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Conserved domains on  [gi|1794418386|ref|NP_001364366|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform 11 [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;
154-632 5.09e-50

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.41  E-value: 5.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 311 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 390
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 391 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 470
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 471 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 550
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 551 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 627
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                  ....*
gi 1794418386 628 GTASS 632
Cdd:pfam00443 264 GSLSS 268
DUSP smart00695
Domain in ubiquitin-specific proteases;
702-786 3.39e-30

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.99  E-value: 3.39e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386  702 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 778
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 1794418386  779 LRPPVVHV 786
Cdd:smart00695  81 PRKVVCQG 88
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 6.67e-18

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.07  E-value: 6.67e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418386  30 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-632 5.09e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.41  E-value: 5.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 311 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 390
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 391 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 470
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 471 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 550
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 551 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 627
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                  ....*
gi 1794418386 628 GTASS 632
Cdd:pfam00443 264 GSLSS 268
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-632 5.73e-38

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: 141.66  E-value: 5.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 442 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvks 521
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 522 wfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL 601
Cdd:cd02674    82 ----PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1794418386 602 DLQPFLAKDSPAQIVTYDLLSVICHHGTASS 632
Cdd:cd02674   158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNG 188
DUSP smart00695
Domain in ubiquitin-specific proteases;
702-786 3.39e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.99  E-value: 3.39e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386  702 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 778
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 1794418386  779 LRPPVVHV 786
Cdd:smart00695  81 PRKVVCQG 88
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
149-632 3.21e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.45  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 149 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKK---PAICKSYLKLMTELwHKSRPGSVVPTTL 222
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLgmhGSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 223 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 288
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 289 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 341
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 342 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 419
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 420 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 496
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 497 VKAGSCgeAYAPQGWIAFFmEYVKSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFP 570
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF-SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLP 717
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1794418386 571 EILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASS 632
Cdd:COG5560   718 MILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSG 778
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
708-780 6.67e-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: 6.67e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418386 708 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 780
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 6.67e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.07  E-value: 6.67e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418386  30 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
29-81 1.75e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1794418386   29 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 81
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-632 5.09e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.41  E-value: 5.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 311 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 390
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 391 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 470
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 471 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 550
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 551 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 627
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                  ....*
gi 1794418386 628 GTASS 632
Cdd:pfam00443 264 GSLSS 268
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-632 5.73e-38

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: 141.66  E-value: 5.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 442 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvks 521
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 522 wfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL 601
Cdd:cd02674    82 ----PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1794418386 602 DLQPFLAKDSPAQIVTYDLLSVICHHGTASS 632
Cdd:cd02674   158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNG 188
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
430-632 3.74e-34

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: 131.45  E-value: 3.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 430 SPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapq 509
Cdd:cd02257    43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 510 gwiaffmeyvkswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQNFPEILCIHLKRFRH-ELMFST 588
Cdd:cd02257    97 ----------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSFnEDGTKE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1794418386 589 KISTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGTASS 632
Cdd:cd02257   160 KLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTSAD 207
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
154-632 2.36e-30

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 122.00  E-value: 2.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDcGGLARTDKKPAICKS-YLKLMTELWHKSRPGSVVPTTLFQGIKTVNPT 232
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 233 FRGYSQQDAQEFLRCLMDLLHEelkeqvmeveedpqtitteetmeedksqsdvdfqsceSCSNSdraenengsrcfsedn 312
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQK-------------------------------------ACLDR---------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 313 nettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndlstp 392
Cdd:cd02661       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 393 qilpsnegvNPRLSASPPKSgnlwpglapphkkaqsaspkrkkqhkKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQ 472
Cdd:cd02661   108 ---------FKKLKAVDPSS--------------------------QETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 473 DLSLPIPGkedlaklhssshptsivkagscgeayapqgwiaffmeyvkswfwgpVVTLQDCLAAFFARDELKGDNMYSCE 552
Cdd:cd02661   153 DLSLDIKG----------------------------------------------ADSLEDALEQFTKPEQLDGENKYKCE 186
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 553 KCKKLRNGVKFCKVQNFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGTASS 632
Cdd:cd02661   187 RCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFSPH 262
DUSP smart00695
Domain in ubiquitin-specific proteases;
702-786 3.39e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.99  E-value: 3.39e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386  702 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 778
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 1794418386  779 LRPPVVHV 786
Cdd:smart00695  81 PRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-629 3.16e-28

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 116.32  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLD---CGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNP 231
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 232 TFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenenGSRCFSED 311
Cdd:cd02660    82 NLAGYSQQDAHEFFQFLLDQLHTHYG----------------------------------------------GDKNEAND 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 312 NNEttmliqddennsemskdwqkekmCNKInkvnsegefdkdrdsisetvdlnnqetvkvqIHSraseyitdvhsndlst 391
Cdd:cd02660   116 ESH-----------------------CNCI-------------------------------IHQ---------------- 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 392 pqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrkkqhkkyrsvisdIFDGTIISSVQCLTCDRVSVTLETF 471
Cdd:cd02660   126 -------------------------------------------------------TFSGSLQSSVTCQRCGGVSTTVDPF 150
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 472 QDLSLPIPGKEdlaklhssshpTSIVKAGSCGEAYAPqgwiaffmeyvkswfwgpvvTLQDCLAaFFARDELKGDNMYSC 551
Cdd:cd02660   151 LDLSLDIPNKS-----------TPSWALGESGVSGTP--------------------TLSDCLD-RFTRPEKLGDFAYKC 198
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 552 EKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPAQIVTYDLLS 622
Cdd:cd02660   199 SGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFA 277

                  ....*..
gi 1794418386 623 VICHHGT 629
Cdd:cd02660   278 VVVHKGT 284
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
149-632 3.21e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.45  E-value: 3.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 149 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKK---PAICKSYLKLMTELwHKSRPGSVVPTTL 222
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLgmhGSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 223 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 288
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 289 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 341
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 342 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 419
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 420 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 496
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 497 VKAGSCgeAYAPQGWIAFFmEYVKSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFP 570
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF-SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLP 717
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1794418386 571 EILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASS 632
Cdd:COG5560   718 MILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSG 778
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
444-632 7.47e-24

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 103.49  E-value: 7.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 444 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLaklhssshptsivkagscgeayapqgwiaffmeyvkswf 523
Cdd:cd02659   113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 524 wgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH--ELMFSTKISTHVSFPLEgL 601
Cdd:cd02659   154 -------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-L 225
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1794418386 602 DLQPFLAKDSPAQIV----------TYDLLSVICHHGTASS 632
Cdd:cd02659   226 DMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHG 266
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-632 6.43e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 93.61  E-value: 6.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 441 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvk 520
Cdd:cd02667    66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 521 swfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQNFPEILCIHLKRFRHELMFST-KISTHVSFPlE 599
Cdd:cd02667   109 -----SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP-E 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1794418386 600 GLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASS 632
Cdd:cd02667   180 ILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRS 216
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
708-780 6.67e-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: 6.67e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418386 708 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 780
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
444-672 6.20e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 91.22  E-value: 6.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 444 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklHSSshptsivkagscgeayapqgwiaffmeyvkswf 523
Cdd:cd02663   109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 524 wgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS--TKISTHVSFPLEgl 601
Cdd:cd02663   149 ------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYRVVFPLE-- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 602 dLQPF-LAKDSPAQIVTYDLLSVICH------HGTASSVPPRKAGYI---EDLVLMLPQNiwdNLYSRYGGGPAVNHLYI 671
Cdd:cd02663   221 -LRLFnTTDDAENPDRLYELVAVVVHigggpnHGHYVSIVKSHGGWLlfdDETVEKIDEN---AVEEFFGDSPNQATAYV 296

                  .
gi 1794418386 672 C 672
Cdd:cd02663   297 L 297
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
434-632 8.16e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 91.33  E-value: 8.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 434 KKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshptsivkagscgeayapqgwia 513
Cdd:cd02668   108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 514 ffmeyvkswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL--MFSTKIS 591
Cdd:cd02668   157 ---------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLN 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1794418386 592 THVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGTASS 632
Cdd:cd02668   222 ASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVSAY 260
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 6.67e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.07  E-value: 6.67e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418386  30 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
153-258 5.93e-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: 5.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 153 LTGLKNIGNTCYMNAALQALSNCPPLTQ--FFLDCGGLARTDKKpaickSYLKLMTELWHkSRPGSVVPTTLFQGIKTVN 230
Cdd:cd02671    24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHglKHLVSLISSVEQLQ-----SSFLLNPEKYN-DELANQAPRRLLNALREVN 97
                          90       100
                  ....*....|....*....|....*...
gi 1794418386 231 PTFRGYSQQDAQEFLRCLMDLLHEELKE 258
Cdd:cd02671    98 PMYEGYLQHDAQEVLQCILGNIQELVEK 125
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
448-632 3.23e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 73.17  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 448 FDGTIISSVQCLTCDRVS-VTLETFQDLSLPIPGKedlaklhSSSHPTsivkagscgeayapqgwiaffmeyvkswfwgp 526
Cdd:cd02662    56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 527 vvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQNFPEILCIHLKRFR-HELMFSTKISTHVSFPLegldlqp 605
Cdd:cd02662    97 --TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFPE------- 156
                         170       180
                  ....*....|....*....|....*..
gi 1794418386 606 FLakdspaQIVTYDLLSVICHHGTASS 632
Cdd:cd02662   157 RL------PKVLYRLRAVVVHYGSHSS 177
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-631 1.16e-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: 72.91  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 442 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPgkedlaklhssshptsivkagscgeayapqgwiaffmeyvks 521
Cdd:cd02664    97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------------------------------------ 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 522 wfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFR--HELMFSTKISTHVSFPlE 599
Cdd:cd02664   135 -------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIMDNVSIN-E 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1794418386 600 GLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS 631
Cdd:cd02664   207 VLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSS 256
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-633 2.57e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 71.85  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 441 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdLAKLHSSSHPTSIVKAgscgeayapqgwiaffmeyvk 520
Cdd:cd02671   120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 521 swfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS------TKISTHV 594
Cdd:cd02671   178 -----EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPL 252
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1794418386 595 SFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHGTASSV 633
Cdd:cd02671   253 LTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGATISS 287
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-257 8.22e-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: 8.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPTTLFQGIKTVNPT 232
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1794418386 233 F------RGYSQQDAQEFLRCLMDLLHEELK 257
Cdd:cd02657    79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLP 109
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-253 8.11e-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: 8.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 155 GLKNIGNTCYMNAALQALSNCpplTQFFLDC--GGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQgiKTVNPT 232
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMA---KDFRRQVlsLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLE--ASRPPW 75
                          90       100
                  ....*....|....*....|.
gi 1794418386 233 FRGYSQQDAQEFLRCLMDLLH 253
Cdd:cd02664    76 FTPGSQQDCSEYLRYLLDRLH 96
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
39-256 4.10e-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: 62.72  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386  39 NLWACLENRCSYVGCGESQvdHSTIHSQETKHYLTVNLTTLRVWC----YACSKEVFLDRKLGTQPslphVRQPHQIQEN 114
Cdd:cd02669    27 NVYACLVCGKYFQGRGKGS--HAYTHSLEDNHHVFLNLETLKFYClpdnYEIIDSSLDDIKYVLNP----TYTKEQISDL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 115 SVQdfkipsnttlktplVAVFDDLDieadeeDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLdcggLARTDKK 194
Cdd:cd02669   101 DRD--------------PKLSRDLD------GKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL----LYENYEN 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1794418386 195 PAICKSYL-----KLMTELWH-KSRPGSVVPTTLFQGIKTV-NPTFRGYSQQDAQEFLRCLMDLLHEEL 256
Cdd:cd02669   157 IKDRKSELvkrlsELIRKIWNpRNFKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL 225
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
29-81 1.75e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1794418386   29 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 81
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
433-629 1.83e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 60.03  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 433 RKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSshptsivkagscgEAYAPqgwi 512
Cdd:cd02658   115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP---- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 513 affmeyvkswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMF-STKIS 591
Cdd:cd02658   178 ---------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLD 238
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1794418386 592 THVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT 629
Cdd:cd02658   239 VPIDVPEELGP-------------GKYELIAFISHKGT 263
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
529-628 3.19e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 60.65  E-value: 3.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386  529 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQNFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 604
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
                           90       100
                   ....*....|....*....|....*..
gi 1794418386  605 PFLAKD---SPAQIVTYDLLSVICHHG 628
Cdd:COG5077    415 PFLDRDadkSENSDAVYVLYGVLVHSG 441
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
155-252 1.62e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.73  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 155 GLKNIGNTCYMNAALQALS-NCPPLTQFFLDCGGLART-------DKKPAICKSYLKLMTELWHKSRPgsvvpttlfqgi 226
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
                          90       100
                  ....*....|....*....|....*.
gi 1794418386 227 kTVNPTFRGYSQQDAQEFLRCLMDLL 252
Cdd:COG5533    69 -KVGWIPPMGSQEDAHELLGKLLDEL 93
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-257 2.86e-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: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKK-PAIC------------KS--YLKLMTELW-HKSRPGSVV 218
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVdPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1794418386 219 PTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELK 257
Cdd:cd02658    81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-257 2.77e-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: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 155 GLKNIGNTCYMNAALQALSNCPPLTqffldcgglartdkkpaickSYLKLMTElwhksrpgsvvpttlfqgiktvnptfr 234
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLI--------------------EYLEEFLE--------------------------- 33
                          90       100
                  ....*....|....*....|...
gi 1794418386 235 gysQQDAQEFLRCLMDLLHEELK 257
Cdd:cd02662    34 ---QQDAHELFQVLLETLEQLLK 53
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
438-629 1.68e-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: 48.08  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 438 KKYRSVISDIFDGTII--------------SSVQCLTCDRVSVTLET-FQDLSLPIPgkedlaklhssshPTSIVKAGSc 502
Cdd:cd02669   230 KPNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVSpFLLLTLDLP-------------PPPLFKDGN- 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418386 503 GEAYAPQgwiaffmeyvkswfwgpvVTLQDCLAAFFArdelkgdnmyscEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH 582
Cdd:cd02669   296 EENIIPQ------------------VPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSK 345
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1794418386 583 ELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT 629
Cdd:cd02669   346 NNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGT 394
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
551-626 1.56e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 1.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418386 551 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHElmFSTKISTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH 626
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVH 268
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
154-184 7.37e-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: 7.37e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1794418386 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLD 184
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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