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Conserved domains on  [gi|21489969|ref|NP_081880|]
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ubiquitin carboxyl-terminal hydrolase 15 isoform 1 [Mus musculus]

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

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-932 8.54e-144

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: 448.95  E-value: 8.54e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560  29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560  98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 165 IRKIFNIPDEkEARLWNKYMSNTFEPLNKPDSTI-QDAGLYQGQVLVIEQKNEDGTwprgpstpkspgASNFSTLPKISp 243
Cdd:COG5560 176 VMNAFVDPSD-DFRLWDVVPEIMGLRLGLDSFFRrYRVLASDGRVLHPLTRLELFE------------DRSVLLLSKIT- 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 244 sslsnnynninnrnvknSNYCLPSYTAYKNYDYSepgrNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQ 323
Cdd:COG5560 242 -----------------RNPDWLVDSIVDDHNRS----INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 324 EELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKP 403
Cdd:COG5560 301 ESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKP 380
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 404 YIQ---LKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 480
Cdd:COG5560 381 YTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVV 460
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 481 VRMDPLAKPMQ-YKVIVPKIGNILDLCTALSALSGVpaDKMIVTDIYNHRFHRIF--AVDENLSSIMERDDIYVFEININ 557
Cdd:COG5560 461 FPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGC--FEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN 538
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 558 raedteHVVIPVclrekFRHSSYTHHTGSSLFGQPFLM--AIPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGHLRCce 635
Cdd:COG5560 539 ------GIEVPV-----VHLRIEKGYKSKRLFGDPFLQlnVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL-- 605
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 636 dqNINGNGPNGLHeegsPSEMETDEPDDESSQDQELPSENENSqsedsvggdndseNGLCTEEtckgqltgHKKRLFTFQ 715
Cdd:COG5560 606 --LREESSPSSWL----KLETEIDTKREEQVEEEGQMNFNDAV-------------VISCEWE--------EKRYLSLFS 658
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 716 FNNLGNNdinyikddtshirfddRQLRLDERSflaldwdpdlkkryfdenaaedfekhesveykppkrpfVKLKDCIELF 795
Cdd:COG5560 659 YDPLWTI----------------REIGAAERT--------------------------------------ITLQDCLNEF 684
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 796 TTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRY 875
Cdd:COG5560 685 SKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIY 764
                       890       900       910       920       930
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21489969 876 NLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQR 932
Cdd:COG5560 765 DLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-932 8.54e-144

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 448.95  E-value: 8.54e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560  29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560  98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 165 IRKIFNIPDEkEARLWNKYMSNTFEPLNKPDSTI-QDAGLYQGQVLVIEQKNEDGTwprgpstpkspgASNFSTLPKISp 243
Cdd:COG5560 176 VMNAFVDPSD-DFRLWDVVPEIMGLRLGLDSFFRrYRVLASDGRVLHPLTRLELFE------------DRSVLLLSKIT- 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 244 sslsnnynninnrnvknSNYCLPSYTAYKNYDYSepgrNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQ 323
Cdd:COG5560 242 -----------------RNPDWLVDSIVDDHNRS----INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 324 EELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKP 403
Cdd:COG5560 301 ESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKP 380
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 404 YIQ---LKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 480
Cdd:COG5560 381 YTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVV 460
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 481 VRMDPLAKPMQ-YKVIVPKIGNILDLCTALSALSGVpaDKMIVTDIYNHRFHRIF--AVDENLSSIMERDDIYVFEININ 557
Cdd:COG5560 461 FPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGC--FEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN 538
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 558 raedteHVVIPVclrekFRHSSYTHHTGSSLFGQPFLM--AIPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGHLRCce 635
Cdd:COG5560 539 ------GIEVPV-----VHLRIEKGYKSKRLFGDPFLQlnVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL-- 605
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 636 dqNINGNGPNGLHeegsPSEMETDEPDDESSQDQELPSENENSqsedsvggdndseNGLCTEEtckgqltgHKKRLFTFQ 715
Cdd:COG5560 606 --LREESSPSSWL----KLETEIDTKREEQVEEEGQMNFNDAV-------------VISCEWE--------EKRYLSLFS 658
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 716 FNNLGNNdinyikddtshirfddRQLRLDERSflaldwdpdlkkryfdenaaedfekhesveykppkrpfVKLKDCIELF 795
Cdd:COG5560 659 YDPLWTI----------------REIGAAERT--------------------------------------ITLQDCLNEF 684
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 796 TTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRY 875
Cdd:COG5560 685 SKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIY 764
                       890       900       910       920       930
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21489969 876 NLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQR 932
Cdd:COG5560 765 DLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
784-931 1.01e-59

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: 203.67  E-value: 1.01e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 784 PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSE 863
Cdd:cd02674  82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21489969 864 FLINPN-AGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 931
Cdd:cd02674 162 YVDTRSfTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
289-480 4.46e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.04  E-value: 4.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   289 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDkyqEELNFDNPLGMRGEIAKSYAELIKQMWSG-KFSYVTPRAFKTQVG 367
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   368 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRirkkpyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLV 447
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 21489969   448 CPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 480
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASL 164
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 3.06e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 3.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969     24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 21489969    104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-932 8.54e-144

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 448.95  E-value: 8.54e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560  29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560  98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 165 IRKIFNIPDEkEARLWNKYMSNTFEPLNKPDSTI-QDAGLYQGQVLVIEQKNEDGTwprgpstpkspgASNFSTLPKISp 243
Cdd:COG5560 176 VMNAFVDPSD-DFRLWDVVPEIMGLRLGLDSFFRrYRVLASDGRVLHPLTRLELFE------------DRSVLLLSKIT- 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 244 sslsnnynninnrnvknSNYCLPSYTAYKNYDYSepgrNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQ 323
Cdd:COG5560 242 -----------------RNPDWLVDSIVDDHNRS----INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 324 EELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKP 403
Cdd:COG5560 301 ESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKP 380
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 404 YIQ---LKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 480
Cdd:COG5560 381 YTSkpdLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVV 460
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 481 VRMDPLAKPMQ-YKVIVPKIGNILDLCTALSALSGVpaDKMIVTDIYNHRFHRIF--AVDENLSSIMERDDIYVFEININ 557
Cdd:COG5560 461 FPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGC--FEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYETNDN 538
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 558 raedteHVVIPVclrekFRHSSYTHHTGSSLFGQPFLM--AIPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGHLRCce 635
Cdd:COG5560 539 ------GIEVPV-----VHLRIEKGYKSKRLFGDPFLQlnVLIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRL-- 605
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 636 dqNINGNGPNGLHeegsPSEMETDEPDDESSQDQELPSENENSqsedsvggdndseNGLCTEEtckgqltgHKKRLFTFQ 715
Cdd:COG5560 606 --LREESSPSSWL----KLETEIDTKREEQVEEEGQMNFNDAV-------------VISCEWE--------EKRYLSLFS 658
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 716 FNNLGNNdinyikddtshirfddRQLRLDERSflaldwdpdlkkryfdenaaedfekhesveykppkrpfVKLKDCIELF 795
Cdd:COG5560 659 YDPLWTI----------------REIGAAERT--------------------------------------ITLQDCLNEF 684
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 796 TTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRY 875
Cdd:COG5560 685 SKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIY 764
                       890       900       910       920       930
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21489969 876 NLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQR 932
Cdd:COG5560 765 DLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
784-931 1.01e-59

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: 203.67  E-value: 1.01e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 784 PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSE 863
Cdd:cd02674  82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21489969 864 FLINPN-AGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 931
Cdd:cd02674 162 YVDTRSfTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
289-480 4.46e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.04  E-value: 4.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   289 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDkyqEELNFDNPLGMRGEIAKSYAELIKQMWSG-KFSYVTPRAFKTQVG 367
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRI---SPLSEDSRYNKDINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   368 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRirkkpyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLV 447
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 21489969   448 CPECAKISVTFDPFCYLTLPLPMKKERSLEVYL 480
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELKTASL 164
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
775-930 4.42e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 179.56  E-value: 4.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   775 SVEYKPPKR--PFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLV 852
Cdd:pfam00443 149 SLPIPGDSAelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   853 DFPIsDLDMSEFLINPNAGP----CRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASED-QIVSKAAYV 927
Cdd:pfam00443 229 EFPL-ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYI 307

                  ...
gi 21489969   928 LFY 930
Cdd:pfam00443 308 LFY 310
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
135-222 6.03e-46

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 159.25  E-value: 6.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   135 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 214
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 21489969   215 NEDGTWPR 222
Cdd:pfam14836  81 NEDGNWPR 88
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
775-931 2.01e-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: 141.08  E-value: 2.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 775 SVEYKPPKRPFVKLKDCIELFTTKEKLGAEDPWYCpNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMR-DKLDTLVD 853
Cdd:cd02257  88 SLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVS 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 854 FPISdLDMSEFLI------NPNAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNKDDGKWYYFDDSSVSTASEDQIV----- 921
Cdd:cd02257 167 FPLE-LDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSADSgHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgsl 245
                       170
                ....*....|
gi 21489969 922 SKAAYVLFYQ 931
Cdd:cd02257 246 SSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
788-930 1.02e-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: 132.01  E-value: 1.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 788 LKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYmrDKLDTLVDFPiSDLDMSEFLIN 867
Cdd:cd02661 164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQ 240
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21489969 868 PNAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNkDDGKWYYFDDSSVSTASEDQIVSKAAYVLFY 930
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSgHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
787-930 3.32e-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: 128.26  E-value: 3.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 787 KLKDCIELFTTKEKLGaEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRY-MRDKLDTLVDFPiSDLDMSEFL 865
Cdd:cd02660 177 TLSDCLDRFTRPEKLG-DFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFP-LELNMTPYT 254
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21489969 866 I---------NPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDgKWYYFDDSSVSTASEDQIVSKAAYVLFY 930
Cdd:cd02660 255 SssigdtqdsNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDG-QWFKFDDAMITRVSEEEVLKSQAYLLFY 327
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 3.06e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 3.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969     24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 21489969    104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-475 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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 105.15  E-value: 2.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMrgeIAKSYAELIKQMW-SGKFSYVTPRAFKTQVGR 368
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSC---LSCAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 369 FAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPyiqlkdadgrpdkvvaeeaweNHLKRNDSIIVDIFHGLFKSTLVC 448
Cdd:cd02660  79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVTC 137
                       170       180
                ....*....|....*....|....*..
gi 21489969 449 PECAKISVTFDPFCYLTLPLPMKKERS 475
Cdd:cd02660 138 QRCGGVSTTVDPFLDLSLDIPNKSTPS 164
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
289-477 2.62e-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: 101.58  E-value: 2.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 289 CGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRgEIAKsyaeLIKQMWSGKFSYVTPRAFKTQVGR 368
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC-ALEA----HVERALASSGPGSAPRIFSSNLKQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 369 FAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIqlkdadgrpdkvvaeeawENHLKRNDSIIVDIFHGLFKSTLVC 448
Cdd:cd02661  77 ISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKA------------------VDPSSQETTLVQQIFGGYLRSQVKC 138
                       170       180
                ....*....|....*....|....*....
gi 21489969 449 PECAKISVTFDPFcyLTLPLPMKKERSLE 477
Cdd:cd02661 139 LNCKHVSNTYDPF--LDLSLDIKGADSLE 165
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
27-119 4.49e-23

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 93.97  E-value: 4.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969    27 GDTWYLVDSRWFKQWKKYVGfdswdkyqmgDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYtl 106
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWY-- 68
                          90
                  ....*....|...
gi 21489969   107 mEGQEPIARKVVE 119
Cdd:pfam06337  69 -GGGPEIKRNVVN 80
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
785-930 1.55e-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: 99.80  E-value: 1.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 785 FVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYM--RDKLDTLVDFPiSDLDMS 862
Cdd:cd02668 155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTgaKKKLNASISFP-EILDMG 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 863 EFLINPNAGPCRYNLIAVSNHY-GGMGGGHYTAFAKNKDDGKWYYFDDSSVS--------------TASEDQ-------I 920
Cdd:cd02668 234 EYLAESDEGSYVYELSGVLIHQgVSAYSGHYIAHIKDEQTGEWYKFNDEDVEempgkplklgnsedPAKPRKseikkgtH 313
                       170
                ....*....|
gi 21489969 921 VSKAAYVLFY 930
Cdd:cd02668 314 SSRTAYMLVY 323
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-480 2.18e-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: 96.97  E-value: 2.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNtpplteyflndkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvtprafktqvgrf 369
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 370 apqfsgyQQQDCQELLAFLLDGLHedlnrirkkpyiqlkdadgrpdkvvaeeawenhlkrndSIIVDIFHGLFKSTLVCP 449
Cdd:cd02674  21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                       170       180       190
                ....*....|....*....|....*....|.
gi 21489969 450 ECAKISVTFDPFCYLTLPLPMKKERSLEVYL 480
Cdd:cd02674  56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKVTL 86
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
783-935 8.89e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 97.71  E-value: 8.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 783 RPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYS--RYMRDKLDTLVDFPISdLD 860
Cdd:cd02659 148 KGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LD 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 861 MSEFLINPNA-----------GPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSK------ 923
Cdd:cd02659 227 MEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEEcfggee 306
                       170       180
                ....*....|....*....|....*...
gi 21489969 924 ----------------AAYVLFYQRQDT 935
Cdd:cd02659 307 tqktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-931 1.89e-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: 95.53  E-value: 1.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 777 EYKPPKRPfVKLKDCIELFTTKEKLGAEDPWYCPNCkehQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD-KLDTLVDFP 855
Cdd:cd02667 103 RSDEIKSE-CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 856 iSDLDMSEFLiNPNAGPC------RYNLIAVSNHYGGMGGGHYTAFAK---------------------NKDDGKWYYFD 908
Cdd:cd02667 179 -EILDLAPFC-DPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeaGPGSGQWYYIS 256
                       170       180
                ....*....|....*....|...
gi 21489969 909 DSSVSTASEDQIVSKAAYVLFYQ 931
Cdd:cd02667 257 DSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-477 2.48e-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: 92.06  E-value: 2.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNdkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvTPRAFKTQVGRF 369
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------------------------------------TPKELFSQVCRK 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 370 APQFSGYQQQDCQELLAFLLDGLhedlnrirkKPYIqlkdadgrpdkvvaeeawenhlkrnDSiivdIFHGLFKSTLVCP 449
Cdd:cd02667  43 APQFKGYQQQDSHELLRYLLDGL---------RTFI-------------------------DS----IFGGELTSTIMCE 84
                       170       180       190
                ....*....|....*....|....*....|
gi 21489969 450 ECAKISVTFDPFCYLTLPL--PMKKERSLE 477
Cdd:cd02667  85 SCGTVSLVYEPFLDLSLPRsdEIKSECSIE 114
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
290-479 7.27e-20

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: 90.24  E-value: 7.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNtpplteyflndkyqeelnfdnplgmrgeiaksyaelikqmwsgkfsyvtprafktqvgrf 369
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 370 apqfsgyQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdadgrpdkvvaeeawENHLKRNDSIIVDIFHGLFKSTLVCP 449
Cdd:cd02257  21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                       170       180       190
                ....*....|....*....|....*....|
gi 21489969 450 ECAKISVTFDPFCYLTLPLPMKKERSLEVY 479
Cdd:cd02257  73 ECGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
781-931 2.93e-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: 80.83  E-value: 2.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 781 PKRPFVKLKDCIELFTTKEKLgaEDpwYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD-KLDTLVDFPisdl 859
Cdd:cd02658 173 LVYEPVPLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP---- 244
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21489969 860 dmsEFLinpnaGPCRYNLIAVSNHY-GGMGGGHYTAFAKNKDD--GKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 931
Cdd:cd02658 245 ---EEL-----GPGKYELIAFISHKgTSVHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
769-931 6.54e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 79.66  E-value: 6.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 769 DFEKHESVEYkppkrpfvklkdCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYS-RYMR-D 846
Cdd:cd02663 142 DVEQNTSITS------------CLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyI 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 847 KLDTLVDFPisdLDMSEFLINPNA-GPCR-YNLIAVSNHY-GGMGGGHYTAFAKNKddGKWYYFDDSSVSTASEDQIV-- 921
Cdd:cd02663 210 KLFYRVVFP---LELRLFNTTDDAeNPDRlYELVAVVVHIgGGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEef 284
                       170
                ....*....|....*.
gi 21489969 922 ------SKAAYVLFYQ 931
Cdd:cd02663 285 fgdspnQATAYVLFYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
826-930 2.43e-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: 2.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 826 SLPPVLVVHLKRFSYSRYMRDKLDTL--VDFPIsDLDMSEFLinpnAGPCRYNLIAVSNHYGGMGGG-HYTAFAKNKDDG 902
Cdd:cd02657 195 RLPKYLTVQFVRFFWKRDIQKKAKILrkVKFPF-ELDLYELC----TPSGYYELVAVITHQGRSADSgHYVAWVRRKNDG 269
                        90       100       110
                ....*....|....*....|....*....|....*
gi 21489969 903 KWYYFDDSSVSTASEDQIVSKA-------AYVLFY 930
Cdd:cd02657 270 KWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-470 5.54e-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: 73.90  E-value: 5.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNP-LGMRGEIAKsyaeLIKQMWSGKFSY------------ 356
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPaNDLNCQLIK----LADGLLSGRYSKpaslksendpyq 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 357 --VTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDglhedlnRIRKKPYIQLKDADGRPDKVVAEEawenhlkrndsii 434
Cdd:cd02658  77 vgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLNPNDLFKFMIED------------- 136
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21489969 435 vdifhglfksTLVCPECAKISVTFDPFCYLTLPLPM 470
Cdd:cd02658 137 ----------RLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-403 1.19e-13

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: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLteyflndkyQEELNFDNPLGMRGE-----IAKSYAELIKQMwSGKFSYVTPRAFKT 364
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPEL---------RDALKNYNPARRGANqssdnLTNALRDLFDTM-DKKQEPVPPIEFLQ 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21489969 365 QVGRFAPQFS------GYQQQDCQELLAFLLDGLHEDLNRIRKKP 403
Cdd:cd02657  71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG 115
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
286-505 1.62e-12

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: 70.81  E-value: 1.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 286 PGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFL-NDKYQEELNFDNPLGmrgeiaKSYAELIKQMWSgkfsyvtPRAFKT 364
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDRKSELV------KRLSELIRKIWN-------PRNFKG 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 365 QVG----------RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdadgrpdkvvaeeawenhlkrNDSII 434
Cdd:cd02669 184 HVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSII 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 435 VDIFHGLFK---------------STLVCPECAKISVTFDPFCYLTLPLPMKkerslevylvrmdPLAKPMQYKVIVPKI 499
Cdd:cd02669 237 HDCFQGKVQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLLLTLDLPPP-------------PLFKDGNEENIIPQV 303

                ....*.
gi 21489969 500 gNILDL 505
Cdd:cd02669 304 -PLKQL 308
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
780-931 4.14e-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: 66.19  E-value: 4.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 780 PPKRPF--VKLKDCIELFTTKEKLGAEDPwycPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPIS 857
Cdd:cd02669 286 PPPPLFkdGNEENIIPQVPLKQLLKKYDG---KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIK 362
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21489969 858 DLDMSEFLINPNAGPCR---YNLIA-VSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQ 931
Cdd:cd02669 363 NLDLSDYVHFDKPSLNLstkYNLVAnIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
785-931 1.26e-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: 64.05  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 785 FVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSR--YMRDKL------DTLVDFPI 856
Cdd:cd02664 133 FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPV 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 857 SD-LDMSEFLINPNAGPCR-----------YNLIAV---------SNHY-----------GGMGGGHYTAFAKNKDDGK- 903
Cdd:cd02664 213 RVeSKSSESPLEKKEEESGddgelvtrqvhYRLYAVvvhsgysseSGHYftyardqtdadSTGQECPEPKDAEENDESKn 292
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21489969 904 WYYFDDSSVS--TASEDQIV-----SKAAYVLFYQ 931
Cdd:cd02664 293 WYLFNDSRVTfsSFESVQNVtsrfpKDTPYILFYE 327
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
788-931 1.41e-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: 62.38  E-value: 1.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 788 LKDCIELFTTKEKLgaEDPwYCPNCkehQQATKKLdlwslPPVLVVHLKRFSYS-RYMRDKLDTLVDFPisdldmsEFLi 866
Cdd:cd02662  98 LEHCLDDFLSTEII--DDY-KCDRC---QTVIVRL-----PQILCIHLSRSVFDgRGTSTKNSCKVSFP-------ERL- 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 867 npnaGPCRYNLIAVSNHYGGMGGGHYTAF--------------------AKNKDDGKWYYFDDSSVSTASEDQIV-SKAA 925
Cdd:cd02662 159 ----PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSA 234

                ....*.
gi 21489969 926 YVLFYQ 931
Cdd:cd02662 235 YMLFYE 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
809-920 1.97e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 64.89  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969  809 CPNCKEH--QQATKKLDLWSLPPVLVVHLKRFSYS--RYMRDKLDTLVDFPISdLDMSEFLiNPNA-----GPCRYNLIA 879
Cdd:COG5077  358 RYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLE-IDLLPFL-DRDAdksenSDAVYVLYG 435
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 21489969  880 VSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQI 920
Cdd:COG5077  436 VLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
768-930 2.12e-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: 63.37  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 768 EDFEKHESVEYKP-PKRPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRD 846
Cdd:cd02671 161 ELSKSEESSEISPdPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFD 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 847 ------KLDTLVDFPIsDLDMSEFLINPNAGpcRYNLIAVSNHY-GGMGGGHYTAFAknkddgKWYYFDDSSVSTASEDQ 919
Cdd:cd02671 241 cygglsKVNTPLLTPL-KLSLEEWSTKPKND--VYRLFAVVMHSgATISSGHYTAYV------RWLLFDDSEVKVTEEKD 311
                       170       180
                ....*....|....*....|
gi 21489969 920 IV---------SKAAYVLFY 930
Cdd:cd02671 312 FLealspntssTSTPYLLFY 331
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-469 1.38e-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: 60.58  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSntppLTEYFLNDKYQEelnfdNPLGMRGEIAKSYAELIKQMW---SGKFSYVTPRAFKTQV 366
Cdd:cd02664   1 GLINLGNTCYMNSVLQALF----MAKDFRRQVLSL-----NLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 367 grFAPQFSGYQQQDCQELLAFLLDGLHedlnrirkkpyiqlkdadgrpdkvvaeeawenhlkrndSIIVDIFHGLFKSTL 446
Cdd:cd02664  72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                       170       180
                ....*....|....*....|...
gi 21489969 447 VCPECAKISVTFDPFCYLTLPLP 469
Cdd:cd02664 112 RCLNCNSTSARTERFRDLDLSFP 134
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
290-403 2.12e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 59.82  E-value: 2.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLS-NTPPLTEYFLNDKYQ-----EELNFDNPLGMRGEIAKsyaeLIKQMWSGKfsyvtprafK 363
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPDLNQEEALK----LFTALWSSK---------E 67
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 21489969 364 TQVGRFAPQfsgYQQQDCQELLAFLLDGLHEDL---NRIRKKP 403
Cdd:COG5533  68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDLvnsFTIRIFK 107
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
287-477 3.14e-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: 53.42  E-value: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 287 GLCGLSNLGNTCFMNSAIQCLSNTPplteYFLNDKYQEELNFDNPlgmrGEIAKSYAeLIKQMwsgKFSYVTPRAFKTQV 366
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD----DNKSVPLA-LQRLF---LFLQLSESPVKTTE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 367 GRFAPQFSG------YQQQDCQELLAFLLDglhedlnrirkkpyiqlkdadgrpdkvvaeeAWENHLKRN--DSIIVDIF 438
Cdd:cd02659  69 LTDKTRSFGwdslntFEQHDVQEFFRVLFD-------------------------------KLEEKLKGTgqEGLIKNLF 117
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21489969 439 HGLFKSTLVCPECAKISVTFDPFcyLTLPLPMKKERSLE 477
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYF--LDLQVAVKGKKNLE 154
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
279-394 3.21e-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: 53.36  E-value: 3.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 279 PGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPplteyflndKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVT 358
Cdd:cd02671  15 CEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQA 85
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21489969 359 PRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHE 394
Cdd:cd02671  86 PRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-469 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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 53.08  E-value: 3.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLsntpplteYFLNdkyqeelnfdnplgmrgeIAKSYAELIKQMWSGKFSY--VTPRAFKTQVG 367
Cdd:cd02663   1 GLENFGNTCYCNSVLQAL--------YFEN------------------LLTCLKDLFESISEQKKRTgvISPKKFITRLK 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 368 RFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKpyiqlkdaDGRPDKVVAEEAWENHlkrnDSIIVDIFHGLFKSTLV 447
Cdd:cd02663  55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKA--------EKANRKLNNNNNAEPQ----PTWVHEIFQGILTNETR 122
                       170       180
                ....*....|....*....|..
gi 21489969 448 CPECAKISVTFDPFCYLTLPLP 469
Cdd:cd02663 123 CLTCETVSSRDETFLDLSIDVE 144
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-477 1.53e-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: 51.27  E-value: 1.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLN-----DKYQEELNFDNPLGMRGeIAKSYAELIKQMWSGKFSYVTPRAFKT 364
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 365 QVGrfapqFSGYQQQDCQELLAFLLDGLHEDLNrirkkpyiQLKDADGRpdkvvaeeawenhlkrndSIIVDIFHGLFKS 444
Cdd:cd02668  80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLS--------KSKNPDLK------------------NIVQDLFRGEYSY 128
                       170       180       190
                ....*....|....*....|....*....|...
gi 21489969 445 TLVCPECAKISVTFDPFcyLTLPLPMKKERSLE 477
Cdd:cd02668 129 VTQCSKCGRESSLPSKF--YELELQLKGHKTLE 159
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-316 1.14e-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: 47.75  E-value: 1.14e-05
                        10        20
                ....*....|....*....|....*..
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLTEY 316
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
460-597 1.29e-05

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: 47.09  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   460 PFCYLTLPLPMK---KERSLEVYLVrMDPLAKPMQYKVIVPKIGNILDLCTALSALSGVP---ADKMIVTDIYNHRFHRI 533
Cdd:pfam14533   1 ALYYEVLDISLSeleNKKSIKVTWL-SPGLKKEEELELLVPKNGTVADLLEELQKKVKLSeegSGKIRLYEVSNHKIYKE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21489969   534 FAVDENLSSIMERDDIYVFEI---NINrAEDTEHvVIPVClrekfrHssYtHHTGSSLFGQPFLMAI 597
Cdd:pfam14533  80 LSEDEPIDSLNDYLTLYAEEIpeeELN-LDEGER-LIPVF------H--F-QKEPSRTHGIPFLFVL 135
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
809-930 1.77e-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: 44.44  E-value: 1.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 809 CPNCKeHQQATKKLDLWSLPPVLVVHLKRFsYSRYMRDKldtlvdfpisDLDMSEFLINPNAG-PCRYNLIAVSNHY-GG 886
Cdd:cd02673 129 CSSCK-CESAISSERIMTFPECLSINLKRY-KLRIATSD----------YLKKNEEIMKKYCGtDAKYSLVAVICHLgES 196
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 21489969 887 MGGGHYTAFAKNKDDG-KWYYFDDSSVSTASEDQI---VSKAAYVLFY 930
Cdd:cd02673 197 PYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
290-447 1.08e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 42.48  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 290 GLSNLGNTCFMNSAIQCLSNTPPLTEYFLN-DKYQEELNFDNPLGMR-GEIAKSYAE-------------LIKQMWSGKF 354
Cdd:cd02666   3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfDESKAELASDYPTERRiGGREVSRSElqrsnqfvyelrsLFNDLIHSNT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 355 SYVTPRAfktqvgRFApqFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDAD------------GRPDKVVAEEA 422
Cdd:cd02666  83 RSVTPSK------ELA--YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDkeqsdlikrlfsGKTKQQLVPES 154
                       170       180
                ....*....|....*....|....*
gi 21489969 423 WenhlkrNDSIIVDIFHGLFKSTLV 447
Cdd:cd02666 155 M------GNQPSVRTKTERFLSLLV 173
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
791-931 3.15e-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: 40.57  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 791 CIELFTTKEKlgaEDPWYCPNCKEHQQATKKLDLWSLPP----VLVVHLKRFSYSRYMR-------DKLDTLVDFPISDL 859
Cdd:cd02672 122 LLKRSLDLEK---VTKAWCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTNGEFDDInvvlpsgKVMQNKVSPKAIDH 198
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21489969 860 DmSEFLINPNAGPCRYNLIA-VSNHYGGMGGGHYTAF----AKNKDDGKWYYFDDSSVSTasedqiVSKAAYVLFYQ 931
Cdd:cd02672 199 D-KLVKNRGQESIYKYELVGyVCEINDSSRGQHNVVFvikvNEESTHGRWYLFNDFLVTP------VSELAYILLYQ 268
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
809-912 4.93e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 40.33  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969   809 CPNCKEHQQATKKLDLWSLPPVLVVHLKRfsYSRYMRDKLDTLVDFPIS-DLDMSEFLINPNAGpCRYNLIA-VSNHYGG 886
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAAL--TNEEWRQLWKTPGWLPPEiGLTLSDDLQGDNEI-VKYELRGvVVHIGDS 272
                          90       100       110
                  ....*....|....*....|....*....|...
gi 21489969   887 MGGGHYTAFAK-------NKDDGKWYYFDDSSV 912
Cdd:pfam13423 273 GTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
827-930 8.07e-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: 8.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21489969 827 LPPVLVVHLKRFSYSRYMRDKLDTLVDFPisdldmSEFLINPnagpcrYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYY 906
Cdd:cd02665 128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------QIIQQVP------YELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195
                        90       100       110
                ....*....|....*....|....*....|..
gi 21489969 907 FDDSSVSTASEDQIVSKA--------AYVLFY 930
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.
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