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Conserved domains on  [gi|474094769|gb|EMS55035|]
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Ubiquitin carboxyl-terminal hydrolase 5 [Triticum urartu]

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];
6-856 3.83e-137

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: 428.53  E-value: 3.83e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769   6 SEPApELPAEEEMTLIRDITAASEahaKEGDIFFLITNRWWQSWIDYVIQDlagvpsngshhhefgsntPRRPGAIDNTN 85
Cdd:COG5560   19 IAPA-SLPLMMQEELIDEKPAESS---KQCEYAVIFAYAWYEGMFDRASCD------------------GGSPGPIVQGP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  86 LLD-DMASEVSDMQielhdtlvEGRDYILLPQQVWEKLHGWYG-GGPTLPRKAINTGlSQTDLAIEVYPLRLQLLLMpkg 163
Cdd:COG5560   77 IVDfEPESLKKSLR--------EGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLP-SESAPEVESYPVVFKLHWL--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 164 eqavvriskkvtVDELRKKACEVFDLVPDEVciwdyygRTKHALMDNLEKTLDDANIQMDQDILVEVATDANGSLDGACM 243
Cdd:COG5560  145 ------------FSINGSLINLGHDPVPHSA-------SSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDS 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 244 SSIQEDYFGSASTYLMTDASKSGFSN--ENLASLCYGSRSYSSSLMQSQYLRSSSGDLdnvpgtvgvttrgspsGLTGLL 321
Cdd:COG5560  206 FFRRYRVLASDGRVLHPLTRLELFEDrsVLLLSKITRNPDWLVDSIVDDHNRSINKEA----------------GTCGLR 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 322 NLGNTCFMNSAVQCLVHTPEFARYFRED-YHCEINWHNPLGMVGELALAFGELLRKLWAPSRTPVSPRPFKTKLSRFAPQ 400
Cdd:COG5560  270 NLGNTCYMNSALQCLMHTWELRDYFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEE 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 401 FSGYNQHDSQELLAFLLDGLHEDLNRVKHRPYLKSKDAEGRSDEEV---ADEYWANHIARNDSIIVDVCQGQYKSTLVCP 477
Cdd:COG5560  350 FSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCP 429
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 478 VCGKVSVTFDPFMYLSLPLQFASTRSMTVVVFTCDGSAPPIPY------TIRNHRIHLILEDPVLQLSTIKDDDhlaVYR 551
Cdd:COG5560  430 GCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIeldassTIRGLKKLVDAEYGKLGCFEIKVMC---IYY 506
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 552 -------------LPRLEKRASYVQFVHRRED------LDLGNNSSSTSWKPYGVPLLaQISRNETVTGSDihEMARKML 612
Cdd:COG5560  507 ggnynmlepadkvLLQDIPQTDFVYLYETNDNgievpvVHLRIEKGYKSKRLFGDPFL-QLNVLIKASIYD--KLVKEFE 583
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 613 VPMFRNHVAQHSAVQSSLSTRTQSYHTDSSKFqLQLIDDSNTVIEQTDYVIRVPQSSVATVIFVNWSKLDLKKLntnhhl 692
Cdd:COG5560  584 ELLVLVEMKKTDVDLVSEQVRLLREESSPSSW-LKLETEIDTKREEQVEEEGQMNFNDAVVISCEWEEKRYLSL------ 656
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 693 pevFKYAP--PAKRT--RGEPLSLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRST 768
Cdd:COG5560  657 ---FSYDPlwTIREIgaAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 769 KHKLETFVNFPIHDLDLTNYIANKIPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEVKSGA 848
Cdd:COG5560  734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813

                 ....*...
gi 474094769 849 AYVLFYRR 856
Cdd:COG5560  814 AYVLFYRR 821
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
6-856 3.83e-137

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 428.53  E-value: 3.83e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769   6 SEPApELPAEEEMTLIRDITAASEahaKEGDIFFLITNRWWQSWIDYVIQDlagvpsngshhhefgsntPRRPGAIDNTN 85
Cdd:COG5560   19 IAPA-SLPLMMQEELIDEKPAESS---KQCEYAVIFAYAWYEGMFDRASCD------------------GGSPGPIVQGP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  86 LLD-DMASEVSDMQielhdtlvEGRDYILLPQQVWEKLHGWYG-GGPTLPRKAINTGlSQTDLAIEVYPLRLQLLLMpkg 163
Cdd:COG5560   77 IVDfEPESLKKSLR--------EGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLP-SESAPEVESYPVVFKLHWL--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 164 eqavvriskkvtVDELRKKACEVFDLVPDEVciwdyygRTKHALMDNLEKTLDDANIQMDQDILVEVATDANGSLDGACM 243
Cdd:COG5560  145 ------------FSINGSLINLGHDPVPHSA-------SSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDS 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 244 SSIQEDYFGSASTYLMTDASKSGFSN--ENLASLCYGSRSYSSSLMQSQYLRSSSGDLdnvpgtvgvttrgspsGLTGLL 321
Cdd:COG5560  206 FFRRYRVLASDGRVLHPLTRLELFEDrsVLLLSKITRNPDWLVDSIVDDHNRSINKEA----------------GTCGLR 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 322 NLGNTCFMNSAVQCLVHTPEFARYFRED-YHCEINWHNPLGMVGELALAFGELLRKLWAPSRTPVSPRPFKTKLSRFAPQ 400
Cdd:COG5560  270 NLGNTCYMNSALQCLMHTWELRDYFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEE 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 401 FSGYNQHDSQELLAFLLDGLHEDLNRVKHRPYLKSKDAEGRSDEEV---ADEYWANHIARNDSIIVDVCQGQYKSTLVCP 477
Cdd:COG5560  350 FSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCP 429
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 478 VCGKVSVTFDPFMYLSLPLQFASTRSMTVVVFTCDGSAPPIPY------TIRNHRIHLILEDPVLQLSTIKDDDhlaVYR 551
Cdd:COG5560  430 GCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIeldassTIRGLKKLVDAEYGKLGCFEIKVMC---IYY 506
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 552 -------------LPRLEKRASYVQFVHRRED------LDLGNNSSSTSWKPYGVPLLaQISRNETVTGSDihEMARKML 612
Cdd:COG5560  507 ggnynmlepadkvLLQDIPQTDFVYLYETNDNgievpvVHLRIEKGYKSKRLFGDPFL-QLNVLIKASIYD--KLVKEFE 583
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 613 VPMFRNHVAQHSAVQSSLSTRTQSYHTDSSKFqLQLIDDSNTVIEQTDYVIRVPQSSVATVIFVNWSKLDLKKLntnhhl 692
Cdd:COG5560  584 ELLVLVEMKKTDVDLVSEQVRLLREESSPSSW-LKLETEIDTKREEQVEEEGQMNFNDAVVISCEWEEKRYLSL------ 656
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 693 pevFKYAP--PAKRT--RGEPLSLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRST 768
Cdd:COG5560  657 ---FSYDPlwTIREIgaAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 769 KHKLETFVNFPIHDLDLTNYIANKIPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEVKSGA 848
Cdd:COG5560  734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813

                 ....*...
gi 474094769 849 AYVLFYRR 856
Cdd:COG5560  814 AYVLFYRR 821
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
318-854 4.32e-81

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 263.92  E-value: 4.32e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  318 TGLLNLGNTCFMNSAVQCLVHTPEFARYFREDYHceINWHNPLGMVGELALAFGELLRKLWAPSR-TPVSPRPFKTKLSR 396
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISP--LSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  397 FAPQFSGYNQHDSQELLAFLLDGLHEDLNRvkhrpylkskdaegrsdeevadeywaNHIARNDSIIVDVCQGQYKSTLVC 476
Cdd:pfam00443  79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLKC 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  477 PvcgkvsvtfdpfmylslplqfastrsmtvvvfTCDgsappipytirnhrihliledpvlqlstikdddhlavyrlprlE 556
Cdd:pfam00443 133 L--------------------------------SCG-------------------------------------------E 137
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  557 KRASYVQFvhrredldlgnnssstswkpygvpllaqisrnetvtgSDIhemarkmlvpmfrnhvaqhsavqsslstrtqs 636
Cdd:pfam00443 138 VSETFEPF-------------------------------------SDL-------------------------------- 148
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  637 yhtdsskfQLQLIDDSNTVIEqtdyvirvpqssvatvifvnwskldlkklntnhhlpevfkyappakrtrgepLSLYACL 716
Cdd:pfam00443 149 --------SLPIPGDSAELKT----------------------------------------------------ASLQICF 168
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  717 DAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKHKLETFVNFPIhDLDLTNYIAN----K 792
Cdd:pfam00443 169 LQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPL-ELDLSRYLAEelkpK 247
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 474094769  793 IPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEE-EVKSGAAYVLFY 854
Cdd:pfam00443 248 TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
701-855 1.06e-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: 1.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 701 PAKRTRGEPLSLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKHKLETFVNFPI 780
Cdd:cd02674   75 PSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPL 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 474094769 781 HDLDLTNYIANKIPQRQ-TYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEVKSGAAYVLFYR 855
Cdd:cd02674  155 NDLDLTPYVDTRSFTGPfKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
DUSP smart00695
Domain in ubiquitin-specific proteases;
33-140 3.92e-23

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 93.96  E-value: 3.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769    33 KEGDIFFLITNRWWQSWIDYVIQDlagvpsngshhhefgsnTPRRPGAIDNTNLLDdmasevSDMQIELHDTLVEGRDYI 112
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEGK-----------------DGKDPGPIDNSGILC------SHGGPRLKEHLVEGEDYV 59
                           90       100
                   ....*....|....*....|....*....
gi 474094769   113 LLPQQVWEKLHGWYGGGPT-LPRKAINTG 140
Cdd:smart00695  60 LIPEELWNKLVRWYGGGPGpIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
6-856 3.83e-137

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 428.53  E-value: 3.83e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769   6 SEPApELPAEEEMTLIRDITAASEahaKEGDIFFLITNRWWQSWIDYVIQDlagvpsngshhhefgsntPRRPGAIDNTN 85
Cdd:COG5560   19 IAPA-SLPLMMQEELIDEKPAESS---KQCEYAVIFAYAWYEGMFDRASCD------------------GGSPGPIVQGP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  86 LLD-DMASEVSDMQielhdtlvEGRDYILLPQQVWEKLHGWYG-GGPTLPRKAINTGlSQTDLAIEVYPLRLQLLLMpkg 163
Cdd:COG5560   77 IVDfEPESLKKSLR--------EGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLP-SESAPEVESYPVVFKLHWL--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 164 eqavvriskkvtVDELRKKACEVFDLVPDEVciwdyygRTKHALMDNLEKTLDDANIQMDQDILVEVATDANGSLDGACM 243
Cdd:COG5560  145 ------------FSINGSLINLGHDPVPHSA-------SSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDS 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 244 SSIQEDYFGSASTYLMTDASKSGFSN--ENLASLCYGSRSYSSSLMQSQYLRSSSGDLdnvpgtvgvttrgspsGLTGLL 321
Cdd:COG5560  206 FFRRYRVLASDGRVLHPLTRLELFEDrsVLLLSKITRNPDWLVDSIVDDHNRSINKEA----------------GTCGLR 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 322 NLGNTCFMNSAVQCLVHTPEFARYFRED-YHCEINWHNPLGMVGELALAFGELLRKLWAPSRTPVSPRPFKTKLSRFAPQ 400
Cdd:COG5560  270 NLGNTCYMNSALQCLMHTWELRDYFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEE 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 401 FSGYNQHDSQELLAFLLDGLHEDLNRVKHRPYLKSKDAEGRSDEEV---ADEYWANHIARNDSIIVDVCQGQYKSTLVCP 477
Cdd:COG5560  350 FSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCP 429
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 478 VCGKVSVTFDPFMYLSLPLQFASTRSMTVVVFTCDGSAPPIPY------TIRNHRIHLILEDPVLQLSTIKDDDhlaVYR 551
Cdd:COG5560  430 GCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPLKIeldassTIRGLKKLVDAEYGKLGCFEIKVMC---IYY 506
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 552 -------------LPRLEKRASYVQFVHRRED------LDLGNNSSSTSWKPYGVPLLaQISRNETVTGSDihEMARKML 612
Cdd:COG5560  507 ggnynmlepadkvLLQDIPQTDFVYLYETNDNgievpvVHLRIEKGYKSKRLFGDPFL-QLNVLIKASIYD--KLVKEFE 583
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 613 VPMFRNHVAQHSAVQSSLSTRTQSYHTDSSKFqLQLIDDSNTVIEQTDYVIRVPQSSVATVIFVNWSKLDLKKLntnhhl 692
Cdd:COG5560  584 ELLVLVEMKKTDVDLVSEQVRLLREESSPSSW-LKLETEIDTKREEQVEEEGQMNFNDAVVISCEWEEKRYLSL------ 656
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 693 pevFKYAP--PAKRT--RGEPLSLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRST 768
Cdd:COG5560  657 ---FSYDPlwTIREIgaAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF 733
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 769 KHKLETFVNFPIHDLDLTNYIANKIPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEVKSGA 848
Cdd:COG5560  734 RDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS 813

                 ....*...
gi 474094769 849 AYVLFYRR 856
Cdd:COG5560  814 AYVLFYRR 821
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
318-854 4.32e-81

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 263.92  E-value: 4.32e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  318 TGLLNLGNTCFMNSAVQCLVHTPEFARYFREDYHceINWHNPLGMVGELALAFGELLRKLWAPSR-TPVSPRPFKTKLSR 396
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISP--LSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  397 FAPQFSGYNQHDSQELLAFLLDGLHEDLNRvkhrpylkskdaegrsdeevadeywaNHIARNDSIIVDVCQGQYKSTLVC 476
Cdd:pfam00443  79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLKC 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  477 PvcgkvsvtfdpfmylslplqfastrsmtvvvfTCDgsappipytirnhrihliledpvlqlstikdddhlavyrlprlE 556
Cdd:pfam00443 133 L--------------------------------SCG-------------------------------------------E 137
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  557 KRASYVQFvhrredldlgnnssstswkpygvpllaqisrnetvtgSDIhemarkmlvpmfrnhvaqhsavqsslstrtqs 636
Cdd:pfam00443 138 VSETFEPF-------------------------------------SDL-------------------------------- 148
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  637 yhtdsskfQLQLIDDSNTVIEqtdyvirvpqssvatvifvnwskldlkklntnhhlpevfkyappakrtrgepLSLYACL 716
Cdd:pfam00443 149 --------SLPIPGDSAELKT----------------------------------------------------ASLQICF 168
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  717 DAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKHKLETFVNFPIhDLDLTNYIAN----K 792
Cdd:pfam00443 169 LQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPL-ELDLSRYLAEelkpK 247
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 474094769  793 IPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEE-EVKSGAAYVLFY 854
Cdd:pfam00443 248 TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
701-855 1.06e-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: 1.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 701 PAKRTRGEPLSLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKHKLETFVNFPI 780
Cdd:cd02674   75 PSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPL 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 474094769 781 HDLDLTNYIANKIPQRQ-TYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEVKSGAAYVLFYR 855
Cdd:cd02674  155 NDLDLTPYVDTRSFTGPfKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
708-855 2.10e-43

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: 158.03  E-value: 2.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 708 EPLSLYACLDAFLREEPLVPEEMWYCPRCKEQRqASKKLDLWRLPEVLVIHLKRFSFSRS-TKHKLETFVNFPIhDLDLT 786
Cdd:cd02257   97 PQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQE-ATKRLKIKKLPPVLIIHLKRFSFNEDgTKEKLNTKVSFPL-ELDLS 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 787 NYIANKIP------QRQTYELYAVSNHYGSMA-SGHYTAYIKLLDENRWYNFDDSHVSAINEEEV-----KSGAAYVLFY 854
Cdd:cd02257  175 PYLSEGEKdsdsdnGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFY 254

                 .
gi 474094769 855 R 855
Cdd:cd02257  255 E 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
319-854 4.24e-43

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: 159.85  E-value: 4.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 319 GLLNLGNTCFMNSAVQCLVHTPEFARYFREDYH---CEINwhNPLG-MVGELALAFGELLRKLwapSRTPVSPRPFKTKL 394
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHsctCLSC--SPNScLSCAMDEIFQEFYYSG---DRSPYGPINLLYLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 395 SRFAPQFSGYNQHDSQELLAFLLDGLHEDlnrvkhrpylkskdaEGRSDEEVADEYWANhiarndSIIVDVCQGQYKSTL 474
Cdd:cd02660   77 WKHSRNLAGYSQQDAHEFFQFLLDQLHTH---------------YGGDKNEANDESHCN------CIIHQTFSGSLQSSV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 475 VCPVCGKVSVTFDPFMYLSlplqfastrsmtvvvftcdgsappipytirnhrihliledpvlqlstikdddhlavyrlpr 554
Cdd:cd02660  136 TCQRCGGVSTTVDPFLDLS------------------------------------------------------------- 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 555 lekrasyvqfvhrredLDLGNNSSSTSWKPYGVPllaqisrnetvtgsdihemarkmlvpmfrnhvaqhsavqsslstrt 634
Cdd:cd02660  155 ----------------LDIPNKSTPSWALGESGV---------------------------------------------- 172
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 635 qsyhtdsskfqlqliddsntvieqtdyvirvpqssvatvifvnwskldlkklntnhhlpevfkyappakrtrGEPLSLYA 714
Cdd:cd02660  173 ------------------------------------------------------------------------SGTPTLSD 180
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 715 CLDAFLREEPLvpEEMWY-CPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFS-RSTKHKLETFVNFPIHdLDLTNYIANK 792
Cdd:cd02660  181 CLDRFTRPEKL--GDFAYkCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSS 257
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 474094769 793 IPQRQ---------TYELYAVSNHYGSMASGHYTAYIKLLDeNRWYNFDDSHVSAINEEEVKSGAAYVLFY 854
Cdd:cd02660  258 IGDTQdsnsldpdyTYDLFAVVVHKGTLDTGHYTAYCRQGD-GQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-854 5.28e-43

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: 158.59  E-value: 5.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 318 TGLLNLGNTCFMNSAVQCLVHTPEFARY-FREDYHCEINWHNPlGMVGELAlAFGELLRklwAPSRTPVSPRPFKTKLSR 396
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYlLSREHSKDCCNEGF-CMMCALE-AHVERAL---ASSGPGSAPRIFSSNLKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 397 FAPQFSGYNQHDSQELLAFLLDGLHedlnRVKHRPYLKSKDaegrsdeevadeywANHIARNDSIIVDVCQGQYKSTLVC 476
Cdd:cd02661   77 ISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKA--------------VDPSSQETTLVQQIFGGYLRSQVKC 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 477 PVCGKVSVTFDPFMYLSLplqfastrsmtvvvftcdgsappipytirnhrihliledpvlqlsTIKDDDHLAvyrlPRLE 556
Cdd:cd02661  139 LNCKHVSNTYDPFLDLSL---------------------------------------------DIKGADSLE----DALE 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 557 krasyvQFVhRREDLDlGNNSsstswkpygvpllaqisrnetvtgsdihemarkmlvpmfrnhvaqhsavqsslstrtqs 636
Cdd:cd02661  170 ------QFT-KPEQLD-GENK----------------------------------------------------------- 182
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 637 yhtdsskfqlqliddsntvieqtdyvirvpqssvatvifvnwskldlkklntnhhlpevfkyappakrtrgeplslYACl 716
Cdd:cd02661  183 ----------------------------------------------------------------------------YKC- 185
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 717 daflreeplvpeemwycPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRStkHKLETFVNFPIHdLDLTNYIANKIPQR 796
Cdd:cd02661  186 -----------------ERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFPET-LDLSPYMSQPNDGP 245
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 474094769 797 QTYELYAVSNHYG-SMASGHYTAYIKLLDeNRWYNFDDSHVSAINEEEVKSGAAYVLFY 854
Cdd:cd02661  246 LKYKLYAVLVHSGfSPHSGHYYCYVKSSN-GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
711-858 4.52e-29

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: 118.90  E-value: 4.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 711 SLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFS--RSTKHKLETFVNFPIHdLDLTNY 788
Cdd:cd02659  152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LDMEPY 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 789 I-----------ANKIPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEV------------- 844
Cdd:cd02659  231 TekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqkt 310
                        170       180
                 ....*....|....*....|...
gi 474094769 845 ---------KSGAAYVLFYRRVR 858
Cdd:cd02659  311 ydsgprafkRTTNAYMLFYERKS 333
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
710-855 2.47e-28

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 116.75  E-value: 2.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 710 LSLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKH--KLETFVNFPiHDLDLTN 787
Cdd:cd02668  156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkkKLNASISFP-EILDMGE 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 788 YIANKIPQRQTYELYAVSNHYGSMA-SGHYTAYIKllDENR--WYNFDDSHVS---------AINEEEVK---------- 845
Cdd:cd02668  235 YLAESDEGSYVYELSGVLIHQGVSAySGHYIAHIK--DEQTgeWYKFNDEDVEempgkplklGNSEDPAKprkseikkgt 312
                        170
                 ....*....|..
gi 474094769 846 --SGAAYVLFYR 855
Cdd:cd02668  313 hsSRTAYMLVYK 324
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
708-855 1.77e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 110.17  E-value: 1.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 708 EPLSLYACLDAFLREEPLVPEEMWYCPRCKEqrqASKKLDLWRLPEVLVIHLKRFS-FSRSTKHKLETFVNFPiHDLDLT 786
Cdd:cd02667  109 SECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQqPRSANLRKVSRHVSFP-EILDLA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 787 NYIANK--IPQRQT---YELYAVSNHYGSMASGHYTAYIKL---------------------LDENRWYNFDDSHVSAIN 840
Cdd:cd02667  185 PFCDPKcnSSEDKSsvlYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVS 264
                        170
                 ....*....|....*
gi 474094769 841 EEEVKSGAAYVLFYR 855
Cdd:cd02667  265 LEEVLKSEAYLLFYE 279
DUSP smart00695
Domain in ubiquitin-specific proteases;
33-140 3.92e-23

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 93.96  E-value: 3.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769    33 KEGDIFFLITNRWWQSWIDYVIQDlagvpsngshhhefgsnTPRRPGAIDNTNLLDdmasevSDMQIELHDTLVEGRDYI 112
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEGK-----------------DGKDPGPIDNSGILC------SHGGPRLKEHLVEGEDYV 59
                           90       100
                   ....*....|....*....|....*....
gi 474094769   113 LLPQQVWEKLHGWYGGGPT-LPRKAINTG 140
Cdd:smart00695  60 LIPEELWNKLVRWYGGGPGpIPRKVVCQG 88
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
711-854 1.22e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 99.31  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 711 SLYACLDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKH--KLETFVNFPIhDLDLTNY 788
Cdd:cd02663  148 SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyiKLFYRVVFPL-ELRLFNT 226
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 474094769 789 IANKIPQRQTYELYAVSNHYGSMAS-GHYTAYIKLldENRWYNFDDSHVSAINEEEVK--------SGAAYVLFY 854
Cdd:cd02663  227 TDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFY 299
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
35-138 5.92e-21

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: 87.81  E-value: 5.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769   35 GDIFFLITNRWWQSWIDYViqdlagvpsngshhhefgsNTPR-RPGAIDNTNLLDDMASEvsdmqiELHDTLVEGRDYIL 113
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYV-------------------KEPNnEPGPIDNSDLLDDESNG------QLKPNLQEGVDYVI 55
                          90       100
                  ....*....|....*....|....*
gi 474094769  114 LPQQVWEKLHGWYGGGPTLPRKAIN 138
Cdd:pfam06337  56 VPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
750-855 1.58e-18

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: 87.39  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 750 RLPEVLVIHLKRFSFSRSTKHKLETF--VNFPIhDLDLTNYIANKipqrQTYELYAVSNHYGSMA-SGHYTAYIKLLDEN 826
Cdd:cd02657  195 RLPKYLTVQFVRFFWKRDIQKKAKILrkVKFPF-ELDLYELCTPS----GYYELVAVITHQGRSAdSGHYVAWVRRKNDG 269
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 474094769 827 RWYNFDDSHVSAINEEEVKSGA-------AYVLFYR 855
Cdd:cd02657  270 KWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
719-855 4.21e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 83.40  E-value: 4.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 719 FLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKH------KLETFVNFPihdLDLTNYIANK 792
Cdd:cd02671  189 FASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTP---LKLSLEEWST 265
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 474094769 793 IPQRQTYELYAVSNHYG-SMASGHYTAYIklldenRWYNFDDSHVSAINEEEVK---------SGAAYVLFYR 855
Cdd:cd02671  266 KPKNDVYRLFAVVMHSGaTISSGHYTAYV------RWLLFDDSEVKVTEEKDFLealspntssTSTPYLLFYK 332
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
687-854 1.65e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 79.72  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 687 NTNHHLPevfkyaPPAKRtRGEPLSLYACLDAFLREEPLvpeEMWYCPRCKeqrqaskkLDLWRLPEVLVIHLKRFSFS- 765
Cdd:cd02662   80 FTMLSLP------VPNQS-SGSGTTLEHCLDDFLSTEII---DDYKCDRCQ--------TVIVRLPQILCIHLSRSVFDg 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 766 RSTKHKLETFVNFPihdLDLTNYIankipqrqtYELYAVSNHYGSMASGHYTAY--------------------IKLLDE 825
Cdd:cd02662  142 RGTSTKNSCKVSFP---ERLPKVL---------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTS 209
                        170       180       190
                 ....*....|....*....|....*....|
gi 474094769 826 NRWYNFDDSHVSAINEEEVK-SGAAYVLFY 854
Cdd:cd02662  210 HPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
708-855 2.26e-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 hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 80.83  E-value: 2.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 708 EPLSLYACLDAFLREEPLvpEEmwYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSR-STKHKLETFVNFPihdldlt 786
Cdd:cd02658  176 EPVPLEDCLKAYFAPETI--ED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEnWVPKKLDVPIDVP------- 244
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 474094769 787 NYIANKipqrqTYELYAVSNHYG-SMASGHYTAYIK--LLDENRWYNFDDSHVSAINEEEVKSGAAYVLFYR 855
Cdd:cd02658  245 EELGPG-----KYELIAFISHKGtSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
735-856 3.29e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 79.85  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 735 RCKEQRQASKKldlwRLPEVLVIHLKRFSFSrSTKHKLETFVNFPIHdldLTNYIANKIPQRQT--YELYAVSNHYGSMA 812
Cdd:COG5533  167 QAKQEYEVSFV----KLPKILTIQLKRFANL-GGNQKIDTEVDEKFE---LPVKHDQILNIVKEtyYDLVGFVLHQGSLE 238
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 474094769 813 SGHYTAYIKLldENRWYNFDDSHVSAINEEE---VKSGAAYVLFYRR 856
Cdd:COG5533  239 GGHYIAYVKK--GGKWEKANDSDVTPVSEEEainEKAKNAYLYFYER 283
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
716-855 3.27e-14

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 74.84  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 716 LDAFLREEPLVPEEMWYCPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTkHKLETFVNFPIHDLDLT--------- 786
Cdd:cd02664  140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKT-HVREKIMDNVSINEVLSlpvrvesks 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 787 ---NYIANKIPQRQT---------YELYAVSNHYG-SMASGHYTAYIK--------------------LLDENRWYNFDD 833
Cdd:cd02664  219 sesPLEKKEEESGDDgelvtrqvhYRLYAVVVHSGySSESGHYFTYARdqtdadstgqecpepkdaeeNDESKNWYLFND 298
                        170       180
                 ....*....|....*....|....*....
gi 474094769 834 SHVSAINEEEVK-------SGAAYVLFYR 855
Cdd:cd02664  299 SRVTFSSFESVQnvtsrfpKDTPYILFYE 327
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
319-424 9.44e-13

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 70.05  E-value: 9.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 319 GLLNLGNTCFMNSAVQCLVHTPEF----ARYFREDYHCEinwHNPLGMVGELALAFGELLRKlwapsRTPVSPRPFKTKL 394
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELrdalKNYNPARRGAN---QSSDNLTNALRDLFDTMDKK-----QEPVPPIEFLQLL 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 474094769 395 SRFAPQFS------GYNQHDSQELLAFLLDGLHEDL 424
Cdd:cd02657   73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL 108
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
319-497 1.45e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 69.66  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 319 GLLNLGNTCFMNSAVQCLVHTPEFARYFREDYHC-EINWHNP-LGMVGELA-LAFGELLRKLWAPSRTP---------VS 386
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfPSDVVDPaNDLNCQLIkLADGLLSGRYSKPASLKsendpyqvgIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 387 PRPFKTKLSRFAPQFSGYNQHDSQELLAFLLDglhedlnrvkhrpylkskdaegrsdeEVADEYWANHIArNDSIIVDVC 466
Cdd:cd02658   81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLID--------------------------KLDRESFKNLGL-NPNDLFKFM 133
                        170       180       190
                 ....*....|....*....|....*....|.
gi 474094769 467 QGQyksTLVCPVCGKVSVTFDPFMYLSLPLQ 497
Cdd:cd02658  134 IED---RLECLSCKKVKYTSELSEILSLPVP 161
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
751-844 8.10e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 66.05  E-value: 8.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  751 LPEVLVIHLKRFS--FSRSTKHKLETFVNFPIhDLDLTNYIANKIPQRQ----TYELYAVSNHYGSMASGHYTAYIKLLD 824
Cdd:COG5077   378 LPPVLHLQLKRFEydFERDMMVKINDRYEFPL-EIDLLPFLDRDADKSEnsdaVYVLYGVLVHSGDLHEGHYYALLKPEK 456
                          90       100
                  ....*....|....*....|
gi 474094769  825 ENRWYNFDDSHVSAINEEEV 844
Cdd:COG5077   457 DGRWYKFDDTRVTRATEKEV 476
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
734-855 1.79e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 64.26  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 734 PRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSRSTKHKLETFVNFPIHDLDLTNYIANKIPQ---RQTYELYAVSNHYGS 810
Cdd:cd02669  315 KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGT 394
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 474094769 811 MA-SGHYTAYIKLLDENRWYNFDDSHVSAINEEEVKSGAAYVLFYR 855
Cdd:cd02669  395 PQeDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
294-496 2.48e-10

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 63.49  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 294 SSSGDLDN---VPGTVGVTtrgspsgltgllNLGNTCFMNSAVQCLVHTPEFARYFredyhceINWHNPLGMV---GELA 367
Cdd:cd02669  105 KLSRDLDGkpyLPGFVGLN------------NIKNNDYANVIIQALSHVKPIRNFF-------LLYENYENIKdrkSELV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 368 LAFGELLRKLWapsrtpvSPRPFKTKLS----------RFAPQFSGYNQHDSQELLAFLLDGLHEDLNRVKhrpylkskd 437
Cdd:cd02669  166 KRLSELIRKIW-------NPRNFKGHVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSK--------- 229
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 474094769 438 aegrsdeevadeywanhiARNDSIIVDVCQG--QYKSTLVCPV------------CGKVSVTFD-PFMYLSLPL 496
Cdd:cd02669  230 ------------------KPNSSIIHDCFQGkvQIETQKIKPHaeeegskdkffkDSRVKKTSVsPFLLLTLDL 285
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
319-421 3.87e-10

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 62.12  E-value: 3.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 319 GLLNLGNTCFMNSAVQCLVhtpeFARYFREDYHCEinwhNPLGMVGELALAFGE-LLRKLWAPSRTPVSPRPFKTKLSRF 397
Cdd:cd02664    1 GLINLGNTCYMNSVLQALF----MAKDFRRQVLSL----NLPRLGDSQSVMKKLqLLQAHLMHTQRRAEAPPDYFLEASR 72
                         90       100
                 ....*....|....*....|....
gi 474094769 398 APQFSGYNQHDSQELLAFLLDGLH 421
Cdd:cd02664   73 PPWFTPGSQQDCSEYLRYLLDRLH 96
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
751-854 2.55e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 55.64  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 751 LPEVLVIHLKRFSFSRSTKHKLETFVNFPihdldltnyianKIPQRQTYELYAVSNHYGSMASGHYTAYIKLLDENRWYN 830
Cdd:cd02665  128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------------QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195
                         90       100       110
                 ....*....|....*....|....*....|..
gi 474094769 831 FDDSHVSAINEEEVKSGA--------AYVLFY 854
Cdd:cd02665  196 YNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
733-854 3.22e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 55.61  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 733 CPRCKEQRQASKKlDLWRLPEVLVIHLKRFSFSRST----KHKLETFVNFPIHDldltnyiankipqrQTYELYAVSNHY 808
Cdd:cd02673  129 CSSCKCESAISSE-RIMTFPECLSINLKRYKLRIATsdylKKNEEIMKKYCGTD--------------AKYSLVAVICHL 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 474094769 809 G-SMASGHYTAYIK-LLDENRWYNFDDSHVSAINEEEVK---SGAAYVLFY 854
Cdd:cd02673  194 GeSPYDGHYIAYTKeLYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
705-844 4.33e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 52.88  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 705 TRGEPLSLYACLD----------------AFLREEPLVPEEMWYCPRcKEQRQASKKLD---LWRLPEVLVIHLKRFSFS 765
Cdd:cd02666  184 VLLEPKDLYDALDryfdydsltklpqrsqVQAQLAQPLQRELISMDR-YELPSSIDDIDeliREAIQSESSLVRQAQNEL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 766 RSTKHKLE-TFVNFPIHDldltnyiankipqrqtYELYAVSNHYGSMASGHYTAYIKLLDENRWYNFDDSHVSAINEEEV 844
Cdd:cd02666  263 AELKHEIEkQFDDLKSYG----------------YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
319-442 1.68e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 50.57  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 319 GLLNLGNTCFMNSAVQCLV-HTPEFARYFREDYHC------EINWHNPLgMVGELALAFgelLRKLWAPSrtpvsprpfK 391
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlknVIRKPEPD-LNQEEALKL---FTALWSSK---------E 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 474094769 392 TKLSRFAPQfsgYNQHDSQELLAFLLDGLHEDLNRVKHRPYLKSKDAEGRS 442
Cdd:COG5533   68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTKDKKKT 115
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
736-855 1.35e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 44.44  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 736 CKEQRQASKklDLWRLPEVLVIHLKRFSFSRSTKHKLETFVnFPIHDLDLTNYIA----------------------NKI 793
Cdd:cd02670   85 CLEQYFNNS--VFAKAPSCLIICLKRYGKTEGKAQKMFKKI-LIPDEIDIPDFVAddpracskcqlecrvcyddkdfSPT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 794 PQRQTYELYAVSNHYG-SMASGHYTAYIK-----------LLDENRWYNFDD-------SHVSAInEEEVKSGAAYVLFY 854
Cdd:cd02670  162 CGKFKLSLCSAVCHRGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDmadrdgvSNGFNI-PAARLLEDPYMLFY 240

                 .
gi 474094769 855 R 855
Cdd:cd02670  241 Q 241
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
319-345 4.02e-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: 43.12  E-value: 4.02e-04
                         10        20
                 ....*....|....*....|....*..
gi 474094769 319 GLLNLGNTCFMNSAVQCLVHTPEFARY 345
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
315-420 1.20e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 42.55  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  315 SGLTGLLNLGNTCFMNSAVQCLVhtpeFARYFREDYHcEINWHNPLGMvGELALAFGELLRKLwAPSRTPVSprpfKTKL 394
Cdd:COG5077   191 TGYVGLRNQGATCYMNSLLQSLF----FIAKFRKDVY-GIPTDHPRGR-DSVALALQRLFYNL-QTGEEPVD----TTEL 259
                          90       100
                  ....*....|....*....|....*...
gi 474094769  395 SR-FA-PQFSGYNQHDSQELLAFLLDGL 420
Cdd:COG5077   260 TRsFGwDSDDSFMQHDIQEFNRVLQDNL 287
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
733-836 2.02e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.10  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769  733 CPRCKEQRQASKKLDLWRLPEVLVIHLKRFSFSrstKHKLETFVNFPIHDLDLTNYIANKIPQR-QTYELYA-VSNHYGS 810
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE---WRQLWKTPGWLPPEIGLTLSDDLQGDNEiVKYELRGvVVHIGDS 272
                          90       100       110
                  ....*....|....*....|....*....|...
gi 474094769  811 MASGHYTAYIKLLD-------ENRWYNFDDSHV 836
Cdd:pfam13423 273 GTSGHLVSFVKVADseledptESQWYLFNDFLV 305
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
710-854 5.04e-03

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 39.80  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 710 LSLYACLDAFLREEPLVPEemWYCPRCKEQRQASKKlDLWRLP----EVLVIHLKRFSFSRSTKH-------KLETFVNF 778
Cdd:cd02672  117 STFLQLLKRSLDLEKVTKA--WCDTCCKYQPLEQTT-SIRHLPdillLVLVINLSVTNGEFDDINvvlpsgkVMQNKVSP 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 474094769 779 PIHDLDLTNYIaNKIPQRQTYELYA-VSNHYGSMASGHY-TAYIKL---LDENRWYNFDDSHVSAINEEevksgaAYVLF 853
Cdd:cd02672  194 KAIDHDKLVKN-RGQESIYKYELVGyVCEINDSSRGQHNvVFVIKVneeSTHGRWYLFNDFLVTPVSEL------AYILL 266

                 .
gi 474094769 854 Y 854
Cdd:cd02672  267 Y 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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