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Conserved domains on  [gi|530400880|ref|XP_005269229|]
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ubiquitin carboxyl-terminal hydrolase 44 isoform X1 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031653)

ubiquitin carboxyl-terminal hydrolase catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin on target proteins; belongs to the peptidase C19 family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
273-706 5.04e-64

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 215.77  E-value: 5.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  273 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlamtasektrsckhppvtdtvvyqmnecqekdtgfvcsrqssl 352
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------------------------------------------------- 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  353 ssglsggaskgrkMELIQPKEPTSQYISLCHELHTLFQVMWSGKW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:pfam00443  32 -------------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFL 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  432 LDKIQRELEttgtslpaliptsqRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryqcsgkDIA 511
Cdd:pfam00443  99 LDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-------DSA 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  512 SQPCLV-TEMLAKFTETEALEGKI-YVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNslcilintl 589
Cdd:pfam00443 158 ELKTASlQICFLQFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN--------- 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  590 lamlrssngkydqqtekitgwsgRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGkGFGSGHYT 669
Cdd:pfam00443 218 -----------------------RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-DYRLVAVVVHSG-SLSSGHYI 272
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 530400880  670 AYCYNSEGGFWVHCNDSKLSMCTMD-EVCKAQAYILFY 706
Cdd:pfam00443 273 AYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
29-90 5.70e-23

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.71  E-value: 5.70e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400880   29 CVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDN 90
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
273-706 5.04e-64

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 215.77  E-value: 5.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  273 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlamtasektrsckhppvtdtvvyqmnecqekdtgfvcsrqssl 352
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------------------------------------------------- 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  353 ssglsggaskgrkMELIQPKEPTSQYISLCHELHTLFQVMWSGKW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:pfam00443  32 -------------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFL 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  432 LDKIQRELEttgtslpaliptsqRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryqcsgkDIA 511
Cdd:pfam00443  99 LDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-------DSA 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  512 SQPCLV-TEMLAKFTETEALEGKI-YVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNslcilintl 589
Cdd:pfam00443 158 ELKTASlQICFLQFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN--------- 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  590 lamlrssngkydqqtekitgwsgRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGkGFGSGHYT 669
Cdd:pfam00443 218 -----------------------RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-DYRLVAVVVHSG-SLSSGHYI 272
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 530400880  670 AYCYNSEGGFWVHCNDSKLSMCTMD-EVCKAQAYILFY 706
Cdd:pfam00443 273 AYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-707 6.22e-55

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: 191.82  E-value: 6.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrSCKHPPVTDTvvyqmnecqekdtgfvcsrqssls 353
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkepTSQYISLCHELHTLFQVMW-SGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELL 432
Cdd:cd02660   41 ---------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLL 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 433 DKIQRELettGTSLPALIPTSQRKLIkqvlnvVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIAS 512
Cdd:cd02660  100 DQLHTHY---GGDKNEANDESHCNCI------IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGES 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 513 ----QPCLvTEMLAKFTETEALEGKIYVCDQCNSKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFSTNSLCIlint 588
Cdd:cd02660  171 gvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKT---- 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 589 llamlrssngkydqqtekitgwsgrnnREKIGVHVGFEEILNMEPYCCRET----LKSLRPECFIYDLSAVVMHHGKgFG 664
Cdd:cd02660  235 ---------------------------SRKIDTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LD 286
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 530400880 665 SGHYTAYCYNsEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYT 707
Cdd:cd02660  287 TGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
29-90 5.70e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.71  E-value: 5.70e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400880   29 CVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDN 90
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
274-708 9.22e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 84.47  E-value: 9.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLShllifrqcfLKLDLNQWLAMTASEKTRSCKHppvtdtvVYQMNEcqekdtgfvcsrqssls 353
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILA---------LYLPKLDELLDDLSKELKVLKN-------VIRKPE----------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkEPTSQyislcHELHTLFQVMWSGKwalvspfamlhsVWRLIPAFRGYAQQDAQEFLCELLD 433
Cdd:COG5533   48 -------------------PDLNQ-----EEALKLFTALWSSK------------EHKVGWIPPMGSQEDAHELLGKLLD 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 434 KIQRELETTGTslpaliptsqrKLIKQVLNvvnnifhgqllsqvtclacDNKSNTIEPFWDLSLEFPerYQCSGKDIASQ 513
Cdd:COG5533   92 ELKLDLVNSFT-----------IRIFKTTK-------------------DKKKTSTGDWFDIIIELP--DQTWVNNLKTL 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 514 PCLVTEMlakftetealegKIYVCDQCNSKRRRFSSKPVVlTEAQKQLMICHLPQVLRLHLKRFSTNSlcilintllaml 593
Cdd:COG5533  140 QEFIDNM------------EELVDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLG------------ 194
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 594 rsSNGKYDQQTEkitgwsgrnnrEKIGVHVGFEEILNMEPYccretlkslrpecFIYDLSAVVMHHGkGFGSGHYTAYCy 673
Cdd:COG5533  195 --GNQKIDTEVD-----------EKFELPVKHDQILNIVKE-------------TYYDLVGFVLHQG-SLEGGHYIAYV- 246
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 530400880 674 nSEGGFWVHCNDSKLSMCTMDEVCKA---QAYILFYTQ 708
Cdd:COG5533  247 -KKGGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
28-73 1.97e-13

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 65.08  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 530400880    28 HCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVN 73
Cdd:smart00290   1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLG 46
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
273-706 5.04e-64

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 215.77  E-value: 5.04e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  273 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlamtasektrsckhppvtdtvvyqmnecqekdtgfvcsrqssl 352
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------------------------------------------------- 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  353 ssglsggaskgrkMELIQPKEPTSQYISLCHELHTLFQVMWSGKW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:pfam00443  32 -------------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFL 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  432 LDKIQRELEttgtslpaliptsqRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPEryqcsgkDIA 511
Cdd:pfam00443  99 LDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG-------DSA 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  512 SQPCLV-TEMLAKFTETEALEGKI-YVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNslcilintl 589
Cdd:pfam00443 158 ELKTASlQICFLQFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN--------- 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  590 lamlrssngkydqqtekitgwsgRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGkGFGSGHYT 669
Cdd:pfam00443 218 -----------------------RSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-DYRLVAVVVHSG-SLSSGHYI 272
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 530400880  670 AYCYNSEGGFWVHCNDSKLSMCTMD-EVCKAQAYILFY 706
Cdd:pfam00443 273 AYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-707 6.22e-55

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: 191.82  E-value: 6.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrSCKHPPVTDTvvyqmnecqekdtgfvcsrqssls 353
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkepTSQYISLCHELHTLFQVMW-SGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELL 432
Cdd:cd02660   41 ---------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLL 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 433 DKIQRELettGTSLPALIPTSQRKLIkqvlnvVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIAS 512
Cdd:cd02660  100 DQLHTHY---GGDKNEANDESHCNCI------IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGES 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 513 ----QPCLvTEMLAKFTETEALEGKIYVCDQCNSKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFSTNSLCIlint 588
Cdd:cd02660  171 gvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKT---- 234
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 589 llamlrssngkydqqtekitgwsgrnnREKIGVHVGFEEILNMEPYCCRET----LKSLRPECFIYDLSAVVMHHGKgFG 664
Cdd:cd02660  235 ---------------------------SRKIDTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LD 286
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 530400880 665 SGHYTAYCYNsEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYT 707
Cdd:cd02660  287 TGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
421-706 1.06e-51

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: 180.37  E-value: 1.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 421 QQDAQEFLCELLDKIQRELETTgtslpalipTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 500
Cdd:cd02257   22 QQDAHEFLLFLLDKLHEELKKS---------SKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 501 ERyqcsgkdiASQPCLVTEMLAKFTETEALEGkiYVCDQCNSKRrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFStn 580
Cdd:cd02257   93 VK--------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLKRFS-- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 581 slcilintllamlrssngkydqqtekitgWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRP-ECFIYDLSAVVMHH 659
Cdd:cd02257  152 -----------------------------FNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDnGSYKYELVAVVVHS 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530400880 660 GKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEV-----CKAQAYILFY 706
Cdd:cd02257  203 GTSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
273-706 2.00e-49

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: 175.93  E-value: 2.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 273 TGLRNLGNTCYMNSVLQVLSHLlifrqcflkldlnqwlamtasektrsckhPPVTDTVVYQM--NECQEKDTGFVCsrqs 350
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHT-----------------------------PPLANYLLSREhsKDCCNEGFCMMC---- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 351 slssglsggaskgrkmeliqpkeptsqyislCHELHTLfQVMWSGKWALVSPFamLHSVWRLI-PAFRGYAQQDAQEFLC 429
Cdd:cd02661   49 -------------------------------ALEAHVE-RALASSGPGSAPRI--FSSNLKQIsKHFRIGRQEDAHEFLR 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 430 ELLDKIQRelettgTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefperyqcsgkD 509
Cdd:cd02661   95 YLLDAMQK------ACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSL-----------D 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 510 IASQPCLvTEMLAKFTETEALEGK-IYVCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNslcilint 588
Cdd:cd02661  158 IKGADSL-EDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRFSNF-------- 217
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 589 llamlrssngkydqqtekitgwsgrnNREKIGVHVGFEEILNMEPYCCRETLKSLrpecfIYDLSAVVMHHGKGFGSGHY 668
Cdd:cd02661  218 --------------------------RGGKINKQISFPETLDLSPYMSQPNDGPL-----KYKLYAVLVHSGFSPHSGHY 266
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 530400880 669 TAYCYNSEGgFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02661  267 YCYVKSSNG-KWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
377-706 1.48e-41

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: 152.93  E-value: 1.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 377 QYISLCHELHTLFQVmwsgkwalvSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQrelettgtslpaliptsqrk 456
Cdd:cd02667   16 QNLSQTPALRELLSE---------TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR-------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 457 likqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLefPEryqcsgKDIASQPCLVTEMLAKFTETEALEGK-IY 535
Cdd:cd02667   67 ------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL--PR------SDEIKSECSIESCLKQFTEVEILEGNnKF 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 536 VCDQCnskrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNSLCILIntllamlrssngkydqqtekitgwsgrnn 615
Cdd:cd02667  133 ACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR----------------------------- 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 616 reKIGVHVGFEEILNMEPYCcreTLKSLRPEC---FIYDLSAVVMHHGkGFGSGHYTAYCY------------------N 674
Cdd:cd02667  170 --KVSRHVSFPEILDLAPFC---DPKCNSSEDkssVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaD 243
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 530400880 675 SEG---GFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02667  244 EAGpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
421-707 3.72e-39

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: 144.74  E-value: 3.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 421 QQDAQEFLCELLDKIQrelettgtslpaliptsqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFP 500
Cdd:cd02674   22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 501 ERYQCSGKdiasqpCLVTEMLAKFTETEALEGKIYV-CDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFST 579
Cdd:cd02674   76 SGSGDAPK------VTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLKRFSF 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 580 NslcilintllamlrssngkydqqtekitgwsgRNNREKIGVHVGFE-EILNMEPYCcretLKSLRPECFIYDLSAVVMH 658
Cdd:cd02674  139 S--------------------------------RGSTRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNH 182
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530400880 659 HGKGFGsGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYT 707
Cdd:cd02674  183 YGSLNG-GHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-706 1.14e-37

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 143.55  E-value: 1.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWlamtasekTRSCKHPPVTDTVVYQMNECQEKDtgfvcsrqssls 353
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED--------DDDNKSVPLALQRLFLFLQLSESP------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmelIQPKEPTSqyislchelhtLFQVMWsgkwalvspfamlhsvWRLIPAFRgyaQQDAQEFLCELLD 433
Cdd:cd02659   64 ---------------VKTTELTD-----------KTRSFG----------------WDSLNTFE---QHDVQEFFRVLFD 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 434 KIQRELEttgtslpaliPTSQRKLIKqvlnvvnNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEfperyqcsGKDIASq 513
Cdd:cd02659   99 KLEEKLK----------GTGQEGLIK-------NLFGGKLVNYIICKECPHESEREEYFLDLQVA--------VKGKKN- 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 514 pclVTEMLAKFTETEALEG-KIYVCDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFStnslcilintllam 592
Cdd:cd02659  153 ---LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFE-------------- 204
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 593 lrssngkYDQQTekitgwsgrNNREKIGVHVGFEEILNMEPYCCR------ETLKSLRPECFIYDLSAVVMHHGkGFGSG 666
Cdd:cd02659  205 -------FDFET---------MMRIKINDRFEFPLELDMEPYTEKglakkeGDSEKKDSESYIYELHGVLVHSG-DAHGG 267
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400880 667 HYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQ----------------------AYILFY 706
Cdd:cd02659  268 HYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsgprafkrttnAYMLFY 329
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-689 3.75e-34

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: 133.31  E-value: 3.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQwlamTASEKTRSCKHPPVTDTVVYQMnecqekdtgfvcsrqssls 353
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTE----DAELKNMPPDKPHEPQTIIDQL------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkeptsQYIslchelhtlFQVMWSGKWALVSPFAmlhsvwrLIPAFR--GYAQQDAQEFLCEL 431
Cdd:cd02668   58 -----------------------QLI---------FAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLF 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 432 LDKIQRELettgtslpaliptsQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFperyqcsgKDIA 511
Cdd:cd02668   99 LSLLEAKL--------------SKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--------KGHK 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 512 SqpclVTEMLAKFTETEALEG-KIYVCDQCNSKRRrfsskpvvlteAQKQLMICHLPQVLRLHLKRFStnslcilintll 590
Cdd:cd02668  157 T----LEECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFV------------ 209
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 591 amlrssngkYDQQTEKitgwsgrnnREKIGVHVGFEEILNMEPYCCRETLKSlrpecFIYDLSAVVMHHGKGFGSGHYTA 670
Cdd:cd02668  210 ---------FDRKTGA---------KKKLNASISFPEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIA 266
                        410
                 ....*....|....*....
gi 530400880 671 YCYNSEGGFWVHCNDSKLS 689
Cdd:cd02668  267 HIKDEQTGEWYKFNDEDVE 285
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
385-707 1.42e-31

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: 125.11  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 385 LHTLFQVMWSGK--WALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVL 462
Cdd:cd02663   27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 463 NVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQcsgkdiasqpclVTEMLAKFTETEALEGK-IYVCDQCN 541
Cdd:cd02663  107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTS------------ITSCLRQFSATETLCGRnKFYCDECC 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 542 SKRrrfsskpvvltEAQKQLMICHLPQVLRLHLKRFstnslcilintllamlrssngKYDQQTEKITGWSGRnnrekigv 621
Cdd:cd02663  175 SLQ-----------EAEKRMKIKKLPKILALHLKRF---------------------KYDEQLNRYIKLFYR-------- 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 622 hVGFEEILNMepycCRETLKSLRPeCFIYDLSAVVMHHGKGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMDEVCK--- 698
Cdd:cd02663  215 -VVFPLELRL----FNTTDDAENP-DRLYELVAVVVHIGGGPNHGHYVSIV--KSHGGWLLFDDETVEKIDENAVEEffg 286
                        330
                 ....*....|....
gi 530400880 699 -----AQAYILFYT 707
Cdd:cd02663  287 dspnqATAYVLFYQ 300
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-706 1.91e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 104.88  E-value: 1.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlamtasektrsckhPPVTDTVVyqmnecqekdTGFVcsrqssls 353
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNL-----------------PRLGDSQS----------VMKK-------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkeptsqyislchELHTLFQVMWSGKWALVSPFAMLHSVWRliPAFRGYAQQDAQEFLCELLD 433
Cdd:cd02664   46 ------------------------------LQLLQAHLMHTQRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRYLLD 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 434 KIQRELETTgtslpaliptsqrklikqvlnvvnniFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPeryqcsgkdiasq 513
Cdd:cd02664   94 RLHTLIEKM--------------------------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------- 134
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 514 pcLVTEMLAKFTETEALEGK-IYVCDQCNSkrrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFStnslcilintllam 592
Cdd:cd02664  135 --SVQDLLNYFLSPEKLTGDnQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFS-------------- 187
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 593 lrssngkYDQQTekitgwsgrNNREKIGVHVGFEEILNMEPYCCRETLKSLRPE-----------CFI---YDLSAVVMH 658
Cdd:cd02664  188 -------YDQKT---------HVREKIMDNVSINEVLSLPVRVESKSSESPLEKkeeesgddgelVTRqvhYRLYAVVVH 251
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400880 659 HGKGFGSGHYtaYCY----------------------NSEGGFWVHCNDSKLSMCTMDEV-------CKAQAYILFY 706
Cdd:cd02664  252 SGYSSESGHY--FTYardqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
29-90 5.70e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.71  E-value: 5.70e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400880   29 CVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDN 90
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
270-706 1.80e-21

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 96.12  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 270 PGVTGLRNLGNTCYMNSVLQVLshllifrqCFlkldlnqwlamtASEKTRSCKHppvtdtvvyqmnecqekdtgfVCSrq 349
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVL--------YF------------CPGFKHGLKH---------------------LVS-- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 350 sslssglsggaskgrkmeLIQPKEPTSQYISLCHELHTlfqvmwsGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLC 429
Cdd:cd02671   59 ------------------LISSVEQLQSSFLLNPEKYN-------DELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQ 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 430 ELLDKIQrelettgtslpaliptsqrklikqvlNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKD 509
Cdd:cd02671  114 CILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEE 167
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 510 IAS-QPCLVTEM------LAKFTETEALEGK-IYVCDQCNSkrrrfsskpvvLTEAQKQLMICHLPQVLRLHLKRFSTNS 581
Cdd:cd02671  168 SSEiSPDPKTEMktlkwaISQFASVERIVGEdKYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANG 236
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 582 LCILINTLLamlrssngkydqqtekitgwsgrnnrEKIGVHVGFEEILNMEPYCCRETLKSlrpecfiYDLSAVVMHHGK 661
Cdd:cd02671  237 SEFDCYGGL--------------------------SKVNTPLLTPLKLSLEEWSTKPKNDV-------YRLFAVVMHSGA 283
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530400880 662 GFGSGHYTAYCYnseggfWVHCNDSKLSMCTMDEVCKAQA---------YILFY 706
Cdd:cd02671  284 TISSGHYTAYVR------WLLFDDSEVKVTEEKDFLEALSpntsststpYLLFY 331
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-706 1.42e-19

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 90.08  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLshllifrqcflkldlnqwlamtasektRSCkhpPVTDTVVYQMNECQEKDTGfvcsrqssls 353
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL---------------------------RSV---PELRDALKNYNPARRGANQ---------- 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkepTSQYISLchELHTLFQVMwSGKWALVSPFAMLHSVWRLIPAF------RGYAQQDAQEF 427
Cdd:cd02657   41 ---------------------SSDNLTN--ALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEEC 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 428 LCELLDKIQRELEttgtslpalIPTSQRKLIKQvlnvvnnIFHGQLLSQVTCLACDN-KSNTIEPFWDLSLefperyQCS 506
Cdd:cd02657   97 WSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESPDeEEVSTESEYKLQC------HIS 154
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 507 GKDIASQpcLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSkpvvlteaqkqlmichLPQVLRLHLKRFStnslcili 586
Cdd:cd02657  155 ITTEVNY--LQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISR----------------LPKYLTVQFVRFF-------- 208
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 587 ntllamlrssngkYDQQTEKitgwsgrnnREKIGVHVGFEEILNMEPYCCretlkslrpECFIYDLSAVVMHHGKGFGSG 666
Cdd:cd02657  209 -------------WKRDIQK---------KAKILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSG 257
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 530400880 667 HYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQ-------AYILFY 706
Cdd:cd02657  258 HYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
274-708 9.22e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 84.47  E-value: 9.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLShllifrqcfLKLDLNQWLAMTASEKTRSCKHppvtdtvVYQMNEcqekdtgfvcsrqssls 353
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILA---------LYLPKLDELLDDLSKELKVLKN-------VIRKPE----------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 354 sglsggaskgrkmeliqpkEPTSQyislcHELHTLFQVMWSGKwalvspfamlhsVWRLIPAFRGYAQQDAQEFLCELLD 433
Cdd:COG5533   48 -------------------PDLNQ-----EEALKLFTALWSSK------------EHKVGWIPPMGSQEDAHELLGKLLD 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 434 KIQRELETTGTslpaliptsqrKLIKQVLNvvnnifhgqllsqvtclacDNKSNTIEPFWDLSLEFPerYQCSGKDIASQ 513
Cdd:COG5533   92 ELKLDLVNSFT-----------IRIFKTTK-------------------DKKKTSTGDWFDIIIELP--DQTWVNNLKTL 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 514 PCLVTEMlakftetealegKIYVCDQCNSKRRRFSSKPVVlTEAQKQLMICHLPQVLRLHLKRFSTNSlcilintllaml 593
Cdd:COG5533  140 QEFIDNM------------EELVDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLG------------ 194
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 594 rsSNGKYDQQTEkitgwsgrnnrEKIGVHVGFEEILNMEPYccretlkslrpecFIYDLSAVVMHHGkGFGSGHYTAYCy 673
Cdd:COG5533  195 --GNQKIDTEVD-----------EKFELPVKHDQILNIVKE-------------TYYDLVGFVLHQG-SLEGGHYIAYV- 246
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 530400880 674 nSEGGFWVHCNDSKLSMCTMDEVCKA---QAYILFYTQ 708
Cdd:COG5533  247 -KKGGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
413-706 4.74e-17

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 81.26  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 413 IPAFRGY-----AQQDAQEFLCELLDKIQRELEttgtslpaliptsqrklikqvlnvvnNIFHGQLLSQVTCLACDNKSN 487
Cdd:cd02662   21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 488 -TIEPFWDLSLEFPERYQCSGkdiasqpCLVTEMLAKFTETEALEGkiYVCDQCnskrrrfsskpvvlteaqkQLMICHL 566
Cdd:cd02662   75 vRYESFTMLSLPVPNQSSGSG-------TTLEHCLDDFLSTEIIDD--YKCDRC-------------------QTVIVRL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 567 PQVLRLHLKRFStnslcilintllamlrssngkydqqtekitgWSGRNNREKIGVHVGFEEILNMepyccretlkslrpe 646
Cdd:cd02662  127 PQILCIHLSRSV-------------------------------FDGRGTSTKNSCKVSFPERLPK--------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 647 cFIYDLSAVVMHHGkGFGSGHYTAY--------------------CYNSEGGFWVHCNDSKLSMCTMDEVC-KAQAYILF 705
Cdd:cd02662  161 -VLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLF 238

                 .
gi 530400880 706 Y 706
Cdd:cd02662  239 Y 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
271-709 6.72e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 85.32  E-value: 6.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 271 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlamtasektrsckhppvTDTVVYQMNEcqekdtgfvcsrqs 350
Cdd:COG5560  264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------SDEYEESINE-------------- 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 351 slssglsggaskgrkmeliqpKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCE 430
Cdd:COG5560  306 ---------------------ENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAF 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 431 LLDKIQREL----ETTGTSLPALIPTSQRKlIKQVLN------------VVNNIFHGQLLSQVTCLACDNKSNTIEPFWD 494
Cdd:COG5560  365 LLDGLHEDLnriiKKPYTSKPDLSPGDDVV-VKKKAKecwwehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMD 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 495 LSLEFPERYQCSGK------DIASQPCLV------TEMLAKFTETEALE----GKIYVCDQCNSKRRRFSSK-------- 550
Cdd:COG5560  444 LTLPLPVSMVWKHTivvfpeSGRRQPLKIeldassTIRGLKKLVDAEYGklgcFEIKVMCIYYGGNYNMLEPadkvllqd 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 551 -------------------PVVLTEAQKQLMICHL------------PQVLRLHLKRFSTNSLCIL-INTLLAMLRSSNG 598
Cdd:COG5560  524 ipqtdfvylyetndngievPVVHLRIEKGYKSKRLfgdpflqlnvliKASIYDKLVKEFEELLVLVeMKKTDVDLVSEQV 603
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 599 KYDQQTEKITGW-----SGRNNREKIGVHVG------------------------------FEEILNMEP---------- 633
Cdd:COG5560  604 RLLREESSPSSWlkletEIDTKREEQVEEEGqmnfndavvisceweekrylslfsydplwtIREIGAAERtitlqdclne 683
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 634 -------------YCcrETLKSLRP-----------------------------------------------------EC 647
Cdd:COG5560  684 fskpeqlglsdswYC--PGCKEFRQaskqmelwrlpmiliihlkrfssvrsfrdkiddlveypiddldlsgveymvddPR 761
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400880 648 FIYDLSAVVMHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQR 709
Cdd:COG5560  762 LIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-706 9.84e-16

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 78.90  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 274 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlamtaseKTRSCKHPPVTDTvvyqmnECQ--EKDTGFVCSRqss 351
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEN----------KFPSDVVDPANDL------NCQliKLADGLLSGR--- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 352 lssglsggasKGRKMELIQPKEPTSQYIslchelhtlfqvmwsgkwalvSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 431
Cdd:cd02658   62 ----------YSKPASLKSENDPYQVGI---------------------KPSMFKALIGKGHPEFSTMRQQDALEFLLHL 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 432 LDKIQRELETTGTSLPaliptsqrklikqvlnvvNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPER---YQCSGK 508
Cdd:cd02658  111 IDKLDRESFKNLGLNP------------------NDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeatEKEEGE 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 509 DIASQPCLVtEMLAKFTETEALEGKiyvCDQCNSKrrrfsskpvvlTEAQKQLMICHLPQVLRLHLKRFSTNSlcilint 588
Cdd:cd02658  173 LVYEPVPLE-DCLKAYFAPETIEDF---CSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQLLE------- 230
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 589 llamlrssngkydqqtekitGWSGRnnreKIGVHVGFEEILNMEPyccretlkslrpecfiYDLSAVVMHHGKGFGSGHY 668
Cdd:cd02658  231 --------------------NWVPK----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHY 270
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 530400880 669 TAYCY--NSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02658  271 VAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
271-696 3.82e-15

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 79.91  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  271 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNqwlamtasektrsckHPPVTDTVVYQMNECqekdtgFvcsrqs 350
Cdd:COG5077   192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTD---------------HPRGRDSVALALQRL------F------ 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  351 slssglsggaskgrkMELIQPKEPTSQyislchelhTLFQVmwSGKWAlvspfamlhsvwrlipAFRGYAQQDAQEFLCE 430
Cdd:COG5077   245 ---------------YNLQTGEEPVDT---------TELTR--SFGWD----------------SDDSFMQHDIQEFNRV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  431 LLDKIQRELETTgtslpaliptsqrklikQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLslefperyQCSGKDI 510
Cdd:COG5077   283 LQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDI--------QLNVKGM 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  511 ASqpclVTEMLAKFTETEALEGKiyvcdqcnskrRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFstnslcilintll 590
Cdd:COG5077   338 KN----LQESFRRYIQVETLDGD-----------NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRF------------- 389
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880  591 amlrssngKYDQQtekitgwsgRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECfIYDLSAVVMHHGKgFGSGHYTA 670
Cdd:COG5077   390 --------EYDFE---------RDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYA 450
                         410       420
                  ....*....|....*....|....*.
gi 530400880  671 YCYNSEGGFWVHCNDSKLSMCTMDEV 696
Cdd:COG5077   451 LLKPEKDGRWYKFDDTRVTRATEKEV 476
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
28-73 1.97e-13

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 65.08  E-value: 1.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 530400880    28 HCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVN 73
Cdd:smart00290   1 RCSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLG 46
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
270-706 2.77e-09

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 60.02  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 270 PGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEktrsckhppvtdtvvyqmnecqekdtgfvcsrq 349
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSE--------------------------------- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 350 sslssglsggaskgrkmeliqpkeptsqyisLCHELHTLFQVMWSGKW--ALVSPFAMLHSVWRLIPA-FRGYAQQDAQE 426
Cdd:cd02669  164 -------------------------------LVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKVSKKkFSITEQSDPVE 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 427 FLCELLDKIQRELETTGTSLPALIPTS-QRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIePFWDLSLEFPER--Y 503
Cdd:cd02669  213 FLSWLLNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPplF 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 504 QCS-GKDIASQPCLvTEMLAKFTETEalegkiyvCDQCNSKRRRFsskpvvlteaqkqlMICHLPQVLRLHLKRFSTNSL 582
Cdd:cd02669  292 KDGnEENIIPQVPL-KQLLKKYDGKT--------ETELKDSLKRY--------------LISRLPKYLIFHIKRFSKNNF 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 583 cilintllamlrssngkydqqtekitgwsgrnNREKIGVHVGFEEILNMEPYCCRETLKSLrPECFIYDLSAVVMHHGKG 662
Cdd:cd02669  349 --------------------------------FKEKNPTIVNFPIKNLDLSDYVHFDKPSL-NLSTKYNLVANIVHEGTP 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 530400880 663 FGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFY 706
Cdd:cd02669  396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
273-706 8.50e-07

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 51.72  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 273 TGLRNLGNTCYMNSVLQVLSHLLIFRQcfLKLDLNQWLAMTASEKTRSCKHPPvtdtvvyqmnecQEKdtgfvcsrqssl 352
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTIKPLRD--LVLNFDESKAELASDYPTERRIGG------------REV------------ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 353 ssglsggaskgRKMELIQPKEptsqyisLCHELHTLFQVMWSGKWALVSPFAMLhsvwrlipAFRGYAQQDAQEflceLL 432
Cdd:cd02666   56 -----------SRSELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE----CI 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 433 DKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVT-CLACDNKSNTIEPFWDLSLEFPERYQCSGKDIA 511
Cdd:cd02666  106 DNVLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVDVGKKGREIVVL 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 512 SQPCLVTEMLAKFTETEALEgkiyvcdqcnskrrrfSSKPVVLTEAQkqlmichLPQVLRLHLKRFSTNSLCILINTLLA 591
Cdd:cd02666  186 LEPKDLYDALDRYFDYDSLT----------------KLPQRSQVQAQ-------LAQPLQRELISMDRYELPSSIDDIDE 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 592 MLRSSNGKYDQQTEKITgWSGRNNREKIgvhvgfEEILnmepyccrETLKSlrpecFIYDLSAVVMHHGKGfGSGHYTAY 671
Cdd:cd02666  243 LIREAIQSESSLVRQAQ-NELAELKHEI------EKQF--------DDLKS-----YGYRLHAVFIHRGEA-SSGHYWVY 301
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 530400880 672 CYNSEGGFWVHCNDSKLSMCTMDEV------CKAQAYILFY 706
Cdd:cd02666  302 IKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
406-706 2.98e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 49.06  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 406 LHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIptsqrKLIKQvLNVVNnIFHGQLLSQVTCLACDNK 485
Cdd:cd02673   18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSN-----IEIKR-LNPLE-AFKYTIESSYVCIGCSFE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 486 SNTIEPFWDLSLEFPERYQCSGKDIASQpclvtemLAKFTETEAlegkiyVCDQCNSKRRRFSSKpvvlteaqkqlmICH 565
Cdd:cd02673   91 ENVSDVGNFLDVSMIDNKLDIDELLISN-------FKTWSPIEK------DCSSCKCESAISSER------------IMT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400880 566 LPQVLRLHLKRFStnslcilintllamLRSSNGKYDQQTEKItgwsgrnnrekigvhvgfeeilnMEPYCcrETLKSlrp 645
Cdd:cd02673  146 FPECLSINLKRYK--------------LRIATSDYLKKNEEI-----------------------MKKYC--GTDAK--- 183
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400880 646 ecfiYDLSAVVMHHGKGFGSGHYTAYCYN-SEGGFWVHCNDSKLSMCTMDEVCKA---QAYILFY 706
Cdd:cd02673  184 ----YSLVAVICHLGESPYDGHYIAYTKElYNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
 
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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