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Conserved domains on  [gi|202070754|ref|NP_001128484|]
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ubiquitin carboxyl-terminal hydrolase 4 [Rattus norvegicus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 1000871)

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

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0046872|GO:0003723

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-921 4.40e-146

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 454.34  E-value: 4.40e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWNK 186
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 187 YMSNTYEQLSKLDNTIqdaglyqgqvlviepqnedgtwprqtlqsKSSTAPSRNFTTSSKPSASPYSSMSASLIANgdst 266
Cdd:COG5560  193 VPEIMGLRLGLDSFFR-----------------------------RYRVLASDGRVLHPLTRLELFEDRSVLLLSK---- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 267 nssgmhnsgVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLG 346
Cdd:COG5560  240 ---------ITRNPDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLG 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 347 MKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKPYLE-PKDANG 425
Cdd:COG5560  311 MHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkPDLSPG 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 426 RPDAV--VAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRIMEVFLVPADPHCRPI 503
Cdd:COG5560  391 DDVVVkkKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPL 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 504 Q-YRVTVPLMGAISDLCEALSKLSGIAaeNMVVTDVYNHRFHKIF-QMDEGLSH-ITPRDDIFVYEicttpmDGSEYITL 580
Cdd:COG5560  471 KiELDASSTIRGLKKLVDAEYGKLGCF--EIKVMCIYYGGNYNMLePADKVLLQdIPQTDFVYLYE------TNDNGIEV 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 581 PVYfrekKSRPSSTSSGAVLYGQPLLvsvpkhRLTLeslyqavceRISRYIKQPLPEEFLSSP--LEPGACNGSRGSYeg 658
Cdd:COG5560  543 PVV----HLRIEKGYKSKRLFGDPFL------QLNV---------LIKASIYDKLVKEFEELLvlVEMKKTDVDLVSE-- 601
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 659 dEEEMDHQEEGKEQLSEVEESGEDSQGGDPTETTQKakgpprhkrLFTFSLVNSCgtadinslatdgkllklnsrstlai 738
Cdd:COG5560  602 -QVRLLREESSPSSWLKLETEIDTKREEQVEEEGQM---------NFNDAVVISC------------------------- 646
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 739 DWdSETRSLYFDEQESEACEKHTSMSQPQkkkkaaIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKI 818
Cdd:COG5560  647 EW-EEKRYLSLFSYDPLWTIREIGAAERT------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 819 LVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDS 898
Cdd:COG5560  720 LIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDS 799
                        890       900
                 ....*....|....*....|...
gi 202070754 899 SVSLASEDQIVTKAAYVLFYQRR 921
Cdd:COG5560  800 RITEVDPEDSVTSSAYVLFYRRK 822
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-921 4.40e-146

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 454.34  E-value: 4.40e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWNK 186
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 187 YMSNTYEQLSKLDNTIqdaglyqgqvlviepqnedgtwprqtlqsKSSTAPSRNFTTSSKPSASPYSSMSASLIANgdst 266
Cdd:COG5560  193 VPEIMGLRLGLDSFFR-----------------------------RYRVLASDGRVLHPLTRLELFEDRSVLLLSK---- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 267 nssgmhnsgVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLG 346
Cdd:COG5560  240 ---------ITRNPDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLG 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 347 MKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKPYLE-PKDANG 425
Cdd:COG5560  311 MHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkPDLSPG 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 426 RPDAV--VAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRIMEVFLVPADPHCRPI 503
Cdd:COG5560  391 DDVVVkkKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPL 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 504 Q-YRVTVPLMGAISDLCEALSKLSGIAaeNMVVTDVYNHRFHKIF-QMDEGLSH-ITPRDDIFVYEicttpmDGSEYITL 580
Cdd:COG5560  471 KiELDASSTIRGLKKLVDAEYGKLGCF--EIKVMCIYYGGNYNMLePADKVLLQdIPQTDFVYLYE------TNDNGIEV 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 581 PVYfrekKSRPSSTSSGAVLYGQPLLvsvpkhRLTLeslyqavceRISRYIKQPLPEEFLSSP--LEPGACNGSRGSYeg 658
Cdd:COG5560  543 PVV----HLRIEKGYKSKRLFGDPFL------QLNV---------LIKASIYDKLVKEFEELLvlVEMKKTDVDLVSE-- 601
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 659 dEEEMDHQEEGKEQLSEVEESGEDSQGGDPTETTQKakgpprhkrLFTFSLVNSCgtadinslatdgkllklnsrstlai 738
Cdd:COG5560  602 -QVRLLREESSPSSWLKLETEIDTKREEQVEEEGQM---------NFNDAVVISC------------------------- 646
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 739 DWdSETRSLYFDEQESEACEKHTSMSQPQkkkkaaIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKI 818
Cdd:COG5560  647 EW-EEKRYLSLFSYDPLWTIREIGAAERT------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 819 LVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDS 898
Cdd:COG5560  720 LIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDS 799
                        890       900
                 ....*....|....*....|...
gi 202070754 899 SVSLASEDQIVTKAAYVLFYQRR 921
Cdd:COG5560  800 RITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
774-919 4.82e-59

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: 201.75  E-value: 4.82e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 774 IALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFV 853
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 202070754 854 CDRAAR-PYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIVTKAAYVLFYQ 919
Cdd:cd02674  164 DTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
763-918 2.26e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 186.11  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  763 MSQPQKKKKAAIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEF 842
Cdd:pfam00443 151 PIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEF 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  843 PVRaLNMSEFVCD----RAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASED-QIVTKAAYVLF 917
Cdd:pfam00443 231 PLE-LDLSRYLAEelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILF 309

                  .
gi 202070754  918 Y 918
Cdd:pfam00443 310 Y 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 3.64e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 120.16  E-value: 3.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 202070754   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-921 4.40e-146

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 454.34  E-value: 4.40e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLWNK 186
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLWDV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 187 YMSNTYEQLSKLDNTIqdaglyqgqvlviepqnedgtwprqtlqsKSSTAPSRNFTTSSKPSASPYSSMSASLIANgdst 266
Cdd:COG5560  193 VPEIMGLRLGLDSFFR-----------------------------RYRVLASDGRVLHPLTRLELFEDRSVLLLSK---- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 267 nssgmhnsgVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLG 346
Cdd:COG5560  240 ---------ITRNPDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLG 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 347 MKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKPYLE-PKDANG 425
Cdd:COG5560  311 MHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSkPDLSPG 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 426 RPDAV--VAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRIMEVFLVPADPHCRPI 503
Cdd:COG5560  391 DDVVVkkKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQPL 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 504 Q-YRVTVPLMGAISDLCEALSKLSGIAaeNMVVTDVYNHRFHKIF-QMDEGLSH-ITPRDDIFVYEicttpmDGSEYITL 580
Cdd:COG5560  471 KiELDASSTIRGLKKLVDAEYGKLGCF--EIKVMCIYYGGNYNMLePADKVLLQdIPQTDFVYLYE------TNDNGIEV 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 581 PVYfrekKSRPSSTSSGAVLYGQPLLvsvpkhRLTLeslyqavceRISRYIKQPLPEEFLSSP--LEPGACNGSRGSYeg 658
Cdd:COG5560  543 PVV----HLRIEKGYKSKRLFGDPFL------QLNV---------LIKASIYDKLVKEFEELLvlVEMKKTDVDLVSE-- 601
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 659 dEEEMDHQEEGKEQLSEVEESGEDSQGGDPTETTQKakgpprhkrLFTFSLVNSCgtadinslatdgkllklnsrstlai 738
Cdd:COG5560  602 -QVRLLREESSPSSWLKLETEIDTKREEQVEEEGQM---------NFNDAVVISC------------------------- 646
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 739 DWdSETRSLYFDEQESEACEKHTSMSQPQkkkkaaIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKI 818
Cdd:COG5560  647 EW-EEKRYLSLFSYDPLWTIREIGAAERT------ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMI 719
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 819 LVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDS 898
Cdd:COG5560  720 LIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDS 799
                        890       900
                 ....*....|....*....|...
gi 202070754 899 SVSLASEDQIVTKAAYVLFYQRR 921
Cdd:COG5560  800 RITEVDPEDSVTSSAYVLFYRRK 822
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
774-919 4.82e-59

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: 201.75  E-value: 4.82e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 774 IALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFV 853
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 202070754 854 CDRAAR-PYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIVTKAAYVLFYQ 919
Cdd:cd02674  164 DTRSFTgPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
763-918 2.26e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 186.11  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  763 MSQPQKKKKAAIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEF 842
Cdd:pfam00443 151 PIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEF 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  843 PVRaLNMSEFVCD----RAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASED-QIVTKAAYVLF 917
Cdd:pfam00443 231 PLE-LDLSRYLAEelkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSAYILF 309

                  .
gi 202070754  918 Y 918
Cdd:pfam00443 310 Y 310
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
302-485 2.08e-51

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 183.03  E-value: 2.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  302 CGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPlgmKGEIAEAYAELIKQMWSG-RDTHVAPRMFKTQVG 380
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  381 RFAPQFSGYQQQDSQELLAFILDGLHEDLNRvkkkpylepkdangrpdavvakeaweNHRLRNDSVIVDTFHGLFKSTLV 460
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLK 131
                         170       180
                  ....*....|....*....|....*
gi 202070754  461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDS 156
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
776-919 1.73e-39

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: 147.24  E-value: 1.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 776 LRECIELFTTMETLGEHDPWYCPtCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWR-DKLDTVVEFPVRaLNMSEFVC 854
Cdd:cd02257  101 LEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSFPLE-LDLSPYLS 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 202070754 855 DRAA------RPYVYDLIAVSNHYG-AMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIV-----TKAAYVLFYQ 919
Cdd:cd02257  179 EGEKdsdsdnGSYKYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
139-226 2.74e-36

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 131.90  E-value: 2.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTIQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 202070754  219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 3.64e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 120.16  E-value: 3.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 202070754   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-918 8.89e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 124.02  E-value: 8.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 776 LRECIELFTTMETLGEhDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRD-KLDTVVEFPVRaLNMSEFVC 854
Cdd:cd02660  178 LSDCLDRFTRPEKLGD-FAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSrKIDTYVQFPLE-LNMTPYTS 255
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 202070754 855 ---------DRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRlNGKWYYFDDSSVSLASEDQIVTKAAYVLFY 918
Cdd:cd02660  256 ssigdtqdsNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-918 1.02e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 123.15  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 776 LRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYwrDKLDTVVEFPVRaLNMSEFVCD 855
Cdd:cd02661  164 LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFPET-LDLSPYMSQ 240
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 202070754 856 RAARPYVYDLIAVSNHYGA-MGVGHYTAYAKNrLNGKWYYFDDSSVSLASEDQIVTKAAYVLFY 918
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
31-123 4.52e-27

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: 105.14  E-value: 4.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754   31 GAQWYLIDSRWFKQWKKYVGfdswdmynvgEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGc 110
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG- 69
                          90
                  ....*....|...
gi 202070754  111 veGQQPIVRKVVE 123
Cdd:pfam06337  70 --GGPEIKRNVVN 80
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
302-486 1.00e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 102.74  E-value: 1.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 302 CGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLGMKgeIAEAYAELIkqMWSGRDThVAPRMFKTQVGR 381
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMC--ALEAHVERA--LASSGPG-SAPRIFSSNLKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 382 FAPQFSGYQQQDSQELLAFILDGLHedlnrvkkKPYLEPKdangrpdavvAKEAWENHRLRNDSVIVDTFHGLFKSTLVC 461
Cdd:cd02661   77 ISKHFRIGRQEDAHEFLRYLLDAMQ--------KACLDRF----------KKLKAVDPSSQETTLVQQIFGGYLRSQVKC 138
                        170       180
                 ....*....|....*....|....*
gi 202070754 462 PECAKVSVTFDPFcyLTLPLPLKKD 486
Cdd:cd02661  139 LNCKHVSNTYDPF--LDLSLDIKGA 161
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-923 1.37e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 103.11  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 776 LRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYN--RYWRDKLDTVVEFPVRaLNMSEFV 853
Cdd:cd02659  153 LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LDMEPYT 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 854 CDRAAR-----------PYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIV------------- 909
Cdd:cd02659  232 EKGLAKkegdsekkdseSYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEeecfggeetqkty 311
                        170       180
                 ....*....|....*....|...
gi 202070754 910 ---------TKAAYVLFYQRRDD 923
Cdd:cd02659  312 dsgprafkrTTNAYMLFYERKSP 334
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-491 3.03e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 96.59  E-value: 3.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNtgplteyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdthvaprmfktqvgrf 382
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 383 apqfsgyQQQDSQELLAFILDGLHedlnrvkkkpylepkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTLVCP 462
Cdd:cd02674   21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
                        170       180
                 ....*....|....*....|....*....
gi 202070754 463 ECAKVSVTFDPFCYLTLPLPLKKDRIMEV 491
Cdd:cd02674   56 TCGKTSTTFEPFTYLSLPIPSGSGDAPKV 84
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-485 1.56e-21

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 96.67  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLGMKG-EIAEAYAELikqMWSGRDTHVAPRMFKTQVGR 381
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLScAMDEIFQEF---YYSGDRSPYGPINLLYLSWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 382 FAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKkPYLEPKDANgrpdavvakeawenhrlrndsVIVD-TFHGLFKSTLV 460
Cdd:cd02660   79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN-EANDESHCN---------------------CIIHqTFSGSLQSSVT 136
                        170       180
                 ....*....|....*....|....*
gi 202070754 461 CPECAKVSVTFDPFCYLTLPLPLKK 485
Cdd:cd02660  137 CQRCGGVSTTVDPFLDLSLDIPNKS 161
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
778-919 2.56e-21

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 95.45  E-value: 2.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 778 ECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYN-RYWR-DKLDTVVEFP--VRALNMSEFv 853
Cdd:cd02663  151 SCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRyIKLFYRVVFPleLRLFNTTDD- 229
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 202070754 854 CDRAARpyVYDLIAVSNHYGAMGV-GHYTAYAKNrlNGKWYYFDDSSVSLASEDQIV--------TKAAYVLFYQ 919
Cdd:cd02663  230 AENPDR--LYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
776-918 3.80e-21

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 95.57  E-value: 3.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 776 LRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY--WRDKLDTVVEFPvRALNMSEFV 853
Cdd:cd02668  158 LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKtgAKKKLNASISFP-EILDMGEYL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 854 CDRAARPYVYDLIAVSNHYG--AMGvGHYTAYAKNRLNGKWYYFDDSSVS--------------LASEDQ-------IVT 910
Cdd:cd02668  237 AESDEGSYVYELSGVLIHQGvsAYS-GHYIAHIKDEQTGEWYKFNDEDVEempgkplklgnsedPAKPRKseikkgtHSS 315

                 ....*...
gi 202070754 911 KAAYVLFY 918
Cdd:cd02668  316 RTAYMLVY 323
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
762-919 4.82e-21

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 94.38  E-value: 4.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 762 SMSQPQKKK-KAAIALRECIELFTTMETLGEHDPWYCPTCKKhqqATKKFDLWSLPKILVVHLKRFSYNRYWRD-KLDTV 839
Cdd:cd02667   98 DLSLPRSDEiKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRH 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 840 VEFPVRaLNMSEFV-----CDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNR---------------------LNGKWY 893
Cdd:cd02667  175 VSFPEI-LDLAPFCdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrlsdltkskpaadeagpGSGQWY 253
                        170       180
                 ....*....|....*....|....*.
gi 202070754 894 YFDDSSVSLASEDQIVTKAAYVLFYQ 919
Cdd:cd02667  254 YISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
303-486 2.83e-20

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: 91.39  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNtgplteyflkdeyeaeinrdnplgmkgeiaeayaelikqmwsgrdthvaprmfktqvgrf 382
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 383 apqfsgyQQQDSQELLAFILDGLHEDLNRVKKKpylepkdangrpdavvakeawENHRLRNDSVIVDTFHGLFKSTLVCP 462
Cdd:cd02257   21 -------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCL 72
                        170       180
                 ....*....|....*....|....
gi 202070754 463 ECAKVSVTFDPFCYLTLPLPLKKD 486
Cdd:cd02257   73 ECGHESVSTEPELFLSLPLPVKGL 96
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-491 5.97e-20

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 90.91  E-value: 5.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNTGPLTEYFLKDeyeaeinrdnplgmkgeiaeayaelikqmwsgrdthvaPRMFKTQVGRF 382
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 383 APQFSGYQQQDSQELLAFILDGLhedlnrvkkkpylepkdangrpdavvakeawenhRLRNDSVivdtFHGLFKSTLVCP 462
Cdd:cd02667   43 APQFKGYQQQDSHELLRYLLDGL----------------------------------RTFIDSI----FGGELTSTIMCE 84
                        170       180
                 ....*....|....*....|....*....
gi 202070754 463 ECAKVSVTFDPFcyLTLPLPLKKDRIMEV 491
Cdd:cd02667   85 SCGTVSLVYEPF--LDLSLPRSDEIKSEC 111
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
764-919 9.40e-18

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: 85.07  E-value: 9.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 764 SQPQKKKKAAIALRECIELFTTMETLGEhdpwYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRdkldtvvefP 843
Cdd:cd02658  168 KEEGELVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWV---------P 234
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 202070754 844 VRaLNMSEFVCDRaARPYVYDLIAVSNHYGA-MGVGHYTAYAKNRLN--GKWYYFDDSSVSLASEDQIVTKAAYVLFYQ 919
Cdd:cd02658  235 KK-LDVPIDVPEE-LGPGKYELIAFISHKGTsVHSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
814-920 7.12e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 79.08  E-value: 7.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 814 SLPKILVVHLKRFSYNRYWRdKLDTVVEFPVRaLNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNrlNGKWY 893
Cdd:COG5533  178 KLPKILTIQLKRFANLGGNQ-KIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWE 253
                         90       100       110
                 ....*....|....*....|....*....|
gi 202070754 894 YFDDSSVSLASEDQIVT---KAAYVLFYQR 920
Cdd:COG5533  254 KANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
807-918 6.20e-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: 76.60  E-value: 6.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 807 TKKFDlwSLPKILVVHLKRFsynrYWRDKLDT------VVEFPVrALNMSEFVCDRAarpyVYDLIAVSNHYGAMG-VGH 879
Cdd:cd02657  190 TSRIS--RLPKYLTVQFVRF----FWKRDIQKkakilrKVKFPF-ELDLYELCTPSG----YYELVAVITHQGRSAdSGH 258
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 202070754 880 YTAYAKNRLNGKWYYFDDSSVSLASEDQIVTKA-------AYVLFY 918
Cdd:cd02657  259 YVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-483 6.67e-15

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 76.59  E-value: 6.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNP----------LGmKGEIAEAYAELIKQMWSGRDT--HV 370
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPandlncqlikLA-DGLLSGRYSKPASLKSENDPYqvGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 371 APRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLnrvKKKPYLEPKDangrpdavvakeawenhrlrndsvivdt 450
Cdd:cd02658   80 KPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES---FKNLGLNPND---------------------------- 128
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 202070754 451 fhgLFK----STLVCPECAKVSVTFDPFCYLTLPLPL 483
Cdd:cd02658  129 ---LFKfmieDRLECLSCKKVKYTSELSEILSLPVPK 162
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
752-918 8.72e-15

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 76.86  E-value: 8.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 752 QESEACEKHTSMSQPQKKKKAAIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRY 831
Cdd:cd02671  158 QESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGS 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 832 WRD------KLDTVVEFPVRaLNMSEFvCDRAARPyVYDLIAVSNHYGA-MGVGHYTAYAknrlngKWYYFDDSSVSLAS 904
Cdd:cd02671  238 EFDcygglsKVNTPLLTPLK-LSLEEW-STKPKND-VYRLFAVVMHSGAtISSGHYTAYV------RWLLFDDSEVKVTE 308
                        170       180
                 ....*....|....*....|...
gi 202070754 905 EDQIV---------TKAAYVLFY 918
Cdd:cd02671  309 EKDFLealspntssTSTPYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
757-919 7.68e-14

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 72.01  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 757 CEKHTSMSQPQKKKKAAIALRECIELFTTMETLGEhdpwycPTCKKHQQATKKfdlwsLPKILVVHLKRFSYN-RYWRDK 835
Cdd:cd02662   79 SFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDD------YKCDRCQTVIVR-----LPQILCIHLSRSVFDgRGTSTK 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 836 LDTVVEFPvralnmsEFVcdraaRPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGK--------------------WYYF 895
Cdd:cd02662  148 NSCKVSFP-------ERL-----PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRI 215
                        170       180
                 ....*....|....*....|....*
gi 202070754 896 DDSSVSLASEDQIV-TKAAYVLFYQ 919
Cdd:cd02662  216 SDTTVKEVSESEVLeQKSAYMLFYE 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
776-908 1.67e-12

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 71.83  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  776 LRECIELFTTMETLGEHDPWYCptcKKH--QQATKKFDLWSLPKILVVHLKRFSYNrYWRD---KLDTVVEFPVrALNMS 850
Cdd:COG5077   340 LQESFRRYIQVETLDGDNRYNA---EKHglQDAKKGVIFESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPL-EIDLL 414
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 202070754  851 EFVCDRAAR----PYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQI 908
Cdd:COG5077   415 PFLDRDADKsensDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
808-919 3.45e-12

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: 69.65  E-value: 3.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 808 KKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAA---RPYVYDLIAVSNHYGAMGV-GHYTAY 883
Cdd:cd02669  325 KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPslnLSTKYNLVANIVHEGTPQEdGTWRVQ 404
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 202070754 884 AKNRLNGKWYYFDDSSVSLASEDQIVTKAAYVLFYQ 919
Cdd:cd02669  405 LRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
780-919 6.36e-12

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: 67.90  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 780 IELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNR--YWRDKL------DTVVEFPVRALNMSE 851
Cdd:cd02664  140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKImdnvsiNEVLSLPVRVESKSS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 852 FVCDRAA------------RPYVYDLIAVSNHYG-AMGVGHYTAYAKN--------------------RLNGKWYYFDDS 898
Cdd:cd02664  220 ESPLEKKeeesgddgelvtRQVHYRLYAVVVHSGySSESGHYFTYARDqtdadstgqecpepkdaeenDESKNWYLFNDS 299
                        170       180
                 ....*....|....*....|....*...
gi 202070754 899 SVSLAS--EDQIVTK-----AAYVLFYQ 919
Cdd:cd02664  300 RVTFSSfeSVQNVTSrfpkdTPYILFYE 327
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
299-484 6.91e-12

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: 68.88  E-value: 6.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 299 PGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFL-KDEYEAEINRdnplgmKGEIAEAYAELIKQMWSgrdthvaPRMFKT 377
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDR------KSELVKRLSELIRKIWN-------PRNFKG 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 378 QVG----------RFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKpylepkdangrpdavvakeawenhrlrNDSVI 447
Cdd:cd02669  184 HVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP---------------------------NSSII 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 202070754 448 VDTFHGLFK---------------STLVCPECAKVSVTFDPFCYLTLPLPLK 484
Cdd:cd02669  237 HDCFQGKVQietqkikphaeeegsKDKFFKDSRVKKTSVSPFLLLTLDLPPP 288
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-481 1.72e-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 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: 66.20  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLsntgplteyFLKDEYEAEINRDNPLGMKGEIAE-----AYAELIKQMWSGRDThVAPRMFKT 377
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL---------RSVPELRDALKNYNPARRGANQSSdnltnALRDLFDTMDKKQEP-VPPIEFLQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 378 QVGRFAPQFS------GYQQQDSQELLAFILDGLHEDLNRVKKKPylepkdangrpdavvakeawenhrlrndSVIVDTF 451
Cdd:cd02657   71 LLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG----------------------------SFIDQLF 122
                        170       180       190
                 ....*....|....*....|....*....|.
gi 202070754 452 HGLFKSTLVCPEC-AKVSVTFDPFCYLTLPL 481
Cdd:cd02657  123 GIELETKMKCTESpDEEEVSTESEYKLQCHI 153
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
303-409 1.38e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 63.28  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLS-NTGPLTEYFLKDEYE-----AEINRDNPLgMKGEIAEAyaeLIKQMWSGRdthvaprmfK 376
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlkNVIRKPEPD-LNQEEALK---LFTALWSSK---------E 67
                         90       100       110
                 ....*....|....*....|....*....|...
gi 202070754 377 TQVGRFAPQfsgYQQQDSQELLAFILDGLHEDL 409
Cdd:COG5533   68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDL 97
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-495 2.02e-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: 57.12  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLsntgplteyFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMW---SGRDTHVAPRMFKTQV 379
Cdd:cd02664    1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHlmhTQRRAEAPPDYFLEAS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 380 grFAPQFSGYQQQDSQELLAFILDGLHedlnrvkkkpylepkdangrpdavvakeawenhrlrndSVIVDTFHGLFKSTL 459
Cdd:cd02664   72 --RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTI 111
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 202070754 460 VCPECAKVSVTFDPFCYLTLPLPLKKDrIMEVFLVP 495
Cdd:cd02664  112 RCLNCNSTSARTERFRDLDLSFPSVQD-LLNYFLSP 146
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-482 4.07e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 55.78  E-value: 4.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNTGPLTEyfLKDEYEAEINRDNPLGMkgeiaeayaelikqmwsgrdthVAPRMFKTQVGRF 382
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLLTC--LKDLFESISEQKKRTGV----------------------ISPKKFITRLKRE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 383 APQFSGYQQQDSQELLAFILDGLHEDLNRVKKKpYLEPKDANGRPDAVVAKEaWenhrlrndsvIVDTFHGLFKSTLVCP 462
Cdd:cd02663   57 NELFDNYMHQDAHEFLNFLLNEIAEILDAERKA-EKANRKLNNNNNAEPQPT-W----------VHEIFQGILTNETRCL 124
                        170       180
                 ....*....|....*....|
gi 202070754 463 ECAKVSVTFDPFCYLTLPLP 482
Cdd:cd02663  125 TCETVSSRDETFLDLSIDVE 144
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
299-407 4.46e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 52.97  E-value: 4.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 299 PGLCGLGNLGNTCFMNSALQCLsntgplteYFLKDeYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQ 378
Cdd:cd02671   22 LPFVGLNNLGNTCYLNSVLQVL--------YFCPG-FKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAPRRLLNA 92
                         90       100
                 ....*....|....*....|....*....
gi 202070754 379 VGRFAPQFSGYQQQDSQELLAFILDGLHE 407
Cdd:cd02671   93 LREVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
815-918 1.10e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 47.55  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 815 LPKILVVHLKRFSYNRYWRDKLDTVVEFPvralnmsefvcdRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYY 894
Cdd:cd02665  128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------------QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEK 195
                         90       100       110
                 ....*....|....*....|....*....|..
gi 202070754 895 FDDSSVSLASEDQIVTKA--------AYVLFY 918
Cdd:cd02665  196 YNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-485 3.74e-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: 46.21  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNTGPLTEYflkdeyeaeinrdnplgmkgeiaeayaeLIKQMwsgrdthvaprmfktqvgrf 382
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY----------------------------LEEFL-------------------- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 383 apqfsgyQQQDSQELLAFILDGLHEDLnrvkKKPylepkdangrpdavvakeawenhrlrndsvivdtFHGLFKSTLVCP 462
Cdd:cd02662   33 -------EQQDAHELFQVLLETLEQLL----KFP----------------------------------FDGLLASRIVCL 67
                        170       180
                 ....*....|....*....|....
gi 202070754 463 ECAKVS-VTFDPFCYLTLPLPLKK 485
Cdd:cd02662   68 QCGESSkVRYESFTMLSLPVPNQS 91
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-919 6.97e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 45.58  E-value: 6.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 766 PQKKKKAAIALRECIELFTTMEtlgEHDPWYCPTCKKHQQATKKFDLWSLPKI----LVVHLKRFSYNRywrdKLDTVVE 841
Cdd:cd02672  109 GSTKTSKESTFLQLLKRSLDLE---KVTKAWCDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTNGEF----DDINVVL 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 842 FPVRALN----MSEFVCDRAARP------YVYDLIAV-----SNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASED 906
Cdd:cd02672  182 PSGKVMQnkvsPKAIDHDKLVKNrgqesiYKYELVGYvceinDSSRGQHNVVFVIKVNEESTHGRWYLFNDFLVTPVSEL 261
                        170
                 ....*....|...
gi 202070754 907 qivtkaAYVLFYQ 919
Cdd:cd02672  262 ------AYILLYQ 268
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-484 1.84e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 44.72  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 303 GLGNLGNTCFMNSALQCLSNTGPLTEYFLK-----DEYEAEINRDNPLGMKGeIAEAYAELIKQMWSGRDTHVAPRMFKT 377
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQT-IIDQLQLIFAQLQFGNRSVVDPSGFVK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 378 QVGrfapqFSGYQQQDSQELLAFILDGLHEDLNRVKKkpylepkdangrPDAVvakeawenhrlrndSVIVDTFHGLFKS 457
Cdd:cd02668   80 ALG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKN------------PDLK--------------NIVQDLFRGEYSY 128
                        170       180
                 ....*....|....*....|....*..
gi 202070754 458 TLVCPECAKVSVTFDPFcyLTLPLPLK 484
Cdd:cd02668  129 VTQCSKCGRESSLPSKF--YELELQLK 153
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
797-900 5.20e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 43.03  E-value: 5.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  797 CPTCKKHQQATKKFDLWSLPKILVVHLKRfsYNRYWRDKLDTVVEFPVRaLNMSEFVCDRAARP-YVYDLIAV------- 868
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAAL--TNEEWRQLWKTPGWLPPE-IGLTLSDDLQGDNEiVKYELRGVvvhigds 272
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 202070754  869 --SNHYGAM-GVGHytAYAKNRLNGKWYYFDDSSV 900
Cdd:pfam13423 273 gtSGHLVSFvKVAD--SELEDPTESQWYLFNDFLV 305
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
300-484 5.87e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 43.01  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 300 GLCGLGNLGNTCFMNSALQCLSNTGplteYFLKDEYEAEINRDNPlGMKGEIaeayAELIKQMWSgrdTHVAPRMFKTQV 379
Cdd:cd02659    1 GYVGLKNQGATCYMNSLLQQLYMTP----EFRNAVYSIPPTEDDD-DNKSVP----LALQRLFLF---LQLSESPVKTTE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754 380 GRFAPQFSG------YQQQDSQELLAFILDGLHEDLNRVKKKPylepkdangrpdavvakeawenhrlrndsVIVDTFHG 453
Cdd:cd02659   69 LTDKTRSFGwdslntFEQHDVQEFFRVLFDKLEEKLKGTGQEG-----------------------------LIKNLFGG 119
                        170       180       190
                 ....*....|....*....|....*....|.
gi 202070754 454 LFKSTLVCPECAKVSVTFDPFcyLTLPLPLK 484
Cdd:cd02659  120 KLVNYIICKECPHESEREEYF--LDLQVAVK 148
USP7_C2 pfam14533
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ...
504-567 2.06e-03

Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.


Pssm-ID: 464201  Cd Length: 204  Bit Score: 40.54  E-value: 2.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 202070754  504 QYRVTVPLMGAISDLCEALSKLSGIAAE---NMVVTDVYNHRFHKIFQMDEGLSHITPRDDIFVYEI 567
Cdd:pfam14533  34 ELELLVPKNGTVADLLEELQKKVKLSEEgsgKIRLYEVSNHKIYKELSEDEPIDSLNDYLTLYAEEI 100
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
297-405 2.38e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 41.78  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 202070754  297 IQPGLCGLGNLGNTCFMNSALQCLSntgpLTEYFLKDEYeaEINRDNPLGmKGEIAEAYAELIKQMWSGR---DTHVAPR 373
Cdd:COG5077   189 KETGYVGLRNQGATCYMNSLLQSLF----FIAKFRKDVY--GIPTDHPRG-RDSVALALQRLFYNLQTGEepvDTTELTR 261
                          90       100       110
                  ....*....|....*....|....*....|..
gi 202070754  374 MFKTQvgrfapQFSGYQQQDSQELLAFILDGL 405
Cdd:COG5077   262 SFGWD------SDDSFMQHDIQEFNRVLQDNL 287
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
859-909 2.76e-03

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 40.94  E-value: 2.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 202070754 859 RPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIV 909
Cdd:cd02666  277 KSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVF 327
 
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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