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Conserved domains on  [gi|2217265316|ref|XP_047305691|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform X2 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031705)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-663 8.06e-50

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.02  E-value: 8.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 581
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 658
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                  ....*
gi 2217265316 659 GTASS 663
Cdd:pfam00443 264 GSLSS 268
DUSP smart00695
Domain in ubiquitin-specific proteases;
733-817 2.74e-30

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316  733 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 809
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 2217265316  810 LRPPVVHV 817
Cdd:smart00695  81 PRKVVCQG 88
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 5.33e-18

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 5.33e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217265316  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-663 8.06e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.02  E-value: 8.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 581
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 658
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                  ....*
gi 2217265316 659 GTASS 663
Cdd:pfam00443 264 GSLSS 268
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
473-663 5.95e-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: 5.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvks 552
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 553 wfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL 632
Cdd:cd02674    82 ----PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217265316 633 DLQPFLAKDSPAQIVTYDLLSVICHHGTASS 663
Cdd:cd02674   158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNG 188
DUSP smart00695
Domain in ubiquitin-specific proteases;
733-817 2.74e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316  733 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 809
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 2217265316  810 LRPPVVHV 817
Cdd:smart00695  81 PRKVVCQG 88
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-663 3.51e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.45  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 180 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKK---PAICKSYLKLMTELwHKSRPGSVVPTTL 253
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLgmhGSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 254 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 319
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 320 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 372
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 373 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 450
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 451 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 527
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 528 VKAGSCgeAYAPQGWIAFFmEYVKSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFP 601
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF-SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLP 717
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217265316 602 EILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASS 663
Cdd:COG5560   718 MILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSG 778
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
739-811 7.14e-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: 7.14e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217265316 739 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 811
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 5.33e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 5.33e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217265316  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
60-112 1.70e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217265316   60 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 112
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-663 8.06e-50

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 178.02  E-value: 8.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 581
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 658
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                  ....*
gi 2217265316 659 GTASS 663
Cdd:pfam00443 264 GSLSS 268
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
473-663 5.95e-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: 5.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvks 552
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 553 wfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL 632
Cdd:cd02674    82 ----PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217265316 633 DLQPFLAKDSPAQIVTYDLLSVICHHGTASS 663
Cdd:cd02674   158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNG 188
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
461-663 4.05e-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: 4.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 461 SPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapq 540
Cdd:cd02257    43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 541 gwiaffmeyvkswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQNFPEILCIHLKRFRH-ELMFST 619
Cdd:cd02257    97 ----------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSFnEDGTKE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217265316 620 KISTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGTASS 663
Cdd:cd02257   160 KLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTSAD 207
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
185-663 2.45e-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: 2.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDcGGLARTDKKPAICKS-YLKLMTELWHKSRPGSVVPTTLFQGIKTVNPT 263
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 264 FRGYSQQDAQEFLRCLMDLLHEelkeqvmeveedpqtitteetmeedksqsdvdfqsceSCSNSdraenengsrcfsedn 343
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQK-------------------------------------ACLDR---------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 344 nettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndlstp 423
Cdd:cd02661       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 424 qilpsnegvNPRLSASPPKSgnlwpglapphkkaqsaspkrkkqhkKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQ 503
Cdd:cd02661   108 ---------FKKLKAVDPSS--------------------------QETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 504 DLSLPIPGkedlaklhssshptsivkagscgeayapqgwiaffmeyvkswfwgpVVTLQDCLAAFFARDELKGDNMYSCE 583
Cdd:cd02661   153 DLSLDIKG----------------------------------------------ADSLEDALEQFTKPEQLDGENKYKCE 186
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 584 KCKKLRNGVKFCKVQNFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGTASS 663
Cdd:cd02661   187 RCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFSPH 262
DUSP smart00695
Domain in ubiquitin-specific proteases;
733-817 2.74e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 114.38  E-value: 2.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316  733 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 809
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 2217265316  810 LRPPVVHV 817
Cdd:smart00695  81 PRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-660 3.50e-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: 3.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLD---CGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNP 262
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 263 TFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenenGSRCFSED 342
Cdd:cd02660    82 NLAGYSQQDAHEFFQFLLDQLHTHYG----------------------------------------------GDKNEAND 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 343 NNEttmliqddennsemskdwqkekmCNKInkvnsegefdkdrdsisetvdlnnqetvkvqIHSraseyitdvhsndlst 422
Cdd:cd02660   116 ESH-----------------------CNCI-------------------------------IHQ---------------- 125
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 423 pqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrkkqhkkyrsvisdIFDGTIISSVQCLTCDRVSVTLETF 502
Cdd:cd02660   126 -------------------------------------------------------TFSGSLQSSVTCQRCGGVSTTVDPF 150
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 503 QDLSLPIPGKEdlaklhssshpTSIVKAGSCGEAYAPqgwiaffmeyvkswfwgpvvTLQDCLAaFFARDELKGDNMYSC 582
Cdd:cd02660   151 LDLSLDIPNKS-----------TPSWALGESGVSGTP--------------------TLSDCLD-RFTRPEKLGDFAYKC 198
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 583 EKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPAQIVTYDLLS 653
Cdd:cd02660   199 SGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFA 277

                  ....*..
gi 2217265316 654 VICHHGT 660
Cdd:cd02660   278 VVVHKGT 284
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-663 3.51e-27

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.45  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 180 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKK---PAICKSYLKLMTELwHKSRPGSVVPTTL 253
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLgmhGSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 254 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 319
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 320 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 372
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 373 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 450
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 451 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 527
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 528 VKAGSCgeAYAPQGWIAFFmEYVKSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFP 601
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF-SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLP 717
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217265316 602 EILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASS 663
Cdd:COG5560   718 MILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSG 778
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
475-663 7.46e-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: 7.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 475 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLaklhssshptsivkagscgeayapqgwiaffmeyvkswf 554
Cdd:cd02659   113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 555 wgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH--ELMFSTKISTHVSFPLEgL 632
Cdd:cd02659   154 -------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-L 225
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217265316 633 DLQPFLAKDSPAQIV----------TYDLLSVICHHGTASS 663
Cdd:cd02659   226 DMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHG 266
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
472-663 6.50e-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: 6.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 472 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvk 551
Cdd:cd02667    66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 552 swfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQNFPEILCIHLKRFRHELMFST-KISTHVSFPlE 630
Cdd:cd02667   109 -----SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP-E 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217265316 631 GLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASS 663
Cdd:cd02667   180 ILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRS 216
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
739-811 7.14e-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: 7.14e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217265316 739 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 811
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
475-703 6.71e-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: 6.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 475 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklHSSshptsivkagscgeayapqgwiaffmeyvkswf 554
Cdd:cd02663   109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 555 wgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS--TKISTHVSFPLEgl 632
Cdd:cd02663   149 ------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYRVVFPLE-- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 633 dLQPF-LAKDSPAQIVTYDLLSVICH------HGTASSVPPRKAGYI---EDLVLMLPQNiwdNLYSRYGGGPAVNHLYI 702
Cdd:cd02663   221 -LRLFnTTDDAENPDRLYELVAVVVHigggpnHGHYVSIVKSHGGWLlfdDETVEKIDEN---AVEEFFGDSPNQATAYV 296

                  .
gi 2217265316 703 C 703
Cdd:cd02663   297 L 297
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
465-663 8.52e-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: 8.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 465 KKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshptsivkagscgeayapqgwia 544
Cdd:cd02668   108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 545 ffmeyvkswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL--MFSTKIS 622
Cdd:cd02668   157 ---------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLN 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217265316 623 THVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGTASS 663
Cdd:cd02668   222 ASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVSAY 260
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 5.33e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.46  E-value: 5.33e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217265316  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 6.42e-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: 6.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 184 LTGLKNIGNTCYMNAALQALSNCPPLTQ--FFLDCGGLARTDKKpaickSYLKLMTELWHkSRPGSVVPTTLFQGIKTVN 261
Cdd:cd02671    24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHglKHLVSLISSVEQLQ-----SSFLLNPEKYN-DELANQAPRRLLNALREVN 97
                          90       100
                  ....*....|....*....|....*...
gi 2217265316 262 PTFRGYSQQDAQEFLRCLMDLLHEELKE 289
Cdd:cd02671    98 PMYEGYLQHDAQEVLQCILGNIQELVEK 125
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
479-663 3.38e-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: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 479 FDGTIISSVQCLTCDRVS-VTLETFQDLSLPIPGKedlaklhSSSHPTsivkagscgeayapqgwiaffmeyvkswfwgp 557
Cdd:cd02662    56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 558 vvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQNFPEILCIHLKRFR-HELMFSTKISTHVSFPLegldlqp 636
Cdd:cd02662    97 --TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFPE------- 156
                         170       180
                  ....*....|....*....|....*..
gi 2217265316 637 FLakdspaQIVTYDLLSVICHHGTASS 663
Cdd:cd02662   157 RL------PKVLYRLRAVVVHYGSHSS 177
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
473-662 1.21e-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: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPgkedlaklhssshptsivkagscgeayapqgwiaffmeyvks 552
Cdd:cd02664    97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------------------------------------ 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 553 wfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFR--HELMFSTKISTHVSFPlE 630
Cdd:cd02664   135 -------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIMDNVSIN-E 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217265316 631 GLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS 662
Cdd:cd02664   207 VLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSS 256
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
472-664 2.79e-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: 2.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 472 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdLAKLHSSSHPTSIVKAgscgeayapqgwiaffmeyvk 551
Cdd:cd02671   120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 552 swfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS------TKISTHV 625
Cdd:cd02671   178 -----EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPL 252
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217265316 626 SFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHGTASSV 664
Cdd:cd02671   253 LTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGATISS 287
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-288 8.88e-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: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPTTLFQGIKTVNPT 263
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2217265316 264 F------RGYSQQDAQEFLRCLMDLLHEELK 288
Cdd:cd02657    79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLP 109
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-284 8.52e-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: 8.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 186 GLKNIGNTCYMNAALQALSNCpplTQFFLDC--GGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQgiKTVNPT 263
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMA---KDFRRQVlsLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLE--ASRPPW 75
                          90       100
                  ....*....|....*....|.
gi 2217265316 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 5.43e-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: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316  70 NLWACLENRCSYVGCGESQvdHSTIHSQETKHYLTVNLTTLRVWC----YACSKEVFLDRKLGTQPslphVRQPHQIQEN 145
Cdd:cd02669    27 NVYACLVCGKYFQGRGKGS--HAYTHSLEDNHHVFLNLETLKFYClpdnYEIIDSSLDDIKYVLNP----TYTKEQISDL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 146 SVQdfkipsnttlktplVAVFDDLDieadeeDELRARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLdcggLARTDKK 225
Cdd:cd02669   101 DRD--------------PKLSRDLD------GKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFL----LYENYEN 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217265316 226 PAICKSYL-----KLMTELWH-KSRPGSVVPTTLFQGIKTV-NPTFRGYSQQDAQEFLRCLMDLLHEEL 287
Cdd:cd02669   157 IKDRKSELvkrlsELIRKIWNpRNFKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL 225
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
60-112 1.70e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217265316   60 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 112
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
464-660 2.20e-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: 59.64  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 464 RKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSshptsivkagscgEAYAPqgwi 543
Cdd:cd02658   115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP---- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 544 affmeyvkswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMF-STKIS 622
Cdd:cd02658   178 ---------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLD 238
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217265316 623 THVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT 660
Cdd:cd02658   239 VPIDVPEELGP-------------GKYELIAFISHKGT 263
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
560-659 3.43e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 60.65  E-value: 3.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316  560 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQNFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 635
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
                           90       100
                   ....*....|....*....|....*..
gi 2217265316  636 PFLAKD---SPAQIVTYDLLSVICHHG 659
Cdd:COG5077    415 PFLDRDadkSENSDAVYVLYGVLVHSG 441
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
186-283 2.02e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 186 GLKNIGNTCYMNAALQALS-NCPPLTQFFLDCGGLART-------DKKPAICKSYLKLMTELWHKSRPgsvvpttlfqgi 257
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
                          90       100
                  ....*....|....*....|....*.
gi 2217265316 258 kTVNPTFRGYSQQDAQEFLRCLMDLL 283
Cdd:COG5533    69 -KVGWIPPMGSQEDAHELLGKLLDEL 93
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
186-288 3.22e-08

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 56.18  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKK-PAIC------------KS--YLKLMTELW-HKSRPGSVV 249
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVdPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217265316 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 2.90e-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: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 186 GLKNIGNTCYMNAALQALSNCPPLTqffldcgglartdkkpaickSYLKLMTElwhksrpgsvvpttlfqgiktvnptfr 265
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLI--------------------EYLEEFLE--------------------------- 33
                          90       100
                  ....*....|....*....|...
gi 2217265316 266 gysQQDAQEFLRCLMDLLHEELK 288
Cdd:cd02662    34 ---QQDAHELFQVLLETLEQLLK 53
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
469-660 2.36e-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: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 469 KKYRSVISDIFDGTII--------------SSVQCLTCDRVSVTLET-FQDLSLPIPgkedlaklhssshPTSIVKAGSc 533
Cdd:cd02669   230 KPNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSVSpFLLLTLDLP-------------PPPLFKDGN- 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217265316 534 GEAYAPQgwiaffmeyvkswfwgpvVTLQDCLAAFFArdelkgdnmyscEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH 613
Cdd:cd02669   296 EENIIPQ------------------VPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSK 345
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217265316 614 ELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT 660
Cdd:cd02669   346 NNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGT 394
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
582-657 1.68e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217265316 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHElmFSTKISTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH 657
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVH 268
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
185-215 7.71e-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: 7.71e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217265316 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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