTZ00488  39 GTTTLAFKYGGGIIIAVDSKATAGpyiASQSVKKVIEINPTLLGTMAGGAADCSFWERELAMQCRLYELRNGELISVAAA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 109 ITNLGNKMqtttqrYDRRPYGV--GLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNkfLDSSKDE 186
Cdd:PTZ00488 119 SKILANIV------WNYKGMGLsmGTMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFK--WDLNDEE 190

                 ....*....
gi 665407395 187 IIRHGIRAI 195
Cdd:PTZ00488 191 AQDLGRRAI 199
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
36-145 1.18e-06

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: 47.97  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  36 VGLKNKDYAVLVALCKPTSE---LSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKhsYDTTYPVSrlITNL 112
Cdd:cd03758    5 IGIKGKDFVILAADTSAARSilvLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYK--MRNGYELS--PKAA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 665407395 113 GNKMQTTTQRYDRR--PYGVGLLVAGYDER-GPHIY 145
Cdd:cd03758   81 ANFTRRELAESLRSrtPYQVNLLLAGYDKVeGPSLY 116
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
33-196 6.79e-05

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: 42.57  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  33 TATVGLKNKDYAVLVALCKPTSE--LSD-TQRKIIPIDDHLGISIAGLTADARVLSRYLRSEcLNYkHSYDTTYPVsRLI 109
Cdd:cd03763    1 TTIVGVVFKDGVVLGADTRATEGpiVADkNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSN-LEL-HRLNTGRKP-RVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395 110 TNLgNKMQTTTQRYdrRPY-GVGLLVAGYDERGPHIYQVTPSATffNCKAN--SIGSRSQSARTYLEKNLNKflDSSKDE 186
Cdd:cd03763   78 TAL-TMLKQHLFRY--QGHiGAALVLGGVDYTGPHLYSIYPHGS--TDKLPfvTMGSGSLAAMSVLEDRYKP--DMTEEE 150
                        170
                 ....*....|
gi 665407395 187 IIRHGIRAIL 196
Cdd:cd03763  151 AKKLVCEAIE 160
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
59-152 8.33e-03

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: 36.43  E-value: 8.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407395  59 TQRKIIPIDDHLGISIAGLTADARVLSRYLRseclNYKHSYD-------TTYPVSRLITNL--GNKMQTTTqrydrrpyg 129
Cdd:cd03762   30 VTDKLTQLHDRIYCCRSGSAADTQAIADYVR----YYLDMHSielgeppLVKTAASLFKNLcyNYKEMLSA--------- 96
                         90       100
                 ....*....|....*....|....
gi 665407395 130 vGLLVAGYDE-RGPHIYQVTPSAT 152
Cdd:cd03762   97 -GIIVAGWDEqNGGQVYSIPLGGM 119
 
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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