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Conserved domains on  [gi|667667715|ref|NP_001288104|]
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ubiquitin carboxyl-terminal hydrolase 30 isoform 2 [Homo sapiens]

Protein Classification

Peptidase_C19 and Peptidase_C19F domain-containing protein( domain architecture ID 12927860)

Peptidase_C19 and Peptidase_C19F domain-containing protein

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 ...
 38-469 4.52e-84

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: 259.22  E-value: 4.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 117
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 118 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 197
Cdd:cd02662   35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 198 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 277
Cdd:cd02662   61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 278 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 357
Cdd:cd02662  120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 358 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 431
Cdd:cd02662  159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 667667715 432 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 469
Cdd:cd02662  196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
38-234 5.67e-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: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 116
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 117 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 191
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 667667715 192 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 234
Cdd:COG5560  417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
 
Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-469 4.52e-84

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: 259.22  E-value: 4.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 117
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 118 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 197
Cdd:cd02662   35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 198 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 277
Cdd:cd02662   61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 278 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 357
Cdd:cd02662  120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 358 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 431
Cdd:cd02662  159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 667667715 432 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 469
Cdd:cd02662  196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
38-468 7.91e-40

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 146.05  E-value: 7.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715   38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 117
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  118 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 197
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  198 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 273
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  274 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 353
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  354 gaptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsar 433
Cdd:pfam00443 240 ----------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY---- 278

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 667667715  434 nplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 468
Cdd:pfam00443 279 ----ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
233-470 8.56e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 51.81  E-value: 8.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 233 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 309
Cdd:COG5560  675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 310 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 389
Cdd:COG5560  739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 390 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 469
Cdd:COG5560  763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820


                 .
gi 667667715 470 R 470
Cdd:COG5560  821 R 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
38-234 5.67e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 45.64  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 116
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 117 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 191
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 667667715 192 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 234
Cdd:COG5560  417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 30-144 2.55e-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: 42.96  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  30 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 107
Cdd:cd02671   16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 667667715 108 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 144
Cdd:cd02671   83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
 
Name Accession Description Interval E-value
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-469 4.52e-84

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: 259.22  E-value: 4.52e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 117
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 118 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 197
Cdd:cd02662   35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 198 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 277
Cdd:cd02662   61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 278 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 357
Cdd:cd02662  120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 358 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 431
Cdd:cd02662  159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 667667715 432 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 469
Cdd:cd02662  196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 38-469 1.87e-46

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: 161.88  E-value: 1.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 117
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 118 myrwqissfEEQDAHELFHVITSSLEDERDRQPRVTHlfdvhsleqqseitpkqitcrtrgspHPTSNHWKSQHPFHGRL 197
Cdd:cd02257   21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRTS--------------------------DSSSLKSLIHDLFGGKL 65

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 198 TSNMVCKHCEHQSpVRFDTFDSLSLSIPAATWgHPLTLDHCLHHFISSESVRDVVCDNCTKieakgtlngekveHQRTTF 277
Cdd:cd02257   66 ESTIVCLECGHES-VSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILEGDNCYKCEK-------------KKKQEA 130

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 278 VKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPklnknpgptlelqdgpgapt 357
Cdd:cd02257  131 TKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGS-------------------- 190

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 358 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssstYLFRLMAVVVHHGD-MHSGHFVTYRRSPPsarnpl 436
Cdd:cd02257  191 ---------------------------------------------YKYELVAVVVHSGTsADSGHYVAYVKDPS------ 219

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 667667715 437 stSNQWLWVSDDTVRKASLQEVL-----SSSAYLLFYE 469
Cdd:cd02257  220 --DGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
38-468 7.91e-40

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 146.05  E-value: 7.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715   38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 117
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  118 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 197
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  198 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 273
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  274 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 353
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  354 gaptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsar 433
Cdd:pfam00443 240 ----------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY---- 278

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 667667715  434 nplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 468
Cdd:pfam00443 279 ----ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-469 1.35e-32

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 125.19  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLeeftsqysrdqKEPPSHqylsltllhllkalscqevtddevldascLLDVLR 117
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----------SETPKE-----------------------------LFSQVC 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 118 MYRWQISSFEEQDAHELFHVITSSLEDERDRQprvthlfdvhsleqqseitpkqitcrtrgsphptsnhwksqhpFHGRL 197
Cdd:cd02667   41 RKAPQFKGYQQQDSHELLRYLLDGLRTFIDSI-------------------------------------------FGGEL 77

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 198 TSNMVCKHCEHQSPVRFdTFDSLSLSIPAATWGhPLTLDHCLHHFISSESVRD---VVCDNCTKieAKgtlngekvehqr 274
Cdd:cd02667   78 TSTIMCESCGTVSLVYE-PFLDLSLPRSDEIKS-ECSIESCLKQFTEVEILEGnnkFACENCTK--AK------------ 141

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 275 ttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYhllghkpsqhnpklnknpgptlelqdgpg 354
Cdd:cd02667  142 ----KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEIL--DLAPF----------------------------- 186

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 355 aptpvlnqpgapktqifmngaCSPSllptlsapmpfplpVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRR------- 427
Cdd:cd02667  187 ---------------------CDPK--------------CNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqr 231

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 667667715 428 ------SPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 469
Cdd:cd02667  232 lsdltkSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-468 9.48e-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: 107.46  E-value: 9.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIR-WLEEFTSQYSRDQKEPPShqylsltllhllkaLSCQevTDDEVLDASCLLDV- 115
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSC--------------LSCA--MDEIFQEFYYSGDRs 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 116 ------LRMYRWQIS----SFEEQDAHELFHVITSSLEderdrqprvTHLFDVHSLEQqseiTPKQITCRTrgspHPTsn 185
Cdd:cd02660   66 pygpinLLYLSWKHSrnlaGYSQQDAHEFFQFLLDQLH---------THYGGDKNEAN----DESHCNCII----HQT-- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 186 hwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIP----------AATWGHPLTLDHCLHHFISSESVRDVV--C 253
Cdd:cd02660  127 -------FSGSLQSSVTCQRCGGVS-TTVDPFLDLSLDIPnkstpswalgESGVSGTPTLSDCLDRFTRPEKLGDFAykC 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 254 DNCtkieakgtlngekveHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYkyhllghkps 333
Cdd:cd02660  199 SGC---------------GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPY---------- 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 334 qhnpklnknpgptlelqdgpgaptpvlnqpgapktqifmngaCSPSLLPTLSAPMPfplpvvpdysSSTYLFRLMAVVVH 413
Cdd:cd02660  254 ------------------------------------------TSSSIGDTQDSNSL----------DPDYTYDLFAVVVH 281

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 667667715 414 HGDMHSGHFVTYRRsppsarnplSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFY 468
Cdd:cd02660  282 KGTLDTGHYTAYCR---------QGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-469 8.97e-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: 93.89  E-value: 8.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 117
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 118 myrwqissfEEQDAHELFhvitsslederdrqprvTHLFD-VHSLeqqseitpkqITcrtrgsphptsnhwksqHPFHGR 196
Cdd:cd02674   21 ---------DQQDAQEFL-----------------LFLLDgLHSI----------IV-----------------DLFQGQ 47

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 197 LTSNMVCKHCEHQSpVRFDTFDSLSLSIPAA-TWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKgtlngekvehqrT 275
Cdd:cd02674   48 LKSRLTCLTCGKTS-TTFEPFTYLSLPIPSGsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKK------------R 114

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 276 TFVKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRHEHVQF--NEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 353
Cdd:cd02674  115 KATKKLTISRLPKVLIIHLKRFS-FSRGSTRKLTTPVTFplNDLDLTPYV------------------------------ 163

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 354 gaptpvlnqpgapktqifmngacspsllPTLSAPMPFplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYRRSPpsar 433
Cdd:cd02674  164 ----------------------------DTRSFTGPF-------------KYDLYAVVNHYGSLNGGHYTAYCKNN---- 198

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 667667715 434 nplsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 469
Cdd:cd02674  199 ----ETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 37-468 1.09e-19

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: 89.26  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  37 PGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 116
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 117 RMYRwqissfeEQDAHELFHVITSSLE----DERDRQPRVTHLFDVHSLeqqseitpkqitcrtrgsphptsnhwkSQHP 192
Cdd:cd02661   82 RIGR-------QEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSSQETTL---------------------------VQQI 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 193 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngeK 269
Cdd:cd02661  128 FGGYLRSQVKCLNCKHVSN-TYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCKK----------K 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 270 VEHQrttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKrheHVQFNEflmmdiykyhllghkpsqhnpklnknpgpTLEL 349
Cdd:cd02661  192 VKAS-----KQLTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPE-----------------------------TLDL 234

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 350 QDgpgaptpvlnqpgapktqiFMNGACSPSLLptlsapmpfplpvvpdyssstylFRLMAVVVHHG-DMHSGHFVTYRRS 428
Cdd:cd02661  235 SP-------------------YMSQPNDGPLK-----------------------YKLYAVLVHSGfSPHSGHYYCYVKS 272

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 667667715 429 PPsarnplstsNQWLWVSDDTVRKASLQEVLSSSAYLLFY 468
Cdd:cd02661  273 SN---------GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 34-471 8.35e-17

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 81.53  E-value: 8.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  34 GLVpGLVNLGNTCFMNSLLQGLSACPAF----IRWLEEftsqysrDQKEPPSH---QYLSLTLLHLLKALSCQEVTDdev 106
Cdd:cd02659    1 GYV-GLKNQGATCYMNSLLQQLYMTPEFrnavYSIPPT-------EDDDDNKSvplALQRLFLFLQLSESPVKTTEL--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 107 ldasclLDVLRMYRWQ-ISSFEEQDAHELFHVitsslederdrqprvthLFDvhSLEQQSEITP-KQITCRTrgsphpts 184
Cdd:cd02659   70 ------TDKTRSFGWDsLNTFEQHDVQEFFRV-----------------LFD--KLEEKLKGTGqEGLIKNL-------- 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 185 nhwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAATwghplTLDHCLHHFISSEsvrdvVCDNCTKIEAKGT 264
Cdd:cd02659  117 --------FGGKLVNYIICKECPHES-EREEYFLDLQVAVKGKK-----NLEESLDAYVQGE-----TLEGDNKYFCEKC 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 265 lnGEKVEHqrttfVKQLKLGKLPQCLCIHLQRLswsshgtplkrhehvQFNeFLMMDIYKYhllghkpsqhN-----P-K 338
Cdd:cd02659  178 --GKKVDA-----EKGVCFKKLPPVLTLQLKRF---------------EFD-FETMMRIKI----------NdrfefPlE 224

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 339 LNKNP--GPTLELQDGPGAPTPvlnqpgapktqifmngacspsllptlsapmpfplpvvpdysSSTYLFRLMAVVVHHGD 416
Cdd:cd02659  225 LDMEPytEKGLAKKEGDSEKKD-----------------------------------------SESYIYELHGVLVHSGD 263

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 667667715 417 MHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL----------------------SSSAYLLFYERV 471
Cdd:cd02659  264 AHGGHYYSYIKD--------RDDGKWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-335 1.45e-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: 62.34  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPP---------------SHQYLSLTLLHLLKAlSCQEVt 102
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladgllSGRYSKPASLKSEND-PYQVG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 103 ddevLDASCLLDVLRMYRWQISSFEEQDAHELFhvitsslederdrqprvTHLFDVhsLEQQseitpkqitCRTRGSPHP 182
Cdd:cd02658   79 ----IKPSMFKALIGKGHPEFSTMRQQDALEFL-----------------LHLIDK--LDRE---------SFKNLGLNP 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 183 TSNhwksqhpFHGRLTSNMVCKHCEHqspVRFDTFDS--LSLSIPAATWGH---------PLTLDHCLHHFISSESVRDV 251
Cdd:cd02658  127 NDL-------FKFMIEDRLECLSCKK---VKYTSELSeiLSLPVPKDEATEkeegelvyePVPLEDCLKAYFAPETIEDF 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 252 VCDNCTKieakgtlngekvehqrTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYHLLG-- 329
Cdd:cd02658  197 CSTCKEK----------------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--GPGKYELIAfi 258


                 ....*...
gi 667667715 330 -HK-PSQH 335
Cdd:cd02658  259 sHKgTSVH 266
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 405-469 2.29e-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: 57.92  E-value: 2.29e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667667715 405 FRLMAVVVHHGDM-HSGHFVTYRRSppsarnpLSTSNQWLWVSDDTVRKASLQEVL---SSSAYLLFYE 469
Cdd:cd02673  184 YSLVAVICHLGESpYDGHYIAYTKE-------LYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFYD 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-469 4.21e-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: 57.70  E-value: 4.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSA-----CPAFIrwLEEFTSQYSRDQKEPPSHqylsltllhllkalscqevtddevldascL 112
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFenlltCLKDL--FESISEQKKRTGVISPKK-----------------------------F 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 113 LDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRqprvthlfdvhslEQQSEITPKQITCRTRGSPHPTsnhWKSQHp 192
Cdd:cd02663   50 ITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDA-------------ERKAEKANRKLNNNNNAEPQPT---WVHEI- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 193 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNC-TKIEAKgtlnge 268
Cdd:cd02663  113 FQGILTNETRCLTCETVSS-RDETFLDLSIDVEQNT-----SITSCLRQFSATETLCGrnkFYCDECcSLQEAE------ 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 269 kvehqrttfvKQLKLGKLPQCLCIHLQRlswsshgtplkrhehvqfneflmmdiYKYhllghkpsqhNPKLNKNpgptle 348
Cdd:cd02663  181 ----------KRMKIKKLPKILALHLKR--------------------------FKY----------DEQLNRY------ 208

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 349 lqdgpgaptpvlnqpgapktqifmngacspsllPTLSAPMPFPLPVVP-----DYSSSTYLFRLMAVVVHHGD-MHSGHF 422
Cdd:cd02663  209 ---------------------------------IKLFYRVVFPLELRLfnttdDAENPDRLYELVAVVVHIGGgPNHGHY 255

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 667667715 423 VTYRRsppsarnplsTSNQWLWVSDDTVRK---ASLQEVL-----SSSAYLLFYE 469
Cdd:cd02663  256 VSIVK----------SHGGWLLFDDETVEKideNAVEEFFgdspnQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-323 1.53e-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: 56.27  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKE-PPSHQYLSLTLLHLLKALSCQ-EVTDDEVLDASCLLDV 115
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlQFGNRSVVDPSGFVKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 116 LRmyrwqISSFEEQDAHELFHVITSSLEDErdrqprvthlfdvhsLEQQSEITPKQITcrtrgsphptsnhwksQHPFHG 195
Cdd:cd02668   81 LG-----LDTGQQQDAQEFSKLFLSLLEAK---------------LSKSKNPDLKNIV----------------QDLFRG 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 196 RLTSNMVCKHCEHQSPVRfDTFDSLSLSIPaatwGHpLTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngekveh 272
Cdd:cd02668  125 EYSYVTQCSKCGRESSLP-SKFYELELQLK----GH-KTLEECIDEFLKEEQLTGdnqYFCESCNS-------------- 184

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 667667715 273 qRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKR-HEHVQFNEFLMMDIY 323
Cdd:cd02668  185 -KTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILDMGEY 235
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-469 1.91e-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 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: 55.80  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSqySRDQKEPPSHQYLSLTLLHLLKALSCQE-VTDDEvldascLLDVL 116
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP--ARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIE------FLQLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 117 RMYRWQISSFEE------QDAHE----LFHVITSSLederdrqprvthlfdvhsleqqseitpkqitcrtrgsPHPTSNH 186
Cdd:cd02657   73 RMAFPQFAEKQNqggyaqQDAEEcwsqLLSVLSQKL-------------------------------------PGAGSKG 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 187 WKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATwgHPLTLDHCLHHFISSEsvrdvvcdnctkIEAKGTLN 266
Cdd:cd02657  116 SFIDQLFGIELETKMKCTESPDEEEVSTESEYKLQCHISITT--EVNYLQDGLKKGLEEE------------IEKHSPTL 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 267 GEKVEHQRTTFVKQlklgkLPQCLCIHLQRLSW-SSHGTPLKRHEHVQFNefLMMDIYKYhllghkpsqhnpklnknpgp 345
Cdd:cd02657  182 GRDAIYTKTSRISR-----LPKYLTVQFVRFFWkRDIQKKAKILRKVKFP--FELDLYEL-------------------- 234

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 346 tlelqdgpgaptpvlnqpgapktqifmngaCSPSllptlsapmpfplpvvpdyssstYLFRLMAVVVHHG-DMHSGHFVT 424
Cdd:cd02657  235 ------------------------------CTPS-----------------------GYYELVAVITHQGrSADSGHYVA 261

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 667667715 425 YRRSPpsarnplsTSNQWLWVSDDTVRKASLQEVL-------SSSAYLLFYE 469
Cdd:cd02657  262 WVRRK--------NDGKWIKFDDDKVSEVTEEDILklsgggdWHIAYILLYK 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
233-470 8.56e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 51.81  E-value: 8.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 233 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 309
Cdd:COG5560  675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 310 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 389
Cdd:COG5560  739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 390 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 469
Cdd:COG5560  763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820


                 .
gi 667667715 470 R 470
Cdd:COG5560  821 R 821
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
389-470 2.87e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 45.95  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 389 PFPLPVVPDYSSS---TYLFRLMAVVVHHGDMHSGHFVTYRRsppsarnplsTSNQWLWVSDDTVRKASLQEVL---SSS 462
Cdd:COG5533  206 KFELPVKHDQILNivkETYYDLVGFVLHQGSLEGGHYIAYVK----------KGGKWEKANDSDVTPVSEEEAInekAKN 275


                 ....*...
gi 667667715 463 AYLLFYER 470
Cdd:COG5533  276 AYLYFYER 283
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
38-234 5.67e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 45.64  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 116
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715 117 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 191
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 667667715 192 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 234
Cdd:COG5560  417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 30-144 2.55e-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: 42.96  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667667715  30 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 107
Cdd:cd02671   16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 667667715 108 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 144
Cdd:cd02671   83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 389-459 2.71e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 43.71  E-value: 2.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 667667715  389 PFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL 459
Cdd:COG5077   415 PFLDRDADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKP--------EKDGRWYKFDDTRVTRATEKEVL 477
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 38-63 2.73e-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: 42.86  E-value: 2.73e-04
                         10        20
                 ....*....|....*....|....*.
gi 667667715  38 GLVNLGNTCFMNSLLQGLSACPAFIR 63
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRR 26
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
38-55 4.90e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 42.10  E-value: 4.90e-04
                         10
                 ....*....|....*...
gi 667667715  38 GLVNLGNTCFMNSLLQGL 55
Cdd:COG5533    1 GLPNLGNTCFMNSVLQIL 18
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 407-469 3.16e-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: 3.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 667667715 407 LMAVVVHHG-DMHSGHFVTYRRSPPSARNPLS---TSNQWLWVSDDTVRKASLQEV------LSSSAYLLFYE 469
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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