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Conserved domains on  [gi|530401476|ref|XP_005254019|]
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ubiquitin carboxyl-terminal hydrolase 30 isoform X4 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12927860)

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_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 6.88e-85

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: 262.30  E-value: 6.88e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqseitpkqitcrtrgsphptsnhWKSQHPFHGRLT 228
Cdd:cd02662   35 -----------QDAHELFQVLLETLE------------------------------------------QLLKFPFDGLLA 61

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 229 SNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttfv 308
Cdd:cd02662   62 SRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC---------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 309 kQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptp 388
Cdd:cd02662  120 -QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL---------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 389 vlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------- 461
Cdd:cd02662  159 ------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepg 196

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 530401476 462 -----ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 499
Cdd:cd02662  197 sfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-264 7.26e-05

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 45.64  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQseitpkQITCRTRGSPHPTSNHWKSQHP 222
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVV------KKKAKECWWEHLKRNDSIITDL 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530401476 223 FHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 264
Cdd:COG5560  418 FQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
 
Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 6.88e-85

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: 262.30  E-value: 6.88e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqseitpkqitcrtrgsphptsnhWKSQHPFHGRLT 228
Cdd:cd02662   35 -----------QDAHELFQVLLETLE------------------------------------------QLLKFPFDGLLA 61

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 229 SNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttfv 308
Cdd:cd02662   62 SRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC---------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 309 kQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptp 388
Cdd:cd02662  120 -QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL---------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 389 vlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------- 461
Cdd:cd02662  159 ------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepg 196

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 530401476 462 -----ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 499
Cdd:cd02662  197 sfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
69-498 1.42e-39

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 145.66  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476   69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 148
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  149 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQsEITPKQItcrtrgsphptsnhwksqhpFHGRLT 228
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTEN-ESLITDL--------------------FRGQLK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  229 SNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQR 304
Cdd:pfam00443 128 SRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQD 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  305 TTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgpg 384
Cdd:pfam00443 194 AI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------- 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  385 aptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsarn 464
Cdd:pfam00443 240 ---------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY----- 278

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 530401476  465 plsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 498
Cdd:pfam00443 279 ---ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
263-500 5.69e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.19  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 263 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 339
Cdd:COG5560  675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 340 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 419
Cdd:COG5560  739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 420 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:COG5560  763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820


                 .
gi 530401476 500 R 500
Cdd:COG5560  821 R 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-264 7.26e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 45.64  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQseitpkQITCRTRGSPHPTSNHWKSQHP 222
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVV------KKKAKECWWEHLKRNDSIITDL 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530401476 223 FHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 264
Cdd:COG5560  418 FQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
 
Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 6.88e-85

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: 262.30  E-value: 6.88e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqseitpkqitcrtrgsphptsnhWKSQHPFHGRLT 228
Cdd:cd02662   35 -----------QDAHELFQVLLETLE------------------------------------------QLLKFPFDGLLA 61

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 229 SNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttfv 308
Cdd:cd02662   62 SRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC---------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 309 kQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptp 388
Cdd:cd02662  120 -QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL---------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 389 vlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------- 461
Cdd:cd02662  159 ------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepg 196

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 530401476 462 -----ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 499
Cdd:cd02662  197 sfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 69-499 8.94e-48

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: 166.12  E-value: 8.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 149 myrwqissfEEQDAHELFHVITSSLEDERDRQPRVThlfDVHSLEQSEItpkqitcrtrgsphptsnhwksQHPFHGRLT 228
Cdd:cd02257   21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRT---SDSSSLKSLI----------------------HDLFGGKLE 66

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 229 SNMVCKHCEHQSpVRFDTFDSLSLSIPAATWgHPLTLDHCLHHFISSESVRDVVCDNCTKieakgtlngekveHQRTTFV 308
Cdd:cd02257   67 STIVCLECGHES-VSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILEGDNCYKCEK-------------KKKQEAT 131

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 309 KQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPklnknpgptlelqdgpgaptp 388
Cdd:cd02257  132 KRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGS--------------------- 190

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 389 vlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssstYLFRLMAVVVHHGD-MHSGHFVTYRRSPPsarnpls 467
Cdd:cd02257  191 --------------------------------------------YKYELVAVVVHSGTsADSGHYVAYVKDPS------- 219

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 530401476 468 tSNQWLWVSDDTVRKASLQEVL-----SSSAYLLFYE 499
Cdd:cd02257  220 -DGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
69-498 1.42e-39

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 145.66  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476   69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 148
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  149 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQsEITPKQItcrtrgsphptsnhwksqhpFHGRLT 228
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTEN-ESLITDL--------------------FRGQLK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  229 SNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQR 304
Cdd:pfam00443 128 SRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQD 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  305 TTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgpg 384
Cdd:pfam00443 194 AI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------- 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  385 aptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsarn 464
Cdd:pfam00443 240 ---------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY----- 278

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 530401476  465 plsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 498
Cdd:pfam00443 279 ---ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 3.65e-33

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: 127.50  E-value: 3.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLeeftsqysrdqKEPPSHqylsltllhllkalscqevtddevldascLLDVLR 148
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----------SETPKE-----------------------------LFSQVC 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 149 MYRWQISSFEEQDAHELFHvitsslederdrqprvtHLFDvhsleqSEIT-PKQItcrtrgsphptsnhwksqhpFHGRL 227
Cdd:cd02667   41 RKAPQFKGYQQQDSHELLR-----------------YLLD------GLRTfIDSI--------------------FGGEL 77

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 228 TSNMVCKHCEHQSPVRFdTFDSLSLSIPAATWGhPLTLDHCLHHFISSESVRD---VVCDNCTKieAKgtlngekvehqr 304
Cdd:cd02667   78 TSTIMCESCGTVSLVYE-PFLDLSLPRSDEIKS-ECSIESCLKQFTEVEILEGnnkFACENCTK--AK------------ 141

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 305 ttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYhllghkpsqhnpklnknpgptlelqdgpg 384
Cdd:cd02667  142 ----KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEIL--DLAPF----------------------------- 186

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 385 aptpvlnqpgapktqifmngaCSPSllptlsapmpfplpVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRR------- 457
Cdd:cd02667  187 ---------------------CDPK--------------CNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqr 231

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 530401476 458 ------SPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:cd02667  232 lsdltkSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-498 1.42e-26

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 110.15  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIR-WLEEFTSQYSRDQKEPPShqylsltllhllkaLSCQevTDDEVLDASCLLDV- 146
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSC--------------LSCA--MDEIFQEFYYSGDRs 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 147 ------LRMYRWQIS----SFEEQDAHELFHVITSSLEderdrqprvTHLFDVHSLEQSEitpKQITCRTrgspHPTsnh 216
Cdd:cd02660   66 pygpinLLYLSWKHSrnlaGYSQQDAHEFFQFLLDQLH---------THYGGDKNEANDE---SHCNCII----HQT--- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 217 wksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIP----------AATWGHPLTLDHCLHHFISSESVRDVV--CD 284
Cdd:cd02660  127 ------FSGSLQSSVTCQRCGGVS-TTVDPFLDLSLDIPnkstpswalgESGVSGTPTLSDCLDRFTRPEKLGDFAykCS 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 285 NCtkieakgtlngekveHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYkyhllghkpsq 364
Cdd:cd02660  200 GC---------------GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPY----------- 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 365 hnpklnknpgptlelqdgpgaptpvlnqpgapktqifmngaCSPSLLPTLSAPMPfplpvvpdysSSTYLFRLMAVVVHH 444
Cdd:cd02660  254 -----------------------------------------TSSSIGDTQDSNSL----------DPDYTYDLFAVVVHK 282

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530401476 445 GDMHSGHFVTYRRsppsarnplSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFY 498
Cdd:cd02660  283 GTLDTGHYTAYCR---------QGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 1.49e-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: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 149 myrwqissfEEQDAHELFhvitsslederdrqprvTHLFD-VHSLeqseitpkqITcrtrgsphptsnhwksqHPFHGRL 227
Cdd:cd02674   21 ---------DQQDAQEFL-----------------LFLLDgLHSI---------IV-----------------DLFQGQL 48

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 228 TSNMVCKHCEHQSpVRFDTFDSLSLSIPAA-TWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKgtlngekvehqrTT 306
Cdd:cd02674   49 KSRLTCLTCGKTS-TTFEPFTYLSLPIPSGsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKK------------RK 115

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 307 FVKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRHEHVQF--NEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgpg 384
Cdd:cd02674  116 ATKKLTISRLPKVLIIHLKRFS-FSRGSTRKLTTPVTFplNDLDLTPYV------------------------------- 163

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 385 aptpvlnqpgapktqifmngacspsllPTLSAPMPFplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYRRSPpsarn 464
Cdd:cd02674  164 ---------------------------DTRSFTGPF-------------KYDLYAVVNHYGSLNGGHYTAYCKNN----- 198

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 530401476 465 plsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:cd02674  199 ---ETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 68-498 3.76e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 90.80  E-value: 3.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  68 PGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 148 RMYRwqissfeEQDAHELFHVITSSLE----DERDRQPRVTHLFDVHSLeqseitpkqitcrtrgsphptsnhwkSQHPF 223
Cdd:cd02661   82 RIGR-------QEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSSQETTL--------------------------VQQIF 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 224 HGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngeKV 300
Cdd:cd02661  129 GGYLRSQVKCLNCKHVSN-TYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCKK----------KV 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 301 EHQrttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKrheHVQFNEflmmdiykyhllghkpsqhnpklnknpgpTLELQ 380
Cdd:cd02661  193 KAS-----KQLTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPE-----------------------------TLDLS 235

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 381 DgpgaptpvlnqpgapktqiFMNGACSPSLLptlsapmpfplpvvpdyssstylFRLMAVVVHHG-DMHSGHFVTYRRSP 459
Cdd:cd02661  236 P-------------------YMSQPNDGPLK-----------------------YKLYAVLVHSGfSPHSGHYYCYVKSS 273

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 530401476 460 PsarnplstsNQWLWVSDDTVRKASLQEVLSSSAYLLFY 498
Cdd:cd02661  274 N---------GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 65-501 2.81e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 79.99  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  65 GLVpGLVNLGNTCFMNSLLQGLSACPAF----IRWLEEftsqysrDQKEPPSH---QYLSLTLLHLLKALSCQEVTDdev 137
Cdd:cd02659    1 GYV-GLKNQGATCYMNSLLQQLYMTPEFrnavYSIPPT-------EDDDDNKSvplALQRLFLFLQLSESPVKTTEL--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 138 ldasclLDVLRMYRWQ-ISSFEEQDAHELFHVitsslederdrqprvthLFDvhSLEQSeitpkqitcrTRGSPHPTSnh 216
Cdd:cd02659   70 ------TDKTRSFGWDsLNTFEQHDVQEFFRV-----------------LFD--KLEEK----------LKGTGQEGL-- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 217 wkSQHPFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAATwghplTLDHCLHHFISSEsvrdvVCDNCTKIEAKGTln 296
Cdd:cd02659  113 --IKNLFGGKLVNYIICKECPHES-EREEYFLDLQVAVKGKK-----NLEESLDAYVQGE-----TLEGDNKYFCEKC-- 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 297 GEKVEHqrttfVKQLKLGKLPQCLCIHLQRLswsshgtplkrhehvQFNeFLMMDIYKYhllghkpsqhN-----P-KLN 370
Cdd:cd02659  178 GKKVDA-----EKGVCFKKLPPVLTLQLKRF---------------EFD-FETMMRIKI----------NdrfefPlELD 226

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 371 KNP--GPTLELQDGPGAPTPvlnqpgapktqifmngacspsllptlsapmpfplpvvpdysSSTYLFRLMAVVVHHGDMH 448
Cdd:cd02659  227 MEPytEKGLAKKEGDSEKKD-----------------------------------------SESYIYELHGVLVHSGDAH 265

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530401476 449 SGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL----------------------SSSAYLLFYERV 501
Cdd:cd02659  266 GGHYYSYIKD--------RDDGKWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-365 2.43e-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 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: 64.65  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPP---------------SHQYLSLTLLHLLKAlSCQEVt 133
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladgllSGRYSKPASLKSEND-PYQVG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 134 ddevLDASCLLDVLRMYRWQISSFEEQDAHELFhvitsslederdrqprvTHLFDVhsLEQSeitpkqitCRTRGSPHPT 213
Cdd:cd02658   79 ----IKPSMFKALIGKGHPEFSTMRQQDALEFL-----------------LHLIDK--LDRE--------SFKNLGLNPN 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 214 SNhwksqhpFHGRLTSNMVCKHCEHqspVRFDTFDS--LSLSIPAATWGH---------PLTLDHCLHHFISSESVRDVV 282
Cdd:cd02658  128 DL-------FKFMIEDRLECLSCKK---VKYTSELSeiLSLPVPKDEATEkeegelvyePVPLEDCLKAYFAPETIEDFC 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 283 CDNCTKieakgtlngekvehqrTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYHLLG--- 359
Cdd:cd02658  198 STCKEK----------------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--GPGKYELIAfis 259


                 ....*..
gi 530401476 360 HK-PSQH 365
Cdd:cd02658  260 HKgTSVH 266
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 435-499 1.77e-09

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 58.31  E-value: 1.77e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530401476 435 FRLMAVVVHHGDM-HSGHFVTYRRSppsarnpLSTSNQWLWVSDDTVRKASLQEVL---SSSAYLLFYE 499
Cdd:cd02673  184 YSLVAVICHLGESpYDGHYIAYTKE-------LYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFYD 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 5.79e-09

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 57.32  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSA-----CPAFIrwLEEFTSQYSRDQKEPPSHqylsltllhllkalscqevtddevldascL 143
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFenlltCLKDL--FESISEQKKRTGVISPKK-----------------------------F 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 144 LDVLRMYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthlfdvhsLEQSEITPKQITCRTRGSPHPTSNHWKSQHpF 223
Cdd:cd02663   50 ITRLKRENELFDNYMHQDAHEFLNFLLNEIAEI---------------LDAERKAEKANRKLNNNNNAEPQPTWVHEI-F 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 224 HGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNC-TKIEAKgtlngek 299
Cdd:cd02663  114 QGILTNETRCLTCETVSS-RDETFLDLSIDVEQNT-----SITSCLRQFSATETLCGrnkFYCDECcSLQEAE------- 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 300 vehqrttfvKQLKLGKLPQCLCIHLQRlswsshgtplkrhehvqfneflmmdiYKYhllghkpsqhNPKLNKNpgptlel 379
Cdd:cd02663  181 ---------KRMKIKKLPKILALHLKR--------------------------FKY----------DEQLNRY------- 208

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 380 qdgpgaptpvlnqpgapktqifmngacspsllPTLSAPMPFPL-----PVVPDYSSSTYLFRLMAVVVHHGD-MHSGHFV 453
Cdd:cd02663  209 --------------------------------IKLFYRVVFPLelrlfNTTDDAENPDRLYELVAVVVHIGGgPNHGHYV 256

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530401476 454 TYRRsppsarnplsTSNQWLWVSDDTVRK---ASLQEVL-----SSSAYLLFYE 499
Cdd:cd02663  257 SIVK----------SHGGWLLFDDETVEKideNAVEEFFgdspnQATAYVLFYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 6.24e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 57.34  E-value: 6.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSqySRDQKEPPSHQYLSLTLLHLLKALSCQE-VTDDEvldascLLDVL 147
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP--ARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIE------FLQLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 148 RMYRWQISSFEE------QDAHELFHVITSSLEderdrqprvthlfdvHSLEQSEITPKQITCRtrgsphptsnhwksqh 221
Cdd:cd02657   73 RMAFPQFAEKQNqggyaqQDAEECWSQLLSVLS---------------QKLPGAGSKGSFIDQL---------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 222 pFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATwgHPLTLDHCLHHFISSEsvrdvvcdnctkIEAKGTLNGEKVE 301
Cdd:cd02657  122 -FGIELETKMKCTESPDEEEVSTESEYKLQCHISITT--EVNYLQDGLKKGLEEE------------IEKHSPTLGRDAI 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 302 HQRTTFVKQlklgkLPQCLCIHLQRLSW-SSHGTPLKRHEHVQFNefLMMDIYKYhllghkpsqhnpklnknpgptlelq 380
Cdd:cd02657  187 YTKTSRISR-----LPKYLTVQFVRFFWkRDIQKKAKILRKVKFP--FELDLYEL------------------------- 234

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 381 dgpgaptpvlnqpgapktqifmngaCSPSllptlsapmpfplpvvpdyssstYLFRLMAVVVHHG-DMHSGHFVTYRRSP 459
Cdd:cd02657  235 -------------------------CTPS-----------------------GYYELVAVITHQGrSADSGHYVAWVRRK 266

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 530401476 460 psarnplsTSNQWLWVSDDTVRKASLQEVL-------SSSAYLLFYE 499
Cdd:cd02657  267 --------NDGKWIKFDDDKVSEVTEEDILklsgggdWHIAYILLYK 305
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-353 6.87e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 54.35  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKE-PPSHQYLSLTLLHLLKALSCQ-EVTDDEVLDASCLLDV 146
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlQFGNRSVVDPSGFVKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 147 LRmyrwqISSFEEQDAHELFHVITSSLEDERDRQPRVthlfdvhslEQSEITPKQitcrtrgsphptsnhwksqhpFHGR 226
Cdd:cd02668   81 LG-----LDTGQQQDAQEFSKLFLSLLEAKLSKSKNP---------DLKNIVQDL---------------------FRGE 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 227 LTSNMVCKHCEHQSPVRfDTFDSLSLSIPaatwGHpLTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngekvehq 303
Cdd:cd02668  126 YSYVTQCSKCGRESSLP-SKFYELELQLK----GH-KTLEECIDEFLKEEQLTGdnqYFCESCNS--------------- 184

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530401476 304 RTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKR-HEHVQFNEFLMMDIY 353
Cdd:cd02668  185 KTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILDMGEY 235
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
263-500 5.69e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.19  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 263 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 339
Cdd:COG5560  675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 340 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 419
Cdd:COG5560  739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 420 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 499
Cdd:COG5560  763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820


                 .
gi 530401476 500 R 500
Cdd:COG5560  821 R 821
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
419-500 3.13e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 45.95  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 419 PFPLPVVPDYSSS---TYLFRLMAVVVHHGDMHSGHFVTYRRsppsarnplsTSNQWLWVSDDTVRKASLQEVL---SSS 492
Cdd:COG5533  206 KFELPVKHDQILNivkETYYDLVGFVLHQGSLEGGHYIAYVK----------KGGKWEKANDSDVTPVSEEEAInekAKN 275


                 ....*...
gi 530401476 493 AYLLFYER 500
Cdd:COG5533  276 AYLYFYER 283
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-264 7.26e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 45.64  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQseitpkQITCRTRGSPHPTSNHWKSQHP 222
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVV------KKKAKECWWEHLKRNDSIITDL 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530401476 223 FHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 264
Cdd:COG5560  418 FQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 61-498 1.26e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 44.11  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476  61 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 138
Cdd:cd02671   16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 139 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED--ERDrqprvthlfdvhsleqseitpkqitcrtrgsphpts 214
Cdd:cd02671   83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQElvEKD------------------------------------ 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 215 nhwksqhpFHGRLTSNMVCKHCEHQSPVRFDTFDslsLSIPAATWGHPL----------------TLDHCLHHFISSESV 278
Cdd:cd02671  127 --------FQGQLVLRTRCLECETFTERREDFQD---ISVPVQESELSKseesseispdpktemkTLKWAISQFASVERI 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 279 R---DVVCDNCtkieakgtlngekveHQRTTFVKQLKLGKLPQCLCIHLQRLSWSShgtplkrhehvqfneflmmdiyky 355
Cdd:cd02671  196 VgedKYFCENC---------------HHYTEAERSLLFDKLPEVITIHLKCFAANG------------------------ 236

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401476 356 hllghkpsqhnpklnknpgptleLQDGPGAPTPVLNQPgapktqifmngacspslLPTlsapmPFPLPVVPDYSSST-YL 434
Cdd:cd02671  237 -----------------------SEFDCYGGLSKVNTP-----------------LLT-----PLKLSLEEWSTKPKnDV 271

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530401476 435 FRLMAVVVHHG-DMHSGHFVTYRRsppsarnplstsnqWLWVSDDTVR---KASLQEVLS------SSAYLLFY 498
Cdd:cd02671  272 YRLFAVVMHSGaTISSGHYTAYVR--------------WLLFDDSEVKvteEKDFLEALSpntsstSTPYLLFY 331
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 419-489 2.52e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 44.09  E-value: 2.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530401476  419 PFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL 489
Cdd:COG5077   415 PFLDRDADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKP--------EKDGRWYKFDDTRVTRATEKEVL 477
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-94 2.58e-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: 2.58e-04
                         10        20
                 ....*....|....*....|....*.
gi 530401476  69 GLVNLGNTCFMNSLLQGLSACPAFIR 94
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRR 26
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-86 5.32e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 42.10  E-value: 5.32e-04
                         10
                 ....*....|....*...
gi 530401476  69 GLVNLGNTCFMNSLLQGL 86
Cdd:COG5533    1 GLPNLGNTCFMNSVLQIL 18
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 437-499 2.72e-03

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 39.43  E-value: 2.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530401476 437 LMAVVVHHG-DMHSGHFVTYRRSPPSARNPLS---TSNQWLWVSDDTVRKASLQEV------LSSSAYLLFYE 499
Cdd:cd02670  169 LCSAVCHRGtSLETGHYVAFVRYGSYSLTETDneaYNAQWVFFDDMADRDGVSNGFnipaarLLEDPYMLFYQ 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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