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Conserved domains on  [gi|183397134|ref|NP_006667|]
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ubiquitin carboxyl-terminal hydrolase 20 [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;
145-682 3.23e-69

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.33  E-value: 3.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  145 TGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGL---VRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVN 221
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLsedSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  222 PMFRGYAQQDTQEFLRCLMDQLHEELKepvvatvalteardsdssdtdekregdrspsedeflscdsssdrgegdgqgrg 301
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  302 ggssqaetellipdeagraisekermkdrkfswgqqrtnseqvdedadvdtamaalddqpaeaqppsprssspcrtpepd 381
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  382 ndahlrsssrpcspvhhheghaklsssppraspvrmapsyvlkkaqvlsagsrRRKEQRYRSVISDIFDGSILSLVQCLT 461
Cdd:pfam00443 108 -----------------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLS 134
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  462 CDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyaaqgwlafiveyirrfvvsctpswfWGPVVTLED 541
Cdd:pfam00443 135 CGEVSETFEPFSDLSLPIPGDSA------------------------------------------------ELKTASLQI 166
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  542 CLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEgLDLRPFLAKE-- 619
Cdd:pfam00443 167 CFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEElk 245
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183397134  620 -CTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVH-ETVVQNAEGYVLFY 682
Cdd:pfam00443 246 pKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
810-895 1.97e-31

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 117.84  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134   810 AEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGS--GHVQLKQGADYGQISEETWTYLNSLYGGGPEIA 887
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 183397134   888 IRQSVAQP 895
Cdd:smart00695  81 PRKVVCQG 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
702-785 2.83e-24

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 97.43  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134   702 MREPSLLRFYVSREWLNKFNTFAE------PGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAvn 775
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
                           90
                   ....*....|
gi 183397134   776 HLYVCSICQV 785
Cdd:smart00695  79 PIPRKVVCQG 88
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 1.18e-16

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 74.99  E-value: 1.18e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183397134   30 CQSCGVTGpNLWACLQvaCPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
145-682 3.23e-69

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.33  E-value: 3.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  145 TGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGL---VRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVN 221
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLsedSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  222 PMFRGYAQQDTQEFLRCLMDQLHEELKepvvatvalteardsdssdtdekregdrspsedeflscdsssdrgegdgqgrg 301
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  302 ggssqaetellipdeagraisekermkdrkfswgqqrtnseqvdedadvdtamaalddqpaeaqppsprssspcrtpepd 381
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  382 ndahlrsssrpcspvhhheghaklsssppraspvrmapsyvlkkaqvlsagsrRRKEQRYRSVISDIFDGSILSLVQCLT 461
Cdd:pfam00443 108 -----------------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLS 134
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  462 CDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyaaqgwlafiveyirrfvvsctpswfWGPVVTLED 541
Cdd:pfam00443 135 CGEVSETFEPFSDLSLPIPGDSA------------------------------------------------ELKTASLQI 166
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  542 CLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEgLDLRPFLAKE-- 619
Cdd:pfam00443 167 CFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEElk 245
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183397134  620 -CTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVH-ETVVQNAEGYVLFY 682
Cdd:pfam00443 246 pKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
443-683 6.30e-60

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: 204.06  E-value: 6.30e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 443 SVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAklhsaiyqnvpakpgacgdsyaaqgwlafiveyirr 522
Cdd:cd02674   38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 523 fvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSH 602
Cdd:cd02674   82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 603 VSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFY 682
Cdd:cd02674  150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229

                 .
gi 183397134 683 R 683
Cdd:cd02674  230 E 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
140-686 2.96e-43

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 169.68  E-value: 2.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 140 KPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECG---GLVRTDKKP---ALCKSYQKLVSEVwHKKRPSYVVPTSL 213
Cdd:COG5560  261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 214 SHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEEL----KEPVVATVALTEARDSDSSDT-----DEKREGDRSPSEDEFL 284
Cdd:COG5560  340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnriiKKPYTSKPDLSPGDDVVVKKKakecwWEHLKRNDSIITDLFQ 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 285 SCDSSSDRGEGDGQGRGGGSSQAETELLIPdeagraISEKERMKDRKFSwgqQRTNSEQVDEDADVDTAMAALDDQ-PAE 363
Cdd:COG5560  420 GMYKSTLTCPGCGSVSITFDPFMDLTLPLP------VSMVWKHTIVVFP---ESGRRQPLKIELDASSTIRGLKKLvDAE 490
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 364 AQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHEGHAKLSSSPP----------------RASPVRMAPSYVLKkaq 427
Cdd:COG5560  491 YGKLGCFEIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYETNDngievpvvhlriekgyKSKRLFGDPFLQLN--- 567
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 428 VLSAGSRRRK-----EQRYRSVISDIFDGSILSLVqcLTCDRVSTTVETFQDLSLPIPGK-EDLAKLHSAIYQNVpAKPG 501
Cdd:COG5560  568 VLIKASIYDKlvkefEELLVLVEMKKTDVDLVSEQ--VRLLREESSPSSWLKLETEIDTKrEEQVEEEGQMNFND-AVVI 644
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 502 ACgdSYAAQGWLafiveyirrFVVSCTPSW------FWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKV 575
Cdd:COG5560  645 SC--EWEEKRYL---------SLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 576 LRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITtYDLLSVICHHGTAGSGHYIAYCQNVINGQ 655
Cdd:COG5560  714 WRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLI-YDLYAVDNHYGGLSGGHYTAYARNFANNG 792
                        570       580       590
                 ....*....|....*....|....*....|.
gi 183397134 656 WYEFDDQYVTEVHETVVQNAEGYVLFYRKSS 686
Cdd:COG5560  793 WYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
DUSP smart00695
Domain in ubiquitin-specific proteases;
810-895 1.97e-31

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 117.84  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134   810 AEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGS--GHVQLKQGADYGQISEETWTYLNSLYGGGPEIA 887
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 183397134   888 IRQSVAQP 895
Cdd:smart00695  81 PRKVVCQG 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
702-785 2.83e-24

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 97.43  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134   702 MREPSLLRFYVSREWLNKFNTFAE------PGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAvn 775
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
                           90
                   ....*....|
gi 183397134   776 HLYVCSICQV 785
Cdd:smart00695  79 PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
817-889 1.38e-22

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: 92.43  E-value: 1.38e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183397134  817 IYCISMQWFREWEAFVKGKdNEPPGPIDNSRIAQV--KGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIR 889
Cdd:pfam06337   4 VYLISSKWLNKWKSYVKEP-NNEPGPIDNSDLLDDesNGQLKPNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 1.18e-16

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 74.99  E-value: 1.18e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183397134   30 CQSCGVTGpNLWACLQvaCPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
710-780 3.34e-14

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: 68.55  E-value: 3.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 183397134  710 FYVSREWLNKFNTFAE-----PGPITNQTFLC--SHGGIPPHKYHYIDdlVVILPQNVWEHLYNRFGGGPAVNHLYVC 780
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLDdeSNGQLKPNLQEGVD--YVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
29-81 1.39e-05

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 43.12  E-value: 1.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 183397134    29 TCQSCGVTGpNLWACLQvaCPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRL 81
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
145-682 3.23e-69

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.33  E-value: 3.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  145 TGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGL---VRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVN 221
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLsedSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  222 PMFRGYAQQDTQEFLRCLMDQLHEELKepvvatvalteardsdssdtdekregdrspsedeflscdsssdrgegdgqgrg 301
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  302 ggssqaetellipdeagraisekermkdrkfswgqqrtnseqvdedadvdtamaalddqpaeaqppsprssspcrtpepd 381
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  382 ndahlrsssrpcspvhhheghaklsssppraspvrmapsyvlkkaqvlsagsrRRKEQRYRSVISDIFDGSILSLVQCLT 461
Cdd:pfam00443 108 -----------------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLS 134
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  462 CDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyaaqgwlafiveyirrfvvsctpswfWGPVVTLED 541
Cdd:pfam00443 135 CGEVSETFEPFSDLSLPIPGDSA------------------------------------------------ELKTASLQI 166
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  542 CLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEgLDLRPFLAKE-- 619
Cdd:pfam00443 167 CFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEElk 245
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183397134  620 -CTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVH-ETVVQNAEGYVLFY 682
Cdd:pfam00443 246 pKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
443-683 6.30e-60

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: 204.06  E-value: 6.30e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 443 SVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAklhsaiyqnvpakpgacgdsyaaqgwlafiveyirr 522
Cdd:cd02674   38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 523 fvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSH 602
Cdd:cd02674   82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 603 VSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFY 682
Cdd:cd02674  150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229

                 .
gi 183397134 683 R 683
Cdd:cd02674  230 E 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
428-683 1.77e-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: 181.14  E-value: 1.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 428 VLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsy 507
Cdd:cd02257   40 LKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL----------------------- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 508 aaqgwlafiveyirrfvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKlRNGVKYCKVLRLPEILCIHLK 587
Cdd:cd02257   97 ---------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 588 RFRH-EVMYSFKINSHVSFPLEgLDLRPFLAKECTSQ-----ITTYDLLSVICHHGTAG-SGHYIAYCQNVINGQWYEFD 660
Cdd:cd02257  149 RFSFnEDGTKEKLNTKVSFPLE-LDLSPYLSEGEKDSdsdngSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFN 227
                        250       260
                 ....*....|....*....|....*...
gi 183397134 661 DQYVTEVHETVVQ-----NAEGYVLFYR 683
Cdd:cd02257  228 DDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
429-682 9.59e-47

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 169.38  E-value: 9.59e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 429 LSAGSRRRKEqryRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGkedlaklhsaiyqnvpakpgacgdsya 508
Cdd:cd02661  111 LKAVDPSSQE---TTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------------------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 509 aqgwlafiveyirrfvvsctpswfwgpVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKR 588
Cdd:cd02661  161 ---------------------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKR 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 589 FrhEVMYSFKINSHVSFPLEgLDLRPFLAKEcTSQITTYDLLSVICHHGT-AGSGHYIAYCQNvINGQWYEFDDQYVTEV 667
Cdd:cd02661  214 F--SNFRGGKINKQISFPET-LDLSPYMSQP-NDGPLKYKLYAVLVHSGFsPHSGHYYCYVKS-SNGKWYNMDDSKVSPV 288
                        250
                 ....*....|....*
gi 183397134 668 HETVVQNAEGYVLFY 682
Cdd:cd02661  289 SIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
444-682 3.72e-45

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: 165.62  E-value: 3.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 444 VISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKedlaklhsaiyqnvpAKPGACGDSYAAQGWLafiveyirrf 523
Cdd:cd02660  122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK---------------STPSWALGESGVSGTP---------- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 524 vvsctpswfwgpvvTLEDCLAaFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSF-KINSH 602
Cdd:cd02660  177 --------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSrKIDTY 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 603 VSFPLEgLDLRPFL-AKECTSQIT-------TYDLLSVICHHGTAGSGHYIAYCQNViNGQWYEFDDQYVTEVHETVVQN 674
Cdd:cd02660  242 VQFPLE-LNMTPYTsSSIGDTQDSnsldpdyTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLK 319

                 ....*...
gi 183397134 675 AEGYVLFY 682
Cdd:cd02660  320 SQAYLLFY 327
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
140-686 2.96e-43

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 169.68  E-value: 2.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 140 KPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECG---GLVRTDKKP---ALCKSYQKLVSEVwHKKRPSYVVPTSL 213
Cdd:COG5560  261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 214 SHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEEL----KEPVVATVALTEARDSDSSDT-----DEKREGDRSPSEDEFL 284
Cdd:COG5560  340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnriiKKPYTSKPDLSPGDDVVVKKKakecwWEHLKRNDSIITDLFQ 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 285 SCDSSSDRGEGDGQGRGGGSSQAETELLIPdeagraISEKERMKDRKFSwgqQRTNSEQVDEDADVDTAMAALDDQ-PAE 363
Cdd:COG5560  420 GMYKSTLTCPGCGSVSITFDPFMDLTLPLP------VSMVWKHTIVVFP---ESGRRQPLKIELDASSTIRGLKKLvDAE 490
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 364 AQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHEGHAKLSSSPP----------------RASPVRMAPSYVLKkaq 427
Cdd:COG5560  491 YGKLGCFEIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYETNDngievpvvhlriekgyKSKRLFGDPFLQLN--- 567
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 428 VLSAGSRRRK-----EQRYRSVISDIFDGSILSLVqcLTCDRVSTTVETFQDLSLPIPGK-EDLAKLHSAIYQNVpAKPG 501
Cdd:COG5560  568 VLIKASIYDKlvkefEELLVLVEMKKTDVDLVSEQ--VRLLREESSPSSWLKLETEIDTKrEEQVEEEGQMNFND-AVVI 644
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 502 ACgdSYAAQGWLafiveyirrFVVSCTPSW------FWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKV 575
Cdd:COG5560  645 SC--EWEEKRYL---------SLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMEL 713
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 576 LRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITtYDLLSVICHHGTAGSGHYIAYCQNVINGQ 655
Cdd:COG5560  714 WRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLI-YDLYAVDNHYGGLSGGHYTAYARNFANNG 792
                        570       580       590
                 ....*....|....*....|....*....|.
gi 183397134 656 WYEFDDQYVTEVHETVVQNAEGYVLFYRKSS 686
Cdd:COG5560  793 WYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
445-686 7.90e-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: 141.63  E-value: 7.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 445 ISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLaklhsaiyqnvpakpgacgdsyaaqgwlafiveyirrfv 524
Cdd:cd02659  113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 525 vsctpswfwgpvvtlEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRH--EVMYSFKINSH 602
Cdd:cd02659  154 ---------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 603 VSFPLEgLDLRPFLAKEC----------TSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEV----- 667
Cdd:cd02659  219 FEFPLE-LDMEPYTEKGLakkegdsekkDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnda 297
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 183397134 668 -------HETVVQ------------NAegYVLFYRKSS 686
Cdd:cd02659  298 eeecfggEETQKTydsgprafkrttNA--YMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-683 4.73e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 132.13  E-value: 4.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 442 RSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyaaqgwlafiveyir 521
Cdd:cd02667   66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 522 rfvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRngvKYCKVLRLPEILCIHLKRFRHEVMYSF-KIN 600
Cdd:cd02667  109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 601 SHVSFPlEGLDLRPFLAKECTSQITT----YDLLSVICHHGTAGSGHYIAY---------------------CQNVINGQ 655
Cdd:cd02667  173 RHVSFP-EILDLAPFCDPKCNSSEDKssvlYRLYGVVEHSGTMRSGHYVAYvkvrppqqrlsdltkskpaadEAGPGSGQ 251
                        250       260
                 ....*....|....*....|....*...
gi 183397134 656 WYEFDDQYVTEVHETVVQNAEGYVLFYR 683
Cdd:cd02667  252 WYYISDSDVREVSLEEVLKSEAYLLFYE 279
DUSP smart00695
Domain in ubiquitin-specific proteases;
810-895 1.97e-31

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 117.84  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134   810 AEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGS--GHVQLKQGADYGQISEETWTYLNSLYGGGPEIA 887
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80

                   ....*...
gi 183397134   888 IRQSVAQP 895
Cdd:smart00695  81 PRKVVCQG 88
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
445-682 9.02e-30

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 120.11  E-value: 9.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 445 ISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGkedlaklHSAIyqnvpakpgacgdsyaaqgwlafiveyirrfv 524
Cdd:cd02663  109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTSI-------------------------------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 525 vsctpswfwgpvvtlEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYS--FKINSH 602
Cdd:cd02663  150 ---------------TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYR 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 603 VSFPLEgldLRPF-LAKECTSQITTYDLLSVICHHG-TAGSGHYIAYCQnvINGQWYEFDDQYVTEVHETVVQN------ 674
Cdd:cd02663  215 VVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEffgdsp 289
                        250
                 ....*....|
gi 183397134 675 --AEGYVLFY 682
Cdd:cd02663  290 nqATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-666 1.81e-29

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 120.22  E-value: 1.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 442 RSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEdlaklhsaiyqnvpakpgacgdsyaaqgwlafiveyir 521
Cdd:cd02668  115 KNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK-------------------------------------- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 522 rfvvsctpswfwgpvvTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKR--FRHEVMYSFKI 599
Cdd:cd02668  157 ----------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRfvFDRKTGAKKKL 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 183397134 600 NSHVSFPLEgLDLRPFLAkECTSQITTYDLLSVICHHGT-AGSGHYIAYCQNVINGQWYEFDDQYVTE 666
Cdd:cd02668  221 NASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
DUSP smart00695
Domain in ubiquitin-specific proteases;
702-785 2.83e-24

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 97.43  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134   702 MREPSLLRFYVSREWLNKFNTFAE------PGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAvn 775
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
                           90
                   ....*....|
gi 183397134   776 HLYVCSICQV 785
Cdd:smart00695  79 PIPRKVVCQG 88
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
449-682 3.18e-23

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 99.36  E-value: 3.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 449 FDGSILSLVQCLTCDRVST-TVETFQDLSLPIPGKEdlaklhsaiyqnvpakpgacgdsyaaqgwlafiveyirrfvvsc 527
Cdd:cd02662   56 FDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQS-------------------------------------------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 528 tpswfWGPVVTLEDCLAAFFAADELKGdnmYSCERCKklrngvkyCKVLRLPEILCIHLKRFR-HEVMYSFKINSHVSFP 606
Cdd:cd02662   92 -----SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 607 LEgldLRPFLakectsqittYDLLSVICHHGTAGSGHYIAY--------------------CQNVINGQWYEFDDQYVTE 666
Cdd:cd02662  156 ER---LPKVL----------YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKE 222
                        250
                 ....*....|....*..
gi 183397134 667 VHE-TVVQNAEGYVLFY 682
Cdd:cd02662  223 VSEsEVLEQKSAYMLFY 239
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
817-889 1.38e-22

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: 92.43  E-value: 1.38e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183397134  817 IYCISMQWFREWEAFVKGKdNEPPGPIDNSRIAQV--KGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIR 889
Cdd:pfam06337   4 VYLISSKWLNKWKSYVKEP-NNEPGPIDNSDLLDDesNGQLKPNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
440-683 1.06e-19

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 91.40  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 440 RYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPgkedlaklhsaiyqnvpakpgacgdsyaaqgwlafivey 519
Cdd:cd02664   94 RLHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP--------------------------------------- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 520 irrfvvsctpswfwgpvvTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFR--------- 590
Cdd:cd02664  135 ------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkthvre 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 591 ---HEVMY----SFKINSHVSFPLEGLDLRPFLAKECTSQITT---YDLLSVICHHGTAG-SGHYIAYCQNV-------- 651
Cdd:cd02664  197 kimDNVSInevlSLPVRVESKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSeSGHYFTYARDQtdadstgq 276
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 183397134 652 ------------INGQWYEFDDQYVTEVHETVVQNAEG-------YVLFYR 683
Cdd:cd02664  277 ecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFYE 327
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
538-669 2.40e-19

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 93.78  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  538 TLEDCLAAFFAADELKGDNMYSCERcKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYS--FKINSHVSFPLEgLDLRPF 615
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDmmVKINDRYEFPLE-IDLLPF 416
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 183397134  616 L---AKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHE 669
Cdd:COG5077   417 LdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATE 473
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 1.18e-16

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 74.99  E-value: 1.18e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183397134   30 CQSCGVTGpNLWACLQvaCPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
445-683 1.40e-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: 81.60  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 445 ISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIyqnvpakpgacgdsyaaqgwlafivEYIRrfv 524
Cdd:cd02658  126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGEL-------------------------VYEP--- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 525 vsctpswfwgpvVTLEDCLAAFFAADELKgdnmYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMY-SFKINSHV 603
Cdd:cd02658  178 ------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPI 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 604 SFPLEgldLRPflAKectsqittYDLLSVICHHGT-AGSGHYIAYCQNVIN--GQWYEFDDQYVtevheTVVQNAE---- 676
Cdd:cd02658  242 DVPEE---LGP--GK--------YELIAFISHKGTsVHSGHYVAHIKKEIDgeGKWVLFNDEKV-----VASQDPPemkk 303

                 ....*...
gi 183397134 677 -GYVLFYR 683
Cdd:cd02658  304 lGYIYFYQ 311
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
442-683 1.59e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 81.86  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 442 RSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGAcgdsyaaqgwlafiveyir 521
Cdd:cd02671  120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMK------------------- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 522 rfvvsctpswfwgpvvTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSF---- 597
Cdd:cd02671  181 ----------------TLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDcygg 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 598 --KINSHVSFPlegLDLRPFlaKECTSQIT-TYDLLSVICHHG-TAGSGHYIAYCqnvingQWYEFDDQYVTEVHETVVQ 673
Cdd:cd02671  245 lsKVNTPLLTP---LKLSLE--EWSTKPKNdVYRLFAVVMHSGaTISSGHYTAYV------RWLLFDDSEVKVTEEKDFL 313
                        250
                 ....*....|....*....
gi 183397134 674 NA---------EGYVLFYR 683
Cdd:cd02671  314 EAlspntsstsTPYLLFYK 332
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
574-683 1.04e-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 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: 78.91  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 574 KVLRLPEILCIHLKRF--RHEVMYSFKINSHVSFPLEgLDLRPFLakeCTSQIttYDLLSVICHHG-TAGSGHYIAYCQN 650
Cdd:cd02657  192 RISRLPKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRR 265
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 183397134 651 VINGQWYEFDDQYVTEVHETVVQNAEG-------YVLFYR 683
Cdd:cd02657  266 KNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLYK 305
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
710-780 3.34e-14

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: 68.55  E-value: 3.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 183397134  710 FYVSREWLNKFNTFAE-----PGPITNQTFLC--SHGGIPPHKYHYIDdlVVILPQNVWEHLYNRFGGGPAVNHLYVC 780
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLDdeSNGQLKPNLQEGVD--YVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-683 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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 74.28  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 535 PVVTLEDCLAAFFAadelkgdnmyscERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRP 614
Cdd:cd02669  301 PQVPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSD 368
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183397134 615 FLAKECTSQI--TTYDLLSVICHHGT-AGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYR 683
Cdd:cd02669  369 YVHFDKPSLNlsTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
144-291 1.66e-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: 72.62  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 144 LTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVrtdkkpaLCKSYQKLVSEVWHKKRPSYV---VPTSLSHGIKLV 220
Cdd:cd02671   24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI-------SSVEQLQSSFLLNPEKYNDELanqAPRRLLNALREV 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183397134 221 NPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTdEKREGDRSPS----EDEFLSCDSSSD 291
Cdd:cd02671   97 NPMYEGYLQHDAQEVLQCILGNIQELVEKDFQGQLVLRTRCLECETFT-ERREDFQDISvpvqESELSKSEESSE 170
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
577-684 5.21e-13

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 70.60  E-value: 5.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 577 RLPEILCIHLKRFRHEVMYSfKINSHVSFPLEgLDLRpFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQnvINGQW 656
Cdd:COG5533  178 KLPKILTIQLKRFANLGGNQ-KIDTEVDEKFE-LPVK-HDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKW 252
                         90       100       110
                 ....*....|....*....|....*....|.
gi 183397134 657 YEFDDQYVTEVHETVVQNA---EGYVLFYRK 684
Cdd:COG5533  253 EKANDSDVTPVSEEEAINEkakNAYLYFYER 283
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
146-243 4.00e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 64.72  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 146 GMKNLGNSCYMNAALQALSNCPPLTQFFLEcgglvrtdkKPALcksyqkLVSEVWHKKrpsyvvptslshgiklvnPMFR 225
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------TPKE------LFSQVCRKA------------------PQFK 47
                         90
                 ....*....|....*...
gi 183397134 226 GYAQQDTQEFLRCLMDQL 243
Cdd:cd02667   48 GYQQQDSHELLRYLLDGL 65
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
537-682 4.38e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 61.01  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 537 VTLEDCLAAFFAADELKGDnmysCERCKKlRNGVKYCKVLRLPEILCIHLKRF--RHEVMYSFKINshvsfplegldlRP 614
Cdd:cd02673  110 DIDELLISNFKTWSPIEKD----CSSCKC-ESAISSERIMTFPECLSINLKRYklRIATSDYLKKN------------EE 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 183397134 615 FLaKECTSQITTYDLLSVICHHG-TAGSGHYIAYCQNVING-QWYEFDDQYVTEVHE-TVVQNA--EGYVLFY 682
Cdd:cd02673  173 IM-KKYCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKnDVSTNArsSGYLIFY 244
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
146-244 4.32e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 55.96  E-value: 4.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 146 GMKNLGNSCYMNAALQALSNCpplTQFFLECGGLVRTDKKP--ALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKlvNPM 223
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMA---KDFRRQVLSLNLPRLGDsqSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR--PPW 75
                         90       100
                 ....*....|....*....|.
gi 183397134 224 FRGYAQQDTQEFLRCLMDQLH 244
Cdd:cd02664   76 FTPGSQQDCSEYLRYLLDRLH 96
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
146-248 4.51e-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 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: 55.80  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 146 GMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDkkpalCKSYQKLVSEVWHK-----KRPSYVVPTSLSHGIKLV 220
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGA-----NQSSDNLTNALRDLfdtmdKKQEPVPPIEFLQLLRMA 75
                         90       100       110
                 ....*....|....*....|....*....|....
gi 183397134 221 NPMF------RGYAQQDTQEFLRCLMDQLHEELK 248
Cdd:cd02657   76 FPQFaekqnqGGYAQQDAEECWSQLLSVLSQKLP 109
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
560-661 1.03e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 54.58  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  560 CERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEvmYSFKINSHVSFPLEgLDLRPFLAKECTSQITTYDLLSVICH-HGT 638
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
                          90       100       110
                  ....*....|....*....|....*....|
gi 183397134  639 AGSGHYIAYC-------QNVINGQWYEFDD 661
Cdd:pfam13423 273 GTSGHLVSFVkvadselEDPTESQWYLFND 302
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
627-682 1.12e-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: 54.80  E-value: 1.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183397134 627 YDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHET-VVQ-----NAEGYVLFY 682
Cdd:cd02666  281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASeVFLftlgnTATPYFLVY 342
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
560-682 1.49e-07

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


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 53.67  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 560 CERCKKLRNGVKYCKVLRLPEI----LCIHLKRF-------RHEVMYSFKINSHVSFPLEgldLRPFLAKECTSQ-ITTY 627
Cdd:cd02672  137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI---DHDKLVKNRGQEsIYKY 213
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183397134 628 DLLSVICH--HGTAGsGHY----IAYCQNVINGQWYEFDDQYVTEVHETvvqnaeGYVLFY 682
Cdd:cd02672  214 ELVGYVCEinDSSRG-QHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
146-255 1.78e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 53.65  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 146 GMKNLGNSCYMNAALQALS-NCPPLTQFFLECGGLVRT-------DKKPALCKSYQKLVSEVWhkkrpsyvvpTSLSHGI 217
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALW----------SSKEHKV 70
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 183397134 218 KLVNPMfrgYAQQDTQEFLRCLMDqlheELKEPVVATV 255
Cdd:COG5533   71 GWIPPM---GSQEDAHELLGKLLD----ELKLDLVNSF 101
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
39-247 7.65e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 52.71  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134  39 NLWACLQVACPYVGCGESfaDHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVfLEQRLAAPLLGSSSKFSEQDspppshp 118
Cdd:cd02669   27 NVYACLVCGKYFQGRGKG--SHAYTHSLEDNHHVFLNLETLKFYCLPDNYEI-IDSSLDDIKYVLNPTYTKEQ------- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 119 lkavpIAVADEGESESEDDDLKP--RGLTGMKNLGNSCYMNAALQALSNCPPLTQFFL-ECGGLVRTDKKPALCKSYQKL 195
Cdd:cd02669   97 -----ISDLDRDPKLSRDLDGKPylPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDRKSELVKRLSEL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 183397134 196 VSEVWHKKR-PSYVVPTSLSHGIKLV-NPMFRGYAQQDTQEFLRCLMDQLHEEL 247
Cdd:cd02669  172 IRKIWNPRNfKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL 225
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
529-683 1.04e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 47.91  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 529 PSWFWGPVVTLEDCLAAFFAADELKgdnmyscerckklrngvkyckvlRLPEILCIHLKRFRHEVMYSFKINSHVsFPLE 608
Cdd:cd02670   72 PDDDDGGGITLEQCLEQYFNNSVFA-----------------------KAPSCLIICLKRYGKTEGKAQKMFKKI-LIPD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 609 GLDLRPFLA----------KECTSQITTYD-----------LLSVICHHGTA-GSGHYIAY-----------CQNVINGQ 655
Cdd:cd02670  128 EIDIPDFVAddpracskcqLECRVCYDDKDfsptcgkfklsLCSAVCHRGTSlETGHYVAFvrygsysltetDNEAYNAQ 207
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 183397134 656 WYEFDD-------QYVTEVHETVVQnAEGYVLFYR 683
Cdd:cd02670  208 WVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
29-81 1.39e-05

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 43.12  E-value: 1.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 183397134    29 TCQSCGVTGpNLWACLQvaCPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRL 81
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
146-172 1.65e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 47.36  E-value: 1.65e-05
                         10        20
                 ....*....|....*....|....*..
gi 183397134 146 GMKNLGNSCYMNAALQALSNCPPLTQF 172
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
146-176 3.98e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 46.13  E-value: 3.98e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 183397134 146 GMKNLGNSCYMNAALQALSN----CPPLTQFFLEC 176
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSAdqqdAQEFLLFLLDG 35
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
578-682 2.00e-04

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


Pssm-ID: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 43.70  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183397134 578 LPEILCIHLKRFRHEVMYSFKINSHVSFPlegldlrpflakECTSQITtYDLLSVICHHGTAGSGHYIAYCQNVINGQWY 657
Cdd:cd02665  128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWAYIYKQSRQEWE 194
                         90       100       110
                 ....*....|....*....|....*....|...
gi 183397134 658 EFDDQYVTEVHETVVQ--------NAEGYVLFY 682
Cdd:cd02665  195 KYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
 
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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