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Conserved domains on  [gi|42516565|ref|NP_963918|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform 2 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031674)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-681 2.04e-70

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 235.80  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   311 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 390
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   391 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 470
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   471 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDE 550
Cdd:pfam00443 145 FSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLEE 176

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   551 LKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYD 627
Cdd:pfam00443 177 LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYR 255

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42516565   628 LLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 681
Cdd:pfam00443 256 LVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
809-893 5.33e-30

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.61  E-value: 5.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565    809 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 885
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*...
gi 42516565    886 LRPPVVHV 893
Cdd:smart00695  81 PRKVVCQG 88
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 7.21e-18

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 7.21e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42516565    30 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP super family cl12116
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 703-772 1.38e-15

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.


The actual alignment was detected with superfamily member smart00695:

Pssm-ID: 416436  Cd Length: 88  Bit Score: 72.78  E-value: 1.38e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42516565    703 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 772
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-681 2.04e-70

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 235.80  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   311 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 390
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   391 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 470
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   471 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDE 550
Cdd:pfam00443 145 FSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLEE 176

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   551 LKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYD 627
Cdd:pfam00443 177 LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYR 255

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42516565   628 LLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 681
Cdd:pfam00443 256 LVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 442-682 5.74e-62

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: 209.45  E-value: 5.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 442 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvkr 521
Cdd:cd02674  38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 522 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTH 601
Cdd:cd02674  82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 602 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 681
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229


                .
gi 42516565 682 R 682
Cdd:cd02674 230 E 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
149-685 6.53e-44

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 171.60  E-value: 6.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 149 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPTTL 222
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 223 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 288
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 289 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 341
Cdd:COG5560 420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 342 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 419
Cdd:COG5560 500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 420 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 496
Cdd:COG5560 569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 497 VKAGSCgeAYAPQGWIAFFmeyvkrfvvSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVK 570
Cdd:COG5560 641 AVVISC--EWEEKRYLSLF---------SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASK 709

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 571 FCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRN 649
Cdd:COG5560 710 QMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARN 787

                       570       580       590
                ....*....|....*....|....*....|....*.
gi 42516565 650 NLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSS 685
Cdd:COG5560 788 FANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
DUSP smart00695
Domain in ubiquitin-specific proteases;
809-893 5.33e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.61  E-value: 5.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565    809 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 885
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*...
gi 42516565    886 LRPPVVHV 893
Cdd:smart00695  81 PRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 815-887 1.51e-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: 86.65  E-value: 1.51e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42516565   815 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 887
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 7.21e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 7.21e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42516565    30 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP smart00695
Domain in ubiquitin-specific proteases;
703-772 1.38e-15

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 72.78  E-value: 1.38e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42516565    703 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 772
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 709-779 5.16e-12

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: 62.39  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   709 FYISRQWLNKFKTFAE-----PGPISNNDFLCihggvPPRKAGYIEDLVL-----MLPQNIWDNLYSRYGGGPAVNHLYI 778
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQEgvdyvIVPEEVWEFLVEWYGGGPEIKRNVV 79


                  .
gi 42516565   779 C 779
Cdd:pfam06337  80 N 80
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
29-81 1.77e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 42516565     29 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 81
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-681 2.04e-70

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 235.80  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   311 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 390
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   391 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 470
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   471 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDE 550
Cdd:pfam00443 145 FSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLEE 176

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   551 LKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYD 627
Cdd:pfam00443 177 LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYR 255

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 42516565   628 LLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 681
Cdd:pfam00443 256 LVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 442-682 5.74e-62

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: 209.45  E-value: 5.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 442 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvkr 521
Cdd:cd02674  38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 522 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTH 601
Cdd:cd02674  82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 602 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 681
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229


                .
gi 42516565 682 R 682
Cdd:cd02674 230 E 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 430-682 1.65e-53

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: 186.92  E-value: 1.65e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 430 SPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapq 509
Cdd:cd02257  43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 510 gwiaffmeyvkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQNFPEILCIHLKRFR 589
Cdd:cd02257  97 ------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFS 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 590 H-ELMFSTKISTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQS 662
Cdd:cd02257 152 FnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDK 230

                       250       260
                ....*....|....*....|....*
gi 42516565 663 VTEVSESTVQ-----NAEAYVLFYR 682
Cdd:cd02257 231 VTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 155-681 8.98e-47

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: 170.25  E-value: 8.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLD---CGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNP 231
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 232 TFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenenGSRCFSED 311
Cdd:cd02660  82 NLAGYSQQDAHEFFQFLLDQLHTHYG----------------------------------------------GDKNEAND 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 312 NNEttmliqddennsemskdwqkekmCNKInkvnsegefdkdrdsisetvdlnnqetvkvqIHSraseyitdvhsndlst 391
Cdd:cd02660 116 ESH-----------------------CNCI-------------------------------IHQ---------------- 125

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 392 pqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrkkqhkkyrsvisdIFDGTIISSVQCLTCDRVSVTLETF 471
Cdd:cd02660 126 -------------------------------------------------------TFSGSLQSSVTCQRCGGVSTTVDPF 150

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 472 QDLSLPIPGKEdlaklhssshpTSIVKAGSCGEAYAPqgwiaffmeyvkrfvvscvpswfwgpvvTLQDCLAaFFARDEL 551
Cdd:cd02660 151 LDLSLDIPNKS-----------TPSWALGESGVSGTP----------------------------TLSDCLD-RFTRPEK 190

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 552 KGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPAQ 622
Cdd:cd02660 191 LGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDP 269

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42516565 623 IVTYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 681
Cdd:cd02660 270 DYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 154-681 4.07e-46

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: 167.84  E-value: 4.07e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDcGGLARTDKKPAICKS-YLKLMTELWHKSRPGSVVPTTLFQGIKTVNPT 232
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 233 FRGYSQQDAQEFLRCLMDLLHEelkeqvmeveedpqtitteetmeedksqsdvdfqsceSCSNSdraenengsrcfsedn 312
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQK-------------------------------------ACLDR---------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 313 nettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndlstp 392
Cdd:cd02661     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 393 qilpsnegvNPRLSASPPKSgnlwpglapphkkaqsaspkrkkqhkKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQ 472
Cdd:cd02661 108 ---------FKKLKAVDPSS--------------------------QETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 473 DLSLPIPGkedlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfwgpVVTLQDCLAAFFARDELK 552
Cdd:cd02661 153 DLSLDIKG------------------------------------------------------ADSLEDALEQFTKPEQLD 178

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 553 GDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVI 632
Cdd:cd02661 179 GENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVL 254

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 42516565 633 CHHGT-ASSGHYIAYCRnNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 681
Cdd:cd02661 255 VHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
149-685 6.53e-44

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 171.60  E-value: 6.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 149 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPTTL 222
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 223 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 288
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 289 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 341
Cdd:COG5560 420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 342 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 419
Cdd:COG5560 500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 420 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 496
Cdd:COG5560 569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 497 VKAGSCgeAYAPQGWIAFFmeyvkrfvvSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVK 570
Cdd:COG5560 641 AVVISC--EWEEKRYLSLF---------SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASK 709

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 571 FCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRN 649
Cdd:COG5560 710 QMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARN 787

                       570       580       590
                ....*....|....*....|....*....|....*.
gi 42516565 650 NLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSS 685
Cdd:COG5560 788 FANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 444-685 4.19e-37

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: 142.78  E-value: 4.19e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 444 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLaklhssshptsivkagscgeayapqgwiaffmeyvkrfv 523
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 524 vscvpswfwgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH--ELMFSTKISTH 601
Cdd:cd02659 154 ---------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 602 VSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 671
Cdd:cd02659 219 FEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDA 297

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42516565 672 QNA----------------------EAYVLFYRKSS 685
Cdd:cd02659 298 EEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 441-682 3.93e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 129.43  E-value: 3.93e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 441 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvk 520
Cdd:cd02667  66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 521 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQNFPEILCIHLKRFRHELMFST-KIS 599
Cdd:cd02667 109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 600 THVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL---------------- 654
Cdd:cd02667 173 RHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagp 247

                       250       260       270
                ....*....|....*....|....*....|..
gi 42516565 655 ----WYEFDDQSVTEVSESTVQNAEAYVLFYR 682
Cdd:cd02667 248 gsgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 444-681 1.61e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 122.42  E-value: 1.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 444 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklHSSshptsivkagscgeayapqgwiaffmeyvkrfv 523
Cdd:cd02663 109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 524 vscvpswfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS--TKISTH 601
Cdd:cd02663 149 --------------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYR 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 602 VSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTVQN------ 673
Cdd:cd02663 215 VVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAVEEffgdsp 289

                       250
                ....*....|
gi 42516565 674 --AEAYVLFY 681
Cdd:cd02663 290 nqATAYVLFY 299
DUSP smart00695
Domain in ubiquitin-specific proteases;
809-893 5.33e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.61  E-value: 5.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565    809 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 885
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*...
gi 42516565    886 LRPPVVHV 893
Cdd:smart00695  81 PRKVVCQG 88
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 434-665 7.58e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 118.29  E-value: 7.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 434 KKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshptsivkagscgeayapqgwia 513
Cdd:cd02668 108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 514 ffmeyvkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL- 592
Cdd:cd02668 157 -----------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRk 213

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42516565 593 -MFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 665
Cdd:cd02668 214 tGAKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 448-681 7.49e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 104.37  E-value: 7.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 448 FDGTIISSVQCLTCDRVS-VTLETFQDLSLPIPGKedlaklhSSSHPTsivkagscgeayapqgwiaffmeyvkrfvvsc 526
Cdd:cd02662  56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 527 vpswfwgpvvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQNFPEILCIHLKRFR-HELMFSTKISTHVSFP 605
Cdd:cd02662  97 ----------TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 606 LegldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTE 665
Cdd:cd02662 156 E-------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKE 222

                       250
                ....*....|....*..
gi 42516565 666 VSESTV-QNAEAYVLFY 681
Cdd:cd02662 223 VSESEVlEQKSAYMLFY 239
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 442-682 1.26e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 99.87  E-value: 1.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 442 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLpipgkedlaklhssshptsivkagscgeayapqgwiaffmeyvkr 521
Cdd:cd02664  97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 522 fvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFR--HELMFSTKIS 599
Cdd:cd02664 132 ----SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIM 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 600 THVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN----------- 649
Cdd:cd02664 200 DNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqec 278

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42516565 650 ---------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 682
Cdd:cd02664 279 pepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 441-682 3.48e-21

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 95.73  E-value: 3.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 441 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdLAKLHSSSHPTSIVKAgscgeayapqgwiaffmeyvk 520
Cdd:cd02671 120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 521 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS----- 595
Cdd:cd02671 178 -------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygg 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 596 -TKISTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------T 664
Cdd:cd02671 245 lSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflE 314

                       250
                ....*....|....*...
gi 42516565 665 EVSESTVQNAEAYVLFYR 682
Cdd:cd02671 315 ALSPNTSSTSTPYLLFYK 332
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 815-887 1.51e-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: 86.65  E-value: 1.51e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42516565   815 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 887
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 537-671 6.89e-19

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 92.24  E-value: 6.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565  537 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQNFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 612
Cdd:COG5077  339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42516565  613 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 671
Cdd:COG5077  415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 7.21e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 7.21e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42516565    30 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 578-682 2.14e-16

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 80.84  E-value: 2.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 578 PEILCIHLKRF--RHELMFSTKISTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 654
Cdd:cd02657 197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270

                        90       100       110
                ....*....|....*....|....*....|....*
gi 42516565 655 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 682
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
DUSP smart00695
Domain in ubiquitin-specific proteases;
703-772 1.38e-15

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 72.78  E-value: 1.38e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42516565    703 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 772
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 433-682 2.45e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 77.75  E-value: 2.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 433 RKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSshptsivkagscgEAYAPqgwi 512
Cdd:cd02658 115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP---- 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 513 affmeyvkrfvvscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL 592
Cdd:cd02658 178 -----------------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLE 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 593 MF-STKISTHVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSE 668
Cdd:cd02658 231 NWvPKKLDVPIDVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQD 297

                       250
                ....*....|....
gi 42516565 669 STVQNAEAYVLFYR 682
Cdd:cd02658 298 PPEMKKLGYIYFYQ 311
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
578-683 6.70e-15

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 75.99  E-value: 6.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 578 PEILCIHLKRFRHELMFsTKISTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlNNL 654
Cdd:COG5533 180 PKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--GGK 251

                        90       100       110
                ....*....|....*....|....*....|..
gi 42516565 655 WYEFDDQSVTEVSESTVQNA---EAYVLFYRK 683
Cdd:COG5533 252 WEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 578-682 4.33e-14

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 75.43  E-value: 4.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 578 PEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT-ASSGHYIAYCRNNLNNL 654
Cdd:cd02669 333 PKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNK 412

                        90       100
                ....*....|....*....|....*...
gi 42516565 655 WYEFDDQSVTEVSESTVQNAEAYVLFYR 682
Cdd:cd02669 413 WFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 155-257 1.03e-12

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 70.05  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPTTLFQGIKTVNPT 232
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 42516565 233 F------RGYSQQDAQEFLRCLMDLLHEELK 257
Cdd:cd02657  79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLP 109
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 709-779 5.16e-12

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: 62.39  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   709 FYISRQWLNKFKTFAE-----PGPISNNDFLCihggvPPRKAGYIEDLVL-----MLPQNIWDNLYSRYGGGPAVNHLYI 778
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQEgvdyvIVPEEVWEFLVEWYGGGPEIKRNVV 79


                  .
gi 42516565   779 C 779
Cdd:pfam06337  80 N 80
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 626-681 3.84e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 62.51  E-value: 3.84e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42516565 626 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 681
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
29-81 1.77e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 42516565     29 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 81
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 559-681 2.17e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 59.08  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 559 CEKCKKlRNGVKFCKVQNFPEILCIHLKRFRhelmFSTKISTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 632
Cdd:cd02673 129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42516565 633 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 681
Cdd:cd02673 191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
155-252 2.04e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.73  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 155 GLKNIGNTCYMNAALQALS-NCPPLTQFFLDCGGLART-------DKKPAICKSYLKLMTELWHKSRPgsvvpttlfqgi 226
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68

                        90       100
                ....*....|....*....|....*.
gi 42516565 227 kTVNPTFRGYSQQDAQEFLRCLMDLL 252
Cdd:COG5533  69 -KVGWIPPMGSQEDAHELLGKLLDEL 93
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 578-681 8.15e-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: 54.10  E-value: 8.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 578 PEILCIHLKRFRHELMFSTKISTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYE 657
Cdd:cd02665 129 PPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195

                        90       100       110
                ....*....|....*....|....*....|..
gi 42516565 658 FDDQSVTEVSESTVQ--------NAEAYVLFY 681
Cdd:cd02665 196 YNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
559-663 1.95e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 53.81  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565   559 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHElmFSTKISTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 637
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272

                          90       100       110
                  ....*....|....*....|....*....|...
gi 42516565   638 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 663
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 559-681 3.13e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 52.90  E-value: 3.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 559 CEKCKKLRNGVKFCKVQNFPEI----LCIHLKRF-------RHELMFSTKISTHVSFPLEglDLQPFLAKDSPAQIVTYD 627
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42516565 628 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 681
Cdd:cd02672 215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 521-682 4.68e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 51.76  E-value: 4.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 521 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscekckklRNGVkFCKVqnfPEILCIHLKRFRHELMFSTKIST 600
Cdd:cd02670  65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV-FAKA---PSCLIICLKRYGKTEGKAQKMFK 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42516565 601 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 650
Cdd:cd02670 122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42516565 651 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 682
Cdd:cd02670 201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
 
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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