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Conserved domains on  [gi|568962894|ref|XP_006511763|]
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ubiquitin carboxyl-terminal hydrolase 4 isoform X4 [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];
35-845 3.34e-113

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: 364.97  E-value: 3.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 186 --KYMSNTYEQLSKLDN--------------TIQDAGLYQGqVLVIEPQNEDGTWPRQSLQSKSSTAPSRnfttsskpsa 249
Cdd:COG5560  193 vpEIMGLRLGLDSFFRRyrvlasdgrvlhplTRLELFEDRS-VLLLSKITRNPDWLVDSIVDDHNRSINK---------- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 250 spycsvsasliangdstnssgmhssgvsrggsgfsasyncqeppsphiQPGLCGLGNLGNTCFMNSALQCLSNTAPLTEY 329
Cdd:COG5560  262 ------------------------------------------------EAGTCGLRNLGNTCYMNSALQCLMHTWELRDY 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 330 FLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDL 409
Cdd:COG5560  294 FLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDL 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 410 NRVKKKPYLE-PKDANGRPDAV--VAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKD 486
Cdd:COG5560  374 NRIIKKPYTSkPDLSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 487 RIMEVFLVPADPQCRPIQ-YRVTVPLMGAISDLCEALSKLSGIAaeNMVVTDVYNHRFHKIF-QMDEGLSH-ITPRDDIF 563
Cdd:COG5560  454 WKHTIVVFPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGCF--EIKVMCIYYGGNYNMLePADKVLLQdIPQTDFVY 531
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 564 VYEvcnTSMDGsecITLPVYfrekKSRPSSASSGAVLYGQPLLvsvpkhKLTLeslyqavcdRISRYIKQPLPDEFlssp 643
Cdd:COG5560  532 LYE---TNDNG---IEVPVV----HLRIEKGYKSKRLFGDPFL------QLNV---------LIKASIYDKLVKEF---- 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 644 lepgacngsrssyegdeeeemdhqeegkEQLSEVEGSGEDDQGDDHSESAQKVKgqpRHKRLFTFSLVNSCGTADINSLA 723
Cdd:COG5560  583 ----------------------------EELLVLVEMKKTDVDLVSEQVRLLRE---ESSPSSWLKLETEIDTKREEQVE 631
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 724 TDGkLLKLNSRSTLAIDWdSETRSLYFDEQESEACEKHLSMSQPQkkkkaaVALRECIELFTTMETLGEHDPWYCPTCKK 803
Cdd:COG5560  632 EEG-QMNFNDAVVISCEW-EEKRYLSLFSYDPLWTIREIGAAERT------ITLQDCLNEFSKPEQLGLSDSWYCPGCKE 703
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|..
gi 568962894 804 HQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPV 845
Cdd:COG5560  704 FRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-845 3.34e-113

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 364.97  E-value: 3.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 186 --KYMSNTYEQLSKLDN--------------TIQDAGLYQGqVLVIEPQNEDGTWPRQSLQSKSSTAPSRnfttsskpsa 249
Cdd:COG5560  193 vpEIMGLRLGLDSFFRRyrvlasdgrvlhplTRLELFEDRS-VLLLSKITRNPDWLVDSIVDDHNRSINK---------- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 250 spycsvsasliangdstnssgmhssgvsrggsgfsasyncqeppsphiQPGLCGLGNLGNTCFMNSALQCLSNTAPLTEY 329
Cdd:COG5560  262 ------------------------------------------------EAGTCGLRNLGNTCYMNSALQCLMHTWELRDY 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 330 FLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDL 409
Cdd:COG5560  294 FLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDL 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 410 NRVKKKPYLE-PKDANGRPDAV--VAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKD 486
Cdd:COG5560  374 NRIIKKPYTSkPDLSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 487 RIMEVFLVPADPQCRPIQ-YRVTVPLMGAISDLCEALSKLSGIAaeNMVVTDVYNHRFHKIF-QMDEGLSH-ITPRDDIF 563
Cdd:COG5560  454 WKHTIVVFPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGCF--EIKVMCIYYGGNYNMLePADKVLLQdIPQTDFVY 531
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 564 VYEvcnTSMDGsecITLPVYfrekKSRPSSASSGAVLYGQPLLvsvpkhKLTLeslyqavcdRISRYIKQPLPDEFlssp 643
Cdd:COG5560  532 LYE---TNDNG---IEVPVV----HLRIEKGYKSKRLFGDPFL------QLNV---------LIKASIYDKLVKEF---- 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 644 lepgacngsrssyegdeeeemdhqeegkEQLSEVEGSGEDDQGDDHSESAQKVKgqpRHKRLFTFSLVNSCGTADINSLA 723
Cdd:COG5560  583 ----------------------------EELLVLVEMKKTDVDLVSEQVRLLRE---ESSPSSWLKLETEIDTKREEQVE 631
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 724 TDGkLLKLNSRSTLAIDWdSETRSLYFDEQESEACEKHLSMSQPQkkkkaaVALRECIELFTTMETLGEHDPWYCPTCKK 803
Cdd:COG5560  632 EEG-QMNFNDAVVISCEW-EEKRYLSLFSYDPLWTIREIGAAERT------ITLQDCLNEFSKPEQLGLSDSWYCPGCKE 703
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|..
gi 568962894 804 HQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPV 845
Cdd:COG5560  704 FRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
302-485 8.27e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 183.80  E-value: 8.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  302 CGLGNLGNTCFMNSALQCLSNTAPLTEYFLKDEYEAEINRDNPlgmKGEIAEAYAELIKQMWSG-RDTHVAPRMFKTQVG 380
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  381 RFAPQFSGYQQQDSQELLAFILDGLHEDLNRvkkkpylepkdangrpdavvakeaweNHRLRNDSVIVDTFHGLFKSTLV 460
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180
                  ....*....|....*....|....*
gi 568962894  461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDS 156
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 2.16e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 120.54  E-value: 2.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 568962894   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
775-847 1.35e-26

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: 108.91  E-value: 1.35e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568962894 775 VALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRH 847
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLND 156
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-845 3.34e-113

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 364.97  E-value: 3.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWN- 185
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDv 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 186 --KYMSNTYEQLSKLDN--------------TIQDAGLYQGqVLVIEPQNEDGTWPRQSLQSKSSTAPSRnfttsskpsa 249
Cdd:COG5560  193 vpEIMGLRLGLDSFFRRyrvlasdgrvlhplTRLELFEDRS-VLLLSKITRNPDWLVDSIVDDHNRSINK---------- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 250 spycsvsasliangdstnssgmhssgvsrggsgfsasyncqeppsphiQPGLCGLGNLGNTCFMNSALQCLSNTAPLTEY 329
Cdd:COG5560  262 ------------------------------------------------EAGTCGLRNLGNTCYMNSALQCLMHTWELRDY 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 330 FLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDL 409
Cdd:COG5560  294 FLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDL 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 410 NRVKKKPYLE-PKDANGRPDAV--VAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKD 486
Cdd:COG5560  374 NRIIKKPYTSkPDLSPGDDVVVkkKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 487 RIMEVFLVPADPQCRPIQ-YRVTVPLMGAISDLCEALSKLSGIAaeNMVVTDVYNHRFHKIF-QMDEGLSH-ITPRDDIF 563
Cdd:COG5560  454 WKHTIVVFPESGRRQPLKiELDASSTIRGLKKLVDAEYGKLGCF--EIKVMCIYYGGNYNMLePADKVLLQdIPQTDFVY 531
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 564 VYEvcnTSMDGsecITLPVYfrekKSRPSSASSGAVLYGQPLLvsvpkhKLTLeslyqavcdRISRYIKQPLPDEFlssp 643
Cdd:COG5560  532 LYE---TNDNG---IEVPVV----HLRIEKGYKSKRLFGDPFL------QLNV---------LIKASIYDKLVKEF---- 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 644 lepgacngsrssyegdeeeemdhqeegkEQLSEVEGSGEDDQGDDHSESAQKVKgqpRHKRLFTFSLVNSCGTADINSLA 723
Cdd:COG5560  583 ----------------------------EELLVLVEMKKTDVDLVSEQVRLLRE---ESSPSSWLKLETEIDTKREEQVE 631
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 724 TDGkLLKLNSRSTLAIDWdSETRSLYFDEQESEACEKHLSMSQPQkkkkaaVALRECIELFTTMETLGEHDPWYCPTCKK 803
Cdd:COG5560  632 EEG-QMNFNDAVVISCEW-EEKRYLSLFSYDPLWTIREIGAAERT------ITLQDCLNEFSKPEQLGLSDSWYCPGCKE 703
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|..
gi 568962894 804 HQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPV 845
Cdd:COG5560  704 FRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
302-485 8.27e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 183.80  E-value: 8.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  302 CGLGNLGNTCFMNSALQCLSNTAPLTEYFLKDEYEAEINRDNPlgmKGEIAEAYAELIKQMWSG-RDTHVAPRMFKTQVG 380
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  381 RFAPQFSGYQQQDSQELLAFILDGLHEDLNRvkkkpylepkdangrpdavvakeaweNHRLRNDSVIVDTFHGLFKSTLV 460
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180
                  ....*....|....*....|....*
gi 568962894  461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDS 156
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
139-226 4.18e-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: 131.13  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTIQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 568962894  219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 2.16e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 120.54  E-value: 2.16e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 568962894   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
31-123 2.79e-27

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: 105.53  E-value: 2.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894   31 GAQWYLIDSRWFKQWKKYVGfdswdmynvgEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGc 110
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG- 69
                          90
                  ....*....|...
gi 568962894  111 veGQQPIVRKVVE 123
Cdd:pfam06337  70 --GGPEIKRNVVN 80
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
775-847 1.35e-26

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: 108.91  E-value: 1.35e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568962894 775 VALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRH 847
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLND 156
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
302-486 6.93e-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: 6.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 302 CGLGNLGNTCFMNSALQCLSNTAPLTEYFLKDEYEAEINRDNPLGMKgeIAEAYAELIkqMWSGRDThVAPRMFKTQVGR 381
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC--ALEAHVERA--LASSGPG-SAPRIFSSNLKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 382 FAPQFSGYQQQDSQELLAFILDGLHedlnrvkkKPYLEPKdangrpdavvAKEAWENHRLRNDSVIVDTFHGLFKSTLVC 461
Cdd:cd02661   77 ISKHFRIGRQEDAHEFLRYLLDAMQ--------KACLDRF----------KKLKAVDPSSQETTLVQQIFGGYLRSQVKC 138
                        170       180
                 ....*....|....*....|....*
gi 568962894 462 PECAKVSVTFDPFcyLTLPLPLKKD 486
Cdd:cd02661  139 LNCKHVSNTYDPF--LDLSLDIKGA 161
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
764-844 4.01e-23

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 100.98  E-value: 4.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  764 MSQPQKKKKAAVALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEF 843
Cdd:pfam00443 151 PIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEF 230

                  .
gi 568962894  844 P 844
Cdd:pfam00443 231 P 231
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-491 5.81e-22

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 95.43  E-value: 5.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNtaplteyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdthvaprmfktqvgrf 382
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 383 apqfsgyQQQDSQELLAFILDGLHedlnrvkkkpylepkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTLVCP 462
Cdd:cd02674   21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                        170       180
                 ....*....|....*....|....*....
gi 568962894 463 ECAKVSVTFDPFCYLTLPLPLKKDRIMEV 491
Cdd:cd02674   56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKV 84
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-485 1.65e-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: 96.67  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNTAPLTEYFLKDEYEAEINRDNPLGMKG-EIAEAYAELikqMWSGRDTHVAPRMFKTQVGR 381
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLScAMDEIFQEF---YYSGDRSPYGPINLLYLSWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 382 FAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKkPYLEPKDANgrpdavvakeawenhrlrndsVIVD-TFHGLFKSTLV 460
Cdd:cd02660   79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN-EANDESHCN---------------------CIIHqTFSGSLQSSVT 136
                        170       180
                 ....*....|....*....|....*
gi 568962894 461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:cd02660  137 CQRCGGVSTTVDPFLDLSLDIPNKS 161
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
303-486 5.68e-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: 5.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNtaplteyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdthvaprmfktqvgrf 382
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 383 apqfsgyQQQDSQELLAFILDGLHEDLNRVKKKpylepkdangrpdavvakeawENHRLRNDSVIVDTFHGLFKSTLVCP 462
Cdd:cd02257   21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                        170       180
                 ....*....|....*....|....
gi 568962894 463 ECAKVSVTFDPFCYLTLPLPLKKD 486
Cdd:cd02257   73 ECGHESVSTEPELFLSLPLPVKGL 96
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-491 1.31e-19

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: 89.75  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNTAPLTEYFLKDeyeaeinrdnplgmkgeiaeayaelikqmwsgrdthvaPRMFKTQVGRF 382
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 383 APQFSGYQQQDSQELLAFILDGLhedlnrvkkkpylepkdangrpdavvakeawenhRLRNDSVivdtFHGLFKSTLVCP 462
Cdd:cd02667   43 APQFKGYQQQDSHELLRYLLDGL----------------------------------RTFIDSI----FGGELTSTIMCE 84
                        170       180
                 ....*....|....*....|....*....
gi 568962894 463 ECAKVSVTFDPFcyLTLPLPLKKDRIMEV 491
Cdd:cd02667   85 SCGTVSLVYEPF--LDLSLPRSDEIKSEC 111
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
751-844 2.93e-14

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: 73.67  E-value: 2.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 751 DEQESEACEKHLSMSQPQKKKKAaVALRECIELFTTMETLGEHDPWYCPtCKKHQQATKKFDLWSLPKILVVHLKRFSYN 830
Cdd:cd02257   76 HESVSTEPELFLSLPLPVKGLPQ-VSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFN 153
                         90
                 ....*....|....*
gi 568962894 831 RYWR-DKLDTVVEFP 844
Cdd:cd02257  154 EDGTkEKLNTKVSFP 168
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-483 3.62e-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: 74.28  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNTAPLTEYFLKDEYEAEINRDNP----------LGmKGEIAEAYAELIKQMWSGRDT--HV 370
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLA-DGLLSGRYSKPASLKSENDPYqvGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 371 APRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLnrvKKKPYLEPKDangrpdavvakeawenhrlrndsvivdt 450
Cdd:cd02658   80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES---FKNLGLNPND---------------------------- 128
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568962894 451 fhgLFK----STLVCPECAKVSVTFDPFCYLTLPLPL 483
Cdd:cd02658  129 ---LFKfmieDRLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
299-484 7.40e-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: 68.50  E-value: 7.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 299 PGLCGLGNLGNTCFMNSALQCLSNTAPLTEYFL-KDEYEAEINRdnplgmKGEIAEAYAELIKQMWSgrdthvaPRMFKT 377
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDR------KSELVKRLSELIRKIWN-------PRNFKG 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 378 QVG----------RFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKpylepkdangrpdavvakeawenhrlrNDSVI 447
Cdd:cd02669  184 HVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSII 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568962894 448 VDTFHGLFK---------------STLVCPECAKVSVTFDPFCYLTLPLPLK 484
Cdd:cd02669  237 HDCFQGKVQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLLLTLDLPPP 288
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-481 9.12e-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: 9.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLsNTAP-----LTEYFLKDEYEAEINRDnplgmkgeIAEAYAELIKQMWSGRDThVAPRMFKT 377
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDN--------LTNALRDLFDTMDKKQEP-VPPIEFLQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 378 QVGRFAPQFS------GYQQQDSQELLAFILDGLHEDLNRVKKKPylepkdangrpdavvakeawenhrlrndSVIVDTF 451
Cdd:cd02657   71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG----------------------------SFIDQLF 122
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568962894 452 HGLFKSTLVCPEC-AKVSVTFDPFCYLTLPL 481
Cdd:cd02657  123 GIELETKMKCTESpDEEEVSTESEYKLQCHI 153
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
303-409 1.03e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 63.67  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLS-NTAPLTEYFLKDEYE-----AEINRDNPLgMKGEIAEAyaeLIKQMWSGRdthvaprmfK 376
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPD-LNQEEALK---LFTALWSSK---------E 67
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568962894 377 TQVGRFAPQfsgYQQQDSQELLAFILDGLHEDL 409
Cdd:COG5533   68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDL 97
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
779-844 1.56e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 63.10  E-value: 1.56e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568962894 779 ECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYN-RYWR-DKLDTVVEFP 844
Cdd:cd02663  151 SCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyIKLFYRVVFP 218
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
763-846 2.53e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 62.78  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 763 SMSQPQKKKKAAVA-----LRECIELFTTMETLGEhDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRD-K 836
Cdd:cd02660  159 NKSTPSWALGESGVsgtptLSDCLDRFTRPEKLGD-FAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSrK 237
                         90
                 ....*....|
gi 568962894 837 LDTVVEFPVR 846
Cdd:cd02660  238 IDTYVQFPLE 247
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-844 2.41e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 59.60  E-value: 2.41e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568962894 777 LRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYwrDKLDTVVEFP 844
Cdd:cd02661  164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFP 229
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-495 2.16e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 56.73  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLsntaplteyFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMW---SGRDTHVAPRMFKTQV 379
Cdd:cd02664    1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 380 grFAPQFSGYQQQDSQELLAFILDGLHedlnrvkkkpylepkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTL 459
Cdd:cd02664   72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568962894 460 VCPECAKVSVTFDPFCYLTLPLPLKKDrIMEVFLVP 495
Cdd:cd02664  112 RCLNCNSTSARTERFRDLDLSFPSVQD-LLNYFLSP 146
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
765-844 2.18e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 56.56  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 765 SQPQKKKKAAVALRECIELFTTMETLGEhdpwYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRD-KLDTVVEF 843
Cdd:cd02658  168 KEEGELVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDV 243

                 .
gi 568962894 844 P 844
Cdd:cd02658  244 P 244
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-482 2.30e-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: 56.55  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNTAPLTEyfLKDEYEAEINRDNPLGMkgeiaeayaelikqmwsgrdthVAPRMFKTQVGRF 382
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLLTC--LKDLFESISEQKKRTGV----------------------ISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 383 APQFSGYQQQDSQELLAFILDGLHEDLNRVKKKpYLEPKDANGRPDAVVAKEaWenhrlrndsvIVDTFHGLFKSTLVCP 462
Cdd:cd02663   57 NELFDNYMHQDAHEFLNFLLNEIAEILDAERKA-EKANRKLNNNNNAEPQPT-W----------VHEIFQGILTNETRCL 124
                        170       180
                 ....*....|....*....|
gi 568962894 463 ECAKVSVTFDPFCYLTLPLP 482
Cdd:cd02663  125 TCETVSSRDETFLDLSIDVE 144
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
759-844 2.60e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 53.16  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 759 EKHLSMSQPQKKK-KAAVALRECIELFTTMETLGEHDPWYCPTCKKhqqATKKFDLWSLPKILVVHLKRFSYNRYWRD-K 836
Cdd:cd02667   94 EPFLDLSLPRSDEiKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLrK 170

                 ....*...
gi 568962894 837 LDTVVEFP 844
Cdd:cd02667  171 VSRHVSFP 178
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
299-407 4.77e-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: 52.59  E-value: 4.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 299 PGLCGLGNLGNTCFMNSALQCLsntaplteYFLKDeYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQ 378
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVL--------YFCPG-FKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAPRRLLNA 92
                         90       100
                 ....*....|....*....|....*....
gi 568962894 379 VGRFAPQFSGYQQQDSQELLAFILDGLHE 407
Cdd:cd02671   93 LREVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-844 1.60e-06

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 50.88  E-value: 1.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 777 LRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY--WRDKLDTVVEFP 844
Cdd:cd02668  158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKtgAKKKLNASISFP 227
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
777-844 6.07e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 49.18  E-value: 6.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 777 LRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYN--RYWRDKLDTVVEFP 844
Cdd:cd02659  153 LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFP 222
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-329 1.01e-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: 44.66  E-value: 1.01e-04
                         10        20
                 ....*....|....*....|....*..
gi 568962894 303 GLGNLGNTCFMNSALQCLSNTAPLTEY 329
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-484 1.37e-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: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 303 GLGNLGNTCFMNSALQCLSNTAPLTEYFLK-----DEYEAEINRDNPLGMKGeIAEAYAELIKQMWSGRDTHVAPRMFKT 377
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 378 QVGrfapqFSGYQQQDSQELLAFILDGLHEDLNRVKKkpylepkdangrPDAVvakeawenhrlrndSVIVDTFHGLFKS 457
Cdd:cd02668   80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKN------------PDLK--------------NIVQDLFRGEYSY 128
                        170       180
                 ....*....|....*....|....*..
gi 568962894 458 TLVCPECAKVSVTFDPFcyLTLPLPLK 484
Cdd:cd02668  129 VTQCSKCGRESSLPSKF--YELELQLK 153
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
781-846 4.68e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 43.25  E-value: 4.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568962894 781 IELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNR--YWRDKL------DTVVEFPVR 846
Cdd:cd02664  140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPVR 213
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
300-484 4.76e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 43.40  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 300 GLCGLGNLGNTCFMNSALQCLSNTAplteYFLKDEYEAEINRDNPlGMKGEIaeayAELIKQMWSgrdTHVAPRMFKTQV 379
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD-DNKSVP----LALQRLFLF---LQLSESPVKTTE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 380 GRFAPQFSG------YQQQDSQELLAFILDGLHEDLNRVKKKPylepkdangrpdavvakeawenhrlrndsVIVDTFHG 453
Cdd:cd02659   69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKLEEKLKGTGQEG-----------------------------LIKNLFGG 119
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568962894 454 LFKSTLVCPECAKVSVTFDPFcyLTLPLPLK 484
Cdd:cd02659  120 KLVNYIICKECPHESEREEYF--LDLQVAVK 148
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
809-846 7.20e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 43.08  E-value: 7.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568962894 809 KKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVR 846
Cdd:cd02669  325 KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIK 362
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
504-586 1.26e-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: 40.93  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  504 QYRVTVPLMGAISDLCEALSKLSGIAAE---NMVVTDVYNHRFHKIFQMDEGLSHITPRDDIFVYEVCNTSMD-GSECIT 579
Cdd:pfam14533  34 ELELLVPKNGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKELSEDEPIDSLNDYLTLYAEEIPEEELNlDEGERL 113

                  ....*....
gi 568962894  580 LPV--YFRE 586
Cdd:pfam14533 114 IPVfhFQKE 122
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
297-405 1.37e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 42.55  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894  297 IQPGLCGLGNLGNTCFMNSALQCLSNTAplteYFLKDEYeaEINRDNPLGmKGEIAEAYAELIKQMWSGR---DTHVAPR 373
Cdd:COG5077   189 KETGYVGLRNQGATCYMNSLLQSLFFIA----KFRKDVY--GIPTDHPRG-RDSVALALQRLFYNLQTGEepvDTTELTR 261
                          90       100       110
                  ....*....|....*....|....*....|..
gi 568962894  374 MFKTQvgrfapQFSGYQQQDSQELLAFILDGL 405
Cdd:COG5077   262 SFGWD------SDDSFMQHDIQEFNRVLQDNL 287
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
753-857 4.44e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 40.26  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962894 753 QESEACEKHLSMSQPQKKKKAAVALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY 832
Cdd:cd02671  158 QESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGS 237
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568962894 833 WRD------KLDTVVEFPVRhCICEEQTERE 857
Cdd:cd02671  238 EFDcygglsKVNTPLLTPLK-LSLEEWSTKP 267
 
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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