NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|410250946|gb|JAA13440|]
View 

ubiquitin specific peptidase 30 [Pan troglodytes]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 69-500 1.03e-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: 261.92  E-value: 1.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 228
Cdd:cd02662   35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 229 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 308
Cdd:cd02662   61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 309 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 388
Cdd:cd02662  120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 389 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 462
Cdd:cd02662  159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 410250946 463 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 500
Cdd:cd02662  196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-265 4.23e-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: 46.41  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 222
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 410250946 223 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 265
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 ...
 69-500 1.03e-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: 261.92  E-value: 1.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 228
Cdd:cd02662   35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 229 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 308
Cdd:cd02662   61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 309 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 388
Cdd:cd02662  120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 389 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 462
Cdd:cd02662  159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 410250946 463 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 500
Cdd:cd02662  196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
69-499 1.83e-40

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 148.36  E-value: 1.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946   69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 148
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  149 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 228
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  229 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 304
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  305 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  385 gaptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsar 464
Cdd:pfam00443 240 ----------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY---- 278

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 410250946  465 nplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 499
Cdd:pfam00443 279 ----ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
264-501 5.71e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.19  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 264 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 340
Cdd:COG5560  675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 341 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 420
Cdd:COG5560  739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 421 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 500
Cdd:COG5560  763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820


                 .
gi 410250946 501 R 501
Cdd:COG5560  821 R 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-265 4.23e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 46.41  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 222
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 410250946 223 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 265
Cdd:COG5560  417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 61-175 1.77e-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: 43.73  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  61 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 138
Cdd:cd02671   16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 410250946 139 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 175
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 ...
 69-500 1.03e-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: 261.92  E-value: 1.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 228
Cdd:cd02662   35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 229 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 308
Cdd:cd02662   61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 309 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 388
Cdd:cd02662  120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 389 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 462
Cdd:cd02662  159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 410250946 463 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 500
Cdd:cd02662  196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 69-500 1.67e-47

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: 165.35  E-value: 1.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 149 myrwqissfEEQDAHELFHVITSSLEDERDRQPRVTHlfdvhsleqqseitpkqitcrtrgspHPTSNHWKSQHPFHGRL 228
Cdd:cd02257   21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRTS--------------------------DSSSLKSLIHDLFGGKL 65

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 229 TSNMVCKHCEHQSpVRFDTFDSLSLSIPAATWgHPLTLDHCLHHFISSESVRDVVCDNCTKieakgtlngekveHQRTTF 308
Cdd:cd02257   66 ESTIVCLECGHES-VSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILEGDNCYKCEK-------------KKKQEA 130

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 309 VKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPklnknpgptlelqdgpgapt 388
Cdd:cd02257  131 TKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGS-------------------- 190

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 389 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssstYLFRLMAVVVHHGD-MHSGHFVTYRRSPPsarnpl 467
Cdd:cd02257  191 ---------------------------------------------YKYELVAVVVHSGTsADSGHYVAYVKDPS------ 219

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 410250946 468 stSNQWLWVSDDTVRKASLQEVL-----SSSAYLLFYE 500
Cdd:cd02257  220 --DGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
69-499 1.83e-40

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 148.36  E-value: 1.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946   69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 148
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  149 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 228
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  229 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 304
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  305 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  385 gaptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsar 464
Cdd:pfam00443 240 ----------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY---- 278

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 410250946  465 nplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 499
Cdd:pfam00443 279 ----ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-500 5.15e-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: 127.12  E-value: 5.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLeeftsqysrdqKEPPSHqylsltllhllkalscqevtddevldascLLDVLR 148
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----------SETPKE-----------------------------LFSQVC 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 149 MYRWQISSFEEQDAHELFHvitsslederdrqprvtHLFDvhsleqqSEIT-PKQItcrtrgsphptsnhwksqhpFHGR 227
Cdd:cd02667   41 RKAPQFKGYQQQDSHELLR-----------------YLLD-------GLRTfIDSI--------------------FGGE 76

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 228 LTSNMVCKHCEHQSPVRFdTFDSLSLSIPAATWGhPLTLDHCLHHFISSESVRD---VVCDNCTKieAKgtlngekvehq 304
Cdd:cd02667   77 LTSTIMCESCGTVSLVYE-PFLDLSLPRSDEIKS-ECSIESCLKQFTEVEILEGnnkFACENCTK--AK----------- 141

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 305 rttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:cd02667  142 -----KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEIL--DLAPF---------------------------- 186

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 385 gaptpvlnqpgapktqifmngaCSPSllptlsapmpfplpVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRR------ 458
Cdd:cd02667  187 ----------------------CDPK--------------CNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqq 230

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 410250946 459 -------SPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 500
Cdd:cd02667  231 rlsdltkSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-499 2.37e-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: 109.38  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIR-WLEEFTSQYSRDQKEPPShqylsltllhllkaLSCQevTDDEVLDASCLLDV- 146
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSC--------------LSCA--MDEIFQEFYYSGDRs 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 147 ------LRMYRWQIS----SFEEQDAHELFHVITSSLEderdrqprvTHLFDVHSLEQqseiTPKQITCRTrgspHPTsn 216
Cdd:cd02660   66 pygpinLLYLSWKHSrnlaGYSQQDAHEFFQFLLDQLH---------THYGGDKNEAN----DESHCNCII----HQT-- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 217 hwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIP----------AATWGHPLTLDHCLHHFISSESVRDVV--C 284
Cdd:cd02660  127 -------FSGSLQSSVTCQRCGGVS-TTVDPFLDLSLDIPnkstpswalgESGVSGTPTLSDCLDRFTRPEKLGDFAykC 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 285 DNCtkieakgtlngekveHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYkyhllghkps 364
Cdd:cd02660  199 SGC---------------GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPY---------- 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 365 qhnpklnknpgptlelqdgpgaptpvlnqpgapktqifmngaCSPSLLPTLSAPMPfplpvvpdysSSTYLFRLMAVVVH 444
Cdd:cd02660  254 ------------------------------------------TSSSIGDTQDSNSL----------DPDYTYDLFAVVVH 281

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 410250946 445 HGDMHSGHFVTYRRsppsarnplSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFY 499
Cdd:cd02660  282 KGTLDTGHYTAYCR---------QGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-500 2.10e-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: 95.82  E-value: 2.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 149 myrwqissfEEQDAHELFhvitsslederdrqprvTHLFD-VHSLeqqseitpkqITcrtrgsphptsnhwksqHPFHGR 227
Cdd:cd02674   21 ---------DQQDAQEFL-----------------LFLLDgLHSI----------IV-----------------DLFQGQ 47

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 228 LTSNMVCKHCEHQSpVRFDTFDSLSLSIPAA-TWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKgtlngekvehqrT 306
Cdd:cd02674   48 LKSRLTCLTCGKTS-TTFEPFTYLSLPIPSGsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKK------------R 114

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 307 TFVKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRHEHVQF--NEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:cd02674  115 KATKKLTISRLPKVLIIHLKRFS-FSRGSTRKLTTPVTFplNDLDLTPYV------------------------------ 163

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 385 gaptpvlnqpgapktqifmngacspsllPTLSAPMPFplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYRRSPpsar 464
Cdd:cd02674  164 ----------------------------DTRSFTGPF-------------KYDLYAVVNHYGSLNGGHYTAYCKNN---- 198

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 410250946 465 nplsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 500
Cdd:cd02674  199 ----ETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 68-499 5.16e-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: 90.41  E-value: 5.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  68 PGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 148 RMYRwqissfeEQDAHELFHVITSSLE----DERDRQPRVTHLFDVHSLeqqseitpkqitcrtrgsphptsnhwkSQHP 223
Cdd:cd02661   82 RIGR-------QEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSSQETTL---------------------------VQQI 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 224 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngeK 300
Cdd:cd02661  128 FGGYLRSQVKCLNCKHVSN-TYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCKK----------K 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 301 VEHQrttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKrheHVQFNEflmmdiykyhllghkpsqhnpklnknpgpTLEL 380
Cdd:cd02661  192 VKAS-----KQLTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPE-----------------------------TLDL 234

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 381 QDgpgaptpvlnqpgapktqiFMNGACSPSLLptlsapmpfplpvvpdyssstylFRLMAVVVHHG-DMHSGHFVTYRRS 459
Cdd:cd02661  235 SP-------------------YMSQPNDGPLK-----------------------YKLYAVLVHSGfSPHSGHYYCYVKS 272

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 410250946 460 PPsarnplstsNQWLWVSDDTVRKASLQEVLSSSAYLLFY 499
Cdd:cd02661  273 SN---------GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 65-502 3.18e-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: 82.69  E-value: 3.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  65 GLVpGLVNLGNTCFMNSLLQGLSACPAF----IRWLEEftsqysrDQKEPPSH---QYLSLTLLHLLKALSCQEVTDdev 137
Cdd:cd02659    1 GYV-GLKNQGATCYMNSLLQQLYMTPEFrnavYSIPPT-------EDDDDNKSvplALQRLFLFLQLSESPVKTTEL--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 138 ldasclLDVLRMYRWQ-ISSFEEQDAHELFHVitsslederdrqprvthLFDvhSLEQQSEITP-KQITCRTrgsphpts 215
Cdd:cd02659   70 ------TDKTRSFGWDsLNTFEQHDVQEFFRV-----------------LFD--KLEEKLKGTGqEGLIKNL-------- 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 216 nhwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAATwghplTLDHCLHHFISSEsvrdvVCDNCTKIEAKGT 295
Cdd:cd02659  117 --------FGGKLVNYIICKECPHES-EREEYFLDLQVAVKGKK-----NLEESLDAYVQGE-----TLEGDNKYFCEKC 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 296 lnGEKVEHqrttfVKQLKLGKLPQCLCIHLQRLswsshgtplkrhehvQFNeFLMMDIYKYhllghkpsqhN-----P-K 369
Cdd:cd02659  178 --GKKVDA-----EKGVCFKKLPPVLTLQLKRF---------------EFD-FETMMRIKI----------NdrfefPlE 224

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 370 LNKNP--GPTLELQDGPGAPTPvlnqpgapktqifmngacspsllptlsapmpfplpvvpdysSSTYLFRLMAVVVHHGD 447
Cdd:cd02659  225 LDMEPytEKGLAKKEGDSEKKD-----------------------------------------SESYIYELHGVLVHSGD 263

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410250946 448 MHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL----------------------SSSAYLLFYERV 502
Cdd:cd02659  264 AHGGHYYSYIKD--------RDDGKWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-366 7.09e-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: 63.50  E-value: 7.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPP---------------SHQYLSLTLLHLLKAlSCQEVt 133
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladgllSGRYSKPASLKSEND-PYQVG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 134 ddevLDASCLLDVLRMYRWQISSFEEQDAHELFhvitsslederdrqprvTHLFDVhsLEQQseitpkqitCRTRGSPHP 213
Cdd:cd02658   79 ----IKPSMFKALIGKGHPEFSTMRQQDALEFL-----------------LHLIDK--LDRE---------SFKNLGLNP 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 214 TSNhwksqhpFHGRLTSNMVCKHCEHqspVRFDTFDS--LSLSIPAATWGH---------PLTLDHCLHHFISSESVRDV 282
Cdd:cd02658  127 NDL-------FKFMIEDRLECLSCKK---VKYTSELSeiLSLPVPKDEATEkeegelvyePVPLEDCLKAYFAPETIEDF 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 283 VCDNCTKieakgtlngekvehqrTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYHLLG-- 360
Cdd:cd02658  197 CSTCKEK----------------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--GPGKYELIAfi 258


                 ....*...
gi 410250946 361 -HK-PSQH 366
Cdd:cd02658  259 sHKgTSVH 266
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-500 1.54e-09

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 59.25  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSA-----CPAFIrwLEEFTSQYSRDQKEPPSHqylsltllhllkalscqevtddevldascL 143
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFenlltCLKDL--FESISEQKKRTGVISPKK-----------------------------F 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 144 LDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRqprvthlfdvhslEQQSEITPKQITCRTRGSPHPTsnhWKSQHp 223
Cdd:cd02663   50 ITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDA-------------ERKAEKANRKLNNNNNAEPQPT---WVHEI- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 224 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNC-TKIEAKgtlnge 299
Cdd:cd02663  113 FQGILTNETRCLTCETVSS-RDETFLDLSIDVEQNT-----SITSCLRQFSATETLCGrnkFYCDECcSLQEAE------ 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 300 kvehqrttfvKQLKLGKLPQCLCIHLQRlswsshgtplkrhehvqfneflmmdiYKYhllghkpsqhNPKLNKNpgptle 379
Cdd:cd02663  181 ----------KRMKIKKLPKILALHLKR--------------------------FKY----------DEQLNRY------ 208

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 380 lqdgpgaptpvlnqpgapktqifmngacspsllPTLSAPMPFPL-----PVVPDYSSSTYLFRLMAVVVHHGD-MHSGHF 453
Cdd:cd02663  209 ---------------------------------IKLFYRVVFPLelrlfNTTDDAENPDRLYELVAVVVHIGGgPNHGHY 255

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 410250946 454 VTYRRsppsarnplsTSNQWLWVSDDTVRK---ASLQEVL-----SSSAYLLFYE 500
Cdd:cd02663  256 VSIVK----------SHGGWLLFDDETVEKideNAVEEFFgdspnQATAYVLFYQ 300
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 436-500 1.76e-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: 1.76e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410250946 436 FRLMAVVVHHGDM-HSGHFVTYRRSppsarnpLSTSNQWLWVSDDTVRKASLQEVL---SSSAYLLFYE 500
Cdd:cd02673  184 YSLVAVICHLGESpYDGHYIAYTKE-------LYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFYD 245
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-354 9.07e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 57.05  E-value: 9.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKE-PPSHQYLSLTLLHLLKALSCQ-EVTDDEVLDASCLLDV 146
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlQFGNRSVVDPSGFVKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 147 LRmyrwqISSFEEQDAHELFHVITSSLEDErdrqprvthlfdvhsLEQQSEITPKQITcrtrgsphptsnhwksQHPFHG 226
Cdd:cd02668   81 LG-----LDTGQQQDAQEFSKLFLSLLEAK---------------LSKSKNPDLKNIV----------------QDLFRG 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 227 RLTSNMVCKHCEHQSPVRfDTFDSLSLSIPaatwGHpLTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngekveh 303
Cdd:cd02668  125 EYSYVTQCSKCGRESSLP-SKFYELELQLK----GH-KTLEECIDEFLKEEQLTGdnqYFCESCNS-------------- 184

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 410250946 304 qRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKR-HEHVQFNEFLMMDIY 354
Cdd:cd02668  185 -KTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILDMGEY 235
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-500 1.37e-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: 56.19  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSqySRDQKEPPSHQYLSLTLLHLLKALSCQE-VTDDEvldascLLDVL 147
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP--ARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIE------FLQLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 148 RMYRWQISSFEE------QDAHE----LFHVITSSLederdrqprvthlfdvhsleqqseitpkqitcrtrgsPHPTSNH 217
Cdd:cd02657   73 RMAFPQFAEKQNqggyaqQDAEEcwsqLLSVLSQKL-------------------------------------PGAGSKG 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 218 WKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATwgHPLTLDHCLHHFISSEsvrdvvcdnctkIEAKGTLN 297
Cdd:cd02657  116 SFIDQLFGIELETKMKCTESPDEEEVSTESEYKLQCHISITT--EVNYLQDGLKKGLEEE------------IEKHSPTL 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 298 GEKVEHQRTTFVKQlklgkLPQCLCIHLQRLSW-SSHGTPLKRHEHVQFNefLMMDIYKYhllghkpsqhnpklnknpgp 376
Cdd:cd02657  182 GRDAIYTKTSRISR-----LPKYLTVQFVRFFWkRDIQKKAKILRKVKFP--FELDLYEL-------------------- 234

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 377 tlelqdgpgaptpvlnqpgapktqifmngaCSPSllptlsapmpfplpvvpdyssstYLFRLMAVVVHHG-DMHSGHFVT 455
Cdd:cd02657  235 ------------------------------CTPS-----------------------GYYELVAVITHQGrSADSGHYVA 261

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 410250946 456 YRRSPpsarnplsTSNQWLWVSDDTVRKASLQEVL-------SSSAYLLFYE 500
Cdd:cd02657  262 WVRRK--------NDGKWIKFDDDKVSEVTEEDILklsgggdWHIAYILLYK 305
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
264-501 5.71e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 52.19  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 264 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 340
Cdd:COG5560  675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 341 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 420
Cdd:COG5560  739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 421 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 500
Cdd:COG5560  763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820


                 .
gi 410250946 501 R 501
Cdd:COG5560  821 R 821
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
420-501 3.14e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 45.95  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 420 PFPLPVVPDYSSS---TYLFRLMAVVVHHGDMHSGHFVTYRRsppsarnplsTSNQWLWVSDDTVRKASLQEVL---SSS 493
Cdd:COG5533  206 KFELPVKHDQILNivkETYYDLVGFVLHQGSLEGGHYIAYVK----------KGGKWEKANDSDVTPVSEEEAInekAKN 275


                 ....*...
gi 410250946 494 AYLLFYER 501
Cdd:COG5533  276 AYLYFYER 283
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-265 4.23e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 46.41  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 222
Cdd:COG5560  344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 410250946 223 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 265
Cdd:COG5560  417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 61-175 1.77e-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: 43.73  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410250946  61 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 138
Cdd:cd02671   16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 410250946 139 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 175
Cdd:cd02671   83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 420-490 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 410250946  420 PFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL 490
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 410250946  69 GLVNLGNTCFMNSLLQGLSACPAFIR 94
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRR 26
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-86 5.33e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 42.10  E-value: 5.33e-04
                         10
                 ....*....|....*...
gi 410250946  69 GLVNLGNTCFMNSLLQGL 86
Cdd:COG5533    1 GLPNLGNTCFMNSVLQIL 18
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 438-500 2.73e-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: 2.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410250946 438 LMAVVVHHG-DMHSGHFVTYRRSPPSARNPLS---TSNQWLWVSDDTVRKASLQEV------LSSSAYLLFYE 500
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH