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Conserved domains on  [gi|939626626|ref|NP_728456|]
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ubiquitin specific protease 2, isoform K [Drosophila melanogaster]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 13432448)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
73-313 1.71e-93

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 276.86  E-value: 1.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  73 NQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSVTF 152
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 153 DPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR--WS 226
Cdd:cd02674   65 EPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgsTR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 227 KLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVSSS 306
Cdd:cd02674  145 KLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVSSS 223

                 ....*..
gi 939626626 307 AYILFYE 313
Cdd:cd02674  224 AYILFYE 230
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1-165 5.70e-40

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 148.88  E-value: 5.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQ 75
Cdd:COG5560  277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  76 DAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 150
Cdd:COG5560  357 DSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                        170
                 ....*....|....*
gi 939626626 151 TFDPFWDLSVPLPSS 165
Cdd:COG5560  437 TFDPFMDLTLPLPVS 451
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
73-313 1.71e-93

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 276.86  E-value: 1.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  73 NQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSVTF 152
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 153 DPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR--WS 226
Cdd:cd02674   65 EPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgsTR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 227 KLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVSSS 306
Cdd:cd02674  145 KLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVSSS 223

                 ....*..
gi 939626626 307 AYILFYE 313
Cdd:cd02674  224 AYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-312 3.96e-90

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 271.24  E-value: 3.96e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626    1 MNSVIQCLSHTQELTRFL--RSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHT-VTPMELKRAFSTKHRMYSDYNQQDA 77
Cdd:pfam00443  12 MNSVLQSLFSIPPFRDYLlrISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLNPDFSGYKQQDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   78 QEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWD 157
Cdd:pfam00443  92 QEFLLFLLDGLHEDLNGNHSTE------------------------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  158 LSVPLPSSSRCKLEA----CLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR--WSKLSNI 231
Cdd:pfam00443 148 LSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRstWEKLNTE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  232 VEFPTsdsELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENHLVSSS 306
Cdd:pfam00443 228 VEFPL---ELDLSRYlaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSSS 304

                  ....*.
gi 939626626  307 AYILFY 312
Cdd:pfam00443 305 AYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1-165 5.70e-40

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 148.88  E-value: 5.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQ 75
Cdd:COG5560  277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  76 DAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 150
Cdd:COG5560  357 DSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                        170
                 ....*....|....*
gi 939626626 151 TFDPFWDLSVPLPSS 165
Cdd:COG5560  437 TFDPFMDLTLPLPVS 451
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
170-314 1.60e-31

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 124.61  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 170 LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS--KLSNIVEFPTSDSELNMGSYg 247
Cdd:COG5560  677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDDLDLSGVEY- 755
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939626626 248 ANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENhLVSSSAYILFYER 314
Cdd:COG5560  756 MVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPED-SVTSSAYVLFYRR 821
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
73-313 1.71e-93

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 276.86  E-value: 1.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  73 NQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSVTF 152
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTF 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 153 DPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR--WS 226
Cdd:cd02674   65 EPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgsTR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 227 KLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVSSS 306
Cdd:cd02674  145 KLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVSSS 223

                 ....*..
gi 939626626 307 AYILFYE 313
Cdd:cd02674  224 AYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-312 3.96e-90

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 271.24  E-value: 3.96e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626    1 MNSVIQCLSHTQELTRFL--RSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHT-VTPMELKRAFSTKHRMYSDYNQQDA 77
Cdd:pfam00443  12 MNSVLQSLFSIPPFRDYLlrISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLNPDFSGYKQQDA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   78 QEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWD 157
Cdd:pfam00443  92 QEFLLFLLDGLHEDLNGNHSTE------------------------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  158 LSVPLPSSSRCKLEA----CLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR--WSKLSNI 231
Cdd:pfam00443 148 LSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRstWEKLNTE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  232 VEFPTsdsELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENHLVSSS 306
Cdd:pfam00443 228 VEFPL---ELDLSRYlaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSSS 304

                  ....*.
gi 939626626  307 AYILFY 312
Cdd:pfam00443 305 AYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
72-313 4.54e-64

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: 202.71  E-value: 4.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  72 YNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltweWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSVT 151
Cdd:cd02257   20 SEQQDAHEFLLFLLDKLHEELKKSSKRT-------------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 152 FDPFWDLSVPLP--SSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtRRKCTKSFTIQRFPKYLVIHLKRFSETRW---S 226
Cdd:cd02257   81 TEPELFLSLPLPvkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDgtkE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 227 KLSNIVEFPtsdSELNMGSY-------GANSNSNVHYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSDALS 298
Cdd:cd02257  160 KLNTKVSFP---LELDLSPYlsegekdSDSDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSE 236
                        250
                 ....*....|....*....
gi 939626626 299 E----NHLVSSSAYILFYE 313
Cdd:cd02257  237 EevleFGSLSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-312 1.62e-63

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: 202.89  E-value: 1.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQDAQEF 80
Cdd:cd02661   13 LNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  81 LRFFLDSLHSA-LNSGVKGETLNIDDNlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLS 159
Cdd:cd02661   93 LRYLLDAMQKAcLDRFKKLKAVDPSSQ-----------------ETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 160 VPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPtsdS 239
Cdd:cd02661  156 LDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFP---E 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939626626 240 ELNMGSYGANSNSN-VHYSLYAISNHMG-STAGGHYVALCKHPvSRKWHEFNDNIVSdALSENHLVSSSAYILFY 312
Cdd:cd02661  231 TLDLSPYMSQPNDGpLKYKLYAVLVHSGfSPHSGHYYCYVKSS-NGKWYNMDDSKVS-PVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-312 4.97e-47

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: 161.00  E-value: 4.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSH-HgsrSLSTKDQQILH----EFAKLIQEMW-TANVHTVTPMELKRAFSTKHRMYSDYNQ 74
Cdd:cd02660   12 MNVILQALLHNPLLRNYFLSDrH---SCTCLSCSPNSclscAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  75 QDAQEFLRFFLDSLHSAlNSGVKGETlniddnlSDNKkadltwewytrHENSLVRDLFVGQLKSTLKCTTCGNTSVTFDP 154
Cdd:cd02660   89 QDAHEFFQFLLDQLHTH-YGGDKNEA-------NDES-----------HCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 155 FWDLSVPLPSSSRC-------------KLEACLDLFIREEVLdGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF- 220
Cdd:cd02660  150 FLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFe 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 221 --SETRWSKLSNIVEFPTsdsELNMGSYGANS----------NSNVHYSLYAISNHMGSTAGGHYVALCKHPVSrKWHEF 288
Cdd:cd02660  229 hsLNKTSRKIDTYVQFPL---ELNMTPYTSSSigdtqdsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG-QWFKF 304
                        330       340
                 ....*....|....*....|....
gi 939626626 289 NDNIVSdALSENHLVSSSAYILFY 312
Cdd:cd02660  305 DDAMIT-RVSEEEVLKSQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-313 5.42e-46

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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 156.78  E-value: 5.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   2 NSVIQCLSHTQELTRflrshhgsrslstkdqqilhefakLIQEmwtanvhtvTPMELKRAFSTKHRMYSDYNQQDAQEFL 81
Cdd:cd02667   12 NAVMQNLSQTPALRE------------------------LLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELL 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  82 RFFLDSLhsalnsgvkgetlniddnlsdnkkadltwewytrheNSLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLSVP 161
Cdd:cd02667   59 RYLLDGL------------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 162 L--PSSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtrrKCTKSFTIQRFPKYLVIHLKRFSETRWS---KLSNIVEFPt 236
Cdd:cd02667  103 RsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFP- 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 237 sdSELNMGSY------GANSNSNVHYSLYAISNHMGSTAGGHYVA----------LCKH-----------PVSRKWHEFN 289
Cdd:cd02667  179 --EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAyvkvrppqqrLSDLtkskpaadeagPGSGQWYYIS 256
                        330       340
                 ....*....|....*....|....
gi 939626626 290 DNIVSdALSENHLVSSSAYILFYE 313
Cdd:cd02667  257 DSDVR-EVSLEEVLKSEAYLLFYE 279
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1-165 5.70e-40

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 148.88  E-value: 5.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQ 75
Cdd:COG5560  277 MNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQ 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  76 DAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 150
Cdd:COG5560  357 DSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSI 436
                        170
                 ....*....|....*
gi 939626626 151 TFDPFWDLSVPLPSS 165
Cdd:COG5560  437 TFDPFMDLTLPLPVS 451
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-313 1.02e-39

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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 141.79  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFL--------RSHHGSRSLSTKDQQ-ILHEFAKLIQEMWTANVHTVTPMELKRAFStkhrmYSD 71
Cdd:cd02668   11 VNSFLQLWFMNLEFRKAVyecnstedAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPSGFVKALG-----LDT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  72 YNQQDAQEFLRFFLDSLHSALNSgvkgetlniddnlSDNKKAdltwewytrheNSLVRDLFVGQLKSTLKCTTCGNTSVT 151
Cdd:cd02668   86 GQQQDAQEFSKLFLSLLEAKLSK-------------SKNPDL-----------KNIVQDLFRGEYSYVTQCSKCGRESSL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 152 FDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS----K 227
Cdd:cd02668  142 PSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTgakkK 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 228 LSNIVEFPtsdSELNMGSYGANSNSNVH-YSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSD---------- 295
Cdd:cd02668  220 LNASISFP---EILDMGEYLAESDEGSYvYELSGVLIHQGVSAySGHYIAHIKDEQTGEWYKFNDEDVEEmpgkplklgn 296
                        330       340
                 ....*....|....*....|....*...
gi 939626626 296 ----------ALSENHLVSSSAYILFYE 313
Cdd:cd02668  297 sedpakprksEIKKGTHSSRTAYMLVYK 324
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-313 9.68e-39

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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 138.60  E-value: 9.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   2 NSVIQCLSHTQELTrflrshhgsrslSTKD--QQILHEFAKliqemwtanVHTVTPMELKRAFSTKHRMYSDYNQQDAQE 79
Cdd:cd02663   12 NSVLQALYFENLLT------------CLKDlfESISEQKKR---------TGVISPKKFITRLKRENELFDNYMHQDAHE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  80 FLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKADLTWewytrhenslVRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLS 159
Cdd:cd02663   71 FLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 160 VPLPSSsrCKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF--SET--RWSKLSNIVEFP 235
Cdd:cd02663  141 IDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQlnRYIKLFYRVVFP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 236 TsdsELNM-GSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHpvSRKWHEFNDNIVsDALSENHLV--------SS 305
Cdd:cd02663  219 L---ELRLfNTTDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETV-EKIDENAVEeffgdspnQA 292

                 ....*...
gi 939626626 306 SAYILFYE 313
Cdd:cd02663  293 TAYVLFYQ 300
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-314 1.17e-37

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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 136.62  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELtRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQDAQEF 80
Cdd:cd02659   14 MNSLLQQLYMTPEF-RNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  81 LRFFLDSLHSALnsgvKGetlniddnlsdnkkadltwewyTRHENsLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLSV 160
Cdd:cd02659   93 FRVLFDKLEEKL----KG----------------------TGQEG-LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 161 PLpssSRCK-LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF-----SETRwSKLSNIVEF 234
Cdd:cd02659  146 AV---KGKKnLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeTMMR-IKINDRFEF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 235 PtsdSELNMGSY------------GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVS-----DAL 297
Cdd:cd02659  222 P---LELDMEPYtekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTpfdpnDAE 298
                        330       340       350
                 ....*....|....*....|....*....|...
gi 939626626 298 SEN----------------HLVSSSAYILFYER 314
Cdd:cd02659  299 EECfggeetqktydsgpraFKRTTNAYMLFYER 331
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
170-314 1.60e-31

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 124.61  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 170 LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS--KLSNIVEFPTSDSELNMGSYg 247
Cdd:COG5560  677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDDLDLSGVEY- 755
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939626626 248 ANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENhLVSSSAYILFYER 314
Cdd:COG5560  756 MVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPED-SVTSSAYVLFYRR 821
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-313 5.53e-28

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: 110.66  E-value: 5.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSHHGSRslsTKDQQILheFAKLIQEMWTANVHTVTPMELKRAF--STKHRMYSDYNQQDAQ 78
Cdd:cd02664   11 MNSVLQALFMAKDFRRQVLSLNLPR---LGDSQSV--MKKLQLLQAHLMHTQRRAEAPPDYFleASRPPWFTPGSQQDCS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  79 EFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSVTFD--PFW 156
Cdd:cd02664   86 EYLRYLLDRLHT------------------------------------LIEKMFGGKLSTTIRCLNCNSTSARTErfRDL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 157 DLSVPLpsssrckLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS-----ETRWSKLSNI 231
Cdd:cd02664  130 DLSFPS-------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqktHVREKIMDNV 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 232 -----VEFPTSDS-----------ELNMGSYGANSNSNVHYSLYAISNHMG-STAGGHYVALCKHPVSRK---------- 284
Cdd:cd02664  203 sinevLSLPVRVEskssesplekkEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQTDADstgqecpepk 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 939626626 285 ----------WHEFNDNIVSDALSE---NHLV---SSSAYILFYE 313
Cdd:cd02664  283 daeendesknWYLFNDSRVTFSSFEsvqNVTSrfpKDTPYILFYE 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-313 5.01e-25

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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 102.02  E-value: 5.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--QQILHEFAKLIQEM-----------WTANVHT---VTPMELKRAFST 64
Cdd:cd02658   11 LNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKLADGLlsgryskpaslKSENDPYqvgIKPSMFKALIGK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  65 KHRMYSDYNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTwewytrhenslvrDLFVGQLKSTLKCTT 144
Cdd:cd02658   91 GHPEFSTMRQQDALEFLLHLIDK---------------LDRESFKNLGLNPN-------------DLFKFMIEDRLECLS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 145 CGNTSVTFDPFWDLSVPLPSS------------SRCKLEACLDLFIREEVLDGdempTCAKCKTRRKCTKSFTIQRFPKY 212
Cdd:cd02658  143 CKKVKYTSELSEILSLPVPKDeatekeegelvyEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDY 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 213 LVIHLKRFS-ETRW--SKLSNIVEFPtsdSELNMGSygansnsnvhYSLYAISNHMG-STAGGHYVALCKHPVSR--KWH 286
Cdd:cd02658  219 LVINMKRFQlLENWvpKKLDVPIDVP---EELGPGK----------YELIAFISHKGtSVHSGHYVAHIKKEIDGegKWV 285
                        330       340
                 ....*....|....*....|....*...
gi 939626626 287 EFNDNIVsdALSEN-HLVSSSAYILFYE 313
Cdd:cd02658  286 LFNDEKV--VASQDpPEMKKLGYIYFYQ 311
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-313 6.37e-25

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: 101.64  E-value: 6.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQEL-TRFLRSHHGSRSLSTKDQQILHEFAKLIQEMwTANVHTVTPMELKRAFSTKHRMYSD------YN 73
Cdd:cd02657   11 LNSTLQCLRSVPELrDALKNYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFAEkqnqggYA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  74 QQDAQEFLRFFLDSLHSALNSGVKgetlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGN-TSVTF 152
Cdd:cd02657   90 QQDAEECWSQLLSVLSQKLPGAGS--------------------------KGSFIDQLFGIELETKMKCTESPDeEEVST 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 153 DPFWDLSVPLPSSSRCK-LEACLDLFIREEV------LDGDEMPTcakcKTRRkctksftIQRFPKYLVIHLKRF----S 221
Cdd:cd02657  144 ESEYKLQCHISITTEVNyLQDGLKKGLEEEIekhsptLGRDAIYT----KTSR-------ISRLPKYLTVQFVRFfwkrD 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 222 ETRWSKLSNIVEFPtsdseLNMGSYGANSNSNVhYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVS------ 294
Cdd:cd02657  213 IQKKAKILRKVKFP-----FELDLYELCTPSGY-YELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDDDKVSevteed 286
                        330       340
                 ....*....|....*....|...
gi 939626626 295 -DALS---ENHlvssSAYILFYE 313
Cdd:cd02657  287 iLKLSgggDWH----IAYILLYK 305
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-313 2.71e-24

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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 102.01  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   2 NSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANV--HTVTPMELKRAFSTK-HRMYSDYNQQDAQ 78
Cdd:cd02669  132 NVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKVsKKKFSITEQSDPV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  79 EFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKadLTWEWYTRHENSLvrdlfvGQLKSTLKCTTCGNTSVTfdPFWDL 158
Cdd:cd02669  212 EFLSWLLNTLHKDLGGSKKPNSSIIHDCFQGKVQ--IETQKIKPHAEEE------GSKDKFFKDSRVKKTSVS--PFLLL 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 159 SVPLPSSSrckleacldLFIRE------------EVLDGDEMPTCAKCKTRRKctkSFTIQRFPKYLVIHLKRFSETRWS 226
Cdd:cd02669  282 TLDLPPPP---------LFKDGneeniipqvplkQLLKKYDGKTETELKDSLK---RYLISRLPKYLIFHIKRFSKNNFF 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 227 KLSN--IVEFPTSDSELN--MGSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHPVSRKWHEFNDNIVSDALSENH 301
Cdd:cd02669  350 KEKNptIVNFPIKNLDLSdyVHFDKPSLNLSTKYNLVANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLI 429
                        330
                 ....*....|..
gi 939626626 302 LVSSSaYILFYE 313
Cdd:cd02669  430 FLSES-YIQIWE 440
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
73-313 1.94e-22

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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 93.58  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  73 NQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCG-NTSVT 151
Cdd:cd02662   33 EQQDAHELFQVLLETLEQ------------------------------------LLKFPFDGLLASRIVCLQCGeSSKVR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 152 FDPFWDLSVPLPSSSR---CKLEACLDLFIREEVLDGdemPTCAKCKTrrkctksfTIQRFPKYLVIHLKRFSETRW--- 225
Cdd:cd02662   77 YESFTMLSLPVPNQSSgsgTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRSVFDGRgts 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 226 SKLSNIVEFPtsdSELnmgsygansnSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRK--------------------W 285
Cdd:cd02662  146 TKNSCKVSFP---ERL----------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpW 212
                        250       260
                 ....*....|....*....|....*...
gi 939626626 286 HEFNDNIVSDALSENHLVSSSAYILFYE 313
Cdd:cd02662  213 WRISDTTVKEVSESEVLEQKSAYMLFYE 240
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-312 3.44e-20

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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 89.18  E-value: 3.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCLSHTQELTRFLrsHHGSRSLSTKDQqiLHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQDAQEF 80
Cdd:cd02671   36 LNSVLQVLYFCPGFKHGL--KHLVSLISSVEQ--LQSSFLLNPEKYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  81 LRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLSV 160
Cdd:cd02671  112 LQCILGNIQE------------------------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 161 PLPSSSRCKLEACLDL-----------------FIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSET 223
Cdd:cd02671  156 PVQESELSKSEESSEIspdpktemktlkwaisqFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 224 RW--------SKLSNIVEFPTSDSELNMGSyganSNSNVHYSLYAISNHMGST-AGGHYVAlckhpvSRKWHEFNDNIVS 294
Cdd:cd02671  236 GSefdcygglSKVNTPLLTPLKLSLEEWST----KPKNDVYRLFAVVMHSGATiSSGHYTA------YVRWLLFDDSEVK 305
                        330       340
                 ....*....|....*....|....*.
gi 939626626 295 --------DALSENHLVSSSAYILFY 312
Cdd:cd02671  306 vteekdflEALSPNTSSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1-315 1.37e-17

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 81.00  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   1 MNSVIQCL--------SHTQELTRFLRS----HHGSRSLSTKDQQIlhefaKLIQEMWTANVHTVTPmelkrafstKHRM 68
Cdd:COG5533   11 MNSVLQILalylpkldELLDDLSKELKVlknvIRKPEPDLNQEEAL-----KLFTALWSSKEHKVGW---------IPPM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  69 YSdynQQDAQEFLRFFLDSLhsalnsgvkgetlNIDDnlsdnkkadltwewytrhenslvrdlfVGQLKSTLKCTTCGNT 148
Cdd:COG5533   77 GS---QEDAHELLGKLLDEL-------------KLDL---------------------------VNSFTIRIFKTTKDKK 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 149 SVTFDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDEmPTCAKCKT------RRKCTKSFTIQRFPKYLVIHLKRFS- 221
Cdd:COG5533  114 KTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMEELVDD-ETGVKAKEneelevQAKQEYEVSFVKLPKILTIQLKRFAn 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 222 ETRWSKLSNIVefptsDSELNMG---SYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKhpVSRKWHEFNDNIVSDALS 298
Cdd:COG5533  193 LGGNQKIDTEV-----DEKFELPvkhDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSE 265
                        330
                 ....*....|....*....
gi 939626626 299 EN--HLVSSSAYILFYERT 315
Cdd:COG5533  266 EEaiNEKAKNAYLYFYERI 284
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
40-296 3.16e-15

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 76.45  E-value: 3.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   40 KLIQEMWTANvHTVTPMELKRAF---STKHRMysdynQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsDNKKADlt 116
Cdd:COG5077   242 RLFYNLQTGE-EPVDTTELTRSFgwdSDDSFM-----QHDIQEFNRVLQDNL--------------------EKSMRG-- 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  117 wewyTRHENSLvRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDempTCAKCKT 196
Cdd:COG5077   294 ----TVVENAL-NGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGD---NRYNAEK 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  197 R--RKCTKSFTIQRFPKYLVIHLKRFS----ETRWSKLSNIVEFPtsdSELNMGSY-----GANSNSNVHYSLYAISNHM 265
Cdd:COG5077   364 HglQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFP---LEIDLLPFldrdaDKSENSDAVYVLYGVLVHS 440
                         250       260       270
                  ....*....|....*....|....*....|.
gi 939626626  266 GSTAGGHYVALCKHPVSRKWHEFNDNIVSDA 296
Cdd:COG5077   441 GDLHEGHYYALLKPEKDGRWYKFDDTRVTRA 471
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
78-290 1.24e-10

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 61.13  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626   78 QEFLRFFLDSLHSalnsgvkgETLNIDDNLSDNKkadltwewytrhenSLVRDLFVGQLKSTLKCTTCGNTSVTFDPF-- 155
Cdd:pfam13423 100 QSFNRFLLDQLSS--------EENSTPPNPSPAE--------------SPLEQLFGIDAETTIRCSNCGHESVRESSThv 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  156 WDLSVPLPSSSRCKLEACLDL-------FIREEVLDGdempTCAKCK------TRRkctksfTIQRFPKYLVIHLKRFSE 222
Cdd:pfam13423 158 LDLIYPRKPSSNNKKPPNQTFssilkssLERETTTKA----WCEKCKryqpleSRR------TVRNLPPVLSLNAALTNE 227
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939626626  223 TRWSKLSNIVEFPTsdsELNMGSYGANSNSN--VHYSLYAISNHMGSTAG-GHYVALCKHPVSR-------KWHEFND 290
Cdd:pfam13423 228 EWRQLWKTPGWLPP---EIGLTLSDDLQGDNeiVKYELRGVVVHIGDSGTsGHLVSFVKVADSEledptesQWYLFND 302
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
73-313 5.32e-09

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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 56.00  E-value: 5.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  73 NQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTWEWYTRHENSLvrDLFVGQLKSTLKCTTCGNTSVTF 152
Cdd:cd02673   32 DQQDAHEFLLTLLEA---------------IDDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 153 DPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDemptCAKCKtrrkCTKSFTIQR---FPKYLVIHLKRFsetrwsKLS 229
Cdd:cd02673   95 DVGNFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSCK----CESAISSERimtFPECLSINLKRY------KLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 230 NIVEFPTSDSELNMGSYGANSNSnvhYSLYAISNHMG-STAGGHYVALCKHPVS-RKWHEFNDNIV----SDALSENhlV 303
Cdd:cd02673  161 IATSDYLKKNEEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIrpvsKNDVSTN--A 235
                        250
                 ....*....|
gi 939626626 304 SSSAYILFYE 313
Cdd:cd02673  236 RSSGYLIFYD 245
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
70-312 1.03e-05

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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 46.01  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626  70 SDYN-QQDAQEFLRFFLDSLHSALNSGVKGETlniDDNLSDNKKADLTWEwytrhenslvRDLFVGQLKST--LKCTTCG 146
Cdd:cd02665   17 SLFSqQQDVSEFTHLLLDWLEDAFQAAAEAIS---PGEKSKNPMVQLFYG----------TFLTEGVLEGKpfCNCETFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 147 NTSVTFDPFWDLsvplpsssrcklEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKsftiqrFPKYLVIHLKRFS--ETR 224
Cdd:cd02665   84 QYPLQVNGYGNL------------HECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEfnQGR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939626626 225 WSKLSNIVEFPtsdSELNmgsygansnsNVHYSLYAISNHMGSTAGGHYVA-LCKHPVSRkWHEFND---------NIVS 294
Cdd:cd02665  146 PEKIHDKLEFP---QIIQ----------QVPYELHAVLVHEGQANAGHYWAyIYKQSRQE-WEKYNDisvtessweEVER 211
                        250
                 ....*....|....*...
gi 939626626 295 DALSEnhLVSSSAYILFY 312
Cdd:cd02665  212 DSFGG--GRNPSAYCLMY 227
 
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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