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Conserved domains on  [gi|116242839|sp|Q13107|]
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RecName: Full=Ubiquitin carboxyl-terminal hydrolase 4; AltName: Full=Deubiquitinating enzyme 4; AltName: Full=Ubiquitin thioesterase 4; AltName: Full=Ubiquitin-specific-processing protease 4; AltName: Full=Ubiquitous nuclear protein homolog

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];
35-923 1.47e-141

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: 442.79  E-value: 1.47e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 186 --KYMSNTYEQLSKLDNTVQDAGLyqGQVLVIEPQNEDGTWPRQTLQSKSSTAPSrnfttspkssaspyssvsaslianG 263
Cdd:COG5560  193 vpEIMGLRLGLDSFFRRYRVLASD--GRVLHPLTRLELFEDRSVLLLSKITRNPD------------------------W 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 264 DSTSTCGMHSSgvsrggsgfsasyncqeppSSHIQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDN 343
Cdd:COG5560  247 LVDSIVDDHNR-------------------SINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 344 PLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDA 423
Cdd:COG5560  308 PLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 424 NGRPDAVV---AKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPhc 500
Cdd:COG5560  388 SPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESG-- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 501 RPTQYRVTVPLMGAVSDLCEALSRLSGI-AAENMVVADVYNHRFHKIF--QMDEGLNHIMPRDDIFVYEvcsTSVDGsec 577
Cdd:COG5560  466 RRQPLKIELDASSTIRGLKKLVDAEYGKlGCFEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYE---TNDNG--- 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 578 VTLPVYfrerksrpssTSSASALYGQPLLLSVPKHKLTLeslyqavcdRISRYVKQPLPDEFgssplepgacngsrnsce 657
Cdd:COG5560  540 IEVPVV----------HLRIEKGYKSKRLFGDPFLQLNV---------LIKASIYDKLVKEF------------------ 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 658 gedeeemehqeegkEQLSETEGSGEDEPGNDPSETTQKKIKGQPCpkrlFTFSLVNSYGTADINSLAADGkLLKLNSRST 737
Cdd:COG5560  583 --------------EELLVLVEMKKTDVDLVSEQVRLLREESSPS----SWLKLETEIDTKREEQVEEEG-QMNFNDAVV 643
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 738 LAMDWdSETRRLYYDEQESEAYEKHVSMLQPqkkkktTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSL 817
Cdd:COG5560  644 ISCEW-EEKRYLSLFSYDPLWTIREIGAAER------TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRL 716
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 818 PKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYF 897
Cdd:COG5560  717 PMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLF 796
                        890       900
                 ....*....|....*....|....*.
gi 116242839 898 DDSNVSLASEDQIVTKAAYVLFYQRR 923
Cdd:COG5560  797 DDSRITEVDPEDSVTSSAYVLFYRRK 822
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-923 1.47e-141

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 442.79  E-value: 1.47e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 186 --KYMSNTYEQLSKLDNTVQDAGLyqGQVLVIEPQNEDGTWPRQTLQSKSSTAPSrnfttspkssaspyssvsaslianG 263
Cdd:COG5560  193 vpEIMGLRLGLDSFFRRYRVLASD--GRVLHPLTRLELFEDRSVLLLSKITRNPD------------------------W 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 264 DSTSTCGMHSSgvsrggsgfsasyncqeppSSHIQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDN 343
Cdd:COG5560  247 LVDSIVDDHNR-------------------SINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 344 PLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDA 423
Cdd:COG5560  308 PLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 424 NGRPDAVV---AKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPhc 500
Cdd:COG5560  388 SPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESG-- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 501 RPTQYRVTVPLMGAVSDLCEALSRLSGI-AAENMVVADVYNHRFHKIF--QMDEGLNHIMPRDDIFVYEvcsTSVDGsec 577
Cdd:COG5560  466 RRQPLKIELDASSTIRGLKKLVDAEYGKlGCFEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYE---TNDNG--- 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 578 VTLPVYfrerksrpssTSSASALYGQPLLLSVPKHKLTLeslyqavcdRISRYVKQPLPDEFgssplepgacngsrnsce 657
Cdd:COG5560  540 IEVPVV----------HLRIEKGYKSKRLFGDPFLQLNV---------LIKASIYDKLVKEF------------------ 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 658 gedeeemehqeegkEQLSETEGSGEDEPGNDPSETTQKKIKGQPCpkrlFTFSLVNSYGTADINSLAADGkLLKLNSRST 737
Cdd:COG5560  583 --------------EELLVLVEMKKTDVDLVSEQVRLLREESSPS----SWLKLETEIDTKREEQVEEEG-QMNFNDAVV 643
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 738 LAMDWdSETRRLYYDEQESEAYEKHVSMLQPqkkkktTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSL 817
Cdd:COG5560  644 ISCEW-EEKRYLSLFSYDPLWTIREIGAAER------TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRL 716
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 818 PKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYF 897
Cdd:COG5560  717 PMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLF 796
                        890       900
                 ....*....|....*....|....*.
gi 116242839 898 DDSNVSLASEDQIVTKAAYVLFYQRR 923
Cdd:COG5560  797 DDSRITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-921 2.41e-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: 205.60  E-value: 2.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 776 VALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFV 855
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116242839 856 CNLSAR-PYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 921
Cdd:cd02674  164 DTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
753-920 3.39e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.42  E-value: 3.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  753 EQESEAYEKHVS---MLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFS 829
Cdd:pfam00443 136 GEVSETFEPFSDlslPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  830 YNRYWRDKLDTVVEFPIRgLNMSEFVCN----LSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLA 905
Cdd:pfam00443 216 YNRSTWEKLNTEVEFPLE-LDLSRYLAEelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEV 294
                         170
                  ....*....|....*.
gi 116242839  906 SED-QIVTKAAYVLFY 920
Cdd:pfam00443 295 DEEtAVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 5.28e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 119.39  E-value: 5.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 116242839   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-923 1.47e-141

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 442.79  E-value: 1.47e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 186 --KYMSNTYEQLSKLDNTVQDAGLyqGQVLVIEPQNEDGTWPRQTLQSKSSTAPSrnfttspkssaspyssvsaslianG 263
Cdd:COG5560  193 vpEIMGLRLGLDSFFRRYRVLASD--GRVLHPLTRLELFEDRSVLLLSKITRNPD------------------------W 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 264 DSTSTCGMHSSgvsrggsgfsasyncqeppSSHIQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDN 343
Cdd:COG5560  247 LVDSIVDDHNR-------------------SINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 344 PLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDA 423
Cdd:COG5560  308 PLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 424 NGRPDAVV---AKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPhc 500
Cdd:COG5560  388 SPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESG-- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 501 RPTQYRVTVPLMGAVSDLCEALSRLSGI-AAENMVVADVYNHRFHKIF--QMDEGLNHIMPRDDIFVYEvcsTSVDGsec 577
Cdd:COG5560  466 RRQPLKIELDASSTIRGLKKLVDAEYGKlGCFEIKVMCIYYGGNYNMLepADKVLLQDIPQTDFVYLYE---TNDNG--- 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 578 VTLPVYfrerksrpssTSSASALYGQPLLLSVPKHKLTLeslyqavcdRISRYVKQPLPDEFgssplepgacngsrnsce 657
Cdd:COG5560  540 IEVPVV----------HLRIEKGYKSKRLFGDPFLQLNV---------LIKASIYDKLVKEF------------------ 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 658 gedeeemehqeegkEQLSETEGSGEDEPGNDPSETTQKKIKGQPCpkrlFTFSLVNSYGTADINSLAADGkLLKLNSRST 737
Cdd:COG5560  583 --------------EELLVLVEMKKTDVDLVSEQVRLLREESSPS----SWLKLETEIDTKREEQVEEEG-QMNFNDAVV 643
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 738 LAMDWdSETRRLYYDEQESEAYEKHVSMLQPqkkkktTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSL 817
Cdd:COG5560  644 ISCEW-EEKRYLSLFSYDPLWTIREIGAAER------TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRL 716
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 818 PKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYF 897
Cdd:COG5560  717 PMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLF 796
                        890       900
                 ....*....|....*....|....*.
gi 116242839 898 DDSNVSLASEDQIVTKAAYVLFYQRR 923
Cdd:COG5560  797 DDSRITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-921 2.41e-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: 205.60  E-value: 2.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 776 VALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFV 855
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116242839 856 CNLSAR-PYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 921
Cdd:cd02674  164 DTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
753-920 3.39e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.42  E-value: 3.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  753 EQESEAYEKHVS---MLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFS 829
Cdd:pfam00443 136 GEVSETFEPFSDlslPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  830 YNRYWRDKLDTVVEFPIRgLNMSEFVCN----LSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLA 905
Cdd:pfam00443 216 YNRSTWEKLNTEVEFPLE-LDLSRYLAEelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEV 294
                         170
                  ....*....|....*.
gi 116242839  906 SED-QIVTKAAYVLFY 920
Cdd:pfam00443 295 DEEtAVLSSSAYILFY 310
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
302-485 3.93e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 185.34  E-value: 3.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  302 CGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPlgmKGEIAEAYAELIKQMWSG-RDAHVAPRMFKTQVG 380
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  381 RFAPQFSGYQQQDSQELLAFLLDGLHEDLNRvkkkpylelkdangrpdavvakeaweNHRLRNDSVIVDTFHGLFKSTLV 460
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180
                  ....*....|....*....|....*
gi 116242839  461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDS 156
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
766-921 1.85e-40

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: 149.94  E-value: 1.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 766 LQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCpNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWR-DKLDTVVEF 844
Cdd:cd02257   89 LPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSF 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 845 PIRgLNMSEFV------CNLSARPYVYDLIAVSNHYG-AMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIV-----T 912
Cdd:cd02257  168 PLE-LDLSPYLsegekdSDSDNGSYKYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgslS 246

                 ....*....
gi 116242839 913 KAAYVLFYQ 921
Cdd:cd02257  247 SSAYILFYE 255
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
139-226 1.65e-36

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: 132.29  E-value: 1.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 116242839  219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 5.28e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 119.39  E-value: 5.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 116242839   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
773-920 4.73e-31

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: 124.79  E-value: 4.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 773 KTTVALRDCIELFTTMETLGEhDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRD-KLDTVVEFPIRgLNM 851
Cdd:cd02660  173 SGTPTLSDCLDRFTRPEKLGD-FAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNM 250
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116242839 852 SEFVC---------NLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKlNGKWYYFDDSNVSLASEDQIVTKAAYVLFY 920
Cdd:cd02660  251 TPYTSssigdtqdsNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-920 5.52e-31

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: 123.93  E-value: 5.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 778 LRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYwrDKLDTVVEFPIRgLNMSEFVCN 857
Cdd:cd02661  164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFPET-LDLSPYMSQ 240
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116242839 858 LSARPYVYDLIAVSNHYGA-MGVGHYTAYAKNkLNGKWYYFDDSNVSLASEDQIVTKAAYVLFY 920
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
31-123 1.20e-26

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: 103.99  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839   31 GAQWYLIDSRWFKQWKKYVGfdswdmynvgEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGc 110
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG- 69
                          90
                  ....*....|...
gi 116242839  111 veGQQPIVRKVVE 123
Cdd:pfam06337  70 --GGPEIKRNVVN 80
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
302-486 7.52e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 103.12  E-value: 7.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 302 CGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKgeIAEAYAELIkqMWSGRDAhVAPRMFKTQVGR 381
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC--ALEAHVERA--LASSGPG-SAPRIFSSNLKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 382 FAPQFSGYQQQDSQELLAFLLDGLHedlnrvkkKPYLELKdangrpdavvAKEAWENHRLRNDSVIVDTFHGLFKSTLVC 461
Cdd:cd02661   77 ISKHFRIGRQEDAHEFLRYLLDAMQ--------KACLDRF----------KKLKAVDPSSQETTLVQQIFGGYLRSQVKC 138
                        170       180
                 ....*....|....*....|....*
gi 116242839 462 PECAKVSVTFDPFcyLTLPLPLKKD 486
Cdd:cd02661  139 LNCKHVSNTYDPF--LDLSLDIKGA 161
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
775-925 4.89e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 101.57  E-value: 4.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 775 TVALRDCIEL------FTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYN--RYWRDKLDTVVEFPI 846
Cdd:cd02659  144 QVAVKGKKNLeesldaYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPL 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 847 RgLNMSEFV-----------CNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIV---- 911
Cdd:cd02659  224 E-LDMEPYTekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEeecf 302
                        170       180       190
                 ....*....|....*....|....*....|..
gi 116242839 912 ------------------TKAAYVLFYQRRDD 925
Cdd:cd02659  303 ggeetqktydsgprafkrTTNAYMLFYERKSP 334
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-491 5.49e-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: 95.82  E-value: 5.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNtapltdyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdahvaprmfktqvgrf 382
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 383 apqfsgyQQQDSQELLAFLLDGLHedlnrvkkkpylelkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTLVCP 462
Cdd:cd02674   21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                        170       180
                 ....*....|....*....|....*....
gi 116242839 463 ECAKVSVTFDPFCYLTLPLPLKKDRVMEV 491
Cdd:cd02674   56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKV 84
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-485 1.36e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 97.06  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKG-EIAEAYAELikqMWSGRDAHVAPRMFKTQVGR 381
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLScAMDEIFQEF---YYSGDRSPYGPINLLYLSWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 382 FAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKkPYLELKDANgrpdavvakeawenhrlrndsVIVD-TFHGLFKSTLV 460
Cdd:cd02660   79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN-EANDESHCN---------------------CIIHqTFSGSLQSSVT 136
                        170       180
                 ....*....|....*....|....*
gi 116242839 461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:cd02660  137 CQRCGGVSTTVDPFLDLSLDIPNKS 161
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
756-921 2.74e-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: 95.15  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 756 SEAYEKHVSMLQPQKKK-KTTVALRDCIELFTTMETLGEHDPWYCPNCKKhqqATKKFDLWSLPKILVVHLKRFSYNRYW 834
Cdd:cd02667   90 SLVYEPFLDLSLPRSDEiKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSA 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 835 RD-KLDTVVEFPIRgLNMSEFV---CNLSA--RPYVYDLIAVSNHYGAMGVGHYTAYAK--------------------- 887
Cdd:cd02667  167 NLrKVSRHVSFPEI-LDLAPFCdpkCNSSEdkSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadea 245
                        170       180       190
                 ....*....|....*....|....*....|....
gi 116242839 888 NKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 921
Cdd:cd02667  246 GPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
780-921 3.95e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 95.07  E-value: 3.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 780 DCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYN-RYWR-DKLDTVVEFP--IRGLNMSEFV 855
Cdd:cd02663  151 SCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyIKLFYRVVFPleLRLFNTTDDA 230
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116242839 856 CNLSArpyVYDLIAVSNHYGAMGV-GHYTAYAKNKlnGKWYYFDDSNVSLASEDQIV--------TKAAYVLFYQ 921
Cdd:cd02663  231 ENPDR---LYELVAVVVHIGGGPNhGHYVSIVKSH--GGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-920 1.37e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 94.02  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 778 LRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY--WRDKLDTVVEFPiRGLNMSEFV 855
Cdd:cd02668  158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKtgAKKKLNASISFP-EILDMGEYL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 856 CNLSARPYVYDLIAVSNHYG--AMGvGHYTAYAKNKLNGKWYYFDDSNVS--------------LASEDQ-------IVT 912
Cdd:cd02668  237 AESDEGSYVYELSGVLIHQGvsAYS-GHYIAHIKDEQTGEWYKFNDEDVEempgkplklgnsedPAKPRKseikkgtHSS 315

                 ....*...
gi 116242839 913 KAAYVLFY 920
Cdd:cd02668  316 RTAYMLVY 323
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-482 1.54e-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: 92.83  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNTAPLTDYFLKDeyeaeinrdnplgmkgeiaeayaelikqmwsgrdahvaPRMFKTQVGRF 382
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 383 APQFSGYQQQDSQELLAFLLDGLhedlnrvkkkpylelkdangrpdavvakeawenhRLRNDSVivdtFHGLFKSTLVCP 462
Cdd:cd02667   43 APQFKGYQQQDSHELLRYLLDGL----------------------------------RTFIDSI----FGGELTSTIMCE 84
                        170       180
                 ....*....|....*....|
gi 116242839 463 ECAKVSVTFDPFcyLTLPLP 482
Cdd:cd02667   85 SCGTVSLVYEPF--LDLSLP 102
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
303-486 5.40e-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: 90.62  E-value: 5.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNtapltdyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdahvaprmfktqvgrf 382
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 383 apqfsgyQQQDSQELLAFLLDGLHEDLNRVKKKpylelkdangrpdavvakeawENHRLRNDSVIVDTFHGLFKSTLVCP 462
Cdd:cd02257   21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                        170       180
                 ....*....|....*....|....
gi 116242839 463 ECAKVSVTFDPFCYLTLPLPLKKD 486
Cdd:cd02257   73 ECGHESVSTEPELFLSLPLPVKGL 96
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
731-921 2.69e-17

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: 83.91  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 731 KLNSRSTLAMDWDSETRRLYYDEQESEAYEKhvsmlqpqkkkkttVALRDCIELFTTMETLGEhdpwYCPNCKKHQQATK 810
Cdd:cd02658  147 KYTSELSEILSLPVPKDEATEKEEGELVYEP--------------VPLEDCLKAYFAPETIED----FCSTCKEKTTATK 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 811 KFDLWSLPKILVVHLKRFSYNRYWRD-KLDTVVEFPIRGLnmsefvcnlsarPYVYDLIAVSNHYGA-MGVGHYTAYAKN 888
Cdd:cd02658  209 TTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVPEELG------------PGKYELIAFISHKGTsVHSGHYVAHIKK 276
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 116242839 889 KLN--GKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 921
Cdd:cd02658  277 EIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
765-922 6.06e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 82.16  E-value: 6.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 765 MLQPQKKKKTTVALRDCIELFTTMET---LGEHDPWYCPNCKKHQQATKKfdlwsLPKILVVHLKRFSYNRYWRdKLDTV 841
Cdd:COG5533  129 DQTWVNNLKTLQEFIDNMEELVDDETgvkAKENEELEVQAKQEYEVSFVK-----LPKILTIQLKRFANLGGNQ-KIDTE 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 842 VEFPIrglnmsefvcNLSARP---------YVYDLIAVSNHYGAMGVGHYTAYAKNklNGKWYYFDDSNVSLASEDQIVT 912
Cdd:COG5533  203 VDEKF----------ELPVKHdqilnivkeTYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVTPVSEEEAIN 270
                        170
                 ....*....|...
gi 116242839 913 ---KAAYVLFYQR 922
Cdd:COG5533  271 ekaKNAYLYFYER 283
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
809-920 1.26e-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 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: 81.61  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 809 TKKFDlwSLPKILVVHLKRFsynrYWRDKLDT------VVEFPIRgLNMSEFvCNLSArpyVYDLIAVSNHYGAMG-VGH 881
Cdd:cd02657  190 TSRIS--RLPKYLTVQFVRF----FWKRDIQKkakilrKVKFPFE-LDLYEL-CTPSG---YYELVAVITHQGRSAdSGH 258
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 116242839 882 YTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKA-------AYVLFY 920
Cdd:cd02657  259 YVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
754-920 9.25e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 79.55  E-value: 9.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 754 QESEAYEKHVSMLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY 833
Cdd:cd02671  158 QESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGS 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 834 WRD------KLDTVVEFPirgLNMSEFVCNLSARPYVYDLIAVSNHYGA-MGVGHYTAYAknklngKWYYFDDSNVSLAS 906
Cdd:cd02671  238 EFDcygglsKVNTPLLTP---LKLSLEEWSTKPKNDVYRLFAVVMHSGAtISSGHYTAYV------RWLLFDDSEVKVTE 308
                        170       180
                 ....*....|....*....|...
gi 116242839 907 EDQIV---------TKAAYVLFY 920
Cdd:cd02671  309 EKDFLealspntssTSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
768-921 3.59e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 73.17  E-value: 3.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 768 PQKKKKTTVALRDCIELFTTMETLgehDPWYCPNCkkhQQATKKfdlwsLPKILVVHLKRFSYNRYwrdkldtvVEFPIR 847
Cdd:cd02662   88 PNQSSGSGTTLEHCLDDFLSTEII---DDYKCDRC---QTVIVR-----LPQILCIHLSRSVFDGR--------GTSTKN 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 848 GLNMSefvCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGK--------------------WYYFDDSNVSLASE 907
Cdd:cd02662  149 SCKVS---FPERLPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKEVSE 225
                        170
                 ....*....|....*
gi 116242839 908 DQIV-TKAAYVLFYQ 921
Cdd:cd02662  226 SEVLeQKSAYMLFYE 240
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
810-921 6.91e-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: 75.05  E-value: 6.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 810 KKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVC---NLSARPYVYDLIAVSNHYGAMGV-GHYTAY 885
Cdd:cd02669  325 KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHfdkPSLNLSTKYNLVANIVHEGTPQEdGTWRVQ 404
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 116242839 886 AKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQ 921
Cdd:cd02669  405 LRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-483 1.25e-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 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: 72.74  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPL------------GMKGEiAEAYAELIKQMWSGRDAHV 370
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladGLLSG-RYSKPASLKSENDPYQVGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 371 APRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDglhedlnrvkkkpylelkdangrpdaVVAKEAWENHrlrnDSVIVDT 450
Cdd:cd02658   80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLID--------------------------KLDRESFKNL----GLNPNDL 129
                        170       180       190
                 ....*....|....*....|....*....|...
gi 116242839 451 FHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPL 483
Cdd:cd02658  130 FKFMIEDRLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
299-484 3.77e-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 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: 72.74  E-value: 3.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 299 PGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFL-KDEYEAEINRdnplgmKGEIAEAYAELIKQMWSGRD--AHVAPRMF 375
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDR------KSELVKRLSELIRKIWNPRNfkGHVSPHEL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 376 KTQVG-RFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKpylelkdangrpdavvakeawenhrlrNDSVIVDTFHGL 454
Cdd:cd02669  191 LQAVSkVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSIIHDCFQGK 243
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 116242839 455 FK---------------STLVCPECAKVSVTFDPFCYLTLPLPLK 484
Cdd:cd02669  244 VQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLLLTLDLPPP 288
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
778-910 1.14e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 72.21  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  778 LRDCIELFTTMETL-GEHdpwyCPNCKKH--QQATKKFDLWSLPKILVVHLKRFSYNrYWRD---KLDTVVEFPIRgLNM 851
Cdd:COG5077   340 LQESFRRYIQVETLdGDN----RYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDL 413
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116242839  852 SEFVCNLSAR----PYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQI 910
Cdd:COG5077   414 LPFLDRDADKsensDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-921 5.27e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 68.29  E-value: 5.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 778 LRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNR--YWRDKL------DTVVEFPIR-G 848
Cdd:cd02664  136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPVRvE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 849 LNMSEFVCN-----------LSARPYVYDLIAVSNHYG-AMGVGHYTAYAKN--------------------KLNGKWYY 896
Cdd:cd02664  216 SKSSESPLEkkeeesgddgeLVTRQVHYRLYAVVVHSGySSESGHYFTYARDqtdadstgqecpepkdaeenDESKNWYL 295
                        170       180       190
                 ....*....|....*....|....*....|..
gi 116242839 897 FDDSNVSLAS--EDQIVTK-----AAYVLFYQ 921
Cdd:cd02664  296 FNDSRVTFSSfeSVQNVTSrfpkdTPYILFYE 327
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-481 9.01e-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 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: 66.97  E-value: 9.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLsNTAP-----LTDYFLKDEYEAEINRDnplgmkgeIAEAYAELIKQMWSGRDAhVAPRMFKT 377
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDN--------LTNALRDLFDTMDKKQEP-VPPIEFLQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 378 QVGRFAPQFS------GYQQQDSQELLAFLLDGLHEDLNRVKKKPylelkdangrpdavvakeawenhrlrndSVIVDTF 451
Cdd:cd02657   71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG----------------------------SFIDQLF 122
                        170       180       190
                 ....*....|....*....|....*....|.
gi 116242839 452 HGLFKSTLVCPEC-AKVSVTFDPFCYLTLPL 481
Cdd:cd02657  123 GIELETKMKCTESpDEEEVSTESEYKLQCHI 153
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
303-409 2.96e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 62.13  E-value: 2.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLS-NTAPLTDYFLKDEYE-----AEINRDNPLgMKGEIAEAyaeLIKQMWSGRdahvaprmfK 376
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPD-LNQEEALK---LFTALWSSK---------E 67
                         90       100       110
                 ....*....|....*....|....*....|...
gi 116242839 377 TQVGRFAPQfsgYQQQDSQELLAFLLDGLHEDL 409
Cdd:COG5533   68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDL 97
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-495 8.50e-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: 61.35  E-value: 8.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLsntapltdyFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMW---SGRDAHVAPRMFKTQV 379
Cdd:cd02664    1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 380 grFAPQFSGYQQQDSQELLAFLLDGLHedlnrvkkkpylelkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTL 459
Cdd:cd02664   72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 116242839 460 VCPECAKVSVTFDPFCYLTLPLPLKKDrVMEVFLVP 495
Cdd:cd02664  112 RCLNCNSTSARTERFRDLDLSFPSVQD-LLNYFLSP 146
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-482 1.02e-08

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: 57.70  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNTAPLTDyfLKDEYEAEINRDNPLGMkgeiaeayaelikqmwsgrdahVAPRMFKTQVGRF 382
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLLTC--LKDLFESISEQKKRTGV----------------------ISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 383 APQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKpylelkdangrpDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCP 462
Cdd:cd02663   57 NELFDNYMHQDAHEFLNFLLNEIAEILDAERKA------------EKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCL 124
                        170       180
                 ....*....|....*....|
gi 116242839 463 ECAKVSVTFDPFCYLTLPLP 482
Cdd:cd02663  125 TCETVSSRDETFLDLSIDVE 144
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
799-920 3.57e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 52.53  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 799 CPNCKkHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTvvefpirglNMSEFVCnLSARPYVYDLIAVSNHYG-AM 877
Cdd:cd02673  129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSDYLKK---------NEEIMKK-YCGTDAKYSLVAVICHLGeSP 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 116242839 878 GVGHYTAYAKNKLNG-KWYYFDDSNVSLASEDQIVTKA---AYVLFY 920
Cdd:cd02673  198 YDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDVSTNArssGYLIFY 244
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
299-407 4.80e-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: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 299 PGLCGLGNLGNTCFMNSALQCLsntapltdYFLKDeYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQ 378
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVL--------YFCPG-FKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAPRRLLNA 92
                         90       100
                 ....*....|....*....|....*....
gi 116242839 379 VGRFAPQFSGYQQQDSQELLAFLLDGLHE 407
Cdd:cd02671   93 LREVNPMYEGYLQHDAQEVLQCILGNIQE 121
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
300-484 2.75e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 47.25  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 300 GLCGLGNLGNTCFMNSALQCLSNTApltdYFLKDEYEAEINRDNPlGMKGEIaeayAELIKQMWSgrdAHVAPRMFKTQV 379
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD-DNKSVP----LALQRLFLF---LQLSESPVKTTE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 380 GRFAPQFSG------YQQQDSQELLAFLLDGLHEDLnrvkkkPYLELKDAngrpdavvakeawenhrlrndsvIVDTFHG 453
Cdd:cd02659   69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKLEEKL------KGTGQEGL-----------------------IKNLFGG 119
                        170       180       190
                 ....*....|....*....|....*....|.
gi 116242839 454 LFKSTLVCPECAKVSVTFDPFcyLTLPLPLK 484
Cdd:cd02659  120 KLVNYIICKECPHESEREEYF--LDLQVAVK 148
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
817-920 5.10e-05

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 45.63  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 817 LPKILVVHLKRFSYNRYWRDKLDTVVEFP--IRGLNmsefvcnlsarpyvYDLIAVSNHYGAMGVGHYTAYAKNKLNGKW 894
Cdd:cd02665  128 LPPVLTFELSRFEFNQGRPEKIHDKLEFPqiIQQVP--------------YELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
                         90       100       110
                 ....*....|....*....|....*....|....
gi 116242839 895 YYFDDSNVSLASEDQIVTKA--------AYVLFY 920
Cdd:cd02665  194 EKYNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-484 1.27e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 45.10  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQCLSNTAPLTDYFLK-----DEYEAEINRDNPLGMKGeIAEAYAELIKQMWSGRDAHVAPRMFKT 377
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 378 QVGrfapqFSGYQQQDSQELLAFLLDGLHEDLNRVKKkpylelkdangrPDAVvakeawenhrlrndSVIVDTFHGLFKS 457
Cdd:cd02668   80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKN------------PDLK--------------NIVQDLFRGEYSY 128
                        170       180
                 ....*....|....*....|....*..
gi 116242839 458 TLVCPECAKVSVTFDPFcyLTLPLPLK 484
Cdd:cd02668  129 VTQCSKCGRESSLPSKF--YELELQLK 153
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-485 1.59e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 44.28  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 303 GLGNLGNTCFMNSALQclsntapltdyflkdeyeaeinrdnplgmkgeiaeAYAELikqmwsgrdahvaprmfktqvgrf 382
Cdd:cd02662    1 GLVNLGNTCFMNSVLQ-----------------------------------ALASL------------------------ 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 383 aPQFSGY-----QQQDSQELLAFLLDGLHEDLnrvkKKPylelkdangrpdavvakeawenhrlrndsvivdtFHGLFKS 457
Cdd:cd02662   22 -PSLIEYleeflEQQDAHELFQVLLETLEQLL----KFP----------------------------------FDGLLAS 62
                        170       180
                 ....*....|....*....|....*....
gi 116242839 458 TLVCPECAKVS-VTFDPFCYLTLPLPLKK 485
Cdd:cd02662   63 RIVCLQCGESSkVRYESFTMLSLPVPNQS 91
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
763-902 3.47e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 43.80  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  763 VSMLQPQKKKKTTVA--LRDCIELFTTmetlgeHDPWyCPNCKKHQQATKKFDLWSLPKILVVHLKRfsYNRYWRDKLDT 840
Cdd:pfam13423 165 KPSSNNKKPPNQTFSsiLKSSLERETT------TKAW-CEKCKRYQPLESRRTVRNLPPVLSLNAAL--TNEEWRQLWKT 235
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116242839  841 VVEFPIR-GLNMSEFVCNlSARPYVYDLIAV---------SNHYGAM-GVGHytAYAKNKLNGKWYYFDDSNV 902
Cdd:pfam13423 236 PGWLPPEiGLTLSDDLQG-DNEIVKYELRGVvvhigdsgtSGHLVSFvKVAD--SELEDPTESQWYLFNDFLV 305
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
295-405 5.93e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 43.71  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839  295 SHIQPGLCGLGNLGNTCFMNSALQCLSNTApltdYFLKDEYeaEINRDNPLGmKGEIAEAYAELIKQMWSGRDAhVAPRM 374
Cdd:COG5077   187 SKKETGYVGLRNQGATCYMNSLLQSLFFIA----KFRKDVY--GIPTDHPRG-RDSVALALQRLFYNLQTGEEP-VDTTE 258
                          90       100       110
                  ....*....|....*....|....*....|.
gi 116242839  375 FKTQVGrfAPQFSGYQQQDSQELLAFLLDGL 405
Cdd:COG5077   259 LTRSFG--WDSDDSFMQHDIQEFNRVLQDNL 287
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
504-567 2.16e-03

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: 40.54  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116242839  504 QYRVTVPLMGAVSDLCEALSRLSGIAAE---NMVVADVYNHRFHKIFQMDEGLNHIMPRDDIFVYEV 567
Cdd:pfam14533  34 ELELLVPKNGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKELSEDEPIDSLNDYLTLYAEEI 100
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
764-921 2.26e-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: 40.96  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 764 SMLQPQKKKKTTVALRDCIELFTTMEtlgEHDPWYCPNCKKHQQATKKFDLWSLPKI----LVVHLKRFSYNRywrdKLD 839
Cdd:cd02672  105 SLPLGSTKTSKESTFLQLLKRSLDLE---KVTKAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEF----DDI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242839 840 TVVEFpiRGLNMSEFV-----CNLSARP-------YVYDLIAV-----SNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNV 902
Cdd:cd02672  178 NVVLP--SGKVMQNKVspkaiDHDKLVKnrgqesiYKYELVGYvceinDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLV 255
                        170
                 ....*....|....*....
gi 116242839 903 SLASEDqivtkaAYVLFYQ 921
Cdd:cd02672  256 TPVSEL------AYILLYQ 268
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
861-911 8.14e-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: 39.40  E-value: 8.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 116242839 861 RPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIV 911
Cdd:cd02666  277 KSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVF 327
 
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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