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Conserved domains on  [gi|161077552|ref|NP_570078|]
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echinus, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
76-371 1.62e-19

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


The actual alignment was detected with superfamily member pfam00443:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 310  Bit Score: 91.35  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552    76 GLLN-GpgqNNCFLNCAVQVLWHLDAFRRSFRGLNQH--VCGGQDCI--FCALKELFQQLQ-TSSEPALCPEPLRRALas 149
Cdd:pfam00443    2 GLVNlG---NTCYMNSVLQSLFSIPPFRDYLLRISPLseDSRYNKDInlLCALRDLFKALQkNSKSSSVSPKMFKKSL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   150 gplaGRRFPLGCLG---DAAECFELLLHRVHSHISPDDGDSCESsacIAHRRFAMRVIEQSVCK-CGANS--EQLPFTQM 223
Cdd:pfam00443   77 ----GKLNPDFSGYkqqDAQEFLLFLLDGLHEDLNGNHSTENES---LITDLFRGQLKSRLKCLsCGEVSetFEPFSDLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   224 VHYVSASALTSQKSLAlQSHQQLSFGQLLraagNMGDIRDCPNTCGAKIGICRALLNR-PEVVSIGIvwdsERPAADQVH 302
Cdd:pfam00443  150 LPIPGDSAELKTASLQ-ICFLQFSKLEEL----DDEEKYYCDKCGCKQDAIKQLKISRlPPVLIIHL----KRFSYNRST 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077552   303 AV--LKAVGTSLRLgDVFHQVSE---PRWAQQTQHELVGIVSYYG----KHYTTFFFHTKLKVWVYFDDANVKEVGPS 371
Cdd:pfam00443  221 WEklNTEVEFPLEL-DLSRYLAEelkPKTNNLQDYRLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEE 297
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1717-1739 5.40e-03

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20804:

Pssm-ID: 412127  Cd Length: 57  Bit Score: 36.90  E-value: 5.40e-03
                          10        20
                  ....*....|....*....|...
gi 161077552 1717 CNLCRKRHVIAPAVYCTNCEYYL 1739
Cdd:cd20804    19 CNVCRKRLEDSPAFRCEVCEYYV 41
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
76-371 1.62e-19

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 91.35  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552    76 GLLN-GpgqNNCFLNCAVQVLWHLDAFRRSFRGLNQH--VCGGQDCI--FCALKELFQQLQ-TSSEPALCPEPLRRALas 149
Cdd:pfam00443    2 GLVNlG---NTCYMNSVLQSLFSIPPFRDYLLRISPLseDSRYNKDInlLCALRDLFKALQkNSKSSSVSPKMFKKSL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   150 gplaGRRFPLGCLG---DAAECFELLLHRVHSHISPDDGDSCESsacIAHRRFAMRVIEQSVCK-CGANS--EQLPFTQM 223
Cdd:pfam00443   77 ----GKLNPDFSGYkqqDAQEFLLFLLDGLHEDLNGNHSTENES---LITDLFRGQLKSRLKCLsCGEVSetFEPFSDLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   224 VHYVSASALTSQKSLAlQSHQQLSFGQLLraagNMGDIRDCPNTCGAKIGICRALLNR-PEVVSIGIvwdsERPAADQVH 302
Cdd:pfam00443  150 LPIPGDSAELKTASLQ-ICFLQFSKLEEL----DDEEKYYCDKCGCKQDAIKQLKISRlPPVLIIHL----KRFSYNRST 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077552   303 AV--LKAVGTSLRLgDVFHQVSE---PRWAQQTQHELVGIVSYYG----KHYTTFFFHTKLKVWVYFDDANVKEVGPS 371
Cdd:pfam00443  221 WEklNTEVEFPLEL-DLSRYLAEelkPKTNNLQDYRLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEE 297
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
164-391 2.52e-07

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 54.03  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  164 DAAECFELLLHRVHSHI--SPDDGDSCESSACIAHRRFAMRVIEQSVCK-CGANSeqlpftqmvhYVSASALTSQKSLAL 240
Cdd:cd02257    24 DAHEFLLFLLDKLHEELkkSSKRTSDSSSLKSLIHDLFGGKLESTIVCLeCGHES----------VSTEPELFLSLPLPV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  241 QSHQQLSFGQLLRAAGNMGDIRDCPNTCGAKIGICRA-----LLNRPEVVSIGI---VWDSErpaaDQVHAVLKAVGTSL 312
Cdd:cd02257    94 KGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEAtkrlkIKKLPPVLIIHLkrfSFNED----GTKEKLNTKVSFPL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  313 RLgDVFHQVSEPRWAQQTQH-----ELVGIVSYYGK-----HYTTFFFHTKLKVWVYFDDANVKEVgpSWEGVVDKCSRG 382
Cdd:cd02257   170 EL-DLSPYLSEGEKDSDSDNgsykyELVAVVVHSGTsadsgHYVAYVKDPSDGKWYKFNDDKVTEV--SEEEVLEFGSLS 246

                  ....*....
gi 161077552  383 RyQPLLLLY 391
Cdd:cd02257   247 S-SAYILFY 254
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
1717-1739 5.40e-03

second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410354  Cd Length: 57  Bit Score: 36.90  E-value: 5.40e-03
                          10        20
                  ....*....|....*....|...
gi 161077552 1717 CNLCRKRHVIAPAVYCTNCEYYL 1739
Cdd:cd20804    19 CNVCRKRLEDSPAFRCEVCEYYV 41
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
76-371 1.62e-19

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 91.35  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552    76 GLLN-GpgqNNCFLNCAVQVLWHLDAFRRSFRGLNQH--VCGGQDCI--FCALKELFQQLQ-TSSEPALCPEPLRRALas 149
Cdd:pfam00443    2 GLVNlG---NTCYMNSVLQSLFSIPPFRDYLLRISPLseDSRYNKDInlLCALRDLFKALQkNSKSSSVSPKMFKKSL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   150 gplaGRRFPLGCLG---DAAECFELLLHRVHSHISPDDGDSCESsacIAHRRFAMRVIEQSVCK-CGANS--EQLPFTQM 223
Cdd:pfam00443   77 ----GKLNPDFSGYkqqDAQEFLLFLLDGLHEDLNGNHSTENES---LITDLFRGQLKSRLKCLsCGEVSetFEPFSDLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   224 VHYVSASALTSQKSLAlQSHQQLSFGQLLraagNMGDIRDCPNTCGAKIGICRALLNR-PEVVSIGIvwdsERPAADQVH 302
Cdd:pfam00443  150 LPIPGDSAELKTASLQ-ICFLQFSKLEEL----DDEEKYYCDKCGCKQDAIKQLKISRlPPVLIIHL----KRFSYNRST 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161077552   303 AV--LKAVGTSLRLgDVFHQVSE---PRWAQQTQHELVGIVSYYG----KHYTTFFFHTKLKVWVYFDDANVKEVGPS 371
Cdd:pfam00443  221 WEklNTEVEFPLEL-DLSRYLAEelkPKTNNLQDYRLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEE 297
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
164-391 2.52e-07

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 54.03  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  164 DAAECFELLLHRVHSHI--SPDDGDSCESSACIAHRRFAMRVIEQSVCK-CGANSeqlpftqmvhYVSASALTSQKSLAL 240
Cdd:cd02257    24 DAHEFLLFLLDKLHEELkkSSKRTSDSSSLKSLIHDLFGGKLESTIVCLeCGHES----------VSTEPELFLSLPLPV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  241 QSHQQLSFGQLLRAAGNMGDIRDCPNTCGAKIGICRA-----LLNRPEVVSIGI---VWDSErpaaDQVHAVLKAVGTSL 312
Cdd:cd02257    94 KGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEAtkrlkIKKLPPVLIIHLkrfSFNED----GTKEKLNTKVSFPL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  313 RLgDVFHQVSEPRWAQQTQH-----ELVGIVSYYGK-----HYTTFFFHTKLKVWVYFDDANVKEVgpSWEGVVDKCSRG 382
Cdd:cd02257   170 EL-DLSPYLSEGEKDSDSDNgsykyELVAVVVHSGTsadsgHYVAYVKDPSDGKWYKFNDDKVTEV--SEEEVLEFGSLS 246

                  ....*....
gi 161077552  383 RyQPLLLLY 391
Cdd:cd02257   247 S-SAYILFY 254
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
75-220 1.83e-06

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 51.99  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   75 KGLLN-GpgqNNCFLNCAVQVLWHLDAFRRSFRG----LNQHVCGGQDCIFCALKELFQQLQTSSEPAlcPEPLRRAL-- 147
Cdd:cd02660     1 RGLINlG---ATCFMNVILQALLHNPLLRNYFLSdrhsCTCLSCSPNSCLSCAMDEIFQEFYYSGDRS--PYGPINLLyl 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  148 ---ASGPLAGRRfplgcLGDAAECFELLLHRVHSHISPDDGDSCESSA--CIAHRRFAMRVIEQSVC-KCGANSEQL-PF 220
Cdd:cd02660    76 swkHSRNLAGYS-----QQDAHEFFQFLLDQLHTHYGGDKNEANDESHcnCIIHQTFSGSLQSSVTCqRCGGVSTTVdPF 150
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-368 1.96e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 45.40  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   84 NNCFLNCAVQVLWHLDAFR---RSFRGLNQHVCGGQDCIFCALKELFQQLQTSSE---PALCPEPLRRAlasgplagrrF 157
Cdd:cd02657     7 NTCYLNSTLQCLRSVPELRdalKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEpvpPIEFLQLLRMA----------F 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  158 P----LGCLG-----DAAECFELLLHRVhSHISPDDGDSCESSACIahrrFAMRVIEQSVCKCGANSEQL---PFTQMVH 225
Cdd:cd02657    77 PqfaeKQNQGgyaqqDAEECWSQLLSVL-SQKLPGAGSKGSFIDQL----FGIELETKMKCTESPDEEEVsteSEYKLQC 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552  226 YVSASALTS--QKSLALQSHQQLSfgqllRAAGNMGdiRDCPNTCGAKIgicrallNR-PEVVSIGIV---WDSErpaaD 299
Cdd:cd02657   152 HISITTEVNylQDGLKKGLEEEIE-----KHSPTLG--RDAIYTKTSRI-------SRlPKYLTVQFVrffWKRD----I 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161077552  300 QVHA-VLKAVGTSLRLgDVFHQVSeprwaQQTQHELVGIVSYYGK-----HYTTFFFHTKLKVWVYFDDANVKEV 368
Cdd:cd02657   214 QKKAkILRKVKFPFEL-DLYELCT-----PSGYYELVAVITHQGRsadsgHYVAWVRRKNDGKWIKFDDDKVSEV 282
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
76-181 2.69e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 42.09  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   76 GLLN-GpgqNNCFLNCAVQVLWHLDAFRRSFRGLNQHVCGGQDCIFCALKELFQQLQTSSEPALCPePLRRALASGPLAg 154
Cdd:cd02664     1 GLINlG---NTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAP-PDYFLEASRPPW- 75
                          90       100
                  ....*....|....*....|....*..
gi 161077552  155 rrFPLGCLGDAAECFELLLHRVHSHIS 181
Cdd:cd02664    76 --FTPGSQQDCSEYLRYLLDRLHTLIE 100
C1_DGKtheta_typeV_rpt2 cd20804
second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
1717-1739 5.40e-03

second protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410354  Cd Length: 57  Bit Score: 36.90  E-value: 5.40e-03
                          10        20
                  ....*....|....*....|...
gi 161077552 1717 CNLCRKRHVIAPAVYCTNCEYYL 1739
Cdd:cd20804    19 CNVCRKRLEDSPAFRCEVCEYYV 41
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
76-217 7.61e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 40.34  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077552   76 GLLNgPGqNNCFLNCAVQVLWH---LDAFRRSFRgLNQHVCGGQDCIFCALKELFQQLQTSSEPALCPEPLRRALasgPL 152
Cdd:cd02661     3 GLQN-LG-NTCFLNSVLQCLTHtppLANYLLSRE-HSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNL---KQ 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077552  153 AGRRFPLGCLGDAAECFELLL---HRVHSHISPDDGDSCESSA--CIAHRRFAMRVIEQSVC-KCGANSEQ 217
Cdd:cd02661    77 ISKHFRIGRQEDAHEFLRYLLdamQKACLDRFKKLKAVDPSSQetTLVQQIFGGYLRSQVKClNCKHVSNT 147
 
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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