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Conserved domains on  [gi|31543910|ref|NP_003359|]
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ubiquitin carboxyl-terminal hydrolase 1 [Homo sapiens]

Protein Classification

Peptidase_C19 and Peptidase_C19O domain-containing protein( domain architecture ID 10245588)

Peptidase_C19 and Peptidase_C19O domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
424-599 2.14e-110

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: 339.56  E-value: 2.14e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 424 ELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDK 503
Cdd:cd02671 121 ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDK 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 504 YFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYgGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVM 583
Cdd:cd02671 201 YFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCY-GGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVM 279
                       170
                ....*....|....*.
gi 31543910 584 HSGITISSGHYTASVK 599
Cdd:cd02671 280 HSGATISSGHYTAYVR 295
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
82-222 2.53e-11

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 cd02657:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 305  Bit Score: 65.43  E-value: 2.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFksgvkhlfniisrkKEALKDEanqkdKGNCKEDSLASYELICSLQSLIISVEQLQA 161
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPEL--------------RDALKNY-----NPARRGANQSSDNLTNALRDLFDTMDKKQE 61
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543910 162 SFllnpekytdelatQPRRLLNTLRELNPMYE------GYLQHDAQEVLQCILGNIQETCQLLKKEE 222
Cdd:cd02657  62 PV-------------PPIEFLQLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG 115
 
Name Accession Description Interval E-value
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
424-599 2.14e-110

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: 339.56  E-value: 2.14e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 424 ELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDK 503
Cdd:cd02671 121 ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDK 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 504 YFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYgGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVM 583
Cdd:cd02671 201 YFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCY-GGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVM 279
                       170
                ....*....|....*.
gi 31543910 584 HSGITISSGHYTASVK 599
Cdd:cd02671 280 HSGATISSGHYTAYVR 295
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
81-605 5.81e-28

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 114.85  E-value: 5.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910    81 VGLNNLGNTCYLNSILQVLYFCPGFKsgvkhlfNIISRKKEALKDEANQKDkgnckedslasYELICSLQSLIISveqlq 160
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFR-------DYLLRISPLSEDSRYNKD-----------INLLCALRDLFKA----- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   161 asfLLNPEKYTdelATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQetcqllkkeevknvaelptkveeiphpk 240
Cdd:pfam00443  58 ---LQKNSKSS---SVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLH---------------------------- 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   241 EEMNginsiemdsmrhsedfkeklpkgngkrksdtefgnmkkkvklskehqsleenqrqtrskrkatsdtlesppkiiPK 320
Cdd:pfam00443 104 EDLN--------------------------------------------------------------------------GN 109
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   321 YISENESPrpsqkksrvkinwlksatkqpsilskfcslgkittnqgvkgqskenecdpeedlgkcesdnttngcglespg 400
Cdd:pfam00443 110 HSTENESL------------------------------------------------------------------------ 117
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   401 ntvtpvnvnevkpinkgeeqigfelVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEpkt 480
Cdd:pfam00443 118 -------------------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFL--- 169
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   481 emktlrwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDcyGGGLSKINTPLLTPL 560
Cdd:pfam00443 170 ----------QFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF-----SYN--RSTWEKLNTEVEFPL 232
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 31543910   561 KLSLEEWSTKPTND------SYGLFAVVMHSGiTISSGHYTASVKVTDLNS 605
Cdd:pfam00443 233 ELDLSRYLAEELKPktnnlqDYRLVAVVVHSG-SLSSGHYIAYIKAYENNR 282
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-222 2.53e-11

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 65.43  E-value: 2.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFksgvkhlfniisrkKEALKDEanqkdKGNCKEDSLASYELICSLQSLIISVEQLQA 161
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPEL--------------RDALKNY-----NPARRGANQSSDNLTNALRDLFDTMDKKQE 61
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543910 162 SFllnpekytdelatQPRRLLNTLRELNPMYE------GYLQHDAQEVLQCILGNIQETCQLLKKEE 222
Cdd:cd02657  62 PV-------------PPIEFLQLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG 115
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
482-599 9.54e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 56.03  E-value: 9.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  482 MKTLRWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDCYGGGLSKINTPLLTPLK 561
Cdd:COG5077  337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRF-----EYDFERDMMVKINDRYEFPLE 410
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 31543910  562 LSLEEWSTKPTNDS------YGLFAVVMHSGiTISSGHYTASVK 599
Cdd:COG5077  411 IDLLPFLDRDADKSensdavYVLYGVLVHSG-DLHEGHYYALLK 453
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
82-101 1.18e-03

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 41.71  E-value: 1.18e-03
                        10        20
                ....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYF 101
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAL 20
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
81-112 2.91e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 40.33  E-value: 2.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 31543910    81 VGLNNLGNTCYLNSILQVLYFCPGF-KSGVKHL 112
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLrNLALSHL 33
 
Name Accession Description Interval E-value
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
424-599 2.14e-110

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: 339.56  E-value: 2.14e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 424 ELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDK 503
Cdd:cd02671 121 ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDK 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 504 YFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYgGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVM 583
Cdd:cd02671 201 YFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCY-GGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVM 279
                       170
                ....*....|....*.
gi 31543910 584 HSGITISSGHYTASVK 599
Cdd:cd02671 280 HSGATISSGHYTAYVR 295
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
409-604 2.55e-31

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: 123.36  E-value: 2.55e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 409 NEVKPINKGEEQIGFE--LVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVqedelskveesseisPEPKTEMKTLR 486
Cdd:cd02257  38 EELKKSSKRTSDSSSLksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL---------------PVKGLPQVSLE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 487 WAISQFASVERIVGEDKYFCEnCHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDCYGGGlSKINTPLLTPLKLSLEE 566
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRF-----SFNEDGTK-EKLNTKVSFPLELDLSP 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 31543910 567 WSTKPTNDS--------YGLFAVVMHSGITISSGHYTASVKVTDLN 604
Cdd:cd02257 176 YLSEGEKDSdsdngsykYELVAVVVHSGTSADSGHYVAYVKDPSDG 221
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
81-605 5.81e-28

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 114.85  E-value: 5.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910    81 VGLNNLGNTCYLNSILQVLYFCPGFKsgvkhlfNIISRKKEALKDEANQKDkgnckedslasYELICSLQSLIISveqlq 160
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFR-------DYLLRISPLSEDSRYNKD-----------INLLCALRDLFKA----- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   161 asfLLNPEKYTdelATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQetcqllkkeevknvaelptkveeiphpk 240
Cdd:pfam00443  58 ---LQKNSKSS---SVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLH---------------------------- 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   241 EEMNginsiemdsmrhsedfkeklpkgngkrksdtefgnmkkkvklskehqsleenqrqtrskrkatsdtlesppkiiPK 320
Cdd:pfam00443 104 EDLN--------------------------------------------------------------------------GN 109
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   321 YISENESPrpsqkksrvkinwlksatkqpsilskfcslgkittnqgvkgqskenecdpeedlgkcesdnttngcglespg 400
Cdd:pfam00443 110 HSTENESL------------------------------------------------------------------------ 117
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   401 ntvtpvnvnevkpinkgeeqigfelVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEpkt 480
Cdd:pfam00443 118 -------------------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFL--- 169
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   481 emktlrwaisQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDcyGGGLSKINTPLLTPL 560
Cdd:pfam00443 170 ----------QFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF-----SYN--RSTWEKLNTEVEFPL 232
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 31543910   561 KLSLEEWSTKPTND------SYGLFAVVMHSGiTISSGHYTASVKVTDLNS 605
Cdd:pfam00443 233 ELDLSRYLAEELKPktnnlqDYRLVAVVVHSG-SLSSGHYIAYIKAYENNR 282
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
426-603 1.54e-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 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: 107.78  E-value: 1.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 426 VEKLFQGQLVLRTRCLECESLTERREDFQDISVpvqedelsKVEESSEISpepktemKTLRwaisQFASVERIVGEDKYF 505
Cdd:cd02663 109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSI--------DVEQNTSIT-------SCLR----QFSATETLCGRNKFY 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 506 CENCHHYTEAERSLLFDKMPEVITIHLKCFAasgleFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDS--YGLFAVVM 583
Cdd:cd02663 170 CDECCSLQEAEKRMKIKKLPKILALHLKRFK-----YDEQLNRYIKLFYRVVFPLELRLFNTTDDAENPDrlYELVAVVV 244
                       170       180
                ....*....|....*....|
gi 31543910 584 HSGITISSGHYTASVKVTDL 603
Cdd:cd02663 245 HIGGGPNHGHYVSIVKSHGG 264
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
425-599 4.64e-24

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: 103.51  E-value: 4.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 425 LVEKLFQGQLVLRTRCLECESLTERREDFQDISVpvqedELSKVEesseispepktemkTLRWAISQFASVERIVGEDKY 504
Cdd:cd02661 123 LVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSL-----DIKGAD--------------SLEDALEQFTKPEQLDGENKY 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 505 FCENCHHYTEAERSLLFDKMPEVITIHLKCFAasglefdcyGGGLSKINTPLLTPLKLSLEEWSTKPTNDS--YGLFAVV 582
Cdd:cd02661 184 KCERCKKKVKASKQLTIHRAPNVLTIHLKRFS---------NFRGGKINKQISFPETLDLSPYMSQPNDGPlkYKLYAVL 254
                       170
                ....*....|....*..
gi 31543910 583 MHSGITISSGHYTASVK 599
Cdd:cd02661 255 VHSGFSPHSGHYYCYVK 271
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
425-600 2.89e-22

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 96.20  E-value: 2.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 425 LVEKLFQGQLVLRTRCLECESLTERREDFQDISVPvqedelskVEESSEISPEPktemkTLRWAISQFASVERIVGEDKY 504
Cdd:cd02674  39 IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLP--------IPSGSGDAPKV-----TLEDCLRLFTKEETLDGDNAW 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 505 FCENCHHYTEAERSLLFDKMPEVITIHLKcfaasglEFDCYGGGLSKINTPLLTPLK-LSLEEW---STKPTNDSYGLFA 580
Cdd:cd02674 106 KCPKCKKKRKATKKLTISRLPKVLIIHLK-------RFSFSRGSTRKLTTPVTFPLNdLDLTPYvdtRSFTGPFKYDLYA 178
                       170       180
                ....*....|....*....|
gi 31543910 581 VVMHSGiTISSGHYTASVKV 600
Cdd:cd02674 179 VVNHYG-SLNGGHYTAYCKN 197
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
425-600 1.30e-21

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 95.53  E-value: 1.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 425 LVEKLFQGQLVLRTRCLECESLTERREDFQDISVPvqedelskveesseiSPEPKTEMKTLRWAISQFASVERIVGEDKY 504
Cdd:cd02667  68 FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---------------RSDEIKSECSIESCLKQFTEVEILEGNNKF 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 505 FCENChhyTEAERSLLFDKMPEVITIHLKCFAASGLefdcygGGLSKIN-----------TPLLTPLKLSLEEwstkPTN 573
Cdd:cd02667 133 ACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRS------ANLRKVSrhvsfpeildlAPFCDPKCNSSED----KSS 199
                       170       180
                ....*....|....*....|....*..
gi 31543910 574 DSYGLFAVVMHSGiTISSGHYTASVKV 600
Cdd:cd02667 200 VLYRLYGVVEHSG-TMRSGHYVAYVKV 225
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
416-604 7.93e-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: 7.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 416 KGEEQIGfeLVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVqedelskveesseispepkTEMKTLRWAISQFASV 495
Cdd:cd02659 105 KGTGQEG--LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV-------------------KGKKNLEESLDAYVQG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 496 ERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDCYGGGLSKINTPLLTPLKLSLE---------- 565
Cdd:cd02659 164 ETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-----EFDFETMMRIKINDRFEFPLELDMEpytekglakk 238
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 31543910 566 EWSTKPTNDS---YGLFAVVMHSGiTISSGHYTASVKVTDLN 604
Cdd:cd02659 239 EGDSEKKDSEsyiYELHGVLVHSG-DAHGGHYYSYIKDRDDG 279
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
425-599 1.53e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 93.25  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 425 LVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEdelskveesseispepkteMKTLRWAISQFASVERIVGEDKY 504
Cdd:cd02668 117 IVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG-------------------HKTLEECIDEFLKEEQLTGDNQY 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 505 FCENCHHYTEAERSLLFDKMPEVITIHLKCFAasgleFDCYGGGLSKINTPLLTPLKLSLEEWS--TKPTNDSYGLFAVV 582
Cdd:cd02668 178 FCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-----FDRKTGAKKKLNASISFPEILDMGEYLaeSDEGSYVYELSGVL 252
                       170
                ....*....|....*..
gi 31543910 583 MHSGITISSGHYTASVK 599
Cdd:cd02668 253 IHQGVSAYSGHYIAHIK 269
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
426-602 8.18e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 91.28  E-value: 8.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 426 VEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEdelsKVEESSEISPEPKTEMKTLRWAISQFASVERiVGEDKYF 505
Cdd:cd02660 123 IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN----KSTPSWALGESGVSGTPTLSDCLDRFTRPEK-LGDFAYK 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 506 CENCHHYTEAERSLLFDKMPEVITIHLKCFAASGlefdcyGGGLSKINTPLLTPLKLSLEEWSTKPTNDS---------- 575
Cdd:cd02660 198 CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL------NKTSRKIDTYVQFPLELNMTPYTSSSIGDTqdsnsldpdy 271
                       170       180
                ....*....|....*....|....*...
gi 31543910 576 -YGLFAVVMHSGiTISSGHYTASVKVTD 602
Cdd:cd02660 272 tYDLFAVVVHKG-TLDTGHYTAYCRQGD 298
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
425-594 1.96e-13

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 72.14  E-value: 1.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 425 LVEKLFQGQLVLRTRCLEC--ESLTERREDFQDISVPVQEDelskveesseispepktemktlrwAISQFASVERIVGED 502
Cdd:cd02664  98 LIEKMFGGKLSTTIRCLNCnsTSARTERFRDLDLSFPSVQD------------------------LLNYFLSPEKLTGDN 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 503 KYFCENCHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDCYGGGLSKINTPLLTPLKLSL-------------EEWST 569
Cdd:cd02664 154 QYYCEKCASLQDAEKEMKVTGAPEYLILTLLRF-----SYDQKTHVREKIMDNVSINEVLSLpvrveskssesplEKKEE 228
                       170       180       190
                ....*....|....*....|....*....|...
gi 31543910 570 KPTNDS--------YGLFAVVMHSGITISSGHY 594
Cdd:cd02664 229 ESGDDGelvtrqvhYRLYAVVVHSGYSSESGHY 261
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-222 2.53e-11

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 65.43  E-value: 2.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFksgvkhlfniisrkKEALKDEanqkdKGNCKEDSLASYELICSLQSLIISVEQLQA 161
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPEL--------------RDALKNY-----NPARRGANQSSDNLTNALRDLFDTMDKKQE 61
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543910 162 SFllnpekytdelatQPRRLLNTLRELNPMYE------GYLQHDAQEVLQCILGNIQETCQLLKKEE 222
Cdd:cd02657  62 PV-------------PPIEFLQLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG 115
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
437-599 4.66e-10

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 61.57  E-value: 4.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 437 RTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEpkTEMKTlrwAISQFASVERIvgedKYFCENCHHYTEAE 516
Cdd:cd02658 137 RLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGELVYEP--VPLED---CLKAYFAPETI----EDFCSTCKEKTTAT 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 517 RSLLFDKMPEVITIHLKCFAASglefdcYGGGLSKINTPLLTPLKLsleewstkpTNDSYGLFAVVMHSGITISSGHYTA 596
Cdd:cd02658 208 KTTGFKTFPDYLVINMKRFQLL------ENWVPKKLDVPIDVPEEL---------GPGKYELIAFISHKGTSVHSGHYVA 272

                ...
gi 31543910 597 SVK 599
Cdd:cd02658 273 HIK 275
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
482-599 9.54e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 56.03  E-value: 9.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  482 MKTLRWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKMPEVITIHLKCFaasglEFDCYGGGLSKINTPLLTPLK 561
Cdd:COG5077  337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRF-----EYDFERDMMVKINDRYEFPLE 410
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 31543910  562 LSLEEWSTKPTNDS------YGLFAVVMHSGiTISSGHYTASVK 599
Cdd:COG5077  411 IDLLPFLDRDADKSensdavYVLYGVLVHSG-DLHEGHYYALLK 453
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
82-599 8.49e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.58  E-value: 8.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFKSgvkhlfNIISRKKEALKDEANQKDKGNckedSLASyelicSLQSLIISVeqlqa 161
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRD------YFLSDEYEESINEENPLGMHG----SVAS-----AYADLIKQL----- 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 162 sfllnpekYTDEL-ATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETcqlLKKEEVKNVAELPTKVEEIP-HP 239
Cdd:COG5560 327 --------YDGNLhAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED---LNRIIKKPYTSKPDLSPGDDvVV 395
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 240 KeemnginsiemdsmRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSkehqsleENQRQTRSKRKATSDTLESPPKIIP 319
Cdd:COG5560 396 K--------------KKAKECWWEHLKRNDSIITDLFQGMYKSTLTCP-------GCGSVSITFDPFMDLTLPLPVSMVW 454
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 320 K----YISENESPRPsqkksrVKINWLKSAT-----KQPSILSKFCSLGKITTNQGVKGQ----------------SKEN 374
Cdd:COG5560 455 KhtivVFPESGRRQP------LKIELDASSTirglkKLVDAEYGKLGCFEIKVMCIYYGGnynmlepadkvllqdiPQTD 528
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 375 EC----DPEEDLGKCESDNTTNGCGLESP--GNTVTPVNVNEVKPINKGEEQIGFELVEKLFQGQL-----VLRTRCLEC 443
Cdd:COG5560 529 FVylyeTNDNGIEVPVVHLRIEKGYKSKRlfGDPFLQLNVLIKASIYDKLVKEFEELLVLVEMKKTdvdlvSEQVRLLRE 608
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 444 ES--------LTER---REDFQDISVPVQEDE------------LSKVEESSEISPEPKTEMK----TLRWAISQFASVE 496
Cdd:COG5560 609 ESspsswlklETEIdtkREEQVEEEGQMNFNDavvisceweekrYLSLFSYDPLWTIREIGAAertiTLQDCLNEFSKPE 688
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 497 RIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFaASGLEFDcyggglSKINTPLLTP---LKLSLEEWSTKPTN 573
Cdd:COG5560 689 QLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRF-SSVRSFR------DKIDDLVEYPiddLDLSGVEYMVDDPR 761
                       570       580
                ....*....|....*....|....*.
gi 31543910 574 DSYGLFAVVMHSGITiSSGHYTASVK 599
Cdd:COG5560 762 LIYDLYAVDNHYGGL-SGGHYTAYAR 786
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
82-101 3.30e-06

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: 49.40  E-value: 3.30e-06
                        10        20
                ....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYF 101
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS 20
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-235 4.20e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 49.80  E-value: 4.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  81 VGLNNLGNTCYLNSILQvLYFCpgfksgVKHLFNII-----SRKKEALKDEANQKDKGNCKEDS--LASYELICSLQSLI 153
Cdd:cd02666   2 AGLDNIGNTCYLNSLLQ-YFFT------IKPLRDLVlnfdeSKAELASDYPTERRIGGREVSRSelQRSNQFVYELRSLF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 154 ISVEqlqasfllnpekYTDELATQPRRLLntlrelnpmyeGYLQHDAQEVLQCIlGNIQetCQLLKKEEVKNVAELPTKV 233
Cdd:cd02666  75 NDLI------------HSNTRSVTPSKEL-----------AYLALRQQDVTECI-DNVL--FQLEVALEPISNAFAGPDT 128

                ..
gi 31543910 234 EE 235
Cdd:cd02666 129 ED 130
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-156 1.36e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 47.77  E-value: 1.36e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPG----FKSGVKHLFNIISRKKEALKDeANQKDkgnckedslaSYELICSLQSLIISV 156
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPAlrelLSETPKELFSQVCRKAPQFKG-YQQQD----------SHELLRYLLDGLRTF 68
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-107 2.59e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 46.93  E-value: 2.59e-05
                        10        20
                ....*....|....*....|....*.
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFKS 107
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQW 26
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-117 4.90e-05

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 45.43  E-value: 4.90e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFksgVKHLFNIIS 117
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSL---IEYLEEFLE 33
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
429-596 1.47e-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: 44.28  E-value: 1.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 429 LFQGQLVLRTRCLECESLTERREDFQDI---SVPVQEDELSKVEESseispepktemktlrwAISQFASVERIvgeDKYF 505
Cdd:cd02662  55 PFDGLLASRIVCLQCGESSKVRYESFTMlslPVPNQSSGSGTTLEH----------------CLDDFLSTEII---DDYK 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910 506 CENChhyteaerSLLFDKMPEVITIHLkcfaaSGLEFDCYGGGL---SKINTPLLTPLKLsleewstkptndsYGLFAVV 582
Cdd:cd02662 116 CDRC--------QTVIVRLPQILCIHL-----SRSVFDGRGTSTknsCKVSFPERLPKVL-------------YRLRAVV 169
                       170
                ....*....|....
gi 31543910 583 MHSGiTISSGHYTA 596
Cdd:cd02662 170 VHYG-SHSSGHYVC 182
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-99 1.96e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 43.43  E-value: 1.96e-04
                        10
                ....*....|....*...
gi 31543910  82 GLNNLGNTCYLNSILQVL 99
Cdd:cd02674   1 GLRNLGNTCYMNSILQCL 18
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-226 2.23e-04

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 43.95  E-value: 2.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYFCPGFKSGVkHLFNIisrkkealKDEANQKdkgNCKEDSLASYELICslqsliisvEQLQA 161
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAV-YECNS--------TEDAELK---NMPPDKPHEPQTII---------DQLQL 59
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543910 162 SFLL---NPEKYTDelatqPRRLLNTLRELNPmyegyLQHDAQEVLQCILGNIQETCQLLKKEEVKNV 226
Cdd:cd02668  60 IFAQlqfGNRSVVD-----PSGFVKALGLDTG-----QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNI 117
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
82-101 1.18e-03

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 41.71  E-value: 1.18e-03
                        10        20
                ....*....|....*....|
gi 31543910  82 GLNNLGNTCYLNSILQVLYF 101
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAL 20
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
396-602 1.24e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   396 LESPGNTVTPVNVNEVKPInkgeeqigfelvEKLFQGQLVLRTRCLECESLTERREdfqdiSVPVQEDELSKVEESSEIS 475
Cdd:pfam13423 110 LSSEENSTPPNPSPAESPL------------EQLFGIDAETTIRCSNCGHESVRES-----STHVLDLIYPRKPSSNNKK 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543910   476 PEPKTemktlrwaISQF--ASVERIVGEdKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGGLskin 553
Cdd:pfam13423 173 PPNQT--------FSSIlkSSLERETTT-KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPGWL---- 239
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 31543910   554 tplltPLKLSLEEWSTKPTNDS---YGLFAVVMHSGITISSGHYTASVKVTD 602
Cdd:pfam13423 240 -----PPEIGLTLSDDLQGDNEivkYELRGVVVHIGDSGTSGHLVSFVKVAD 286
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
80-109 1.26e-03

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 42.55  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 31543910   80 FVGLNNLGNTCYLNSILQVLYFCPGFKSGV 109
Cdd:COG5077  193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDV 222
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-100 2.27e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 40.94  E-value: 2.27e-03
                        10
                ....*....|....*....
gi 31543910  82 GLNNLGNTCYLNSILQVLY 100
Cdd:cd02664   1 GLINLGNTCYMNSVLQALF 19
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
81-112 2.91e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 40.33  E-value: 2.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 31543910    81 VGLNNLGNTCYLNSILQVLYFCPGF-KSGVKHL 112
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLrNLALSHL 33
 
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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