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Conserved domains on  [gi|1271034368|gb|PHT55619|]
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Proteasome subunit alpha type-5 [Capsicum baccatum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 1.81e-155

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: 442.93  E-value: 1.81e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEGD--EESMSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNA 474
Cdd:cd03753    81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDdgKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1271034368 475 KAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARV 527
Cdd:cd03753   161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
PMD super family cl46345
Plant mobile domain; This domain was identified by Babu and colleagues in a variety of ...
 2-116 3.50e-23

Plant mobile domain; This domain was identified by Babu and colleagues in a variety of transposases.


The actual alignment was detected with superfamily member pfam09331:

Pssm-ID: 480685  Cd Length: 133  Bit Score: 95.07  E-value: 3.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368   2 LRFSINEFALITGLNCfGNIDDFKYEDSSTSGLMK-----GYFPQSTNgVDKEALVERFLKGNFENKEDALQMAILYFIH 76
Cdd:pfam09331  15 IRFSLREFAIVTGLNC-GKFPKELEDKEKKNRLIKkkpygKLFGEKKE-VTVTDLIRMLENKTWTSDEDRVKLALLYFLH 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1271034368  77 TFIYSQLNASPVPFSYFKMVED-GKYQFFPWGKVSFSRLMA 116
Cdd:pfam09331  93 GVLLATDLNPKIILEHAFLVVDlGEFESYPWGRLSFDELIK 133
 
Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 1.81e-155

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: 442.93  E-value: 1.81e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEGD--EESMSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNA 474
Cdd:cd03753    81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDdgKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1271034368 475 KAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARV 527
Cdd:cd03753   161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
317-547 8.83e-101

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 304.45  E-value: 8.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:PRK03996   10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRF----GegdeesmSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQC 472
Cdd:PRK03996   90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYtqhgG-------VRPFGVALLIAGVDDGGPRLFETDPSGAYLEY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1271034368 473 NAKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARV---SPTYHLYSPSEVEEPLSSLD 547
Cdd:PRK03996  163 KATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIdveTKKFRKLSVEEIEKYLEKLL 240
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 317-528 2.12e-94

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: 287.24  E-value: 2.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLA---LRFGeGdeesmSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCN 473
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKqqyTQHG-G-----VRPFGVALLIAGVDDGGPRLFETDPSGALLEYK 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1271034368 474 AKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARVS 528
Cdd:TIGR03633 157 ATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYIT 211
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 317-538 1.36e-81

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 254.68  E-value: 1.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRIT-SPLLEPSSVEKIMEIDEHIGCAMSGLIADAR 395
Cdd:COG0638     9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVADAR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 396 TLVEHARVETQNHRFSYGEPMTVESTTQALCDLaLRfgEGDEESMsRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNAK 475
Cdd:COG0638    89 ELVRLARVEAQLYELRYGEPISVEGLAKLLSDL-LQ--GYTQYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1271034368 476 AIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEE-KVTPNNVDIARVSPT-YHLYSPSE 538
Cdd:COG0638   165 AIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDgFRELSEEE 229
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 340-527 3.75e-66

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: 212.81  E-value: 3.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 340 IKLGSTAIGLKTKEGVVLAVEKRIT--SPLLEPSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMT 417
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 418 VEStTQALCDLALRFGegdEESMSRPFGVSLLIAGHDENG-PCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDL 496
Cdd:pfam00227  81 VEL-AARIADLLQAYT---QYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1271034368 497 TLKEAETIALSILKQVME-EKVTPNNVDIARV 527
Cdd:pfam00227 157 TLEEAVELAVKALKEAIDrDALSGGNIEVAVI 188
DUF1985 pfam09331
Domain of unknown function (DUF1985); Members of this family of functionally uncharacterized ...
 2-116 3.50e-23

Domain of unknown function (DUF1985); Members of this family of functionally uncharacterized domains are found in a set of Arabidopsis thaliana hypothetical proteins.


Pssm-ID: 462759  Cd Length: 133  Bit Score: 95.07  E-value: 3.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368   2 LRFSINEFALITGLNCfGNIDDFKYEDSSTSGLMK-----GYFPQSTNgVDKEALVERFLKGNFENKEDALQMAILYFIH 76
Cdd:pfam09331  15 IRFSLREFAIVTGLNC-GKFPKELEDKEKKNRLIKkkpygKLFGEKKE-VTVTDLIRMLENKTWTSDEDRVKLALLYFLH 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1271034368  77 TFIYSQLNASPVPFSYFKMVED-GKYQFFPWGKVSFSRLMA 116
Cdd:pfam09331  93 GVLLATDLNPKIILEHAFLVVDlGEFESYPWGRLSFDELIK 133
Proteasome_A_N smart00948
Proteasome subunit A N-terminal signature Add an annotation; This domain is conserved in the A ...
 317-339 1.35e-10

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: 55.97  E-value: 1.35e-10
                           10        20
                   ....*....|....*....|...
gi 1271034368  317 YDRGVNTFSPEGRLFQVEYAIEA 339
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
 
Name Accession Description Interval E-value
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 1.81e-155

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: 442.93  E-value: 1.81e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd03753     1 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKEGVVLAVEKRITSPLMEPSSVEKIMEIDDHIGCAMSGLIADART 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEGD--EESMSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNA 474
Cdd:cd03753    81 LIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDdgKKAMSRPFGVALLIAGVDENGPQLFHTDPSGTFTRCDA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1271034368 475 KAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARV 527
Cdd:cd03753   161 KAIGSGSEGAQSSLQEKYHKDMTLEEAEKLALSILKQVMEEKLNSTNVELATV 213
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 5.07e-119

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: 349.82  E-value: 5.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd01911     1 YDRSITTFSPEGRLFQVEYALEAVKNGSTAVGIKGKDGVVLAVEKKVTSKLLDPSSVEKIFKIDDHIGCAVAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGegdEESMSRPFGVSLLIAGHDEN-GPCLYYTDPSGTFWQCNAK 475
Cdd:cd01911    81 LVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYT---QYGGVRPFGVSLLIAGYDEEgGPQLYQTDPSGTYFGYKAT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1271034368 476 AIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARV 527
Cdd:cd01911   158 AIGKGSQEAKTFLEKRYKKDLTLEEAIKLALKALKEVLEEDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
317-547 8.83e-101

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 304.45  E-value: 8.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:PRK03996   10 YDRAITIFSPDGRLYQVEYAREAVKRGTTAVGVKTKDGVVLAVDKRITSPLIEPSSIEKIFKIDDHIGAASAGLVADARV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRF----GegdeesmSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQC 472
Cdd:PRK03996   90 LIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYtqhgG-------VRPFGVALLIAGVDDGGPRLFETDPSGAYLEY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1271034368 473 NAKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARV---SPTYHLYSPSEVEEPLSSLD 547
Cdd:PRK03996  163 KATAIGAGRDTVMEFLEKNYKEDLSLEEAIELALKALAKANEGKLDPENVEIAYIdveTKKFRKLSVEEIEKYLEKLL 240
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 317-528 2.12e-94

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: 287.24  E-value: 2.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:TIGR03633   3 YDRAITVFSPDGRLYQVEYAREAVKRGTTAVGIKTKDGVVLAVDKRITSKLVEPSSIEKIFKIDDHIGAATSGLVADARV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLA---LRFGeGdeesmSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCN 473
Cdd:TIGR03633  83 LIDRARIEAQINRLTYGEPIDVETLAKKICDLKqqyTQHG-G-----VRPFGVALLIAGVDDGGPRLFETDPSGALLEYK 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1271034368 474 AKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARVS 528
Cdd:TIGR03633 157 ATAIGAGRQAVTEFLEKEYREDLSLDEAIELALKALYSAVEDKLTPENVEVAYIT 211
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-528 2.32e-92

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: 281.53  E-value: 2.32e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd03756     2 YDRAITVFSPDGRLYQVEYAREAVKRGTTALGIKCKEGVVLAVDKRITSKLVEPESIEKIYKIDDHVGAATSGLVADARV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLA---LRFGEgdeesmSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCN 473
Cdd:cd03756    82 LIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKqqyTQHGG------VRPFGVALLIAGVDDGGPRLFETDPSGAYNEYK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1271034368 474 AKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARVS 528
Cdd:cd03756   156 ATAIGSGRQAVTEFLEKEYKEDMSLEEAIELALKALYAALEENETPENVEIAYVT 210
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 317-538 1.36e-81

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


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 254.68  E-value: 1.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRIT-SPLLEPSSVEKIMEIDEHIGCAMSGLIADAR 395
Cdd:COG0638     9 YDRAITIFSPDGRLYQVEYAREAVKRGTTTVGIKTKDGVVLAADRRATmGNLIASKSIEKIFKIDDHIGVAIAGLVADAR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 396 TLVEHARVETQNHRFSYGEPMTVESTTQALCDLaLRfgEGDEESMsRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNAK 475
Cdd:COG0638    89 ELVRLARVEAQLYELRYGEPISVEGLAKLLSDL-LQ--GYTQYGV-RPFGVALLIGGVDDGGPRLFSTDPSGGLYEEKAV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1271034368 476 AIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEE-KVTPNNVDIARVSPT-YHLYSPSE 538
Cdd:COG0638   165 AIGSGSPFARGVLEKEYREDLSLDEAVELALRALYSAAERdSASGDGIDVAVITEDgFRELSEEE 229
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 4.71e-67

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: 216.44  E-value: 4.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPS-SVEKIMEIDEHIGCAMSGLIADAR 395
Cdd:cd03752     3 YDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAKDGIVLAAEKKVTSKLLDQSfSSEKIYKIDDHIACAVAGITSDAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 396 TLVEHARVETQNHRFSYGEPMTVESTTQALCDLA---LRFGEgdeesmSRPFGVSLLIAGHDEN-GPCLYYTDPSGTF-- 469
Cdd:cd03752    83 ILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKqgyTQYGG------LRPFGVSFLYAGWDKHyGFQLYQSDPSGNYsg 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1271034368 470 WQcnAKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVME-EKVTPNNVDIARV 527
Cdd:cd03752   157 WK--ATAIGNNNQAAQSLLKQDYKDDMTLEEALALAVKVLSKTMDsTKLTSEKLEFATL 213
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 340-527 3.75e-66

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: 212.81  E-value: 3.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 340 IKLGSTAIGLKTKEGVVLAVEKRIT--SPLLEPSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMT 417
Cdd:pfam00227   1 VKTGTTIVGIKGKDGVVLAADKRATrgSKLLSKDTVEKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 418 VEStTQALCDLALRFGegdEESMSRPFGVSLLIAGHDENG-PCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDL 496
Cdd:pfam00227  81 VEL-AARIADLLQAYT---QYSGRRPFGVSLLIAGYDEDGgPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRPDL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1271034368 497 TLKEAETIALSILKQVME-EKVTPNNVDIARV 527
Cdd:pfam00227 157 TLEEAVELAVKALKEAIDrDALSGGNIEVAVI 188
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-525 3.58e-65

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: 211.07  E-value: 3.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd03755     1 YDRAITVFSPDGHLFQVEYAQEAVRKGTTAVGVRGKDCVVLGVEKKSVAKLQDPRTVRKICMLDDHVCLAFAGLTADARV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFgegDEESMSRPFGVSLLIAGHDENG-PCLYYTDPSGTFWQCNAK 475
Cdd:cd03755    81 LINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRY---TQSGGVRPFGISTLIVGFDPDGtPRLYQTDPSGTYSAWKAN 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1271034368 476 AIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEkvTPNNVDIA 525
Cdd:cd03755   158 AIGRNSKTVREFLEKNYKEEMTRDDTIKLAIKALLEVVQS--GSKNIELA 205
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-544 7.84e-65

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: 211.03  E-value: 7.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADART 396
Cdd:cd03750     1 YSFSLTTFSPSGKLVQIEYALAAVSSGAPSVGIKAANGVVLATEKKVPSPLIDESSVHKVEQITPHIGMVYSGMGPDFRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 397 LVEHARVETQNHRFSYGEPMTVESTTQalcDLALRFGEGDEESMSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNAKA 476
Cdd:cd03750    81 LVKKARKIAQQYYLVYGEPIPVSQLVR---EIASVMQEYTQSGGVRPFGVSLLIAGWDEGGPYLYQVDPSGSYFTWKATA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 477 IGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKVTPNNVDIARVSPT--YHLYSPSEVEEPLS 544
Cdd:cd03750   158 IGKNYSNAKTFLEKRYNEDLELEDAIHTAILTLKEGFEGQMTEKNIEIGICGETkgFRLLTPAEIKDYLA 227
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 344-527 7.14e-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: 206.96  E-value: 7.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 344 STAIGLKTKEGVVLAVEKRITSPLLE-PSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTT 422
Cdd:cd01906     1 TTIVGIKGKDGVVLAADKRVTSGLLVaSSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 423 QALCDLALRFGEGdeesmSRPFGVSLLIAGHDE-NGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLTLKEA 501
Cdd:cd01906    81 KLLANLLYEYTQS-----LRPLGVSLLVAGVDEeGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPDMTLEEA 155

                         170       180
                  ....*....|....*....|....*..
gi 1271034368 502 ETIALSILKQVMEEKV-TPNNVDIARV 527
Cdd:cd01906   156 IELALKALKSALERDLySGGNIEVAVI 182
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 5.52e-62

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: 202.91  E-value: 5.52e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLlepSSV-EKIMEIDEHIGCAMSGLIADAR 395
Cdd:cd03749     1 YDTDVTTWSPQGRLFQVEYAMEAVKQGSATVGLKSKTHAVLVALKRATSEL---SSYqKKIFKVDDHIGIAIAGLTADAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 396 TLVEHARVETQNHRFSYGEPMTVESTTQALCDLALRfgeGDEESMSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNAK 475
Cdd:cd03749    78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQI---NTQRYGRRPYGVGLLIAGYDESGPHLFQTCPSGNYFEYKAT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1271034368 476 AIGSGSEGADSSLQEQYN--KDLTLKEAETIALSILKQVM--EEKVTPNNVDIARV 527
Cdd:cd03749   155 SIGARSQSARTYLERHFEefEDCSLEELIKHALRALRETLpgEQELTIKNVSIAIV 210
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 315-515 6.59e-61

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: 200.20  E-value: 6.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 315 TEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADA 394
Cdd:cd03751     2 TGYDLSASTFSPDGRVFQVEYANKAVENSGTAIGIRCKDGVVLAVEKLVTSKLYEPGSNKRIFNVDRHIGIAVAGLLADG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 395 RTLVEHARVETQNHRFSYGEPMTVEsttqalcDLALRFGEGDEE----SMSRPFGVSLLIAGHDENGPCLYYTDPSGTFW 470
Cdd:cd03751    82 RHLVSRAREEAENYRDNYGTPIPVK-------VLADRVAMYMHAytlySSVRPFGCSVLLGGYDSDGPQLYMIEPSGVSY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1271034368 471 QCNAKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEE 515
Cdd:cd03751   155 GYFGCAIGKGKQAAKTELEKLKFSELTCREAVKEAAKIIYIVHDE 199
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 317-546 8.98e-60

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 198.54  E-value: 8.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGLKTKEGVVLAVEKRITSPLLEPS-SVEKIMEIDEHIGCAMSGLIADAR 395
Cdd:PTZ00246    5 YDSRTTTFSPEGRLYQVEYALEAINNASLTVGILCKEGVILGADKPISSKLLDPGkINEKIYKIDSHIFCAVAGLTADAN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 396 TLVEHARVETQNHRFSYGEPMTVESTTQALCDLA---LRFGEgdeesmSRPFGVSLLIAGHDEN-GPCLYYTDPSGTFWQ 471
Cdd:PTZ00246   85 ILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKqsyTQFGG------LRPFGVSFLFAGYDENlGYQLYHTDPSGNYSG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 472 CNAKAIGSGSEGADSSLQEQYNKDLTLKEAETIALSILKQVMEEKV-TPNNVDIARVS-------PTYHLYSPSEVEEPL 543
Cdd:PTZ00246  159 WKATAIGQNNQTAQSILKQEWKEDLTLEQGLLLAAKVLTKSMDSTSpKADKIEVGILShgetdgePIQKMLSEKEIAELL 238


                  ...
gi 1271034368 544 SSL 546
Cdd:PTZ00246  239 KKV 241
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 317-527 5.36e-50

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: 171.65  E-value: 5.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEAIKLGS-TAIGLKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDEHIGCAMSGLIADAR 395
Cdd:cd03754     2 FDRHITIFSPEGRLYQVEYAFKAVKNAGlTSVAVRGKDCAVVVTQKKVPDKLIDPSTVTHLFRITDEIGCVMTGMIADSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 396 TLVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEgdEESMsRPFGVSLLIAGHD-ENGPCLYYTDPSGTFWQCNA 474
Cdd:cd03754    82 SQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQ--HAYM-RPLGVSMILIGIDeELGPQLYKCDPAGYFAGYKA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1271034368 475 KAIGSGSEGADSSLQEQYNKD----LTLKEAETIALSILKQVMEEKVTPNNVDIARV 527
Cdd:cd03754   159 TAAGVKEQEATNFLEKKLKKKpdliESYEETVELAISCLQTVLSTDFKATEIEVGVV 215
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 344-510 7.50e-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: 156.02  E-value: 7.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 344 STAIGLKTKEGVVLAVEKRITSPLLEP-SSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTT 422
Cdd:cd01901     1 STSVAIKGKGGVVLAADKRLSSGLPVAgSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 423 QALCDLALRFGEGdeesmsRPFGVSLLIAGHDENGPCLYYTDPSGTFWQC-NAKAIGSGSEGADSSLQEQYNKDLTLKEA 501
Cdd:cd01901    81 KELAKLLQVYTQG------RPFGVNLIVAGVDEGGGNLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPDMTLEEA 154


                  ....*....
gi 1271034368 502 ETIALSILK 510
Cdd:cd01901   155 VELALKALK 163
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 345-527 4.19e-33

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: 124.67  E-value: 4.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 345 TAIGLKTKEGVVLAVEKRIT-SPLLEPSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQ 423
Cdd:cd03764     2 TTVGIVCKDGVVLAADKRASmGNFIASKNVKKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALAT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 424 ALCDLaLRfgegdeESMSRPFGVSLLIAGHDENGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLTLKEAET 503
Cdd:cd03764    82 LLSNI-LN------SSKYFPYIVQLLIGGVDEEGPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKEDMTVEEAKK 154

                         170       180
                  ....*....|....*....|....*
gi 1271034368 504 IALSILKQVMEEKV-TPNNVDIARV 527
Cdd:cd03764   155 LAIRAIKSAIERDSaSGDGIDVVVI 179
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 345-509 9.93e-31

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: 118.32  E-value: 9.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 345 TAIGLKTKEGVVLAVEKRIT-SPLLEPSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQ 423
Cdd:cd01912     2 TIVGIKGKDGVVLAADTRASaGSLVASRNFDKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 424 ALCDLALRFGEGdeesmsrPFGVSLLIAGHDE-NGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLTLKEA- 501
Cdd:cd01912    82 LLSNILYSYRGF-------PYYVSLIVGGVDKgGGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPDMTLEEAv 154


                  ....*...
gi 1271034368 502 ETIALSIL 509
Cdd:cd01912   155 ELVKKAID 162
DUF1985 pfam09331
Domain of unknown function (DUF1985); Members of this family of functionally uncharacterized ...
 2-116 3.50e-23

Domain of unknown function (DUF1985); Members of this family of functionally uncharacterized domains are found in a set of Arabidopsis thaliana hypothetical proteins.


Pssm-ID: 462759  Cd Length: 133  Bit Score: 95.07  E-value: 3.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368   2 LRFSINEFALITGLNCfGNIDDFKYEDSSTSGLMK-----GYFPQSTNgVDKEALVERFLKGNFENKEDALQMAILYFIH 76
Cdd:pfam09331  15 IRFSLREFAIVTGLNC-GKFPKELEDKEKKNRLIKkkpygKLFGEKKE-VTVTDLIRMLENKTWTSDEDRVKLALLYFLH 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1271034368  77 TFIYSQLNASPVPFSYFKMVED-GKYQFFPWGKVSFSRLMA 116
Cdd:pfam09331  93 GVLLATDLNPKIILEHAFLVVDlGEFESYPWGRLSFDELIK 133
proteasome_beta_type_5 cd03761
proteasome beta type-5 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 345-501 2.04e-17

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: 80.37  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 345 TAIGLKTKEGVVLAVEKRITS-PLLEPSSVEKIMEIDEHIGCAMSGLIADA----RTLVEHARVetqnHRFSYGEPMTVE 419
Cdd:cd03761     2 TTLAFIFQGGVIVAVDSRATAgSYIASQTVKKVIEINPYLLGTMAGGAADCqyweRVLGRECRL----YELRNKERISVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 420 STTQALCDLALRFgegdeesmsRPFGVSL--LIAGHDENGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLT 497
Cdd:cd03761    78 AASKLLSNMLYQY---------KGMGLSMgtMICGWDKTGPGLYYVDSDGTRLKGDLFSVGSGSTYAYGVLDSGYRYDLS 148


                  ....
gi 1271034368 498 LKEA 501
Cdd:cd03761   149 VEEA 152
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 345-524 3.52e-17

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: 79.93  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 345 TAIGLKTKEGVVLAVEKRITS-PLLEPSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQ 423
Cdd:cd03763     2 TIVGVVFKDGVVLGADTRATEgPIVADKNCEKIHYIAPNIYCCGAGTAADTEAVTNMISSNLELHRLNTGRKPRVVTALT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 424 ALCDLALRFGEGdeesmsrpFGVSLLIAGHDENGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLTLKEAET 503
Cdd:cd03763    82 MLKQHLFRYQGH--------IGAALVLGGVDYTGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPDMTEEEAKK 153

                         170       180
                  ....*....|....*....|..
gi 1271034368 504 IA-LSILKQVMEEKVTPNNVDI 524
Cdd:cd03763   154 LVcEAIEAGIFNDLGSGSNVDL 175
PTZ00488 PTZ00488
Proteasome subunit beta type-5; Provisional
 343-504 4.27e-13

Proteasome subunit beta type-5; Provisional


Pssm-ID: 185666  Cd Length: 247  Bit Score: 69.25  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 343 GSTAIGLKTKEGVVLAVEKRITS-PLLEPSSVEKIMEIDEHIGCAMSGLIADA----RTLVEHARV-ETQNhrfsyGEPM 416
Cdd:PTZ00488   39 GTTTLAFKYGGGIIIAVDSKATAgPYIASQSVKKVIEINPTLLGTMAGGAADCsfweRELAMQCRLyELRN-----GELI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 417 TVESTTQALCDLALRFgegdeesmsRPFGVSL--LIAGHDENGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNK 494
Cdd:PTZ00488  114 SVAAASKILANIVWNY---------KGMGLSMgtMICGWDKKGPGLFYVDNDGTRLHGNMFSCGSGSTYAYGVLDAGFKW 184

                         170
                  ....*....|
gi 1271034368 495 DLTLKEAETI 504
Cdd:PTZ00488  185 DLNDEEAQDL 194
proteasome_beta_type_2 cd03758
proteasome beta type-2 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 345-515 5.98e-12

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: 64.53  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 345 TAIGLKTKEGVVLAVEKRIT-SPLLEPSSVEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVES--- 420
Cdd:cd03758     3 TLIGIKGKDFVILAADTSAArSILVLKDDEDKIYKLSDHKLMACSGEAGDRLQFAEYIQKNIQLYKMRNGYELSPKAaan 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 421 -TTQALCDlALRfgegdeesmSR-PFGVSLLIAGHDE-NGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLT 497
Cdd:cd03758    83 fTRRELAE-SLR---------SRtPYQVNLLLAGYDKvEGPSLYYIDYLGTLVKVPYAAHGYGAYFCLSILDRYYKPDMT 152

                         170
                  ....*....|....*...
gi 1271034368 498 LKEaetiALSILKQVMEE 515
Cdd:cd03758   153 VEE----ALELMKKCIKE 166
Proteasome_A_N pfam10584
Proteasome subunit A N-terminal signature; This domain is conserved in the A subunits of the ...
 317-339 9.15e-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: 56.59  E-value: 9.15e-11
                          10        20
                  ....*....|....*....|...
gi 1271034368 317 YDRGVNTFSPEGRLFQVEYAIEA 339
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 ...
 317-339 1.35e-10

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: 55.97  E-value: 1.35e-10
                           10        20
                   ....*....|....*....|...
gi 1271034368  317 YDRGVNTFSPEGRLFQVEYAIEA 339
Cdd:smart00948   1 YDRSLTTFSPDGRLFQVEYAMEA 23
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 343-513 7.51e-10

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: 58.81  E-value: 7.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 343 GSTAIGLKTKEGVVLAVEKRITSPLLEPSS-VEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVEST 421
Cdd:cd03757     8 GGTVLAIAGNDFAVIAGDTRLSEGYSILSRdSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 422 TQALCDL--ALRFgegdeesmsRPFGVSLLIAGHDENG-PCLYYTDPSGTFWQCNAKAIGSGSEGA----DSSL-----Q 489
Cdd:cd03757    88 AQLLSTIlySRRF---------FPYYVFNILAGIDEEGkGVVYSYDPVGSYERETYSAGGSASSLIqpllDNQVgrknqN 158

                         170       180
                  ....*....|....*....|....
gi 1271034368 490 EQYNKDLTLKEaetiALSILKQVM 513
Cdd:cd03757   159 NVERTPLSLEE----AVSLVKDAF 178
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 345-514 8.61e-10

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: 58.39  E-value: 8.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 345 TAIGLKTKEGVVLAVEKRITSPLLEPSSV-EKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQ 423
Cdd:cd03762     2 TIIAVEYDGGVVLGADSRTSTGSYVANRVtDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 424 ALCDLALRFgegDEESMSrpfgvSLLIAGHDE-NGPCLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLTLKEAE 502
Cdd:cd03762    82 LFKNLCYNY---KEMLSA-----GIIVAGWDEqNGGQVYSIPLGGMLIRQPFAIGGSGSTYIYGYVDANYKPGMTLEECI 153

                         170
                  ....*....|..
gi 1271034368 503 TIALSILKQVME 514
Cdd:cd03762   154 KFVKNALSLAMS 165
proteasome_beta_type_3 cd03759
proteasome beta type-3 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 343-509 1.57e-03

proteasome beta type-3 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: 239728  Cd Length: 195  Bit Score: 39.92  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 343 GSTAIGLKTKEGVVLAVEKRITSPLLEPSS-VEKIMEIDEHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVEST 421
Cdd:cd03759     3 GGAVVAMAGKDCVAIASDLRLGVQQQTVSTdFQKVFRIGDRLYIGLAGLATDVQTLAQKLRFRVNLYRLREEREIKPKTF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1271034368 422 TQALCDLAL--RFGegdeesmsrPFGVSLLIAGHDENG-PCLYYTDPSGTFWQC-NAKAIGSGSEGADSSLQEQYNKDLT 497
Cdd:cd03759    83 SSLISSLLYekRFG---------PYFVEPVVAGLDPDGkPFICTMDLIGCPSIPsDFVVSGTASEQLYGMCESLWRPDME 153

                         170
                  ....*....|...
gi 1271034368 498 LKEA-ETIALSIL 509
Cdd:cd03759   154 PDELfETISQALL 166
 
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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