NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958787589|ref|XP_038934279|]
View 

ubiquitin carboxyl-terminal hydrolase 15 isoform X8 [Rattus norvegicus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 1000871)

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

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0046872|GO:0003723

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
34-683 8.92e-142

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: 435.85  E-value: 8.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  34 NEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAF 113
Cdd:COG5560   260 NKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 114 KTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQ---LKDADGRPDKVVAEEAWENHLKRNDSIIVDIFH 190
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 191 GLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYLVRMDPLAKPMQ-YKVIVPKIGNILDLCTALSALSGVpaD 269
Cdd:COG5560   420 GMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGC--F 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 270 KMIVTDIYNHRFHRIF--AMDENLSSIMERDDIYVFEININrtedteHVVIPVclrekFRHSSYTHHTGSSLFGQPFLM- 346
Cdd:COG5560   498 EIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN------GIEVPV-----VHLRIEKGYKSKRLFGDPFLQl 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 347 -AVPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGPLRCcedqNINGNGPNGIHeegsPSEMETDEPDDESSQDQELPSE 425
Cdd:COG5560   567 nVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL----LREESSPSSWL----KLETEIDTKREEQVEEEGQMNF 638
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 426 NENSqsedsvggdndseNGLCTEEtckgqltgHKKRLFTFQFNNLGNtdinyikddtrhirfdDRQLRLDERSflaldwd 505
Cdd:COG5560   639 NDAV-------------VISCEWE--------EKRYLSLFSYDPLWT----------------IREIGAAERT------- 674
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 506 pdlkkryfdenaaedfekhesveykppkrpfVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVH 585
Cdd:COG5560   675 -------------------------------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIH 723
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 586 LKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVST 665
Cdd:COG5560   724 LKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITE 803
                         650
                  ....*....|....*...
gi 1958787589 666 ASEDQIVSKAAYVLFYQR 683
Cdd:COG5560   804 VDPEDSVTSSAYVLFYRR 821
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
34-683 8.92e-142

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 435.85  E-value: 8.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  34 NEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAF 113
Cdd:COG5560   260 NKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 114 KTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQ---LKDADGRPDKVVAEEAWENHLKRNDSIIVDIFH 190
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 191 GLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYLVRMDPLAKPMQ-YKVIVPKIGNILDLCTALSALSGVpaD 269
Cdd:COG5560   420 GMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGC--F 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 270 KMIVTDIYNHRFHRIF--AMDENLSSIMERDDIYVFEININrtedteHVVIPVclrekFRHSSYTHHTGSSLFGQPFLM- 346
Cdd:COG5560   498 EIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN------GIEVPV-----VHLRIEKGYKSKRLFGDPFLQl 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 347 -AVPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGPLRCcedqNINGNGPNGIHeegsPSEMETDEPDDESSQDQELPSE 425
Cdd:COG5560   567 nVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL----LREESSPSSWL----KLETEIDTKREEQVEEEGQMNF 638
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 426 NENSqsedsvggdndseNGLCTEEtckgqltgHKKRLFTFQFNNLGNtdinyikddtrhirfdDRQLRLDERSflaldwd 505
Cdd:COG5560   639 NDAV-------------VISCEWE--------EKRYLSLFSYDPLWT----------------IREIGAAERT------- 674
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 506 pdlkkryfdenaaedfekhesveykppkrpfVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVH 585
Cdd:COG5560   675 -------------------------------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIH 723
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 586 LKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVST 665
Cdd:COG5560   724 LKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITE 803
                         650
                  ....*....|....*...
gi 1958787589 666 ASEDQIVSKAAYVLFYQR 683
Cdd:COG5560   804 VDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-682 8.01e-60

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: 201.36  E-value: 8.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 535 PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSE 614
Cdd:cd02674    82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787589 615 FLINPN-AGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 682
Cdd:cd02674   162 YVDTRSfTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
40-231 3.79e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 186.11  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  40 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDkyqEELNFDNPLGMRGEIAKSYAELIKQMWSG-KFSYVTPRAFKTQVG 118
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 119 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRirkkpyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLV 198
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958787589 199 CPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 231
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASL 164
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
34-683 8.92e-142

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 435.85  E-value: 8.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  34 NEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAF 113
Cdd:COG5560   260 NKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 114 KTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQ---LKDADGRPDKVVAEEAWENHLKRNDSIIVDIFH 190
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 191 GLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYLVRMDPLAKPMQ-YKVIVPKIGNILDLCTALSALSGVpaD 269
Cdd:COG5560   420 GMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGC--F 497
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 270 KMIVTDIYNHRFHRIF--AMDENLSSIMERDDIYVFEININrtedteHVVIPVclrekFRHSSYTHHTGSSLFGQPFLM- 346
Cdd:COG5560   498 EIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN------GIEVPV-----VHLRIEKGYKSKRLFGDPFLQl 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 347 -AVPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGPLRCcedqNINGNGPNGIHeegsPSEMETDEPDDESSQDQELPSE 425
Cdd:COG5560   567 nVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL----LREESSPSSWL----KLETEIDTKREEQVEEEGQMNF 638
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 426 NENSqsedsvggdndseNGLCTEEtckgqltgHKKRLFTFQFNNLGNtdinyikddtrhirfdDRQLRLDERSflaldwd 505
Cdd:COG5560   639 NDAV-------------VISCEWE--------EKRYLSLFSYDPLWT----------------IREIGAAERT------- 674
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 506 pdlkkryfdenaaedfekhesveykppkrpfVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVH 585
Cdd:COG5560   675 -------------------------------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIH 723
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 586 LKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVST 665
Cdd:COG5560   724 LKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITE 803
                         650
                  ....*....|....*...
gi 1958787589 666 ASEDQIVSKAAYVLFYQR 683
Cdd:COG5560   804 VDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-682 8.01e-60

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: 201.36  E-value: 8.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 535 PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSE 614
Cdd:cd02674    82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958787589 615 FLINPN-AGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 682
Cdd:cd02674   162 YVDTRSfTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
40-231 3.79e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 186.11  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  40 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDkyqEELNFDNPLGMRGEIAKSYAELIKQMWSG-KFSYVTPRAFKTQVG 118
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 119 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRirkkpyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLV 198
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958787589 199 CPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 231
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASL 164
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
526-681 5.06e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 177.63  E-value: 5.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 526 SVEYKPPKR--PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLV 603
Cdd:pfam00443 149 SLPIPGDSAelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 604 DFPIsDLDMSEFLINPNAGP----CRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASED-QIVSKAAYV 678
Cdd:pfam00443 229 EFPL-ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYI 307

                  ...
gi 1958787589 679 LFY 681
Cdd:pfam00443 308 LFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
526-682 4.69e-37

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: 139.54  E-value: 4.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 526 SVEYKPPKRPFVKLKDCIELFTTKEKLGAEDPWYCpNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMR-DKLDTLVD 604
Cdd:cd02257    88 SLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVS 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 605 FPISdLDMSEFLI------NPNAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNKDDGKWYYFDDSSVSTASEDQIV----- 672
Cdd:cd02257   167 FPLE-LDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSADSgHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgsl 245
                         170
                  ....*....|
gi 1958787589 673 SKAAYVLFYQ 682
Cdd:cd02257   246 SSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
539-681 2.64e-33

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: 130.09  E-value: 2.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 539 LKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYmrDKLDTLVDFPiSDLDMSEFLIN 618
Cdd:cd02661   164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQ 240
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958787589 619 PNAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNkDDGKWYYFDDSSVSTASEDQIVSKAAYVLFY 681
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSgHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
538-681 7.41e-32

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: 126.72  E-value: 7.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 538 KLKDCIELFTTKEKLGaEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRY-MRDKLDTLVDFPiSDLDMSEFL 616
Cdd:cd02660   177 TLSDCLDRFTRPEKLG-DFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFP-LELNMTPYT 254
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958787589 617 I---------NPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDgKWYYFDDSSVSTASEDQIVSKAAYVLFY 681
Cdd:cd02660   255 SssigdtqdsNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG-QWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-226 5.03e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 103.61  E-value: 5.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMrgeIAKSYAELIKQMW-SGKFSYVTPRAFKTQVGR 119
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSC---LSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 120 FAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLVC 199
Cdd:cd02660    79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                         170       180
                  ....*....|....*....|....*..
gi 1958787589 200 PECAKISVTFDPFCYLTLPLPMKKERS 226
Cdd:cd02660   138 QRCGGVSTTVDPFLDLSLDIPNKSTPS 164
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
40-228 5.40e-23

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: 100.04  E-value: 5.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  40 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRgEIAKsyaeLIKQMWSGKFSYVTPRAFKTQVGR 119
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC-ALEA----HVERALASSGPGSAPRIFSSNLKQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 120 FAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIqlkdadgrpdkvvaeeawENHLKRNDSIIVDIFHGLFKSTLVC 199
Cdd:cd02661    77 ISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKA------------------VDPSSQETTLVQQIFGGYLRSQVKC 138
                         170       180
                  ....*....|....*....|....*....
gi 1958787589 200 PECAKISVTFDPFcyLTLPLPMKKERSLE 228
Cdd:cd02661   139 LNCKHVSNTYDPF--LDLSLDIKGADSLE 165
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-681 1.93e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 99.03  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 536 FVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYM--RDKLDTLVDFPiSDLDMS 613
Cdd:cd02668   155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTgaKKKLNASISFP-EILDMG 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 614 EFLINPNAGPCRYNLIAVSNHY-GGMGGGHYTAFAKNKDDGKWYYFDDSSVS--------------TASEDQ-------I 671
Cdd:cd02668   234 EYLAESDEGSYVYELSGVLIHQgVSAYSGHYIAHIKDEQTGEWYKFNDEDVEempgkplklgnsedPAKPRKseikkgtH 313
                         170
                  ....*....|
gi 1958787589 672 VSKAAYVLFY 681
Cdd:cd02668   314 SSRTAYMLVY 323
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-231 5.31e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 95.43  E-value: 5.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNtpplteyflndkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvtprafktqvgrf 120
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 121 apqfsgyQQQDCQELLAFLLDGLHedlnrirkkpyiqlkdadgrpdkvvaeeawenhlkrndSIIVDIFHGLFKSTLVCP 200
Cdd:cd02674    21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958787589 201 ECAKISVTFDPFCYLTLPLPMKKERSLEVYL 231
Cdd:cd02674    56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
534-686 1.14e-21

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: 96.94  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 534 RPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYS--RYMRDKLDTLVDFPISdLD 611
Cdd:cd02659   148 KGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LD 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 612 MSEFLINPNA-----------GPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSK------ 674
Cdd:cd02659   227 MEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEEcfggee 306
                         170       180
                  ....*....|....*....|....*...
gi 1958787589 675 ----------------AAYVLFYQRQDT 686
Cdd:cd02659   307 tqktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
528-682 4.26e-21

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: 93.99  E-value: 4.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 528 EYKPPKRPfVKLKDCIELFTTKEKLGAEDPWYCPNCkehQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD-KLDTLVDFP 606
Cdd:cd02667   103 RSDEIKSE-CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 607 iSDLDMSEFLiNPNAGPC------RYNLIAVSNHYGGMGGGHYTAFAK---------------------NKDDGKWYYFD 659
Cdd:cd02667   179 -EILDLAPFC-DPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeaGPGSGQWYYIS 256
                         170       180
                  ....*....|....*....|...
gi 1958787589 660 DSSVSTASEDQIVSKAAYVLFYQ 682
Cdd:cd02667   257 DSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-228 5.60e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 90.52  E-value: 5.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNdkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvTPRAFKTQVGRF 120
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------------------------------------TPKELFSQVCRK 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 121 APQFSGYQQQDCQELLAFLLDGLhedlnrirkKPYIqlkdadgrpdkvvaeeawenhlkrnDSiivdIFHGLFKSTLVCP 200
Cdd:cd02667    43 APQFKGYQQQDSHELLRYLLDGL---------RTFI-------------------------DS----IFGGELTSTIMCE 84
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958787589 201 ECAKISVTFDPFCYLTLPL--PMKKERSLE 228
Cdd:cd02667    85 SCGTVSLVYEPFLDLSLPRsdEIKSECSIE 114
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
41-230 1.58e-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.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 88.69  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNtpplteyflndkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvtprafktqvgrf 120
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 121 apqfsgyQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdadgrpdkvvaeeawENHLKRNDSIIVDIFHGLFKSTLVCP 200
Cdd:cd02257    21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958787589 201 ECAKISVTFDPFCYLTLPLPMKKERSLEVY 230
Cdd:cd02257    73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
532-682 2.57e-16

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: 80.44  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 532 PKRPFVKLKDCIELFTTKEKLgaEDpwYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD-KLDTLVDFPisdl 610
Cdd:cd02658   173 LVYEPVPLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP---- 244
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958787589 611 dmsEFLinpnaGPCRYNLIAVSNHY-GGMGGGHYTAFAKNKDD--GKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 682
Cdd:cd02658   245 ---EEL-----GPGKYELIAFISHKgTSVHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
539-682 1.15e-15

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: 78.51  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 539 LKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYS-RYMR-DKLDTLVDFPisdLDMSEFL 616
Cdd:cd02663   149 ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyIKLFYRVVFP---LELRLFN 225
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787589 617 INPNA-GPCR-YNLIAVSNHY-GGMGGGHYTAFAKNKddGKWYYFDDSSVSTASEDQIV--------SKAAYVLFYQ 682
Cdd:cd02663   226 TTDDAeNPDRlYELVAVVVHIgGGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
577-681 1.69e-14

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: 75.06  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 577 SLPPVLVVHLKRFSYSRYMRDKLDTL--VDFPIsDLDMSEFLinpnAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNKDDG 653
Cdd:cd02657   195 RLPKYLTVQFVRFFWKRDIQKKAKILrkVKFPF-ELDLYELC----TPSGYYELVAVITHQGRSADSgHYVAWVRRKNDG 269
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958787589 654 KWYYFDDSSVSTASEDQIVSKA-------AYVLFY 681
Cdd:cd02657   270 KWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-221 5.27e-14

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: 73.51  E-value: 5.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNP-LGMRGEIAKsyaeLIKQMWSGKFSY------------ 107
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPaNDLNCQLIK----LADGLLSGRYSKpaslksendpyq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 108 --VTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDglhedlnRIRKKPYIQLKDADGRPDKVVAEEawenhlkrndsii 185
Cdd:cd02658    77 vgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLNPNDLFKFMIED------------- 136
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958787589 186 vdifhglfksTLVCPECAKISVTFDPFCYLTLPLPM 221
Cdd:cd02658   137 ----------RLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
2-256 7.37e-14

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: 74.28  E-value: 7.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589   2 PAYTKDSVKNSNY-CLPSYTaYKNYDYSepgrnneqPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFL-NDKYQEELNF 79
Cdd:cd02669    90 PTYTKEQISDLDRdPKLSRD-LDGKPYL--------PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDR 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  80 DNPLGmrgeiaKSYAELIKQMWSgkfsyvtPRAFKTQVG----------RFAPQFSGYQQQDCQELLAFLLDGLHEDLNR 149
Cdd:cd02669   161 KSELV------KRLSELIRKIWN-------PRNFKGHVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 150 IRKKpyiqlkdadgrpdkvvaeeawenhlkrNDSIIVDIFHGLFK---------------STLVCPECAKISVTFDPFCY 214
Cdd:cd02669   228 SKKP---------------------------NSSIIHDCFQGKVQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLL 280
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958787589 215 LTLPLPMKkerslevylvrmdPLAKPMQYKVIVPKIgNILDL 256
Cdd:cd02669   281 LTLDLPPP-------------PLFKDGNEENIIPQV-PLKQL 308
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-154 8.27e-14

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: 72.75  E-value: 8.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLteyflndkyQEELNFDNPLGMRGE-----IAKSYAELIKQMwSGKFSYVTPRAFKT 115
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPEL---------RDALKNYNPARRGANqssdnLTNALRDLFDTM-DKKQEPVPPIEFLQ 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958787589 116 QVGRFAPQFS------GYQQQDCQELLAFLLDGLHEDLNRIRKKP 154
Cdd:cd02657    71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG 115
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
577-682 3.76e-11

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: 65.80  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 577 SLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCR---YNLIA-VSNHYGGMGGGHYTAFAKNKDD 652
Cdd:cd02669   331 RLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLstkYNLVAnIVHEGTPQEDGTWRVQLRHKST 410
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958787589 653 GKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 682
Cdd:cd02669   411 NKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
560-671 1.78e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 64.51  E-value: 1.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  560 CPNCKEH--QQATKKLDLWSLPPVLVVHLKRFSYS--RYMRDKLDTLVDFPISdLDMSEFLiNPNA-----GPCRYNLIA 630
Cdd:COG5077    358 RYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLE-IDLLPFL-DRDAdksenSDAVYVLYG 435
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958787589  631 VSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQI 671
Cdd:COG5077    436 VLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
539-682 2.27e-10

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: 61.61  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 539 LKDCIELFTTKEKLgaEDPwYCPNCkehQQATKKLdlwslPPVLVVHLKRFSYS-RYMRDKLDTLVDFPisdldmsEFLi 617
Cdd:cd02662    98 LEHCLDDFLSTEII--DDY-KCDRC---QTVIVRL-----PQILCIHLSRSVFDgRGTSTKNSCKVSFP-------ERL- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 618 npnaGPCRYNLIAVSNHYGGMGGGHYTAF--------------------AKNKDDGKWYYFDDSSVSTASEDQIV-SKAA 676
Cdd:cd02662   159 ----PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSA 234

                  ....*.
gi 1958787589 677 YVLFYQ 682
Cdd:cd02662   235 YMLFYE 240
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
536-682 2.48e-10

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: 62.51  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 536 FVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSR--YMRDKL------DTLVDFPI 607
Cdd:cd02664   133 FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPV 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 608 SD-LDMSEFLINPNAGPCR-----------YNLIAV---------SNHY-----------GGMGGGHYTAFAKNKDDGK- 654
Cdd:cd02664   213 RVeSKSSESPLEKKEEESGddgelvtrqvhYRLYAVvvhsgysseSGHYftyardqtdadSTGQECPEPKDAEENDESKn 292
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958787589 655 WYYFDDSSVS--TASEDQIV-----SKAAYVLFYQ 682
Cdd:cd02664   293 WYLFNDSRVTfsSFESVQNVtsrfpKDTPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
519-681 3.61e-10

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: 62.22  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 519 EDFEKHESVEYKP-PKRPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD 597
Cdd:cd02671   161 ELSKSEESSEISPdPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFD 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 598 ------KLDTLVDFPIsDLDMSEFLINPNAGpcRYNLIAVSNHY-GGMGGGHYTAFAknkddgKWYYFDDSSVSTASEDQ 670
Cdd:cd02671   241 cygglsKVNTPLLTPL-KLSLEEWSTKPKND--VYRLFAVVMHSgATISSGHYTAYV------RWLLFDDSEVKVTEEKD 311
                         170       180
                  ....*....|....*....|
gi 1958787589 671 I---------VSKAAYVLFY 681
Cdd:cd02671   312 FlealspntsSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
41-154 1.08e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 60.20  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLS-NTPPLTEYFLNDKYQ-----EELNFDNPLGMRGEIAKsyaeLIKQMWSGKfsyvtprafK 114
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPDLNQEEALK----LFTALWSSK---------E 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958787589 115 TQVGRFAPQfsgYQQQDCQELLAFLLDGLHEDL---NRIRKKP 154
Cdd:COG5533    68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDLvnsFTIRIFK 107
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-220 2.04e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 59.81  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSntppLTEYFLNDKYQEelnfdNPLGMRGEIAKSYAELIKQMW---SGKFSYVTPRAFKTQV 117
Cdd:cd02664     1 GLINLGNTCYMNSVLQALF----MAKDFRRQVLSL-----NLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 118 grFAPQFSGYQQQDCQELLAFLLDGLHedlnrirkkpyiqlkdadgrpdkvvaeeawenhlkrndSIIVDIFHGLFKSTL 197
Cdd:cd02664    72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                         170       180
                  ....*....|....*....|...
gi 1958787589 198 VCPECAKISVTFDPFCYLTLPLP 220
Cdd:cd02664   112 RCLNCNSTSARTERFRDLDLSFP 134
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
30-145 3.48e-07

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: 52.97  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  30 PGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPplteyflndKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVT 109
Cdd:cd02671    15 CEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQA 85
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958787589 110 PRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHE 145
Cdd:cd02671    86 PRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
38-228 3.82e-07

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: 52.64  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  38 GLCGLSNLGNTCFMNSAIQCLSNTPplteYFLNDKYQEELNFDNPlgmrGEIAKSYAeLIKQMwsgKFSYVTPRAFKTQV 117
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD----DNKSVPLA-LQRLF---LFLQLSESPVKTTE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 118 GRFAPQFSG------YQQQDCQELLAFLLDglhedlnrirkkpyiqlkdadgrpdkvvaeeAWENHLKRN--DSIIVDIF 189
Cdd:cd02659    69 LTDKTRSFGwdslntFEQHDVQEFFRVLFD-------------------------------KLEEKLKGTgqEGLIKNLF 117
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958787589 190 HGLFKSTLVCPECAKISVTFDPFcyLTLPLPMKKERSLE 228
Cdd:cd02659   118 GGKLVNYIICKECPHESEREEYF--LDLQVAVKGKKNLE 154
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-220 4.52e-07

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: 52.31  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLsntpplteYFLNdkyqeelnfdnplgmrgeIAKSYAELIKQMWSGKFSY--VTPRAFKTQVG 118
Cdd:cd02663     1 GLENFGNTCYCNSVLQAL--------YFEN------------------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 119 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdaDGRPDKVVAEEAWENHlkrnDSIIVDIFHGLFKSTLV 198
Cdd:cd02663    55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKA--------EKANRKLNNNNNAEPQ----PTWVHEIFQGILTNETR 122
                         170       180
                  ....*....|....*....|..
gi 1958787589 199 CPECAKISVTFDPFCYLTLPLP 220
Cdd:cd02663   123 CLTCETVSSRDETFLDLSIDVE 144
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-228 1.66e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 50.50  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLN-----DKYQEELNFDNPLGMRGeIAKSYAELIKQMWSGKFSYVTPRAFKT 115
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 116 QVGrfapqFSGYQQQDCQELLAFLLDGLHEDLNrirkkpyiQLKDADGRpdkvvaeeawenhlkrndSIIVDIFHGLFKS 195
Cdd:cd02668    80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLS--------KSKNPDLK------------------NIVQDLFRGEYSY 128
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958787589 196 TLVCPECAKISVTFDPFcyLTLPLPMKKERSLE 228
Cdd:cd02668   129 VTQCSKCGRESSLPSKF--YELELQLKGHKTLE 159
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
211-348 3.21e-06

Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.


Pssm-ID: 464201  Cd Length: 204  Bit Score: 48.63  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 211 PFCYLTLPLPMK---KERSLEVYLVrMDPLAKPMQYKVIVPKIGNILDLCTALSALSGVP---ADKMIVTDIYNHRFHRI 284
Cdd:pfam14533   1 ALYYEVLDISLSeleNKKSIKVTWL-SPGLKKEEELELLVPKNGTVADLLEELQKKVKLSeegSGKIRLYEVSNHKIYKE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787589 285 FAMDENLSSIMERDDIYVFEI---NINRTEDTehVVIPVClrekfrHssYtHHTGSSLFGQPFLMAV 348
Cdd:pfam14533  80 LSEDEPIDSLNDYLTLYAEEIpeeELNLDEGE--RLIPVF------H--F-QKEPSRTHGIPFLFVL 135
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-67 1.11e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 47.36  E-value: 1.11e-05
                          10        20
                  ....*....|....*....|....*..
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLTEY 67
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
560-681 2.45e-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 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: 43.29  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 560 CPNCKeHQQATKKLDLWSLPPVLVVHLKRFsYSRYMRDKldtlvdfpisDLDMSEFLINPNAG-PCRYNLIAVSNHY-GG 637
Cdd:cd02673   129 CSSCK-CESAISSERIMTFPECLSINLKRY-KLRIATSD----------YLKKNEEIMKKYCGtDAKYSLVAVICHLgES 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958787589 638 MGGGHYTAFAKNKDDG-KWYYFDDSSVSTASEDQI---VSKAAYVLFY 681
Cdd:cd02673   197 PYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-198 9.21e-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 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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 42.09  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589  41 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLN-DKYQEELNFDNPLGMR-GEIAKSYAE-------------LIKQMWSGKF 105
Cdd:cd02666     3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfDESKAELASDYPTERRiGGREVSRSElqrsnqfvyelrsLFNDLIHSNT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 106 SYVTPRAfktqvgRFApqFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDAD------------GRPDKVVAEEA 173
Cdd:cd02666    83 RSVTPSK------ELA--YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDkeqsdlikrlfsGKTKQQLVPES 154
                         170       180
                  ....*....|....*....|....*
gi 1958787589 174 WenhlkrNDSIIVDIFHGLFKSTLV 198
Cdd:cd02666   155 M------GNQPSVRTKTERFLSLLV 173
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
542-682 4.35e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 39.80  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 542 CIELFTTKEKlgaEDPWYCPNCKEHQQATKKLDLWSLPP----VLVVHLKRFSYSRYMR-------DKLDTLVDFPISDL 610
Cdd:cd02672   122 LLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTNGEFDDInvvlpsgKVMQNKVSPKAIDH 198
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958787589 611 DmSEFLINPNAGPCRYNLIA-VSNHYGGMGGGHYTAF----AKNKDDGKWYYFDDSSVSTasedqiVSKAAYVLFYQ 682
Cdd:cd02672   199 D-KLVKNRGQESIYKYELVGyVCEINDSSRGQHNVVFvikvNEESTHGRWYLFNDFLVTP------VSELAYILLYQ 268
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
560-663 5.22e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 39.56  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 560 CPNCKEHQQATKKLDLWSLPPVLVVHLKRfsYSRYMRDKLDTLVDFPIS-DLDMSEFLINPNAGpCRYNLIA-VSNHYGG 637
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAAL--TNEEWRQLWKTPGWLPPEiGLTLSDDLQGDNEI-VKYELRGvVVHIGDS 272
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958787589 638 MGGGHYTAFAK-------NKDDGKWYYFDDSSV 663
Cdd:pfam13423 273 GTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
578-681 5.97e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.08  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787589 578 LPPVLVVHLKRFSYSRYMRDKLDTLVDFPisdldmSEFLINPnagpcrYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYY 657
Cdd:cd02665   128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------QIIQQVP------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958787589 658 FDDSSVSTASEDQIVSKA--------AYVLFY 681
Cdd:cd02665   196 YNDISVTESSWEEVERDSfgggrnpsAYCLMY 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH