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Conserved domains on  [gi|256013071|gb|EAL71589|]
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UBP-type zinc finger-containing protein [Dictyostelium discoideum AX4]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10489794)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
250-827 2.61e-86

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.


The actual alignment was detected with superfamily member cd02660:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 328  Bit Score: 277.72  E-value: 2.61e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 250 RGLNNLGNTCFMNSILQSFLHNPLLRNYFLSDMHKCDKKnnlnnvnssnnnnnnnfnnnnnnnnnnnnnnnnnnnnnnnn 329
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCL----------------------------------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 330 nnnnnnnnnnnnnnnnnnnnnnnensnddnpniksepIDDNNSeivstppiqnnnnnnsnnnnnnnnnnnnnnnnnnnnn 409
Cdd:cd02660   40 -------------------------------------SCSPNS------------------------------------- 45
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 410 nnnnniskiCLGCEMDKLFTCVF-SGVKFPFTPHHFLYSCWNYSNYFIGYEQQDAHEFFISSLNGIHSHCGGTTGK---- 484
Cdd:cd02660   46 ---------CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEande 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 485 -DCDCIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPktlkdktsnangnsnsngngnnkintstasttasatls 563
Cdd:cd02660  117 sHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP-------------------------------------- 158
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 564 sqddeviSLDGSESVNGENGLGSNShqeqyhqqqqqqqqqqqqqqqqqhqqqqnnTLLSCLERFTQPEKLDE-KYFCPNC 642
Cdd:cd02660  159 -------NKSTPSWALGESGVSGTP------------------------------TLSDCLDRFTRPEKLGDfAYKCSGC 201
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 643 NSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRThKIDTFIEFPTSIDMGPYTTIMKKKadaidlnssgTSIKSEDygg 722
Cdd:cd02660  202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGD----------TQDSNSL--- 267
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 723 dnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhdgDNSFTYELFAVVNHTGKIDSGHYTSFVKHQ-DSW 801
Cdd:cd02660  268 ----------------------------------------------DPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQW 301
                        570       580
                 ....*....|....*....|....*.
gi 256013071 802 YKCDDSMISSTTIHNVLKSKGYLLYY 827
Cdd:cd02660  302 FKFDDAMITRVSEEEVLKSQAYLLFY 327
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
92-190 1.97e-06

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 45.71  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071   92 CMVCNCfNGRLHICLHCVHVSCW--KQGHIHQHLGKSHpnptaannnnnnnnnnntsttsnsnqeeknitnnndiHFLAV 169
Cdd:pfam02148   1 CSLCGN-TSNLWLCLTCGHVGCGryQNSHALEHYEETG-------------------------------------HPLAV 42
                          90       100
                  ....*....|....*....|.
gi 256013071  170 DLNLNQIYCHYCQDYIYDKEF 190
Cdd:pfam02148  43 NLSTLTVYCYPCDDYVHDPSL 63
 
Name Accession Description Interval E-value
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
250-827 2.61e-86

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: 277.72  E-value: 2.61e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 250 RGLNNLGNTCFMNSILQSFLHNPLLRNYFLSDMHKCDKKnnlnnvnssnnnnnnnfnnnnnnnnnnnnnnnnnnnnnnnn 329
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCL----------------------------------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 330 nnnnnnnnnnnnnnnnnnnnnnnensnddnpniksepIDDNNSeivstppiqnnnnnnsnnnnnnnnnnnnnnnnnnnnn 409
Cdd:cd02660   40 -------------------------------------SCSPNS------------------------------------- 45
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 410 nnnnniskiCLGCEMDKLFTCVF-SGVKFPFTPHHFLYSCWNYSNYFIGYEQQDAHEFFISSLNGIHSHCGGTTGK---- 484
Cdd:cd02660   46 ---------CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEande 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 485 -DCDCIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPktlkdktsnangnsnsngngnnkintstasttasatls 563
Cdd:cd02660  117 sHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP-------------------------------------- 158
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 564 sqddeviSLDGSESVNGENGLGSNShqeqyhqqqqqqqqqqqqqqqqqhqqqqnnTLLSCLERFTQPEKLDE-KYFCPNC 642
Cdd:cd02660  159 -------NKSTPSWALGESGVSGTP------------------------------TLSDCLDRFTRPEKLGDfAYKCSGC 201
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 643 NSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRThKIDTFIEFPTSIDMGPYTTIMKKKadaidlnssgTSIKSEDygg 722
Cdd:cd02660  202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGD----------TQDSNSL--- 267
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 723 dnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhdgDNSFTYELFAVVNHTGKIDSGHYTSFVKHQ-DSW 801
Cdd:cd02660  268 ----------------------------------------------DPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQW 301
                        570       580
                 ....*....|....*....|....*.
gi 256013071 802 YKCDDSMISSTTIHNVLKSKGYLLYY 827
Cdd:cd02660  302 FKFDDAMITRVSEEEVLKSQAYLLFY 327
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
250-827 2.39e-41

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 153.75  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  250 RGLNNLGNTCFMNSILQSFLHNPLLRNYFLSDMHKCDKknnlnnvnssnnnnnnnfnnnnnnnnnnnnnnnnnnnnnnnn 329
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED------------------------------------------ 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  330 nnnnnnnnnnnnnnnnnnnnnnnensnddnpnikSEPIDDNNseivstppiqnnnnnnsnnnnnnnnnnnnnnnnnnnnn 409
Cdd:pfam00443  39 ----------------------------------SRYNKDIN-------------------------------------- 46
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  410 nnnnniskicLGCEMDKLFTCVFSGVKF-PFTPHHFLYSCWNYSNYFIGYEQQDAHEFFISSLNGIHSHCGGTTGKDCDC 488
Cdd:pfam00443  47 ----------LLCALRDLFKALQKNSKSsSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENES 116
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  489 IIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPKTLKDKtsnangnsnsngngnnkintstasttasatlssqdde 568
Cdd:pfam00443 117 LITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAEL------------------------------------- 159
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  569 visldgsesvngenglgsnshqeqyhqqqqqqqqqqqqqqqqqhqqqQNNTLLSCLERFTQPEKL--DEKYFCPNCNSKQ 646
Cdd:pfam00443 160 -----------------------------------------------KTASLQICFLQFSKLEELddEEKYYCDKCGCKQ 192
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  647 ESTKQLSFDTLPMVICFHLKRFERSQahRRTHKIDTFIEFPTSIDMGPYTTIMKKKadaidlnssgtsiksedyggdnnn 726
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKRFSYNR--STWEKLNTEVEFPLELDLSRYLAEELKP------------------------ 246
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  727 nningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhDGDNSFTYELFAVVNHTGKIDSGHYTSFVKHQDS--WYKC 804
Cdd:pfam00443 247 ----------------------------------------KTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnrWYKF 286
                         570       580
                  ....*....|....*....|....
gi 256013071  805 DDSMIS-STTIHNVLKSKGYLLYY 827
Cdd:pfam00443 287 DDEKVTeVDEETAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
619-830 1.49e-21

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 100.34  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 619 TLLSCLERFTQPEKLD--EKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRthKIDTFIEFPtsIDmgpyt 696
Cdd:COG5560  676 TLQDCLNEFSKPEQLGlsDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP--ID----- 746
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 697 timkkkadaiDLNSSGTSIKSEDyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfPSIIeqhdgdnsftYEL 776
Cdd:COG5560  747 ----------DLDLSGVEYMVDD----------------------------------------PRLI----------YDL 766
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 256013071 777 FAVVNHTGKIDSGHYTSFVKHQDS--WYKCDDSMISSTTIHNVLKSKGYLLYYLKK 830
Cdd:COG5560  767 YAVDNHYGGLSGGHYTAYARNFANngWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
92-190 1.97e-06

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 45.71  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071   92 CMVCNCfNGRLHICLHCVHVSCW--KQGHIHQHLGKSHpnptaannnnnnnnnnntsttsnsnqeeknitnnndiHFLAV 169
Cdd:pfam02148   1 CSLCGN-TSNLWLCLTCGHVGCGryQNSHALEHYEETG-------------------------------------HPLAV 42
                          90       100
                  ....*....|....*....|.
gi 256013071  170 DLNLNQIYCHYCQDYIYDKEF 190
Cdd:pfam02148  43 NLSTLTVYCYPCDDYVHDPSL 63
 
Name Accession Description Interval E-value
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
250-827 2.61e-86

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: 277.72  E-value: 2.61e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 250 RGLNNLGNTCFMNSILQSFLHNPLLRNYFLSDMHKCDKKnnlnnvnssnnnnnnnfnnnnnnnnnnnnnnnnnnnnnnnn 329
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCL----------------------------------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 330 nnnnnnnnnnnnnnnnnnnnnnnensnddnpniksepIDDNNSeivstppiqnnnnnnsnnnnnnnnnnnnnnnnnnnnn 409
Cdd:cd02660   40 -------------------------------------SCSPNS------------------------------------- 45
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 410 nnnnniskiCLGCEMDKLFTCVF-SGVKFPFTPHHFLYSCWNYSNYFIGYEQQDAHEFFISSLNGIHSHCGGTTGK---- 484
Cdd:cd02660   46 ---------CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEande 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 485 -DCDCIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPktlkdktsnangnsnsngngnnkintstasttasatls 563
Cdd:cd02660  117 sHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP-------------------------------------- 158
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 564 sqddeviSLDGSESVNGENGLGSNShqeqyhqqqqqqqqqqqqqqqqqhqqqqnnTLLSCLERFTQPEKLDE-KYFCPNC 642
Cdd:cd02660  159 -------NKSTPSWALGESGVSGTP------------------------------TLSDCLDRFTRPEKLGDfAYKCSGC 201
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 643 NSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRThKIDTFIEFPTSIDMGPYTTIMKKKadaidlnssgTSIKSEDygg 722
Cdd:cd02660  202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGD----------TQDSNSL--- 267
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 723 dnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhdgDNSFTYELFAVVNHTGKIDSGHYTSFVKHQ-DSW 801
Cdd:cd02660  268 ----------------------------------------------DPDYTYDLFAVVVHKGTLDTGHYTAYCRQGdGQW 301
                        570       580
                 ....*....|....*....|....*.
gi 256013071 802 YKCDDSMISSTTIHNVLKSKGYLLYY 827
Cdd:cd02660  302 FKFDDAMITRVSEEEVLKSQAYLLFY 327
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
250-827 2.39e-41

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 153.75  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  250 RGLNNLGNTCFMNSILQSFLHNPLLRNYFLSDMHKCDKknnlnnvnssnnnnnnnfnnnnnnnnnnnnnnnnnnnnnnnn 329
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED------------------------------------------ 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  330 nnnnnnnnnnnnnnnnnnnnnnnensnddnpnikSEPIDDNNseivstppiqnnnnnnsnnnnnnnnnnnnnnnnnnnnn 409
Cdd:pfam00443  39 ----------------------------------SRYNKDIN-------------------------------------- 46
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  410 nnnnniskicLGCEMDKLFTCVFSGVKF-PFTPHHFLYSCWNYSNYFIGYEQQDAHEFFISSLNGIHSHCGGTTGKDCDC 488
Cdd:pfam00443  47 ----------LLCALRDLFKALQKNSKSsSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENES 116
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  489 IIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPKTLKDKtsnangnsnsngngnnkintstasttasatlssqdde 568
Cdd:pfam00443 117 LITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAEL------------------------------------- 159
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  569 visldgsesvngenglgsnshqeqyhqqqqqqqqqqqqqqqqqhqqqQNNTLLSCLERFTQPEKL--DEKYFCPNCNSKQ 646
Cdd:pfam00443 160 -----------------------------------------------KTASLQICFLQFSKLEELddEEKYYCDKCGCKQ 192
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  647 ESTKQLSFDTLPMVICFHLKRFERSQahRRTHKIDTFIEFPTSIDMGPYTTIMKKKadaidlnssgtsiksedyggdnnn 726
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKRFSYNR--STWEKLNTEVEFPLELDLSRYLAEELKP------------------------ 246
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  727 nningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhDGDNSFTYELFAVVNHTGKIDSGHYTSFVKHQDS--WYKC 804
Cdd:pfam00443 247 ----------------------------------------KTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnrWYKF 286
                         570       580
                  ....*....|....*....|....
gi 256013071  805 DDSMIS-STTIHNVLKSKGYLLYY 827
Cdd:pfam00443 287 DDEKVTeVDEETAVLSSSAYILFY 310
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
419-828 3.21e-36

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: 138.95  E-value: 3.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 419 CLGCEMDKLFTCVFSGVKFPFTPHHFLYSCWNYSNYFIGYEQQDAHEFFISSLNGIHSHCGGTTGKDCDC--------II 490
Cdd:cd02661   45 CMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVdpssqettLV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 491 HCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPKTlkdktsnangnsnsngngnnkintstasttasatlssqddevi 570
Cdd:cd02661  125 QQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGA------------------------------------------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 571 sldgsesvngenglgsnshqeqyhqqqqqqqqqqqqqqqqqhqqqqnNTLLSCLERFTQPEKLD--EKYFCPNCNSKQES 648
Cdd:cd02661  162 -----------------------------------------------DSLEDALEQFTKPEQLDgeNKYKCERCKKKVKA 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 649 TKQLSFDTLPMVICFHLKRFERSqahrRTHKIDTFIEFPTSIDMGPYttiMKKKadaidlnssgtsiksedyggdnnnnn 728
Cdd:cd02661  195 SKQLTIHRAPNVLTIHLKRFSNF----RGGKINKQISFPETLDLSPY---MSQP-------------------------- 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 729 ingnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhdGDNSFTYELFAVVNHTG-KIDSGHYTSFVKHQD-SWYKCDD 806
Cdd:cd02661  242 ---------------------------------------NDGPLKYKLYAVLVHSGfSPHSGHYYCYVKSSNgKWYNMDD 282
                        410       420
                 ....*....|....*....|..
gi 256013071 807 SMISSTTIHNVLKSKGYLLYYL 828
Cdd:cd02661  283 SKVSPVSIETVLSQKAYILFYI 304
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
458-827 1.13e-35

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: 135.69  E-value: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 458 YEQQDAHEFFISSLNGIHSHCGGTTG-----KDCDCIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPKTlkdkt 532
Cdd:cd02257   20 SEQQDAHEFLLFLLDKLHEELKKSSKrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVK----- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 533 snangnsnsngngnnkintstasttasatlssqddevisldgsesvngenglgsnshqeqyhqqqqqqqqqqqqqqqqqh 612
Cdd:cd02257      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 613 qQQQNNTLLSCLERFTQPEKLD--EKYFCpNCNSKQESTKQLSFDTLPMVICFHLKRFERSQaHRRTHKIDTFIEFPTSI 690
Cdd:cd02257   95 -GLPQVSLEDCLEKFFKEEILEgdNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLEL 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 691 DMGPYTTimkkkadaidlnssgtsiksedyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfPSIIEQHDGDN 770
Cdd:cd02257  172 DLSPYLS--------------------------------------------------------------EGEKDSDSDNG 189
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256013071 771 SFTYELFAVVNHTGK-IDSGHYTSFVKHQDS--WYKCDDSMISSTTIHNVLK-----SKGYLLYY 827
Cdd:cd02257  190 SYKYELVAVVVHSGTsADSGHYVAYVKDPSDgkWYKFNDDKVTEVSEEEVLEfgslsSSAYILFY 254
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
459-827 1.35e-35

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: 134.72  E-value: 1.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 459 EQQDAHEFFISSLNGIHShcggttgkdcdcIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIPKTLKDKTSnangn 538
Cdd:cd02674   21 DQQDAQEFLLFLLDGLHS------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPK----- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 539 snsngngnnkintstasttasatlssqddevisldgsesvngenglgsnshqeqyhqqqqqqqqqqqqqqqqqhqqqqnN 618
Cdd:cd02674   84 -------------------------------------------------------------------------------V 84
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 619 TLLSCLERFTQPEKLD--EKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFerSQAHRRTHKIDTFIEFPtsidmgpyt 696
Cdd:cd02674   85 TLEDCLRLFTKEETLDgdNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF--SFSRGSTRKLTTPVTFP--------- 153
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 697 timkkkadaidlnssgtsiksedyggdnnnnningnnsnsnnnnnnnnidssflnqLNDQDKFPSIIEQHDGdNSFTYEL 776
Cdd:cd02674  154 --------------------------------------------------------LNDLDLTPYVDTRSFT-GPFKYDL 176
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 256013071 777 FAVVNHTGKIDSGHYTSFVKHQDS--WYKCDDSMISSTTIHNVLKSKGYLLYY 827
Cdd:cd02674  177 YAVVNHYGSLNGGHYTAYCKNNETndWYKFDDSRVTKVSESSVVSSSAYILFY 229
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
619-830 1.49e-21

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 100.34  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 619 TLLSCLERFTQPEKLD--EKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRthKIDTFIEFPtsIDmgpyt 696
Cdd:COG5560  676 TLQDCLNEFSKPEQLGlsDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD--KIDDLVEYP--ID----- 746
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 697 timkkkadaiDLNSSGTSIKSEDyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfPSIIeqhdgdnsftYEL 776
Cdd:COG5560  747 ----------DLDLSGVEYMVDD----------------------------------------PRLI----------YDL 766
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 256013071 777 FAVVNHTGKIDSGHYTSFVKHQDS--WYKCDDSMISSTTIHNVLKSKGYLLYYLKK 830
Cdd:COG5560  767 YAVDNHYGGLSGGHYTAYARNFANngWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
458-820 8.43e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 94.63  E-value: 8.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 458 YEQQDAHEFFISSLNGIHSHCGGTTGKDcdcIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIpktlKDKTsnang 537
Cdd:cd02659   84 FEQHDVQEFFRVLFDKLEEKLKGTGQEG---LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV----KGKK----- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 538 nsnsngngnnkintstasttasatlssqddevisldgsesvngenglgsnshqeqyhqqqqqqqqqqqqqqqqqhqqqqn 617
Cdd:cd02659      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 618 nTLLSCLERFTQPEKLD--EKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRTHKIDTFIEFPTSIDMGPY 695
Cdd:cd02659  152 -NLEESLDAYVQGETLEgdNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPY 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 696 T--TIMKKKADAidlnssgTSIKSEDYggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhdgdnsfT 773
Cdd:cd02659  231 TekGLAKKEGDS-------EKKDSESY----------------------------------------------------I 251
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 256013071 774 YELFAVVNHTGKIDSGHYTSFVKHQDS--WYKCDDSMISSTTIHNVLKS 820
Cdd:cd02659  252 YELHGVLVHSGDAHGGHYYSYIKDRDDgkWYKFNDDVVTPFDPNDAEEE 300
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
455-827 1.14e-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: 92.83  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 455 FIGYEQQDAHEFFISSLNGIHShcggttgkdcdcIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIpktlkdktsn 534
Cdd:cd02667   46 FKGYQQQDSHELLRYLLDGLRT------------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPR---------- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 535 angnsnsngngnnkintstasttasatlssqddevisldgSESVNGENglgsnshqeqyhqqqqqqqqqqqqqqqqqhqq 614
Cdd:cd02667  104 ----------------------------------------SDEIKSEC-------------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 615 qqnnTLLSCLERFTQPEKLDE--KYFCPNCnskQESTKQLSFDTLPMVICFHLKRFERSQAHrRTHKIDTFIEFPTSIDM 692
Cdd:cd02667  112 ----SIESCLKQFTEVEILEGnnKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSA-NLRKVSRHVSFPEILDL 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 693 GPYTTimkkkadaidlnssgtsiksedyggdnnnnningnnsnsnnnnnnnnidssfLNQLNDQDKFpsiieqhdgdnSF 772
Cdd:cd02667  184 APFCD----------------------------------------------------PKCNSSEDKS-----------SV 200
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256013071 773 TYELFAVVNHTGKIDSGHYTSFVK-----------------------HQDSWYKCDDSMISSTTIHNVLKSKGYLLYY 827
Cdd:cd02667  201 LYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeagpGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
617-810 2.95e-17

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 83.62  E-value: 2.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 617 NNTLLSCLERFTQPEKL--DEKYFCPNCNSKQESTKQLSFDTLPMVICFHLKR--FERSQAHRRthKIDTFIEFPTSIDM 692
Cdd:cd02668  155 HKTLEECIDEFLKEEQLtgDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRfvFDRKTGAKK--KLNASISFPEILDM 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 693 GPYttimkkkadaidlnssgtsiksedyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpsIIEQHDGDnsF 772
Cdd:cd02668  233 GEY------------------------------------------------------------------LAESDEGS--Y 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 256013071 773 TYELFAVVNHTG-KIDSGHYTSFVK--HQDSWYKCDDSMIS 810
Cdd:cd02668  245 VYELSGVLIHQGvSAYSGHYIAHIKdeQTGEWYKFNDEDVE 285
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
455-827 2.28e-16

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 80.82  E-value: 2.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 455 FIGYEQQDAHEFFISSLNGI--------------HSHCGGTTGKDCDCIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDI 520
Cdd:cd02663   60 FDNYMHQDAHEFLNFLLNEIaeildaerkaekanRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 521 SLDIPKtlkdktsnangnsnsngngnnkintstasttasatlssqddevisldgsesvngenglgsnshqeqyhqqqqqq 600
Cdd:cd02663  140 SIDVEQ-------------------------------------------------------------------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 601 qqqqqqqqqqqhqqqqNNTLLSCLERFTQPEKL--DEKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRTH 678
Cdd:cd02663  146 ----------------NTSITSCLRQFSATETLcgRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYI 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 679 KIDTFIEFPTSIDMgpyttimkkkadaidLNSSGTSiksedyggdnnnnningnnsnsnnnnnnnnidssflnqlNDQDK 758
Cdd:cd02663  210 KLFYRVVFPLELRL---------------FNTTDDA---------------------------------------ENPDR 235
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256013071 759 fpsiieqhdgdnsfTYELFAVVNHTGK-IDSGHYTSFVKHQDSWYKCDDSMISSTTIHNVLK--------SKGYLLYY 827
Cdd:cd02663  236 --------------LYELVAVVVHIGGgPNHGHYVSIVKSHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
455-827 1.19e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 69.92  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 455 FIGYEQQDAHEFFISSLNGIHShcggttgkdcdcIIHCTFGGALKSEVSCLTCQFTSSTSDPFIDISLDIpktlkdktsn 534
Cdd:cd02671  100 YEGYLQHDAQEVLQCILGNIQE------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPV---------- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 535 angnsnsngngnnkintstasttasatlssQDDEVISLDGSESVNGENGLgsnshqeqyhqqqqqqqqqqqqqqqqqhqq 614
Cdd:cd02671  158 ------------------------------QESELSKSEESSEISPDPKT------------------------------ 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 615 qQNNTLLSCLERFTQPEKL--DEKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRTH----KIDTFIefPT 688
Cdd:cd02671  178 -EMKTLKWAISQFASVERIvgEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPL--LT 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 689 SIDMgpyttimkkkadaidlnssgtsiksedyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpSIIEQHDG 768
Cdd:cd02671  255 PLKL--------------------------------------------------------------------SLEEWSTK 266
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256013071 769 DNSFTYELFAVVNHTG-KIDSGHYTSFVKhqdsWYKCDDSMISSTTIHNVLK---------SKGYLLYY 827
Cdd:cd02671  267 PKNDVYRLFAVVMHSGaTISSGHYTAYVR----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
763-830 6.87e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 64.05  E-value: 6.87e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256013071 763 IEQHDGDN-SFTYELFAVVNHTGKIDSGHYTSFVKHQDSWYKCDDSMISSTTIHNVLKSK---GYLLYYLKK 830
Cdd:COG5533  213 HDQILNIVkETYYDLVGFVLHQGSLEGGHYIAYVKKGGKWEKANDSDVTPVSEEEAINEKaknAYLYFYERI 284
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
617-819 3.19e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 57.57  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  617 NNTLLSCLE----RFTQPEKL--DEKYFCPNcNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRTHKIDTFIEFPTSI 690
Cdd:COG5077   333 NVKGMKNLQesfrRYIQVETLdgDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEI 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071  691 DMGPYTtimkkkadaidlnsSGTSIKSEdyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkfpsiieqhdgDN 770
Cdd:COG5077   412 DLLPFL--------------DRDADKSE--------------------------------------------------NS 427
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256013071  771 SFTYELFAVVNHTGKIDSGHYTSFVKHQ--DSWYKCDDSMISSTTIHNVLK 819
Cdd:COG5077   428 DAVYVLYGVLVHSGDLHEGHYYALLKPEkdGRWYKFDDTRVTRATEKEVLE 478
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
617-827 9.24e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 53.91  E-value: 9.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 617 NNTLLSCLERFTQPEKLDEkYFCPNCnskqestkQLSFDTLPMVICFHLKRFErsqahrrthkidtfiefptsidMGPYT 696
Cdd:cd02662   95 GTTLEHCLDDFLSTEIIDD-YKCDRC--------QTVIVRLPQILCIHLSRSV----------------------FDGRG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 697 TIMKkkadaidlNSSGTSiksedyggdnnnnningnnsnsnnnnnnnnidssflnqlndqdkFPSIIEQhdgdnsFTYEL 776
Cdd:cd02662  144 TSTK--------NSCKVS--------------------------------------------FPERLPK------VLYRL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256013071 777 FAVVNHTGKIDSGHYTSFVKH----------------------QDSWYKCDDSMISSTTIHNVLKSKG-YLLYY 827
Cdd:cd02662  166 RAVVVHYGSHSSGHYVCYRRKplfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKSaYMLFY 239
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
619-695 5.71e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 52.33  E-value: 5.71e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256013071 619 TLLSCLERFTQPEKLDekYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRThKIDTFIEFPTSIDMGPY 695
Cdd:cd02658  179 PLEDCLKAYFAPETIE--DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPK-KLDVPIDVPEELGPGKY 252
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
92-190 1.97e-06

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 45.71  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071   92 CMVCNCfNGRLHICLHCVHVSCW--KQGHIHQHLGKSHpnptaannnnnnnnnnntsttsnsnqeeknitnnndiHFLAV 169
Cdd:pfam02148   1 CSLCGN-TSNLWLCLTCGHVGCGryQNSHALEHYEETG-------------------------------------HPLAV 42
                          90       100
                  ....*....|....*....|.
gi 256013071  170 DLNLNQIYCHYCQDYIYDKEF 190
Cdd:pfam02148  43 NLSTLTVYCYPCDDYVHDPSL 63
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
440-827 2.51e-06

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 50.18  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 440 TPHHFLYSCWnySNYFIGYEQQDAHEFFISSLNGIHShcggttgkdcdcIIHCTFGGALKSEVSCLTCQFTSSTSDPFID 519
Cdd:cd02664   63 PPDYFLEASR--PPWFTPGSQQDCSEYLRYLLDRLHT------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 520 ISLDIPktlkdktsnangnsnsngngnnkintstasttasatlssqddevisldgsesvngenglgsnshqeqyhqqqqq 599
Cdd:cd02664  129 LDLSFP-------------------------------------------------------------------------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 600 qqqqqqqqqqqqhqqqqnnTLLSCLERFTQPEKL--DEKYFCPNCNSKQESTKQLSFDTLPMVICFHLKRFERSQAHRRT 677
Cdd:cd02664  135 -------------------SVQDLLNYFLSPEKLtgDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVR 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 678 HKIDTFIEFPTSIDMgPYTTIMK--KKADAIDLNSSGTSIKSEdyggdnnnnningnnsnsnnnnnnnnidssflnqlnd 755
Cdd:cd02664  196 EKIMDNVSINEVLSL-PVRVESKssESPLEKKEEESGDDGELV------------------------------------- 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256013071 756 qdkfpsiieqhdgDNSFTYELFAVVNHTG-KIDSGHYTSFVKHQ----------------------DSWYKCDDSMISST 812
Cdd:cd02664  238 -------------TRQVHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpepkdaeendesKNWYLFNDSRVTFS 304
                        410       420
                 ....*....|....*....|..
gi 256013071 813 T---IHNVL----KSKGYLLYY 827
Cdd:cd02664  305 SfesVQNVTsrfpKDTPYILFY 326
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
769-827 3.42e-06

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 49.64  E-value: 3.42e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256013071 769 DNSFTYELFAVVNHTGK-IDSGHYTSFVK--HQDSWYKCDDSMISSTTIHNVLKSKG-------YLLYY 827
Cdd:cd02657  236 TPSGYYELVAVITHQGRsADSGHYVAWVRrkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
752-812 9.86e-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: 44.47  E-value: 9.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256013071 752 QLNDQDKFPSIIEQHDgdnsftYELFAVVNHTGKIDSGHYTSFV--KHQDSWYKCDDsmISST 812
Cdd:cd02665  148 KIHDKLEFPQIIQQVP------YELHAVLVHEGQANAGHYWAYIykQSRQEWEKYND--ISVT 202
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
251-277 1.11e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 44.79  E-value: 1.11e-04
                         10        20
                 ....*....|....*....|....*...
gi 256013071 251 GLNNLGNTCFMNSILQSF-LHNPLLRNY 277
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILaLYLPKLDEL 28
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-280 4.60e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 43.25  E-value: 4.60e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 256013071 251 GLNNLGNTCFMNSILQSFLHNPLLRNYFLS 280
Cdd:cd02666    3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLN 32
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-280 4.76e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 43.25  E-value: 4.76e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 256013071 251 GLNNLGNTCFMNSILQSFLHNPLLRNYFLS 280
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS 30
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
773-827 5.44e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 42.52  E-value: 5.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256013071 773 TYELFAVVNHTGK-IDSGHYTSFVK---HQDSWYKCDDSMISSTTIHNVLK---SKGYLLYY 827
Cdd:cd02673  183 KYSLVAVICHLGEsPYDGHYIAYTKelyNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
247-280 7.51e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 42.69  E-value: 7.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 256013071 247 IGLRGLNNLGNTCFMNSILQSFLHNPLLRNYFLS 280
Cdd:cd02669  117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL 150
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-277 9.42e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 41.58  E-value: 9.42e-04
                         10        20
                 ....*....|....*....|....*..
gi 256013071 251 GLNNLGNTCFMNSILQSFLHNPLLRNY 277
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
762-813 1.04e-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: 42.09  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 256013071 762 IIEQHDGDNSFTYELFAVVNHTGKIDSGHYTSFVKH--QDSWYKCDDSMISSTT 813
Cdd:cd02666  269 IEKQFDDLKSYGYRLHAVFIHRGEASSGHYWVYIKDfeENVWRKYNDETVTVVP 322
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-276 2.59e-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 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: 40.78  E-value: 2.59e-03
                         10        20
                 ....*....|....*....|....*.
gi 256013071 251 GLNNLGNTCFMNSILQSFLHNPLLRN 276
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRD 26
 
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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