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Conserved domains on  [gi|19076030|ref|NP_588530|]
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CSN-associated deubiquitinating enzyme Ubp12 [Schizosaccharomyces pombe]

Protein Classification

UBP12 family protein( domain architecture ID 11475638)

UBP12 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
33-978 0e+00

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


:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 1132.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030  33 ISQKSISLgDASeisknLPsIAEQKQLIGElvnNQPELELGQVDNYILSYSWYERLCSYLAEDGPFPGPVDQEDIADLET 112
Cdd:COG5560  13 ASQNEIIA-PAS-----LP-LMMQEELIDE---KPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPGPIVQGPIVDFEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 113 GTLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPEFPRETVNLGSESHPhlVVEVYPPIFSLTLLST-NAVDANESHKPKK 191
Cdd:COG5560  83 ESLKKSLREGIDYSIISGAVWQLLVRWYGLAGLITPRITVLLPSESAP--EVESYPVVFKLHWLFSiNGSLINLGHDPVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 192 ISLSSKSTLEDLLEGVKYTLSLPSDQFRLWRVDTDQPLHRTIDPSSFIKINSKEIIDFLEKSKTLVELGMDSSCSLVAEC 271
Cdd:COG5560 161 HSASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 272 MINETWPVDRalrlqflIQQRNNQSSNEEqkqekrvPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNES 351
Cdd:COG5560 241 TRNPDWLVDS-------IVDDHNRSINKE-------AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEE 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 352 NPLGMGGQVASIFASLIKSLYSPEHSSFAPRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPD 431
Cdd:COG5560 307 NPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPD 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 432 LYEVDEEKIKNTAEECWRLHKLRNDSLIVDLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTN 511
Cdd:COG5560 387 LSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGR 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 512 LTPLAIEVVLESKAATIEDLVKYVAEKSGCSdyrKILVTETYKGRFYRFLTQLSKSLLMEISEEDEIYLYElerPYEDGs 591
Cdd:COG5560 467 RQPLKIELDASSTIRGLKKLVDAEYGKLGCF---EIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYE---TNDNG- 539
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 592 ddILVPVYHISDDStnsanSYMSSRDFGHPFvLQLSdneVTDASFISEKLklkyqqfttlknlknidSLESLELgheDEQ 671
Cdd:COG5560 540 --IEVPVVHLRIEK-----GYKSKRLFGDPF-LQLN---VLIKASIYDKL-----------------VKEFEEL---LVL 588
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 672 VQKGPLDVDMDHSQTPLfemrvfhDRFEKIPTGWnmsvsnLPLLTERDKKDLEstvdpldahSIEEEDdsefkdvapgsy 751
Cdd:COG5560 589 VEMKKTDVDLVSEQVRL-------LREESSPSSW------LKLETEIDTKREE---------QVEEEG------------ 634
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 752 pepsksnentklTAKENDRLLIQgdllvCEWPEKSYQFVFSVapsspqmgRSLWLESKTILSdkkddsedSRTITLNDCL 831
Cdd:COG5560 635 ------------QMNFNDAVVIS-----CEWEEKRYLSLFSY--------DPLWTIREIGAA--------ERTITLQDCL 681
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 832 DEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYklse 911
Cdd:COG5560 682 NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMV---- 757
                       890       900       910       920       930       940
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076030 912 kENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYRRKT 978
Cdd:COG5560 758 -DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
33-978 0e+00

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 1132.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030  33 ISQKSISLgDASeisknLPsIAEQKQLIGElvnNQPELELGQVDNYILSYSWYERLCSYLAEDGPFPGPVDQEDIADLET 112
Cdd:COG5560  13 ASQNEIIA-PAS-----LP-LMMQEELIDE---KPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPGPIVQGPIVDFEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 113 GTLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPEFPRETVNLGSESHPhlVVEVYPPIFSLTLLST-NAVDANESHKPKK 191
Cdd:COG5560  83 ESLKKSLREGIDYSIISGAVWQLLVRWYGLAGLITPRITVLLPSESAP--EVESYPVVFKLHWLFSiNGSLINLGHDPVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 192 ISLSSKSTLEDLLEGVKYTLSLPSDQFRLWRVDTDQPLHRTIDPSSFIKINSKEIIDFLEKSKTLVELGMDSSCSLVAEC 271
Cdd:COG5560 161 HSASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 272 MINETWPVDRalrlqflIQQRNNQSSNEEqkqekrvPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNES 351
Cdd:COG5560 241 TRNPDWLVDS-------IVDDHNRSINKE-------AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEE 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 352 NPLGMGGQVASIFASLIKSLYSPEHSSFAPRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPD 431
Cdd:COG5560 307 NPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPD 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 432 LYEVDEEKIKNTAEECWRLHKLRNDSLIVDLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTN 511
Cdd:COG5560 387 LSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGR 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 512 LTPLAIEVVLESKAATIEDLVKYVAEKSGCSdyrKILVTETYKGRFYRFLTQLSKSLLMEISEEDEIYLYElerPYEDGs 591
Cdd:COG5560 467 RQPLKIELDASSTIRGLKKLVDAEYGKLGCF---EIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYE---TNDNG- 539
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 592 ddILVPVYHISDDStnsanSYMSSRDFGHPFvLQLSdneVTDASFISEKLklkyqqfttlknlknidSLESLELgheDEQ 671
Cdd:COG5560 540 --IEVPVVHLRIEK-----GYKSKRLFGDPF-LQLN---VLIKASIYDKL-----------------VKEFEEL---LVL 588
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 672 VQKGPLDVDMDHSQTPLfemrvfhDRFEKIPTGWnmsvsnLPLLTERDKKDLEstvdpldahSIEEEDdsefkdvapgsy 751
Cdd:COG5560 589 VEMKKTDVDLVSEQVRL-------LREESSPSSW------LKLETEIDTKREE---------QVEEEG------------ 634
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 752 pepsksnentklTAKENDRLLIQgdllvCEWPEKSYQFVFSVapsspqmgRSLWLESKTILSdkkddsedSRTITLNDCL 831
Cdd:COG5560 635 ------------QMNFNDAVVIS-----CEWEEKRYLSLFSY--------DPLWTIREIGAA--------ERTITLQDCL 681
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 832 DEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYklse 911
Cdd:COG5560 682 NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMV---- 757
                       890       900       910       920       930       940
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076030 912 kENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYRRKT 978
Cdd:COG5560 758 -DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
825-975 2.13e-53

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: 185.95  E-value: 2.13e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 825 ITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMrt 904
Cdd:cd02674  84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP-- 161
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19076030 905 gSYKLSEKENPKLiYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYR 975
Cdd:cd02674 162 -YVDTRSFTGPFK-YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
311-541 1.78e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 180.72  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   311 CGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLGmggQVASIFASLIKSLYSP-EHSSFAPRQFKATIG 389
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI---NLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   390 KFNHSFLGYGQQDSQEFLAFLLDGLHEDLNriyqkpytskpdlyevdeekikntaeecwRLHKLRNDSLIVDLFQGMYRS 469
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN-----------------------------GNHSTENESLITDLFRGQLKS 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076030   470 TLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIpadtnltplaIEVVLESKAATIEDLVKYVAEKSGC 541
Cdd:pfam00443 129 RLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQ----------ICFLQFSKLEELDDEEKYYCDKCGC 190
DUSP smart00695
Domain in ubiquitin-specific proteases;
69-155 1.05e-23

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 95.89  E-value: 1.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030     69 ELELGQVdNYILSYSWYERLCSYLA-EDGPFPGPVDQEDIADLETG-TLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPE 146
Cdd:smart00695   1 PLEEGLT-WYLISTRWYRQWADFVEgKDGKDPGPIDNSGILCSHGGpRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGP 79

                   ....*....
gi 19076030    147 FPRETVNLG 155
Cdd:smart00695  80 IPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
33-978 0e+00

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 1132.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030  33 ISQKSISLgDASeisknLPsIAEQKQLIGElvnNQPELELGQVDNYILSYSWYERLCSYLAEDGPFPGPVDQEDIADLET 112
Cdd:COG5560  13 ASQNEIIA-PAS-----LP-LMMQEELIDE---KPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPGPIVQGPIVDFEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 113 GTLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPEFPRETVNLGSESHPhlVVEVYPPIFSLTLLST-NAVDANESHKPKK 191
Cdd:COG5560  83 ESLKKSLREGIDYSIISGAVWQLLVRWYGLAGLITPRITVLLPSESAP--EVESYPVVFKLHWLFSiNGSLINLGHDPVP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 192 ISLSSKSTLEDLLEGVKYTLSLPSDQFRLWRVDTDQPLHRTIDPSSFIKINSKEIIDFLEKSKTLVELGMDSSCSLVAEC 271
Cdd:COG5560 161 HSASSHGTLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 272 MINETWPVDRalrlqflIQQRNNQSSNEEqkqekrvPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNES 351
Cdd:COG5560 241 TRNPDWLVDS-------IVDDHNRSINKE-------AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEE 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 352 NPLGMGGQVASIFASLIKSLYSPEHSSFAPRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPD 431
Cdd:COG5560 307 NPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPD 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 432 LYEVDEEKIKNTAEECWRLHKLRNDSLIVDLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTN 511
Cdd:COG5560 387 LSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGR 466
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 512 LTPLAIEVVLESKAATIEDLVKYVAEKSGCSdyrKILVTETYKGRFYRFLTQLSKSLLMEISEEDEIYLYElerPYEDGs 591
Cdd:COG5560 467 RQPLKIELDASSTIRGLKKLVDAEYGKLGCF---EIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYE---TNDNG- 539
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 592 ddILVPVYHISDDStnsanSYMSSRDFGHPFvLQLSdneVTDASFISEKLklkyqqfttlknlknidSLESLELgheDEQ 671
Cdd:COG5560 540 --IEVPVVHLRIEK-----GYKSKRLFGDPF-LQLN---VLIKASIYDKL-----------------VKEFEEL---LVL 588
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 672 VQKGPLDVDMDHSQTPLfemrvfhDRFEKIPTGWnmsvsnLPLLTERDKKDLEstvdpldahSIEEEDdsefkdvapgsy 751
Cdd:COG5560 589 VEMKKTDVDLVSEQVRL-------LREESSPSSW------LKLETEIDTKREE---------QVEEEG------------ 634
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 752 pepsksnentklTAKENDRLLIQgdllvCEWPEKSYQFVFSVapsspqmgRSLWLESKTILSdkkddsedSRTITLNDCL 831
Cdd:COG5560 635 ------------QMNFNDAVVIS-----CEWEEKRYLSLFSY--------DPLWTIREIGAA--------ERTITLQDCL 681
                       810       820       830       840       850       860       870       880
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 832 DEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYklse 911
Cdd:COG5560 682 NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMV---- 757
                       890       900       910       920       930       940
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076030 912 kENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYRRKT 978
Cdd:COG5560 758 -DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
825-975 2.13e-53

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: 185.95  E-value: 2.13e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 825 ITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMrt 904
Cdd:cd02674  84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTP-- 161
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19076030 905 gSYKLSEKENPKLiYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYR 975
Cdd:cd02674 162 -YVDTRSFTGPFK-YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
311-541 1.78e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 180.72  E-value: 1.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   311 CGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLGmggQVASIFASLIKSLYSP-EHSSFAPRQFKATIG 389
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDI---NLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   390 KFNHSFLGYGQQDSQEFLAFLLDGLHEDLNriyqkpytskpdlyevdeekikntaeecwRLHKLRNDSLIVDLFQGMYRS 469
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN-----------------------------GNHSTENESLITDLFRGQLKS 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19076030   470 TLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIpadtnltplaIEVVLESKAATIEDLVKYVAEKSGC 541
Cdd:pfam00443 129 RLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQ----------ICFLQFSKLEELDDEEKYYCDKCGC 190
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
807-974 4.52e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 173.78  E-value: 4.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   807 ESKTILSDKKDDSEDSRTITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDK 886
Cdd:pfam00443 144 PFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEK 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   887 IDDLVEFPIDnLDMSmRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETV- 965
Cdd:pfam00443 224 LNTEVEFPLE-LDLS-RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVl 301

                  ....*....
gi 19076030   966 TSAAYLLFY 974
Cdd:pfam00443 302 SSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
818-975 3.26e-35

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: 134.92  E-value: 3.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 818 DSEDSRTITLNDCLDEFEKTEQLGEEDPWYCPTCKEfRQASKQMEIWRCPEILIFHLKRFSSERRFR-DKIDDLVEFPID 896
Cdd:cd02257  92 PVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSFPLE 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 897 NLDMSMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGG-HYTAFAKNPDNGQFYCFDDSRVTPVCPEE-----TVTSAAY 970
Cdd:cd02257 171 LDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADSgHYVAYVKDPSDGKWYKFNDDKVTEVSEEEvlefgSLSSSAY 250

                ....*
gi 19076030 971 LLFYR 975
Cdd:cd02257 251 ILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
798-974 1.29e-33

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 132.50  E-value: 1.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 798 PQMGRSLWLESKTILSDKKDDSEDSRTITLNDCLDEFEKTEQLGEeDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRF 877
Cdd:cd02660 149 PFLDLSLDIPNKSTPSWALGESGVSGTPTLSDCLDRFTRPEKLGD-FAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 878 --SSERRFRdKIDDLVEFPIDnLDM----SMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDnGQFYCF 951
Cdd:cd02660 228 ehSLNKTSR-KIDTYVQFPLE-LNMtpytSSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGD-GQWFKF 304
                       170       180
                ....*....|....*....|...
gi 19076030 952 DDSRVTPVCPEETVTSAAYLLFY 974
Cdd:cd02660 305 DDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
826-974 7.33e-30

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: 120.84  E-value: 7.33e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 826 TLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERrfRDKIDDLVEFPiDNLDMSmrtg 905
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GGKINKQISFP-ETLDLS---- 235
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19076030 906 SYkLSEKENPKLIYELYAVDNHYGGLGGG-HYTAFAKNPdNGQFYCFDDSRVTPVcPEETVTS-AAYLLFY 974
Cdd:cd02661 236 PY-MSQPNDGPLKYKLYAVLVHSGFSPHSgHYYCYVKSS-NGKWYNMDDSKVSPV-SIETVLSqKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-513 5.36e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 119.01  E-value: 5.36e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLG-MGGQVASIFASLiksLYSPEHSSFAPRQFKATIGK 390
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNScLSCAMDEIFQEF---YYSGDRSPYGPINLLYLSWK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 391 FNHSFLGYGQQDSQEFLAFLLDGLHEDlnriyqkpytskpdlyEVDEEKIKNTAEECwrlhklrndSLIVD-LFQGMYRS 469
Cdd:cd02660  79 HSRNLAGYSQQDAHEFFQFLLDQLHTH----------------YGGDKNEANDESHC---------NCIIHqTFSGSLQS 133
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19076030 470 TLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTNLT 513
Cdd:cd02660 134 SVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTPT 177
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
311-491 9.86e-27

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: 111.60  E-value: 9.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 311 CGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLGMggqvaSIFASLIKSLYSPEHSSFAPRQFKATIGK 390
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMM-----CALEAHVERALASSGPGSAPRIFSSNLKQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 391 FNHSFLGYGQQDSQEFLAFLLDGLHED-LNRiyqkpytsKPDLYEVDeekikntaeecwrlHKLRNDSLIVDLFQGMYRS 469
Cdd:cd02661  77 ISKHFRIGRQEDAHEFLRYLLDAMQKAcLDR--------FKKLKAVD--------------PSSQETTLVQQIFGGYLRS 134
                       170       180
                ....*....|....*....|..
gi 19076030 470 TLVCPVCNTVSITFDPFMDLTL 491
Cdd:cd02661 135 QVKCLNCKHVSNTYDPFLDLSL 156
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-504 8.01e-25

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: 103.91  E-value: 8.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTrelrdfftsdewknqvnesnplgmggqvasifaslikslyspehssfaprqfkatigkf 391
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 392 nhsflgygQQDSQEFLAFLLDGLHedlnriyqkpytskpdlyevdeekikntaeecwrlhklrndSLIVDLFQGMYRSTL 471
Cdd:cd02674  22 --------QQDAQEFLLFLLDGLH-----------------------------------------SIIVDLFQGQLKSRL 52
                       170       180       190
                ....*....|....*....|....*....|...
gi 19076030 472 VCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVT 504
Cdd:cd02674  53 TCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVT 85
DUSP smart00695
Domain in ubiquitin-specific proteases;
69-155 1.05e-23

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 95.89  E-value: 1.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030     69 ELELGQVdNYILSYSWYERLCSYLA-EDGPFPGPVDQEDIADLETG-TLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPE 146
Cdd:smart00695   1 PLEEGLT-WYLISTRWYRQWADFVEgKDGKDPGPIDNSGILCSHGGpRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGP 79

                   ....*....
gi 19076030    147 FPRETVNLG 155
Cdd:smart00695  80 IPRKVVCQG 88
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
816-975 4.78e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 97.07  E-value: 4.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 816 KDDSEDSRTItlNDCLDEFEKTEQLGEEDPWYCPTCKEfrqASKQMEIWRCPEILIFHLKRFSSERRFRD-KIDDLVEFP 894
Cdd:cd02667 104 SDEIKSECSI--ESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 895 iDNLDMSMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAK---------------------NPDNGQFYCFDD 953
Cdd:cd02667 179 -EILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeaGPGSGQWYYISD 257
                       170       180
                ....*....|....*....|..
gi 19076030 954 SRVTPVCPEETVTSAAYLLFYR 975
Cdd:cd02667 258 SDVREVSLEEVLKSEAYLLFYE 279
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
78-153 2.70e-20

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: 85.88  E-value: 2.70e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076030    78 YILSYSWYERLCSYLAEDGPFPGPVDQEDIAD-LETGTLKPDLQEEIDFTIISRDVWDLLVRWYGlKGPEFPRETVN 153
Cdd:pfam06337   5 YLISSKWLNKWKSYVKEPNNEPGPIDNSDLLDdESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG-GGPEIKRNVVN 80
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
312-496 4.43e-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: 91.01  E-value: 4.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTrelrdfftsdewknqvnesnplgmggqvasifaslikslyspehssfaprqfkatigkf 391
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 392 nhsflgygQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKpdlyevdeekikntaeecwrlhklRNDSLIVDLFQGMYRSTL 471
Cdd:cd02257  22 --------QQDAHEFLLFLLDKLHEELKKSSKRTSDSS------------------------SLKSLIHDLFGGKLESTI 69
                       170       180
                ....*....|....*....|....*
gi 19076030 472 VCPVCNTVSITFDPFMDLTLPLPVK 496
Cdd:cd02257  70 VCLECGHESVSTEPELFLSLPLPVK 94
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
827-977 1.87e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 84.62  E-value: 1.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 827 LNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFS--SERRFRDKIDDLVEFPiDNLDM---- 900
Cdd:cd02659 153 LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFP-LELDMepyt 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 901 --SMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEE--------------- 963
Cdd:cd02659 232 ekGLAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDaeeecfggeetqkty 311
                       170       180
                ....*....|....*....|.
gi 19076030 964 -------TVTSAAYLLFYRRK 977
Cdd:cd02659 312 dsgprafKRTTNAYMLFYERK 332
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-492 4.43e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 79.74  E-value: 4.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDFFTsdewknqvneSNPLGMGGQVasifaslikslyspehSSFAPRqfkatigkf 391
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLS----------ETPKELFSQV----------------CRKAPQ--------- 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 392 nhsFLGYGQQDSQEFLAFLLDGLhedlnriyqkpytskpdlyevdeekikntaeecwrlhklrndSLIVD-LFQGMYRST 470
Cdd:cd02667  46 ---FKGYQQQDSHELLRYLLDGL------------------------------------------RTFIDsIFGGELTST 80
                       170       180
                ....*....|....*....|..
gi 19076030 471 LVCPVCNTVSITFDPFMDLTLP 492
Cdd:cd02667  81 IMCESCGTVSLVYEPFLDLSLP 102
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
825-974 2.16e-15

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 78.12  E-value: 2.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 825 ITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFS-SERRFR-DKIDDLVEFPidnLDMSM 902
Cdd:cd02663 147 TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRyIKLFYRVVFP---LELRL 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 903 RTGSyklSEKENPKLIYELYAVDNHY-GGLGGGHYTAFAKNpdNGQFYCFDDSRVTPVcPEETVTS---------AAYLL 972
Cdd:cd02663 224 FNTT---DDAENPDRLYELVAVVVHIgGGPNHGHYVSIVKS--HGGWLLFDDETVEKI-DENAVEEffgdspnqaTAYVL 297

                ..
gi 19076030 973 FY 974
Cdd:cd02663 298 FY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
826-975 2.16e-15

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 78.23  E-value: 2.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 826 TLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSER--RFRDKIDDLVEFPiDNLDMSMR 903
Cdd:cd02668 157 TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLNASISFP-EILDMGEY 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 904 tgsykLSEKENPKLIYELYAVDNHY-GGLGGGHYTAFAKNPDNGQFYCFDDSRVTPV--------------------CPE 962
Cdd:cd02668 236 -----LAESDEGSYVYELSGVLIHQgVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMpgkplklgnsedpakprkseIKK 310
                       170
                ....*....|....
gi 19076030 963 ET-VTSAAYLLFYR 975
Cdd:cd02668 311 GThSSRTAYMLVYK 324
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-494 1.81e-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: 75.44  E-value: 1.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNP-LGMGGQVASIFASL------IKSLYSPEHSSF----A 380
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPaNDLNCQLIKLADGLlsgrysKPASLKSENDPYqvgiK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 381 PRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDglhedlnriyqkpytskpdlyEVDEEKIKNTAEEcwrlhklrndslIV 460
Cdd:cd02658  81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLID---------------------KLDRESFKNLGLN------------PN 127
                       170       180       190
                ....*....|....*....|....*....|....
gi 19076030 461 DLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLP 494
Cdd:cd02658 128 DLFKFMIEDRLECLSCKKVKYTSELSEILSLPVP 161
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
826-977 2.71e-13

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 71.37  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 826 TLNDCLDEFE------KTEQLGEEDPWycptcKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRdKIDDLVEfpiDNLD 899
Cdd:COG5533 138 TLQEFIDNMEelvddeTGVKAKENEEL-----EVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQ-KIDTEVD---EKFE 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 900 MSMRTGSYKLSEKEnpkLIYELYAVDNHYGGLGGGHYTAFAKNpdNGQFYCFDDSRVTPVCPEETVTSA---AYLLFYRR 976
Cdd:COG5533 209 LPVKHDQILNIVKE---TYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDSDVTPVSEEEAINEKaknAYLYFYER 283

                .
gi 19076030 977 K 977
Cdd:COG5533 284 I 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-494 2.02e-12

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 69.44  E-value: 2.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLthtrelrdfFTSDEWKNQVNESNPLGMGGQVASIFAsLIKSLYSPEHSSfapRQFKATIGKF 391
Cdd:cd02664   1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKK-LQLLQAHLMHTQ---RRAEAPPDYF 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 392 NHS-----FLGYGQQDSQEFLAFLLDGLHedlnriyqkpytskpdlyevdeekikntaeecwrlhklrndSLIVDLFQGM 466
Cdd:cd02664  68 LEAsrppwFTPGSQQDCSEYLRYLLDRLH-----------------------------------------TLIEKMFGGK 106
                       170       180
                ....*....|....*....|....*...
gi 19076030 467 YRSTLVCPVCNTVSITFDPFMDLTLPLP 494
Cdd:cd02664 107 LSTTIRCLNCNSTSARTERFRDLDLSFP 134
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-494 5.97e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 67.72  E-value: 5.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHT---RELRDFFTSdewknqVNESNPLgmGGQVasifaslikslyspehssfAPRQFKATI 388
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYFEnllTCLKDLFES------ISEQKKR--TGVI-------------------SPKKFITRL 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 389 GKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPDLYEVDEEKIKNtaeecWrlhklrndslIVDLFQGMYR 468
Cdd:cd02663  54 KRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPT-----W----------VHEIFQGILT 118
                       170       180
                ....*....|....*....|....*.
gi 19076030 469 STLVCPVCNTVSITFDPFMDLTLPLP 494
Cdd:cd02663 119 NETRCLTCETVSSRDETFLDLSIDVE 144
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
826-975 7.07e-12

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 67.90  E-value: 7.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 826 TLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFS--SERRFRDKIDDLVEFPIDnLDMSMR 903
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIMDNVSINEV-LSLPVR 213
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 904 TGSYKLSEKENPKLI--------------YELYAVDNHY-GGLGGGHYTAFAKNP--------------------DNGQF 948
Cdd:cd02664 214 VESKSSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSgYSSESGHYFTYARDQtdadstgqecpepkdaeendESKNW 293
                       170       180       190
                ....*....|....*....|....*....|....
gi 19076030 949 YCFDDSRVTPVCPEE--TVTS-----AAYLLFYR 975
Cdd:cd02664 294 YLFNDSRVTFSSFESvqNVTSrfpkdTPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
811-975 9.32e-11

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 64.53  E-value: 9.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 811 ILSDKKDDSEDSRTI---------TLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSER 881
Cdd:cd02671 157 VQESELSKSEESSEIspdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANG 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 882 RFRDKIDDL--VEFPIDN-LDMSMrtgsYKLSEKENpKLIYELYAVDNHY-GGLGGGHYTAFAKnpdngqFYCFDDSRV- 956
Cdd:cd02671 237 SEFDCYGGLskVNTPLLTpLKLSL----EEWSTKPK-NDVYRLFAVVMHSgATISSGHYTAYVR------WLLFDDSEVk 305
                       170       180
                ....*....|....*....|....*..
gi 19076030 957 --------TPVCPEETVTSAAYLLFYR 975
Cdd:cd02671 306 vteekdflEALSPNTSSTSTPYLLFYK 332
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-493 9.54e-11

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 64.36  E-value: 9.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDFF-----TSDEWKNQVNESNPL---GMGGQVASIFASLIKSlyspEHSSFAPRQ 383
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnsTEDAELKNMPPDKPHepqTIIDQLQLIFAQLQFG----NRSVVDPSG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 384 FKATIGKFNHSflgygQQDSQEFLAFLLDGLHEDLnriyqkpytskpdlyevdeEKIKNTaeecwrlhKLRNdsLIVDLF 463
Cdd:cd02668  77 FVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKL-------------------SKSKNP--------DLKN--IVQDLF 122
                       170       180       190
                ....*....|....*....|....*....|
gi 19076030 464 QGMYRSTLVCPVCNTVSITFDPFMDLTLPL 493
Cdd:cd02668 123 RGEYSYVTQCSKCGRESSLPSKFYELELQL 152
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
309-491 1.47e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 63.82  E-value: 1.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 309 GTCGLSNLGNTCYMNSALQCLTHTRELR-DFFTSDEWKNQVNESN-PLGMggQVASIFASL-IKSLYSPEhssfaprqFK 385
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTPEFRnAVYSIPPTEDDDDNKSvPLAL--QRLFLFLQLsESPVKTTE--------LT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 386 ATIGKFNHSFL-GYGQQDSQEFLAFLLDGLhedlnriyqkpytskpdlyevdEEKIKNTAEEcwrlhklrndSLIVDLFQ 464
Cdd:cd02659  71 DKTRSFGWDSLnTFEQHDVQEFFRVLFDKL----------------------EEKLKGTGQE----------GLIKNLFG 118
                       170       180
                ....*....|....*....|....*..
gi 19076030 465 GMYRSTLVCPVCNTVSITFDPFMDLTL 491
Cdd:cd02659 119 GKLVNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-446 4.17e-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 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: 61.96  E-value: 4.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDfftsdewknQVNESNPLGMGGQVAS--IFASLiKSLY---SPEHSSFAPRQFKA 386
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRD---------ALKNYNPARRGANQSSdnLTNAL-RDLFdtmDKKQEPVPPIEFLQ 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076030 387 TIGKFNHSFL------GYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPDLYEVDEEKIKNTAEE 446
Cdd:cd02657  71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQLFGIELETKMKCTESP 136
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
307-494 4.58e-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: 63.11  E-value: 4.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 307 VPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTS-DEWKNQVNESNPLGmggqvaSIFASLIKSLYSPE--HSSFAPRQ 383
Cdd:cd02669 116 LPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyENYENIKDRKSELV------KRLSELIRKIWNPRnfKGHVSPHE 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 384 FKATIGKFNHSFLGYGQQ-DSQEFLAFLLDGLHEDLNRiYQKPYTSKPD-----LYEVDEEKIKNTAEECWRLHKLRNDS 457
Cdd:cd02669 190 LLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHdcfqgKVQIETQKIKPHAEEEGSKDKFFKDS 268
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19076030 458 livdlfqgmyrstlvcpvcNTVSITFDPFMDLTLPLP 494
Cdd:cd02669 269 -------------------RVKKTSVSPFLLLTLDLP 286
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
849-975 1.09e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 61.95  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 849 PTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYKLSekENPKLIYELYAVDNHY 928
Cdd:cd02669 315 KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPS--LNLSTKYNLVANIVHE 392
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19076030 929 GGLGGGH-YTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYR 975
Cdd:cd02669 393 GTPQEDGtWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-423 4.42e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 59.14  E-value: 4.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCL-------THTRELRDFFTSDEWKNQVNESNPlgmggqvasifaslikSLYSPEHSSFAPRQF 384
Cdd:cd02671  26 GLNNLGNTCYLNSVLQVLyfcpgfkHGLKHLVSLISSVEQLQSSFLLNP----------------EKYNDELANQAPRRL 89
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19076030 385 KATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQ 423
Cdd:cd02671  90 LNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEKDFQ 128
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
823-974 1.77e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 56.22  E-value: 1.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 823 RTITLNDCLDEFEKTEQLgeEDPwYCPTCKEFrqaskqmeIWRCPEILIFHLKRFSserrfrdkiddlvefpidnldMSM 902
Cdd:cd02662  94 SGTTLEHCLDDFLSTEII--DDY-KCDRCQTV--------IVRLPQILCIHLSRSV---------------------FDG 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 903 RTGSYKLSEKEN-----PKLIYELYAVDNHYGGLGGGHYTAFAKNPDN--------------------GQFYCFDDSRVT 957
Cdd:cd02662 142 RGTSTKNSCKVSfperlPKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmregpsstsHPWWRISDTTVK 221
                       170
                ....*....|....*....
gi 19076030 958 pVCPEETV--TSAAYLLFY 974
Cdd:cd02662 222 -EVSESEVleQKSAYMLFY 239
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
826-957 2.86e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 57.96  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030  826 TLNDCLDEFEKTEQLGEEDPWYCPTcKEFRQASKQMEIWRCPEILIFHLKRFSS--ERRFRDKIDDLVEFPiDNLDMSMR 903
Cdd:COG5077  339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYdfERDMMVKINDRYEFP-LEIDLLPF 416
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19076030  904 TgSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVT 957
Cdd:COG5077  417 L-DRDADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVT 469
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
838-975 1.89e-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 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: 53.87  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 838 EQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRF--RDKIDDLVEFPIdNLDmsmrtgsykLSEKENP 915
Cdd:cd02657 168 KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIqkKAKILRKVKFPF-ELD---------LYELCTP 237
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19076030 916 KLIYELYAVDNHYGGLGGG-HYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSA-------AYLLFYR 975
Cdd:cd02657 238 SGYYELVAVITHQGRSADSgHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
312-418 2.03e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 53.65  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRE------LRDFFTSDEWKNQVNESNPLGMGGQVASIFASLIKslySPEHssfaprqfk 385
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILALYLPkldellDDLSKELKVLKNVIRKPEPDLNQEEALKLFTALWS---SKEH--------- 68
                        90       100       110
                ....*....|....*....|....*....|...
gi 19076030 386 atigKFNHSFLGYGQQDSQEFLAFLLDGLHEDL 418
Cdd:COG5533  69 ----KVGWIPPMGSQEDAHELLGKLLDELKLDL 97
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
519-648 8.32e-05

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


Pssm-ID: 464201  Cd Length: 204  Bit Score: 44.78  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030   519 VVLESKAATIEDLVKYVAEKSGCSDY--RKILVTETYKGRFYRFLT--------QLSKSLLMEISEEDEIYLYELERpye 588
Cdd:pfam14533  36 ELLVPKNGTVADLLEELQKKVKLSEEgsGKIRLYEVSNHKIYKELSedepidslNDYLTLYAEEIPEEELNLDEGER--- 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19076030   589 dgsddiLVPVYHISDDSTNSansymssrdFGHPFVLQLSDNEvtdaSF------ISEKLKLKYQQF 648
Cdd:pfam14533 113 ------LIPVFHFQKEPSRT---------HGIPFLFVLKPGE----PFsdtkkrLQKRLGLPDKEF 159
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-443 2.11e-04

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 44.79  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDF-FTSDEWKNQVNESNPLG--MGGQ--------VASIFA----SLIKSLYSPEH 376
Cdd:cd02666   3 GLDNIGNTCYLNSLLQYFFTIKPLRDLvLNFDESKAELASDYPTErrIGGRevsrselqRSNQFVyelrSLFNDLIHSNT 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19076030 377 SSFAPRQFKAtigkfnhsFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPDLYEVDEEKIKNT 443
Cdd:cd02666  83 RSVTPSKELA--------YLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRL 141
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-338 7.40e-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: 42.35  E-value: 7.40e-04
                        10        20
                ....*....|....*....|....*..
gi 19076030 312 GLSNLGNTCYMNSALQCLTHTRELRDF 338
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
 
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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