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Conserved domains on  [gi|1794418801|ref|NP_001364362|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform 7 [Homo sapiens]

Protein Classification

Peptidase_C19R and DUSP domain-containing protein( domain architecture ID 12031705)

protein containing domains zf-UBP, Peptidase_C19R, and DUSP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-671 1.04e-48

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDE 581
Cdd:pfam00443 145 FSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLEE 176
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 582 LKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYD 658
Cdd:pfam00443 177 LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYR 255
                         490
                  ....*....|...
gi 1794418801 659 LLSVICHHGTASS 671
Cdd:pfam00443 256 LVAVVVHSGSLSS 268
DUSP smart00695
Domain in ubiquitin-specific proteases;
741-825 2.77e-30

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.77e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801  741 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 817
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 1794418801  818 LRPPVVHV 825
Cdd:smart00695  81 PRKVVCQG 88
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 6.35e-18

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 6.35e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418801  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-671 1.04e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDE 581
Cdd:pfam00443 145 FSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLEE 176
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 582 LKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYD 658
Cdd:pfam00443 177 LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYR 255
                         490
                  ....*....|...
gi 1794418801 659 LLSVICHHGTASS 671
Cdd:pfam00443 256 LVAVVVHSGSLSS 268
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
473-671 7.77e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 138.19  E-value: 7.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvkr 552
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 553 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTH 632
Cdd:cd02674    82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1794418801 633 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASS 671
Cdd:cd02674   150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNG 188
DUSP smart00695
Domain in ubiquitin-specific proteases;
741-825 2.77e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.77e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801  741 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 817
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 1794418801  818 LRPPVVHV 825
Cdd:smart00695  81 PRKVVCQG 88
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-671 1.24e-26

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 116.91  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 180 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKK---PAICKSYLKLMTELwHKSRPGSVVPTTL 253
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLgmhGSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 254 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 319
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 320 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 372
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 373 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 450
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 451 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 527
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 528 VKAGSCgeAYAPQGWIAFFmeyvkrfvvSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVK 601
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF---------SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASK 709
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418801 602 FCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASS 671
Cdd:COG5560   710 QMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSG 778
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
747-819 6.80e-21

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 87.42  E-value: 6.80e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418801 747 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 819
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 6.35e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 6.35e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418801  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
60-112 1.84e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.84e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1794418801   60 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 112
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-671 1.04e-48

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 174.94  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDE 581
Cdd:pfam00443 145 FSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLEE 176
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 582 LKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYD 658
Cdd:pfam00443 177 LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYR 255
                         490
                  ....*....|...
gi 1794418801 659 LLSVICHHGTASS 671
Cdd:pfam00443 256 LVAVVVHSGSLSS 268
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
473-671 7.77e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 138.19  E-value: 7.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvkr 552
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 553 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTH 632
Cdd:cd02674    82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1794418801 633 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASS 671
Cdd:cd02674   150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNG 188
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
461-671 4.89e-33

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: 128.37  E-value: 4.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 461 SPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapq 540
Cdd:cd02257    43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 541 gwiaffmeyvkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQNFPEILCIHLKRFR 620
Cdd:cd02257    97 ------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1794418801 621 H-ELMFSTKISTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGTASS 671
Cdd:cd02257   152 FnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTSAD 207
DUSP smart00695
Domain in ubiquitin-specific proteases;
741-825 2.77e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.77e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801  741 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 817
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 1794418801  818 LRPPVVHV 825
Cdd:smart00695  81 PRKVVCQG 88
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
185-671 3.13e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 118.53  E-value: 3.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDcGGLARTDKKPAICKS-YLKLMTELWHKSRPGSVVPTTLFQGIKTVNPT 263
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 264 FRGYSQQDAQEFLRCLMDLLHEelkeqvmeveedpqtitteetmeedksqsdvdfqsceSCSNSdraenengsrcfsedn 343
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQK-------------------------------------ACLDR---------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 344 nettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndlstp 423
Cdd:cd02661       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 424 qilpsnegvNPRLSASPPKSgnlwpglapphkkaqsaspkrkkqhkKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQ 503
Cdd:cd02661   108 ---------FKKLKAVDPSS--------------------------QETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 504 DLSLPIPGkedlaklhssshptsivkagscgeayapqgwiaffmeyvkrfvvscvpswfwgpVVTLQDCLAAFFARDELK 583
Cdd:cd02661   153 DLSLDIKG------------------------------------------------------ADSLEDALEQFTKPEQLD 178
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 584 GDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVI 663
Cdd:cd02661   179 GENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVL 254

                  ....*...
gi 1794418801 664 CHHGTASS 671
Cdd:cd02661   255 VHSGFSPH 262
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-668 4.08e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 113.24  E-value: 4.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLD---CGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNP 262
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 263 TFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenenGSRCFSED 342
Cdd:cd02660    82 NLAGYSQQDAHEFFQFLLDQLHTHYG----------------------------------------------GDKNEAND 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 343 NNEttmliqddennsemskdwqkekmCNKInkvnsegefdkdrdsisetvdlnnqetvkvqIHSraseyitdvhsndlst 422
Cdd:cd02660   116 ESH-----------------------CNCI-------------------------------IHQ---------------- 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 423 pqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrkkqhkkyrsvisdIFDGTIISSVQCLTCDRVSVTLETF 502
Cdd:cd02660   126 -------------------------------------------------------TFSGSLQSSVTCQRCGGVSTTVDPF 150
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 503 QDLSLPIPGKEdlaklhssshpTSIVKAGSCGEAYAPqgwiaffmeyvkrfvvscvpswfwgpvvTLQDCLAaFFARDEL 582
Cdd:cd02660   151 LDLSLDIPNKS-----------TPSWALGESGVSGTP----------------------------TLSDCLD-RFTRPEK 190
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 583 KGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPAQ 653
Cdd:cd02660   191 LGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDP 269
                         490
                  ....*....|....*
gi 1794418801 654 IVTYDLLSVICHHGT 668
Cdd:cd02660   270 DYTYDLFAVVVHKGT 284
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-671 1.24e-26

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 116.91  E-value: 1.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 180 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKK---PAICKSYLKLMTELwHKSRPGSVVPTTL 253
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLgmhGSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 254 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 319
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 320 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 372
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 373 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 450
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 451 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 527
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 528 VKAGSCgeAYAPQGWIAFFmeyvkrfvvSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVK 601
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF---------SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASK 709
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418801 602 FCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASS 671
Cdd:COG5560   710 QMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSG 778
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
475-671 8.06e-23

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 100.41  E-value: 8.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 475 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLaklhssshptsivkagscgeayapqgwiaffmeyvkrfv 554
Cdd:cd02659   113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 555 vscvpswfwgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH--ELMFSTKISTH 632
Cdd:cd02659   154 ---------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1794418801 633 VSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASS 671
Cdd:cd02659   219 FEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHG 266
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
747-819 6.80e-21

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 87.42  E-value: 6.80e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418801 747 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 819
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
472-671 8.40e-20

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 90.52  E-value: 8.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 472 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvk 551
Cdd:cd02667    66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 552 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQNFPEILCIHLKRFRHELMFST-KIS 630
Cdd:cd02667   109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1794418801 631 THVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASS 671
Cdd:cd02667   173 RHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRS 216
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
475-711 7.61e-19

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 88.14  E-value: 7.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 475 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklHSSshptsivkagscgeayapqgwiaffmeyvkrfv 554
Cdd:cd02663   109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 555 vscvpswfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS--TKISTH 632
Cdd:cd02663   149 --------------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYR 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 633 VSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICH------HGTASSVPPRKAGYI---EDLVLMLPQNiwdNLYSRYGGG 702
Cdd:cd02663   215 VVFPLE---LRLFnTTDDAENPDRLYELVAVVVHigggpnHGHYVSIVKSHGGWLlfdDETVEKIDEN---AVEEFFGDS 288

                  ....*....
gi 1794418801 703 PAVNHLYIC 711
Cdd:cd02663   289 PNQATAYVL 297
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
465-671 8.66e-19

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 88.25  E-value: 8.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 465 KKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshptsivkagscgeayapqgwia 544
Cdd:cd02668   108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 545 ffmeyvkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL- 623
Cdd:cd02668   157 -----------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRk 213
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1794418801 624 -MFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGTASS 671
Cdd:cd02668   214 tGAKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVSAY 260
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 6.35e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 6.35e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418801  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
184-289 6.56e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 76.86  E-value: 6.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 184 LTGLKNIGNTCYMNAALQALSNCPPLTQ--FFLDCGGLARTDKKpaickSYLKLMTELWHkSRPGSVVPTTLFQGIKTVN 261
Cdd:cd02671    24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHglKHLVSLISSVEQLQ-----SSFLLNPEKYN-DELANQAPRRLLNALREVN 97
                          90       100
                  ....*....|....*....|....*...
gi 1794418801 262 PTFRGYSQQDAQEFLRCLMDLLHEELKE 289
Cdd:cd02671    98 PMYEGYLQHDAQEVLQCILGNIQELVEK 125
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
479-671 4.06e-13

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 69.70  E-value: 4.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 479 FDGTIISSVQCLTCDRVS-VTLETFQDLSLPIPGKedlaklhSSSHPTsivkagscgeayapqgwiaffmeyvkrfvvsc 557
Cdd:cd02662    56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 558 vpswfwgpvvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQNFPEILCIHLKRFR-HELMFSTKISTHVSFP 636
Cdd:cd02662    97 ----------TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1794418801 637 LegldlqpFLakdspaQIVTYDLLSVICHHGTASS 671
Cdd:cd02662   156 E-------RL------PKVLYRLRAVVVHYGSHSS 177
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
473-670 7.46e-13

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 70.60  E-value: 7.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLpipgkedlaklhssshptsivkagscgeayapqgwiaffmeyvkr 552
Cdd:cd02664    97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 553 fvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFR--HELMFSTKIS 630
Cdd:cd02664   132 ----SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIM 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1794418801 631 THVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS 670
Cdd:cd02664   200 DNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSS 256
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-288 8.36e-13

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 70.05  E-value: 8.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPTTLFQGIKTVNPT 263
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1794418801 264 F------RGYSQQDAQEFLRCLMDLLHEELK 288
Cdd:cd02657    79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLP 109
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
472-672 2.86e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 68.77  E-value: 2.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 472 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdLAKLHSSSHPTSIVKAgscgeayapqgwiaffmeyvk 551
Cdd:cd02671   120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 552 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS----- 626
Cdd:cd02671   178 -------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygg 244
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1794418801 627 -TKISTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHGTASSV 672
Cdd:cd02671   245 lSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGATISS 287
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-284 9.20e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 64.05  E-value: 9.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 186 GLKNIGNTCYMNAALQALSNCpplTQFFLDC--GGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQgiKTVNPT 263
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMA---KDFRRQVlsLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLE--ASRPPW 75
                          90       100
                  ....*....|....*....|.
gi 1794418801 264 FRGYSQQDAQEFLRCLMDLLH 284
Cdd:cd02664    76 FTPGSQQDCSEYLRYLLDRLH 96
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
70-287 5.36e-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: 62.34  E-value: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801  70 NLWACLENRCSYVGCGESQvdHSTIHSQETKHYLTVNLTTLRVWC----YACSKEVFLDRKLGTQPslphVRQPHQIQEN 145
Cdd:cd02669    27 NVYACLVCGKYFQGRGKGS--HAYTHSLEDNHHVFLNLETLKFYClpdnYEIIDSSLDDIKYVLNP----TYTKEQISDL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 146 SVQdfkipsnttlktplVAVFDDLDieadeeDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLdcggLARTDKK 225
Cdd:cd02669   101 DRD--------------PKLSRDLD------GKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL----LYENYEN 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1794418801 226 PAICKSYL-----KLMTELWH-KSRPGSVVPTTLFQGIKTV-NPTFRGYSQQDAQEFLRCLMDLLHEEL 287
Cdd:cd02669   157 IKDRKSELvkrlsELIRKIWNpRNFKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL 225
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
60-112 1.84e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.84e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1794418801   60 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 112
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
568-667 3.27e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 60.65  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801  568 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQNFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 643
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
                           90       100
                   ....*....|....*....|....*..
gi 1794418801  644 PFLAKD---SPAQIVTYDLLSVICHHG 667
Cdd:COG5077    415 PFLDRDadkSENSDAVYVLYGVLVHSG 441
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
186-283 1.77e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.73  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 186 GLKNIGNTCYMNAALQALS-NCPPLTQFFLDCGGLART-------DKKPAICKSYLKLMTELWHKSRPgsvvpttlfqgi 257
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
                          90       100
                  ....*....|....*....|....*.
gi 1794418801 258 kTVNPTFRGYSQQDAQEFLRCLMDLL 283
Cdd:COG5533    69 -KVGWIPPMGSQEDAHELLGKLLDEL 93
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
464-668 2.22e-08

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 56.56  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 464 RKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSshptsivkagscgEAYAPqgwi 543
Cdd:cd02658   115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP---- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 544 affmeyvkrfvvscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL 623
Cdd:cd02658   178 -----------------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLE 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1794418801 624 MF-STKISTHVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT 668
Cdd:cd02658   231 NWvPKKLDVPIDVPEELGP-------------GKYELIAFISHKGT 263
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-288 3.17e-08

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 56.18  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKK-PAIC------------KS--YLKLMTELW-HKSRPGSVV 249
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVdPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1794418801 250 PTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELK 288
Cdd:cd02658    81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-288 3.09e-06

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 49.29  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418801 186 GLKNIGNTCYMNAALQALSNCPPLTqffldcgglartdkkpaickSYLKLMTElwhksrpgsvvpttlfqgiktvnptfr 265
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLI--------------------EYLEEFLE--------------------------- 33
                          90       100
                  ....*....|....*....|...
gi 1794418801 266 gysQQDAQEFLRCLMDLLHEELK 288
Cdd:cd02662    34 ---QQDAHELFQVLLETLEQLLK 53
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
609-668 2.39e-05

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 47.70  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1794418801 609 PEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT 668
Cdd:cd02669   333 PKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGT 394
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
590-665 1.76e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 1.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418801 590 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHElmFSTKISTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH 665
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVH 268
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
185-215 7.79e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 39.40  E-value: 7.79e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1794418801 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLD 215
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLN 32
 
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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