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Conserved domains on  [gi|1794418471|ref|NP_001364359|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform 4 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031674)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-704 2.23e-71

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 238.50  E-value: 2.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 581
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 658
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1794418471 659 GTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 704
Cdd:pfam00443 264 GSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
832-916 4.42e-30

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.99  E-value: 4.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471  832 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 908
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*...
gi 1794418471  909 LRPPVVHV 916
Cdd:smart00695  81 PRKVVCQG 88
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 4.77e-18

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.84  E-value: 4.77e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418471  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP super family cl12116
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 726-795 1.27e-15

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.


The actual alignment was detected with superfamily member smart00695:

Pssm-ID: 416436  Cd Length: 88  Bit Score: 72.78  E-value: 1.27e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418471  726 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 795
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-704 2.23e-71

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 238.50  E-value: 2.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 581
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 658
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1794418471 659 GTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 704
Cdd:pfam00443 264 GSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 473-705 4.35e-63

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: 212.92  E-value: 4.35e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvks 552
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 553 wfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL 632
Cdd:cd02674    82 ----PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1794418471 633 DLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 705
Cdd:cd02674   158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-708 1.91e-44

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 173.15  E-value: 1.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 180 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPTTL 253
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 254 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 319
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 320 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 372
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 373 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 450
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 451 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 527
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 528 VKAGSCgeAYAPQGWIAFFmEYVKSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFP 601
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF-SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLP 717

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 602 EILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLNNLWYE 680
Cdd:COG5560   718 MILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYL 795

                         570       580
                  ....*....|....*....|....*...
gi 1794418471 681 FDDQSVTEVSESTVQNAEAYVLFYRKSS 708
Cdd:COG5560   796 FDDSRITEVDPEDSVTSSAYVLFYRRKS 823
DUSP smart00695
Domain in ubiquitin-specific proteases;
832-916 4.42e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.99  E-value: 4.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471  832 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 908
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*...
gi 1794418471  909 LRPPVVHV 916
Cdd:smart00695  81 PRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 838-910 1.65e-20

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: 86.27  E-value: 1.65e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418471 838 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 910
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 4.77e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.84  E-value: 4.77e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418471  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP smart00695
Domain in ubiquitin-specific proteases;
726-795 1.27e-15

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 72.78  E-value: 1.27e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418471  726 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 795
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 732-802 5.61e-12

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: 62.00  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 732 FYISRQWLNKFKTFAE-----PGPISNNDFLCihggvPPRKAGYIEDLVL-----MLPQNIWDNLYSRYGGGPAVNHLYI 801
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQEgvdyvIVPEEVWEFLVEWYGGGPEIKRNVV 79


                  .
gi 1794418471 802 C 802
Cdd:pfam06337  80 N 80
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
60-112 1.61e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 54.29  E-value: 1.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1794418471   60 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 112
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
185-704 2.23e-71

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 238.50  E-value: 2.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVN 261
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 262 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenengsrcfse 341
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 342 dnnettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndls 421
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 422 tpqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLET 501
Cdd:pfam00443 108 -------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEP 144

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 502 FQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvkswfWGPVVTLQDCLAAFFARDELKGDNMYS 581
Cdd:pfam00443 145 FSDLSLPIPGDSA----------------------------------------ELKTASLQICFLQFSKLEELDDEEKYY 184

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLLSVICHH 658
Cdd:pfam00443 185 CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLVAVVVHS 263

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1794418471 659 GTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 704
Cdd:pfam00443 264 GSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 473-705 4.35e-63

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: 212.92  E-value: 4.35e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAklhssshptsivkagscgeayapqgwiaffmeyvks 552
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 553 wfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGL 632
Cdd:cd02674    82 ----PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1794418471 633 DLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 705
Cdd:cd02674   158 DLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 461-705 1.57e-54

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: 190.00  E-value: 1.57e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 461 SPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapq 540
Cdd:cd02257    43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 541 gwiaffmeyvkswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQNFPEILCIHLKRFRH-ELMFST 619
Cdd:cd02257    97 ----------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSFnEDGTKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 620 KISTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST 693
Cdd:cd02257   160 KLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEE 238

                         250
                  ....*....|....*..
gi 1794418471 694 VQ-----NAEAYVLFYR 705
Cdd:cd02257   239 VLefgslSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 186-704 8.20e-48

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: 173.33  E-value: 8.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 186 GLKNIGNTCYMNAALQALSNCPPLTQFFLD---CGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNP 262
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 263 TFRGYSQQDAQEFLRCLMDLLHEELKeqvmeveedpqtitteetmeedksqsdvdfqscescsnsdraenenGSRCFSED 342
Cdd:cd02660    82 NLAGYSQQDAHEFFQFLLDQLHTHYG----------------------------------------------GDKNEAND 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 343 NNEttmliqddennsemskdwqkekmCNKInkvnsegefdkdrdsisetvdlnnqetvkvqIHSraseyitdvhsndlst 422
Cdd:cd02660   116 ESH-----------------------CNCI-------------------------------IHQ---------------- 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 423 pqilpsnegvnprlsasppksgnlwpglapphkkaqsaspkrkkqhkkyrsvisdIFDGTIISSVQCLTCDRVSVTLETF 502
Cdd:cd02660   126 -------------------------------------------------------TFSGSLQSSVTCQRCGGVSTTVDPF 150

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 503 QDLSLPIPGKEdlaklhssshpTSIVKAGSCGEAYAPqgwiaffmeyvkswfwgpvvTLQDCLAaFFARDELKGDNMYSC 582
Cdd:cd02660   151 LDLSLDIPNKS-----------TPSWALGESGVSGTP--------------------TLSDCLD-RFTRPEKLGDFAYKC 198

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 583 EKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPAQIVTYDLLS 653
Cdd:cd02660   199 SGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFA 277

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1794418471 654 VICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 704
Cdd:cd02660   278 VVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 185-704 2.81e-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: 170.92  E-value: 2.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 185 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDcGGLARTDKKPAICKS-YLKLMTELWHKSRPGSVVPTTLFQGIKTVNPT 263
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 264 FRGYSQQDAQEFLRCLMDLLHEelkeqvmeveedpqtitteetmeedksqsdvdfqsceSCSNSdraenengsrcfsedn 343
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQK-------------------------------------ACLDR---------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 344 nettmliqddennsemskdwqkekmcnkinkvnsegefdkdrdsisetvdlnnqetvkvqihsraseyitdvhsndlstp 423
Cdd:cd02661       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 424 qilpsnegvNPRLSASPPKSgnlwpglapphkkaqsaspkrkkqhkKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQ 503
Cdd:cd02661   108 ---------FKKLKAVDPSS--------------------------QETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 504 DLSLPIPGkedlaklhssshptsivkagscgeayapqgwiaffmeyvkswfwgpVVTLQDCLAAFFARDELKGDNMYSCE 583
Cdd:cd02661   153 DLSLDIKG----------------------------------------------ADSLEDALEQFTKPEQLDGENKYKCE 186

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 584 KCKKLRNGVKFCKVQNFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-AS 662
Cdd:cd02661   187 RCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFsPH 262

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1794418471 663 SGHYIAYCRnNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 704
Cdd:cd02661   263 SGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
180-708 1.91e-44

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 173.15  E-value: 1.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 180 RARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPTTL 253
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 254 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL-KEQVMEVEEDPQTITTEETMEEDKSQSDVD-------------FQ 319
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsiitdlFQ 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 320 -------SCESCSNSD---------------RAENENGSRCFSEDNNETTMLIQDDENNSEMS-KDWQKEKM----CNKI 372
Cdd:COG5560   420 gmykstlTCPGCGSVSitfdpfmdltlplpvSMVWKHTIVVFPESGRRQPLKIELDASSTIRGlKKLVDAEYgklgCFEI 499

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 373 nKVNsegEFDKDRDSiseTVDLNNQETVKVQIHSRASEYITDVHSNDLSTPQI-LPSNEGV-NPRLSASPPKSGNLwpgl 450
Cdd:COG5560   500 -KVM---CIYYGGNY---NMLEPADKVLLQDIPQTDFVYLYETNDNGIEVPVVhLRIEKGYkSKRLFGDPFLQLNV---- 568

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 451 apphkkaQSASPKRKKQHKKYRSVISDIFDGTI---ISSVQcLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSI 527
Cdd:COG5560   569 -------LIKASIYDKLVKEFEELLVLVEMKKTdvdLVSEQ-VRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFND 640

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 528 VKAGSCgeAYAPQGWIAFFmEYVKSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFP 601
Cdd:COG5560   641 AVVISC--EWEEKRYLSLF-SYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLP 717

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 602 EILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLNNLWYE 680
Cdd:COG5560   718 MILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYL 795

                         570       580
                  ....*....|....*....|....*...
gi 1794418471 681 FDDQSVTEVSESTVQNAEAYVLFYRKSS 708
Cdd:COG5560   796 FDDSRITEVDPEDSVTSSAYVLFYRRKS 823
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 475-708 3.84e-38

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 145.48  E-value: 3.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 475 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLaklhssshptsivkagscgeayapqgwiaffmeyvkswf 554
Cdd:cd02659   113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 555 wgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRH--ELMFSTKISTHVSFPLEgL 632
Cdd:cd02659   154 -------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRFEFPLE-L 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 633 DLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNA----- 697
Cdd:cd02659   226 DMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEEcfgge 305

                         250       260
                  ....*....|....*....|....*...
gi 1794418471 698 -----------------EAYVLFYRKSS 708
Cdd:cd02659   306 etqktydsgprafkrttNAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 472-705 3.05e-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: 132.51  E-value: 3.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 472 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDlaklhssshptsivkagscgeayapqgwiaffmeyvk 551
Cdd:cd02667    66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 552 swfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQNFPEILCIHLKRFRHELMFST-KISTHVSFPlE 630
Cdd:cd02667   109 -----SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP-E 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 631 GLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL--------------------WYEF 681
Cdd:cd02667   180 ILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagpgsgqWYYI 255

                         250       260
                  ....*....|....*....|....
gi 1794418471 682 DDQSVTEVSESTVQNAEAYVLFYR 705
Cdd:cd02667   256 SDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 475-704 1.46e-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: 125.50  E-value: 1.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 475 ISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGkedlaklHSSshptsivkagscgeayapqgwiaffmeyvkswf 554
Cdd:cd02663   109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 555 wgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS--TKISTHVSFPLEgl 632
Cdd:cd02663   149 ------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYRVVFPLE-- 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 633 dLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTVQN--------AEAYVL 702
Cdd:cd02663   221 -LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAVEEffgdspnqATAYVL 297


                  ..
gi 1794418471 703 FY 704
Cdd:cd02663   298 FY 299
DUSP smart00695
Domain in ubiquitin-specific proteases;
832-916 4.42e-30

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 113.99  E-value: 4.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471  832 KEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCG---NVMLRQGADSGQISEETWNFLQSIYGGGPEVI 908
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprlKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*...
gi 1794418471  909 LRPPVVHV 916
Cdd:smart00695  81 PRKVVCQG 88
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 465-688 8.11e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 120.99  E-value: 8.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 465 KKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdlaklhssshptsivkagscgeayapqgwia 544
Cdd:cd02668   108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 545 ffmeyvkswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHEL--MFSTKIS 622
Cdd:cd02668   157 ---------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLN 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1794418471 623 THVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 688
Cdd:cd02668   222 ASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 479-704 6.02e-26

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: 107.45  E-value: 6.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 479 FDGTIISSVQCLTCDRVS-VTLETFQDLSLPIPGKedlaklhSSSHPTsivkagscgeayapqgwiaffmeyvkswfwgp 557
Cdd:cd02662    56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 558 vvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQNFPEILCIHLKRFR-HELMFSTKISTHVSFPLegldlqp 636
Cdd:cd02662    97 --TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFPE------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 637 FLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTEVSESTV-Q 695
Cdd:cd02662   157 RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKEVSESEVlE 230


                  ....*....
gi 1794418471 696 NAEAYVLFY 704
Cdd:cd02662   231 QKSAYMLFY 239
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 473-705 1.93e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 102.57  E-value: 1.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 473 SVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPgkedlaklhssshptsivkagscgeayapqgwiaffmeyvks 552
Cdd:cd02664    97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------------------------------------ 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 553 wfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFR--HELMFSTKISTHVSFPlE 630
Cdd:cd02664   135 -------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIMDNVSIN-E 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 631 GLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN------------------- 672
Cdd:cd02664   207 VLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqecpepkdaee 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1794418471 673 -NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 705
Cdd:cd02664   287 nDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 472-705 3.31e-22

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: 98.81  E-value: 3.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 472 RSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEdLAKLHSSSHPTSIVKAgscgeayapqgwiaffmeyvk 551
Cdd:cd02671   120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 552 swfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMFS------TKISTHV 625
Cdd:cd02671   178 -----EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 626 SFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------TEVSESTVQ 695
Cdd:cd02671   253 LTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflEALSPNTSS 322

                         250
                  ....*....|
gi 1794418471 696 NAEAYVLFYR 705
Cdd:cd02671   323 TSTPYLLFYK 332
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 838-910 1.65e-20

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: 86.27  E-value: 1.65e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418471 838 TFYCISMQWFREWESFVKGKDgDPPGPIDNTKIAVTKCGNVM---LRQGADSGQISEETWNFLQSIYGGGPEVILR 910
Cdd:pfam06337   3 KVYLISSKWLNKWKSYVKEPN-NEPGPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 560-694 7.84e-19

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 92.24  E-value: 7.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471  560 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQNFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 635
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1794418471  636 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 694
Cdd:COG5077    415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
61-121 4.77e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 78.84  E-value: 4.77e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1794418471  61 CQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 121
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 601-705 2.54e-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 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: 80.84  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 601 PEILCIHLKRF--RHELMFSTKISTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 677
Cdd:cd02657   197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1794418471 678 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 705
Cdd:cd02657   271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 464-705 2.80e-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: 80.83  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 464 RKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSshptsivkagscgEAYAPqgwi 543
Cdd:cd02658   115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP---- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 544 affmeyvkswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHELMF-STKIS 622
Cdd:cd02658   178 ---------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 623 THVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSESTVQNAEA 699
Cdd:cd02658   239 VPIDVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKLG 305


                  ....*.
gi 1794418471 700 YVLFYR 705
Cdd:cd02658   306 YIYFYQ 311
DUSP smart00695
Domain in ubiquitin-specific proteases;
726-795 1.27e-15

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 72.78  E-value: 1.27e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1794418471  726 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPA 795
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
601-706 9.85e-15

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 75.61  E-value: 9.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 601 PEILCIHLKRFRHELMFsTKISTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlNNL 677
Cdd:COG5533   180 PKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--GGK 251

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1794418471 678 WYEFDDQSVTEVSESTVQNA---EAYVLFYRK 706
Cdd:COG5533   252 WEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 601-705 4.99e-14

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 75.43  E-value: 4.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 601 PEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT-ASSGHYIAYCRNNLNNL 677
Cdd:cd02669   333 PKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNK 412

                          90       100
                  ....*....|....*....|....*...
gi 1794418471 678 WYEFDDQSVTEVSESTVQNAEAYVLFYR 705
Cdd:cd02669   413 WFEIQDLNVKEVLPQLIFLSESYIQIWE 440
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 732-802 5.61e-12

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: 62.00  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 732 FYISRQWLNKFKTFAE-----PGPISNNDFLCihggvPPRKAGYIEDLVL-----MLPQNIWDNLYSRYGGGPAVNHLYI 801
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQEgvdyvIVPEEVWEFLVEWYGGGPEIKRNVV 79


                  .
gi 1794418471 802 C 802
Cdd:pfam06337  80 N 80
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 649-704 3.97e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 62.51  E-value: 3.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1794418471 649 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 704
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
60-112 1.61e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 54.29  E-value: 1.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1794418471   60 TCQDCKVQGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 112
Cdd:smart00290   1 RCSVCGTIE-NLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 582-704 2.12e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 59.08  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 582 CEKCKKlRNGVKFCKVQNFPEILCIHLKRFRhelmFSTKISTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 655
Cdd:cd02673   129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1794418471 656 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 704
Cdd:cd02673   191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
186-283 2.81e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 56.35  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 186 GLKNIGNTCYMNAALQALS-NCPPLTQFFLDCGGLART-------DKKPAICKSYLKLMTELWHKSRPgsvvpttlfqgi 257
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68

                          90       100
                  ....*....|....*....|....*.
gi 1794418471 258 kTVNPTFRGYSQQDAQEFLRCLMDLL 283
Cdd:COG5533    69 -KVGWIPPMGSQEDAHELLGKLLDEL 93
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 601-704 8.63e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 54.10  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 601 PEILCIHLKRFRHELMFSTKISTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYE 680
Cdd:cd02665   129 PPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1794418471 681 FDDQSVTEVSESTVQ--------NAEAYVLFY 704
Cdd:cd02665   196 YNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
582-686 2.05e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 53.81  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 582 CEKCKKLRNGVKFCKVQNFPEILCIHLKRFRHElmFSTKISTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 660
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1794418471 661 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 686
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 582-704 3.50e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 52.51  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 582 CEKCKKLRNGVKFCKVQNFPEI----LCIHLKRF-------RHELMFSTKISTHVSFPLEglDLQPFLAKDSPAQIVTYD 650
Cdd:cd02672   137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1794418471 651 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 704
Cdd:cd02672   215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 550-705 7.45e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 48.29  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 550 VKSWFWGPVVTLQDCLAAFFardelkgdnmyscekckklRNGVkFCKVqnfPEILCIHLKRFRHELMFSTKISTHVsFPL 629
Cdd:cd02670    71 VPDDDDGGGITLEQCLEQYF-------------------NNSV-FAKA---PSCLIICLKRYGKTEGKAQKMFKKI-LIP 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1794418471 630 EGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-----------LNN 676
Cdd:cd02670   127 DEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetdneaYNA 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1794418471 677 LWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 705
Cdd:cd02670   207 QWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
 
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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