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Conserved domains on  [gi|1034592451|ref|XP_016878252|]
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ubiquitin carboxyl-terminal hydrolase 3 isoform X1 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031653)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
137-486 1.89e-79

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 250.44  E-value: 1.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 137 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQ-TAF 215
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 216 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 295
Cdd:pfam00443  68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 296 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRgLDMKCYLLEPENSG-PESCLYDLAAVVVHHGSgVGSGHYTAY- 453
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYi 275
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034592451 454 -ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 486
Cdd:pfam00443 276 kAYENNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
8-83 4.17e-16

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 72.68  E-value: 4.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451   8 AVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEdaqvpltnhkksekqdKVQHTVCMDCSSYSTYCYRCDDFVVND 83
Cdd:pfam02148   2 SLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYE----------------ETGHPLAVNLSTLTVYCYPCDDYVHDP 61
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
137-486 1.89e-79

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 250.44  E-value: 1.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 137 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQ-TAF 215
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 216 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 295
Cdd:pfam00443  68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 296 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRgLDMKCYLLEPENSG-PESCLYDLAAVVVHHGSgVGSGHYTAY- 453
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYi 275
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034592451 454 -ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 486
Cdd:pfam00443 276 kAYENNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-487 5.62e-75

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: 239.20  E-value: 5.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLsnieqfccyfkeLPAVELRNGKTAGRRTYHTRSQGDNNvSLVEEFRKTLCALWQ-GSQTAFS 216
Cdd:cd02660     2 GLINLGATCFMNVILQAL------------LHNPLLRNYFLSDRHSCTCLSCSPNS-CLSCAMDEIFQEFYYsGDRSPYG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 217 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNkcCIngastvVTAIFGGIL 296
Cdd:cd02660    69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN---------EANDESHCN--CI------IHQTFSGSL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 297 QNEVNCLICGTESRKFDPFLDLSLDIPSQ-FRSKRSKNQENGPVCSLRDCLRSFTDLEELDETElYMCHKCKKKQKSTKK 375
Cdd:cd02660   132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKsTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRF-HWTAYLRNKVDTYVEFPLRgLDMKCYL------LEPENSGPESCLYDLAAVVVHHGSgVGSG 448
Cdd:cd02660   211 LSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLE-LNMTPYTsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTG 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1034592451 449 HYTAYA-THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 487
Cdd:cd02660   289 HYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
331-486 4.03e-28

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.45  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 331 SKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPL 410
Cdd:COG5560   666 REIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034592451 411 RGLDMKCYLLEPENSgpeSCLYDLAAVVVHHGsGVGSGHYTAYA--THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:COG5560   746 DDLDLSGVEYMVDDP---RLIYDLYAVDNHYG-GLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
8-83 4.17e-16

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 72.68  E-value: 4.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451   8 AVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEdaqvpltnhkksekqdKVQHTVCMDCSSYSTYCYRCDDFVVND 83
Cdd:pfam02148   2 SLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYE----------------ETGHPLAVNLSTLTVYCYPCDDYVHDP 61
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
9-46 6.74e-08

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 48.90  E-value: 6.74e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034592451    9 VCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQVPL 46
Cdd:smart00290   4 VCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPL 41
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
137-486 1.89e-79

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 250.44  E-value: 1.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 137 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQ-TAF 215
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 216 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 295
Cdd:pfam00443  68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 296 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRgLDMKCYLLEPENSG-PESCLYDLAAVVVHHGSgVGSGHYTAY- 453
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYi 275
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034592451 454 -ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 486
Cdd:pfam00443 276 kAYENNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-487 5.62e-75

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: 239.20  E-value: 5.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLsnieqfccyfkeLPAVELRNGKTAGRRTYHTRSQGDNNvSLVEEFRKTLCALWQ-GSQTAFS 216
Cdd:cd02660     2 GLINLGATCFMNVILQAL------------LHNPLLRNYFLSDRHSCTCLSCSPNS-CLSCAMDEIFQEFYYsGDRSPYG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 217 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNkcCIngastvVTAIFGGIL 296
Cdd:cd02660    69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN---------EANDESHCN--CI------IHQTFSGSL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 297 QNEVNCLICGTESRKFDPFLDLSLDIPSQ-FRSKRSKNQENGPVCSLRDCLRSFTDLEELDETElYMCHKCKKKQKSTKK 375
Cdd:cd02660   132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKsTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRF-HWTAYLRNKVDTYVEFPLRgLDMKCYL------LEPENSGPESCLYDLAAVVVHHGSgVGSG 448
Cdd:cd02660   211 LSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLE-LNMTPYTsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTG 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1034592451 449 HYTAYA-THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 487
Cdd:cd02660   289 HYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
136-487 1.29e-66

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: 216.76  E-value: 1.29e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 136 ATGLRNLGNTCFMNAILQSLSNIEQFCCYFkelpavelrngktagRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAF 215
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYL---------------LSREHSKDCCNEGFCMMCALEAHVERALASSGPGS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 216 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrSAILQENSTLSASNKccINGASTVVTAIFGGI 295
Cdd:cd02661    66 APRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ------------KACLDRFKKLKAVDP--SSQETTLVQQIFGGY 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 296 LQNEVNCLICGTESRKFDPFLDLSLDIPSqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:cd02661   132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQ 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRFhwTAYLRNKVDTYVEFPLRgLDMKCYLLEPENsgpESCLYDLAAVVVHHGSGVGSGHYTAYA- 454
Cdd:cd02661   198 LTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMSQPND---GPLKYKLYAVLVHSGFSPHSGHYYCYVk 271
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034592451 455 THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 487
Cdd:cd02661   272 SSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 4.81e-64

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: 207.53  E-value: 4.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 217
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGILQ 297
Cdd:cd02674    21 -----------------DQQDAQEFLLFLLDGLH----------------------------------SIIVDLFQGQLK 49
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 377
Cdd:cd02674    50 SRLTCLTCGKTSTTFEPFTYLSLPIP--------SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPEscLYDLAAVVVHHGSgVGSGHYTAYA--T 455
Cdd:cd02674   122 ISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPF--KYDLYAVVNHYGS-LNGGHYTAYCknN 198
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1034592451 456 HEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02674   199 ETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
138-487 2.44e-63

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: 206.57  E-value: 2.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 217
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILqenstlsasnkccingaSTVVTAIFGGILQ 297
Cdd:cd02257    21 -----------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------KSLIHDLFGGKLE 66
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLICGTESRKFDPFLDLSLDIPSQfrskrsknqeNGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkFW 377
Cdd:cd02257    67 STIVCLECGHESVSTEPELFLSLPLPVK----------GLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKR-LK 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKRFHWT-AYLRNKVDTYVEFPLRgLDMKCYLLE---PENSGPESCLYDLAAVVVHHGSGVGSGHYTAY 453
Cdd:cd02257   136 IKKLPPVLIIHLKRFSFNeDGTKEKLNTKVSFPLE-LDLSPYLSEgekDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034592451 454 A--THEGRWFHFNDSTVTLTDEETVVK-----AKAYILFYV 487
Cdd:cd02257   215 VkdPSDGKWYKFNDDKVTEVSEEEVLEfgslsSSAYILFYE 255
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 7.17e-49

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 169.49  E-value: 7.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafSP 217
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------------------TP 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDhlhlelqggfngvsrsailqenstlsasnkccinGASTVVTAIFGGILQ 297
Cdd:cd02667    33 KELFSQVCRKAPQFKGYQQQDSHELLRYLLD----------------------------------GLRTFIDSIFGGELT 78
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkfw 377
Cdd:cd02667    79 STIMCESCGTVSLVYEPFLDLSLPRS----------DEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYL--- 145
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKRFHWTAYLR-NKVDTYVEFPLRgLDMKCYLLEPENS--GPESCLYDLAAVVVHHGSgVGSGHYTAYA 454
Cdd:cd02667   146 ISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFPEI-LDLAPFCDPKCNSseDKSSVLYRLYGVVEHSGT-MRSGHYVAYV 223
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034592451 455 -----------------------THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02667   224 kvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 4.04e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 165.56  E-value: 4.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNIEQFCCyFKELpavelrngktagrrtYHtrsqgdnnvSLVEEFRKTlcalwqGSqtaFSP 217
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFENLLTC-LKDL---------------FE---------SISEQKKRT------GV---ISP 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCcingastvVTAIFGGILQ 297
Cdd:cd02663    47 KKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW--------VHEIFQGILT 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknqengPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 377
Cdd:cd02663   119 NETRCLTCETVSSRDETFLDLSIDVE--------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKRFHWT-AYLRN-KVDTYVEFPlrgLDMKCYLLEPENSGPEScLYDLAAVVVHHGSGVGSGHYTAYAT 455
Cdd:cd02663   185 IKKLPKILALHLKRFKYDeQLNRYiKLFYRVVFP---LELRLFNTTDDAENPDR-LYELVAVVVHIGGGPNHGHYVSIVK 260
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1034592451 456 HEGRWFHFNDSTVTLTDEETVVK--------AKAYILFY 486
Cdd:cd02663   261 SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-487 1.55e-40

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: 148.56  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLsnieqfccYFKelPavELRNGktagRRTYHTRSQGDNNVSLVEEFRK--TLCALWQGSQTAF 215
Cdd:cd02659     4 GLKNQGATCYMNSLLQQL--------YMT--P--EFRNA----VYSIPPTEDDDDNKSVPLALQRlfLFLQLSESPVKTT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 216 SPESLFYVVWKiMPNfRGYQQQDAHEFMRYLLDHLHLELQGgfngvsrsaILQENStlsasnkccingastvVTAIFGGI 295
Cdd:cd02659    68 ELTDKTRSFGW-DSL-NTFEQHDVQEFFRVLFDKLEEKLKG---------TGQEGL----------------IKNLFGGK 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 296 LQNEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:cd02659   121 LVNYIICKECPHESEREEYFLDLQVAV------KGKKN--------LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKG 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRFH--WTAYLRNKVDTYVEFPLRgLDMKCYL--------LEPENSGPESCLYDLAAVVVHHGsGV 445
Cdd:cd02659   187 VCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLE-LDMEPYTekglakkeGDSEKKDSESYIYELHGVLVHSG-DA 264
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451 446 GSGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKA----------------------KAYILFYV 487
Cdd:cd02659   265 HGGHYYSYikDRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYE 330
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-468 4.07e-34

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 131.00  E-value: 4.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKtLCALWQGSQTAFSP 217
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPH------EPQTIIDQLQL-IFAQLQFGNRSVVD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 ESLFYVVWKIMPNfrgyQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqenstlsasnkcciNGASTVVTAIFGGILQ 297
Cdd:cd02668    74 PSGFVKALGLDTG----QQQDAQEFSKLFLSLLEAKLSKSKN----------------------PDLKNIVQDLFRGEYS 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKnqengpvcSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 377
Cdd:cd02668   128 YVTQCSKCGRESSLPSKFYELELQL------KGHK--------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKR--FHWTAYLRNKVDTYVEFPLRgLDMKCYLLEpenSGPESCLYDLAAVVVHHGSGVGSGHYTA--Y 453
Cdd:cd02668   194 LTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEI-LDMGEYLAE---SDEGSYVYELSGVLIHQGVSAYSGHYIAhiK 269
                         330
                  ....*....|....*
gi 1034592451 454 ATHEGRWFHFNDSTV 468
Cdd:cd02668   270 DEQTGEWYKFNDEDV 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 4.60e-32

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: 125.30  E-value: 4.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFkelpaveLRngktagrrtYHTRSQGDNNVSLVEEfrKTLCALWQGSQTAFS- 216
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQV-------LS---------LNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEa 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 217 -PESLFYVVWKimPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGI 295
Cdd:cd02664    63 pPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLH----------------------------------TLIEKMFGGK 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 296 LQNEVNCLICGTESRKFDPFLDLSLDipsqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:cd02664   107 LSTTIRCLNCNSTSARTERFRDLDLS-----------------FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 376 FWIQKLPKVLCLHLKRF------HWTAYLRNKV--DTYVEFPLR-----GLDMKCYLLEPENSGPESC----LYDLAAVV 438
Cdd:cd02664   170 MKVTGAPEYLILTLLRFsydqktHVREKIMDNVsiNEVLSLPVRvesksSESPLEKKEEESGDDGELVtrqvHYRLYAVV 249
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034592451 439 VHHGSGVGSGHYTAYATH----------------------EGRWFHFNDSTVTLTDEETV-------VKAKAYILFY 486
Cdd:cd02664   250 VHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 3.84e-29

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 117.30  E-value: 3.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLsnieQFCCYFKElpavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 217
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVL----YFCPGFKH---------------GLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 ESLFYVVWKIMPNFRGYQQQDAHEFMrylldhlhlelqggfngvsrsailqenstlsasnKCCINGASTVVTAIFGGILQ 297
Cdd:cd02671    87 RRLLNALREVNPMYEGYLQHDAQEVL----------------------------------QCILGNIQELVEKDFQGQLV 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGP-----VCSLRDCLRSFTDLEELDETELYMCHKCKKKQKS 372
Cdd:cd02671   133 LRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 373 TKKFWIQKLPKVLCLHLKRFHWTAYLRN------KVDTYVEFPLrglDMKCyllEPENSGPESCLYDLAAVVVHHGSGVG 446
Cdd:cd02671   213 ERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTPL---KLSL---EEWSTKPKNDVYRLFAVVMHSGATIS 286
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1034592451 447 SGHYTAYAthegRWFHFNDSTVTLTDEE---------TVVKAKAYILFY 486
Cdd:cd02671   287 SGHYTAYV----RWLLFDDSEVKVTEEKdflealspnTSSTSTPYLLFY 331
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
331-486 4.03e-28

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 118.45  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 331 SKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPL 410
Cdd:COG5560   666 REIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034592451 411 RGLDMKCYLLEPENSgpeSCLYDLAAVVVHHGsGVGSGHYTAYA--THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:COG5560   746 DDLDLSGVEYMVDDP---RLIYDLYAVDNHYG-GLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 9.91e-28

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 112.80  E-value: 9.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKEL----------PA-------VELRNGKTAGRrTYHTRSQGDNNVslveef 200
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLenkfpsdvvdPAndlncqlIKLADGLLSGR-YSKPASLKSEND------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 201 rktlcalwqGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailQENSTLSASNkcc 280
Cdd:cd02658    74 ---------PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD----------------RESFKNLGLN--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 281 ingastvVTAIFGGILQNEVNCLICGteSRKFDPFLD--LSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDET 358
Cdd:cd02658   126 -------PNDLFKFMIEDRLECLSCK--KVKYTSELSeiLSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDF 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 359 elymCHKCKKKQKSTKKFWIQKLPKVLCLHLKRF----HWTAylrNKVDTYVEFPLRGLDMKcyllepensgpesclYDL 434
Cdd:cd02658   197 ----CSTCKEKTTATKTTGFKTFPDYLVINMKRFqlleNWVP---KKLDVPIDVPEELGPGK---------------YEL 254
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451 435 AAVVVHHGSGVGSGHYTAY----ATHEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02658   255 IAFISHKGTSVHSGHYVAHikkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
12-486 1.22e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 112.03  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451  12 SNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQvpltnhkksekqdkvqHTVCMDCSSYSTYC----YRCDDFVVNDTKLG 87
Cdd:cd02669    24 SNLNVYACLVCGKYFQGRGKGSHAYTHSLEDN----------------HHVFLNLETLKFYClpdnYEIIDSSLDDIKYV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451  88 LvqkvrehlqnleNSAFTadrhkkRKLLENSTLNSKLLK-VNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQFCCYF- 165
Cdd:cd02669    88 L------------NPTYT------KEQISDLDRDPKLSRdLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 166 -KELPAVELRNGKTAGRRtyhtrsqgdnnvsLVEEFRKtlcaLWqgSQTAF----SP-ESLFYVVWKIMPNFRGYQQQDA 239
Cdd:cd02669   150 lYENYENIKDRKSELVKR-------------LSELIRK----IW--NPRNFkghvSPhELLQAVSKVSKKKFSITEQSDP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 240 HEFMRYLLDHLHLELQGgfngvsrsailqenstlsaSNKCcingASTVVTAIFGGILQNEVNCLI----CGTESRKFD-- 313
Cdd:cd02669   211 VEFLSWLLNTLHKDLGG-------------------SKKP----NSSIIHDCFQGKVQIETQKIKphaeEEGSKDKFFkd 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 314 ---------PFLDLSLDIPSQ--FRSKRSKNQEngPVCSLRDCLRSFTdleELDETELymchkckkkQKSTKKFWIQKLP 382
Cdd:cd02669   268 srvkktsvsPFLLLTLDLPPPplFKDGNEENII--PQVPLKQLLKKYD---GKTETEL---------KDSLKRYLISRLP 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 383 KVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHEGR--W 460
Cdd:cd02669   334 KYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTnkW 413
                         490       500
                  ....*....|....*....|....*.
gi 1034592451 461 FHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02669   414 FEIQDLNVKEVLPQLIFLSESYIQIW 439
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
138-487 1.02e-25

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 106.42  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSnieqfcCYFKELPAVELRNGKTAgrRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 217
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILA------LYLPKLDELLDDLSKEL--KVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 EslfyvvwkimpnFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNKccingastvVTAIFGGILQ 297
Cdd:COG5533    73 I------------PPMGSQEDAHELLGKLLDELKLDLVNSFT---------IRIFKTTKDK---------KKTSTGDWFD 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 NEVNCLI--CGTESRKFDPFLD-LSLDIPSQFRSKRSKNQEngpvcslrdclrsftdLEELDETELYMChkckkkqkstk 374
Cdd:COG5533   123 IIIELPDqtWVNNLKTLQEFIDnMEELVDDETGVKAKENEE----------------LEVQAKQEYEVS----------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 375 kfwIQKLPKVLCLHLKRFhwtAYL--RNKVDTYVEFPLrglDMKCYLLEPENSGPEScLYDLAAVVVHHGSgVGSGHYTA 452
Cdd:COG5533   176 ---FVKLPKILTIQLKRF---ANLggNQKIDTEVDEKF---ELPVKHDQILNIVKET-YYDLVGFVLHQGS-LEGGHYIA 244
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1034592451 453 YATHEGRWFHFNDSTVTLTDEETVVKAK---AYILFYV 487
Cdd:COG5533   245 YVKKGGKWEKANDSDVTPVSEEEAINEKaknAYLYFYE 282
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 5.55e-25

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: 104.72  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLsnieqfccyfKELPAV--ELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKTLCALwQGSQTAF 215
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCL----------RSVPELrdALKNYNPARRGANQ------SSDNLTNALRDLFDTM-DKKQEPV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 216 SPESLFYVVWKIMPNF------RGYQQQDAHEFMRYLLDHLHLELQGGfngvsrsaiLQENStlsasnkccingastVVT 289
Cdd:cd02657    64 PPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKLPGA---------GSKGS---------------FID 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 290 AIFGGILQNEVNCLICGT-ESRKFDPFLDLSLDIPSQFrskrsknqengPVCSLRDCLrsftdLEELDETELYMCHKCKK 368
Cdd:cd02657   120 QLFGIELETKMKCTESPDeEEVSTESEYKLQCHISITT-----------EVNYLQDGL-----KKGLEEEIEKHSPTLGR 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 369 KQKSTKKFWIQKLPKVLCLHLKRFHW--TAYLRNKVDTYVEFPLRgLDMKCYLlepensgPESCLYDLAAVVVHHGSGVG 446
Cdd:cd02657   184 DAIYTKTSRISRLPKYLTVQFVRFFWkrDIQKKAKILRKVKFPFE-LDLYELC-------TPSGYYELVAVITHQGRSAD 255
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1034592451 447 SGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKAK-------AYILFY 486
Cdd:cd02657   256 SGHYVAWvrRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
138-486 1.39e-23

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 99.36  E-value: 1.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 138 GLRNLGNTCFMNAILQSLSNIEQFccyfkelpavelrngktagrrtyhtrsqgdnnVSLVEEFRktlcalwqgsqtafsp 217
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSL--------------------------------IEYLEEFL---------------- 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 218 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSrsailqenstlsasnkccingASTVVtaifggilq 297
Cdd:cd02662    33 -----------------EQQDAHELFQVLLETLEQLLKFPFDGLL---------------------ASRIV--------- 65
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 298 nevnCLICGTESR-KFDPFLDLSLDIPsqfrskrskNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCkkkqkstkkf 376
Cdd:cd02662    66 ----CLQCGESSKvRYESFTMLSLPVP---------NQSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQTV---------- 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 377 wIQKLPKVLCLHLKRFHWT---AYLRNKvdTYVEFPLRgLDMKcyllepensgpescLYDLAAVVVHHGSgVGSGHYTAY 453
Cdd:cd02662   123 -IVRLPQILCIHLSRSVFDgrgTSTKNS--CKVSFPER-LPKV--------------LYRLRAVVVHYGS-HSSGHYVCY 183
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451 454 ----------------------ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 486
Cdd:cd02662   184 rrkplfskdkepgsfvrmregpSSTSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
138-469 2.64e-20

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 94.55  E-value: 2.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451  138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHtrSQGDNNVSLVeefrktLCALWQGSQTAFSP 217
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-------------TDH--PRGRDSVALA------LQRLFYNLQTGEEP 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451  218 -ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLhlelqggfngvsrsailqENSTlsasNKCCINGAstvVTAIFGGIL 296
Cdd:COG5077    254 vDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNL------------------EKSM----RGTVVENA---LNGIFVGKM 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451  297 QNEVNCLICGTESRKFDPFLDLsldipsQFRSKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKF 376
Cdd:COG5077    309 KSYIKCVNVNYESARVEDFWDI------QLNVKGMKN--------LQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVI 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451  377 WiQKLPKVLCLHLKRFHWTaYLRN---KVDTYVEFPLRgLDMKCYL----LEPENSgpeSCLYDLAAVVVHHGSgVGSGH 449
Cdd:COG5077    375 F-ESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDLLPFLdrdaDKSENS---DAVYVLYGVLVHSGD-LHEGH 447
                          330       340
                   ....*....|....*....|..
gi 1034592451  450 YTAYATHE--GRWFHFNDSTVT 469
Cdd:COG5077    448 YYALLKPEkdGRWYKFDDTRVT 469
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
137-323 8.03e-19

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 89.94  E-value: 8.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 137 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelRNGKTAGRRTYHTRSQGdnnvSLVEEFRKTLCALWQGSQTAFS 216
Cdd:COG5560   266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLS------DEYEESINEENPLGMHG----SVASAYADLIKQLYDGNLHAFT 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 217 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNG--VSRSAILQENSTL--SASNKCC---INGASTVVT 289
Cdd:COG5560   336 PSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKpyTSKPDLSPGDDVVvkKKAKECWwehLKRNDSIIT 415
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034592451 290 AIFGGILQNEVNCLICGTESRKFDPFLDLSLDIP 323
Cdd:COG5560   416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
8-83 4.17e-16

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 72.68  E-value: 4.17e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451   8 AVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEdaqvpltnhkksekqdKVQHTVCMDCSSYSTYCYRCDDFVVND 83
Cdd:pfam02148   2 SLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYE----------------ETGHPLAVNLSTLTVYCYPCDDYVHDP 61
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
242-468 3.09e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 70.38  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 242 FMRYLLDHLHLElqggfngvsrsailqENSTLSASNkccinGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLD 321
Cdd:pfam13423 102 FNRFLLDQLSSE---------------ENSTPPNPS-----PAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLI 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 322 IPSQFrskrSKNQENGPVCSLRDCLRSFTDLEELDETelyMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFhwTAYLRNK 401
Cdd:pfam13423 162 YPRKP----SSNNKKPPNQTFSSILKSSLERETTTKA---WCEKCKRYQPLESRRTVRNLPPVLSLNAALT--NEEWRQL 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592451 402 VDTYVEFPLRgldMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAY---------ATHEGRWFHFNDSTV 468
Cdd:pfam13423 233 WKTPGWLPPE---IGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFvkvadseleDPTESQWYLFNDFLV 305
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
137-487 1.54e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 59.43  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 137 TGLRNLGNTCFMNAILQSLSNIE-------QFCCYFKELPAVELRNGKTAGRRTyhTRSQGDNNVSLVEEFRKTLCALWQ 209
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKplrdlvlNFDESKAELASDYPTERRIGGREV--SRSELQRSNQFVYELRSLFNDLIH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 210 GSQTAFSPES-LFYVVwkimpnFRgyqQQDAHEFMRYLLDHLHLEL-QGGFNGVSRSAILQenstlsasnkcciNGASTV 287
Cdd:cd02666    80 SNTRSVTPSKeLAYLA------LR---QQDVTECIDNVLFQLEVALePISNAFAGPDTEDD-------------KEQSDL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 288 VTAIF-GGILQNEVNCLICGTESRKFDPFLDLSLDIPSqFRSKRSKNQENGPvCSLRDCL-RSF-----TDLEELDETEL 360
Cdd:cd02666   138 IKRLFsGKTKQQLVPESMGNQPSVRTKTERFLSLLVDV-GKKGREIVVLLEP-KDLYDALdRYFdydslTKLPQRSQVQA 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 361 YMCHKCKKKQKSTKKFWIQKLPKVLcLHLKRfhWTAYLRNKVDTYVEFPLRGLDMKcylLEPENSGPESCLYDLAAVVVH 440
Cdd:cd02666   216 QLAQPLQRELISMDRYELPSSIDDI-DELIR--EAIQSESSLVRQAQNELAELKHE---IEKQFDDLKSYGYRLHAVFIH 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034592451 441 HGSgVGSGHYTAYATH--EGRWFHFNDSTVTLTDEETVV------KAKAYILFYV 487
Cdd:cd02666   290 RGE-ASSGHYWVYIKDfeENVWRKYNDETVTVVPASEVFlftlgnTATPYFLVYV 343
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
235-487 8.57e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 56.03  E-value: 8.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 235 QQQDAHEFMRYLLDHLHLELQGGFNGVS-RSAILQENSTLsasnkccINGASTVVTAIFGGILQNevnCLICGtesrkfd 313
Cdd:cd02665    21 QQQDVSEFTHLLLDWLEDAFQAAAEAISpGEKSKNPMVQL-------FYGTFLTEGVLEGKPFCN---CETFG------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 314 pfldlslDIPSQFRSKRSknqengpvcsLRDCLRSFT---DLEELDETELYMCHKCKkkqkstkkfWIQKLPKVLCLHLK 390
Cdd:cd02665    84 -------QYPLQVNGYGN----------LHECLEAAMfegEVELLPSDHSVKSGQER---------WFTELPPVLTFELS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 391 RFHWTAYLRNKVDTYVEFPlrgldmKCYLLEPensgpesclYDLAAVVVHHGSgVGSGHYTAYA--THEGRWFHFNDSTV 468
Cdd:cd02665   138 RFEFNQGRPEKIHDKLEFP------QIIQQVP---------YELHAVLVHEGQ-ANAGHYWAYIykQSRQEWEKYNDISV 201
                         250       260
                  ....*....|....*....|....*..
gi 1034592451 469 TLTDEETVVK--------AKAYILFYV 487
Cdd:cd02665   202 TESSWEEVERdsfgggrnPSAYCLMYI 228
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
9-46 6.74e-08

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 48.90  E-value: 6.74e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034592451    9 VCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQVPL 46
Cdd:smart00290   4 VCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPL 41
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
378-486 3.84e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 45.21  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKRFhwtaYLRNKVDTYVEfpLRGLDMKCYLLEPENsgpesclYDLAAVVVHHGSGVGSGHYTAYA--- 454
Cdd:cd02673   143 IMTFPECLSINLKRY----KLRIATSDYLK--KNEEIMKKYCGTDAK-------YSLVAVICHLGESPYDGHYIAYTkel 209
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034592451 455 THEGRWFHFNDSTVTLTDEETVVKA---KAYILFY 486
Cdd:cd02673   210 YNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
279-486 8.72e-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: 44.43  E-value: 8.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 279 CCINGASTVVTAIFGGILQNEVNC------LICGTESRKFDPFLDLSLDIPSQFRSKRSknqengpvcSLRDCLRSFTDL 352
Cdd:cd02672    59 CELGYLFSTLIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPLGSTKTSKES---------TFLQLLKRSLDL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 353 EELDETElymCHKCKKKQKSTKKFWIQKLP----KVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLE---PENS 425
Cdd:cd02672   130 EKVTKAW---CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDklvKNRG 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034592451 426 GPESCLYDLAAVVVH--HGSG-----VGSGHYTAYATHeGRWFHFNDSTVTLTDEetvvkaKAYILFY 486
Cdd:cd02672   207 QESIYKYELVGYVCEinDSSRgqhnvVFVIKVNEESTH-GRWYLFNDFLVTPVSE------LAYILLY 267
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
378-486 6.01e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 38.28  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592451 378 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVeFPLRGLDMKcYLLEPENSGPESCLYD--------------------LAAV 437
Cdd:cd02670    95 FAKAPSCLIICLKRYGKTEGKAQKMFKKI-LIPDEIDIP-DFVADDPRACSKCQLEcrvcyddkdfsptcgkfklsLCSA 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034592451 438 VVHHGSGVGSGHYTAYA-------------THEGRWFHFNDstvtLTDEETV-----VKAK-----AYILFY 486
Cdd:cd02670   173 VCHRGTSLETGHYVAFVrygsysltetdneAYNAQWVFFDD----MADRDGVsngfnIPAArlledPYMLFY 240
 
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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