NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462535088|ref|XP_054229537|]
View 

ubiquitin carboxyl-terminal hydrolase 30 isoform X1 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12927860)

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

Graphical summary

 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 ...
 69-537 1.22e-79

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: 249.98  E-value: 1.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 228
Cdd:cd02662    35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 229 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 308
Cdd:cd02662    61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 309 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 388
Cdd:cd02662   120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 389 pgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyss 468
Cdd:cd02662       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 469 STYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLF 535
Cdd:cd02662   159 PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLF 238


                  ..
gi 2462535088 536 YE 537
Cdd:cd02662   239 YE 240
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-265 2.78e-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: 47.19  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 222
Cdd:COG5560   344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462535088 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 ...
 69-537 1.22e-79

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: 249.98  E-value: 1.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 228
Cdd:cd02662    35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 229 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 308
Cdd:cd02662    61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 309 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 388
Cdd:cd02662   120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 389 pgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyss 468
Cdd:cd02662       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 469 STYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLF 535
Cdd:cd02662   159 PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLF 238


                  ..
gi 2462535088 536 YE 537
Cdd:cd02662   239 YE 240
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
69-536 6.85e-36

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 136.42  E-value: 6.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 148
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 228
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 229 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 304
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 305 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 385 gaptpgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVP 464
Cdd:pfam00443 240 -----------------------------------------------------------LAEELKP--------KTNNLQ 252

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535088 465 DYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsarnplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 536
Cdd:pfam00443 253 DY-------RLVAVVVHSGSLSSGHYIAYIKAY--------ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
466-538 8.27e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 51.81  E-value: 8.27e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535088 466 YSSSTYLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYER 538
Cdd:COG5560   757 VDDPRLIYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-265 2.78e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 47.19  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 222
Cdd:COG5560   344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462535088 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 1.63e-04

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 44.11  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  61 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 138
Cdd:cd02671    16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462535088 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 ...
 69-537 1.22e-79

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: 249.98  E-value: 1.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 228
Cdd:cd02662    35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 229 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 308
Cdd:cd02662    61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 309 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 388
Cdd:cd02662   120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 389 pgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyss 468
Cdd:cd02662       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 469 STYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLF 535
Cdd:cd02662   159 PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkepgsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLF 238


                  ..
gi 2462535088 536 YE 537
Cdd:cd02662   239 YE 240
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 69-537 6.33e-43

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: 153.79  E-value: 6.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSacpafirwleeftsqysrdqkeppSHQylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALF------------------------SEQ---------------------------------- 22

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 myrwqissfeeQDAHELFHVITSSLEDERDRQPRVTHlfdvhsleqqseitpkqitcrtrgspHPTSNHWKSQHPFHGRL 228
Cdd:cd02257    23 -----------QDAHEFLLFLLDKLHEELKKSSKRTS--------------------------DSSSLKSLIHDLFGGKL 65

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 229 TSNMVCKHCEHQSpVRFDTFDSLSLSIPAATWgHPLTLDHCLHHFISSESVRDVVCDNCTKieakgtlngekveHQRTTF 308
Cdd:cd02257    66 ESTIVCLECGHES-VSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILEGDNCYKCEK-------------KKKQEA 130

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 309 VKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPklnknpgptlelqdgpgapt 388
Cdd:cd02257   131 TKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGS-------------------- 190

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 389 pgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyss 468
Cdd:cd02257       --------------------------------------------------------------------------------

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535088 469 stYLFRLMAVVVHHGD-MHSGHFVTYRRSPPsarnplstSNQWLWVSDDTVRKASLQEVL-----SSSAYLLFYE 537
Cdd:cd02257   191 --YKYELVAVVVHSGTsADSGHYVAYVKDPS--------DGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
69-536 6.85e-36

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 136.42  E-value: 6.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 148
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 228
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 229 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 304
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 305 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 385 gaptpgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVP 464
Cdd:pfam00443 240 -----------------------------------------------------------LAEELKP--------KTNNLQ 252

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535088 465 DYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsarnplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 536
Cdd:pfam00443 253 DY-------RLVAVVVHSGSLSSGHYIAYIKAY--------ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-537 3.17e-28

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: 114.02  E-value: 3.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLeeftsqysrdqKEPPSHqylsltllhllkalscqevtddevldascLLDVLR 148
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----------SETPKE-----------------------------LFSQVC 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 MYRWQISSFEEQDAHELFHvitsslederdrqprvtHLFDvhsleqqSEIT-PKQItcrtrgsphptsnhwksqhpFHGR 227
Cdd:cd02667    41 RKAPQFKGYQQQDSHELLR-----------------YLLD-------GLRTfIDSI--------------------FGGE 76

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 228 LTSNMVCKHCEHQSPVRFdTFDSLSLSIPAATWGhPLTLDHCLHHFISSESVRD---VVCDNCTKieAKgtlngekvehq 304
Cdd:cd02667    77 LTSTIMCESCGTVSLVYE-PFLDLSLPRSDEIKS-ECSIESCLKQFTEVEILEGnnkFACENCTK--AK----------- 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 305 rttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYhllghkpsqhnpklnknpgptlelqdgp 384
Cdd:cd02667   142 -----KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEIL--DLAPF---------------------------- 186

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 385 gaptpgvCArgadaagifsteksslasppsgslmtgaqglynvlnqpgaPKTQIfmngacspsllptlsapmpfplpvvp 464
Cdd:cd02667   187 -------CD----------------------------------------PKCNS-------------------------- 193

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 465 DYSSSTYLFRLMAVVVHHGDMHSGHFVTYRR-------------SPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSA 531
Cdd:cd02667   194 SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEA 273


                  ....*.
gi 2462535088 532 YLLFYE 537
Cdd:cd02667   274 YLLFYE 279
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-536 8.93e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 96.29  E-value: 8.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIR-WLEEFTSQYSRDQKEPPShqylsltllhllkaLSCQevTDDEVLDASCLLDV- 146
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSC--------------LSCA--MDEIFQEFYYSGDRs 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 147 ------LRMYRWQIS----SFEEQDAHELFHVITSSLEderdrqprvTHLFDVHSLEQqseiTPKQITCRTrgspHPTsn 216
Cdd:cd02660    66 pygpinLLYLSWKHSrnlaGYSQQDAHEFFQFLLDQLH---------THYGGDKNEAN----DESHCNCII----HQT-- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 217 hwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIP----------AATWGHPLTLDHCLHHFISSESVRDVV--C 284
Cdd:cd02660   127 -------FSGSLQSSVTCQRCGGVS-TTVDPFLDLSLDIPnkstpswalgESGVSGTPTLSDCLDRFTRPEKLGDFAykC 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 285 DNCtkieakgtlngekveHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYkyhllghkps 364
Cdd:cd02660   199 SGC---------------GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPY---------- 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 365 qhnpklnknpgptlelqdgpgaptpgvcargadaagifsteksslasppsgslmtgaqglynvlnqpgapktqifmngaC 444
Cdd:cd02660   254 -------------------------------------------------------------------------------T 254

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 445 SPSLLPTLSAPMPfplpvvpdysSSTYLFRLMAVVVHHGDMHSGHFVTYRRsppsarnplSTSNQWLWVSDDTVRKASLQ 524
Cdd:cd02660   255 SSSIGDTQDSNSL----------DPDYTYDLFAVVVHKGTLDTGHYTAYCR---------QGDGQWFKFDDAMITRVSEE 315

                         490
                  ....*....|..
gi 2462535088 525 EVLSSSAYLLFY 536
Cdd:cd02660   316 EVLKSQAYLLFY 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-537 1.38e-18

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: 85.03  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 148
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 149 myrwqissfEEQDAHELFhvitsslederdrqprvTHLFD-VHSLeqqseitpkqITcrtrgsphptsnhwksqHPFHGR 227
Cdd:cd02674    21 ---------DQQDAQEFL-----------------LFLLDgLHSI----------IV-----------------DLFQGQ 47

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 228 LTSNMVCKHCEHQSpVRFDTFDSLSLSIPAA-TWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKgtlngekvehqrT 306
Cdd:cd02674    48 LKSRLTCLTCGKTS-TTFEPFTYLSLPIPSGsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKK------------R 114

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 307 TFVKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRHEHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpga 386
Cdd:cd02674   115 KATKKLTISRLPKVLIIHLKRFS-FSRGSTRKLTTPVTF----------------------------------------- 152

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 387 ptpgvcargadaagifsteksslasPPSGSLMTgaqglynvlnqpgapktqifmngacspSLLPTLSAPMPFplpvvpdy 466
Cdd:cd02674   153 -------------------------PLNDLDLT---------------------------PYVDTRSFTGPF-------- 172

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535088 467 ssstyLFRLMAVVVHHGDMHSGHFVTYRRSPpsarnplsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 537
Cdd:cd02674   173 -----KYDLYAVVNHYGSLNGGHYTAYCKNN--------ETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 68-536 4.93e-16

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 78.86  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  68 PGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 148 RMYRwqissfeEQDAHELFHVITSSLE----DERDRQPRVTHLFDVHSLeqqseitpkqitcrtrgsphptsnhwkSQHP 223
Cdd:cd02661    82 RIGR-------QEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSSQETTL---------------------------VQQI 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 224 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngeK 300
Cdd:cd02661   128 FGGYLRSQVKCLNCKHVSN-TYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCKK----------K 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 301 VEHQrttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKrheHVQFNEFLmmDIYKYhllghkpsqhnpklnknpgptlel 380
Cdd:cd02661   192 VKAS-----KQLTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPETL--DLSPY------------------------ 237

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 381 qdgpgaptpgvcargadaagifstekssLASPPSGSLMtgaqglynvlnqpgapktqifmngacspsllptlsapmpfpl 460
Cdd:cd02661   238 ----------------------------MSQPNDGPLK------------------------------------------ 247

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535088 461 pvvpdyssstylFRLMAVVVHHG-DMHSGHFVTYRRSPPsarnplstsNQWLWVSDDTVRKASLQEVLSSSAYLLFY 536
Cdd:cd02661   248 ------------YKLYAVLVHSGfSPHSGHYYCYVKSSN---------GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 65-539 5.19e-13

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 70.36  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  65 GLVpGLVNLGNTCFMNSLLQGLSACPAF----IRWLEEftsqysrDQKEPPSH---QYLSLTLLHLLKALSCQEVTDdev 137
Cdd:cd02659     1 GYV-GLKNQGATCYMNSLLQQLYMTPEFrnavYSIPPT-------EDDDDNKSvplALQRLFLFLQLSESPVKTTEL--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 138 ldasclLDVLRMYRWQ-ISSFEEQDAHELFHVitsslederdrqprvthLFDvhSLEQQSEITP-KQITCRTrgsphpts 215
Cdd:cd02659    70 ------TDKTRSFGWDsLNTFEQHDVQEFFRV-----------------LFD--KLEEKLKGTGqEGLIKNL-------- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 216 nhwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAATwghplTLDHCLHHFISSEsvrdvVCDNCTKIEAKGT 295
Cdd:cd02659   117 --------FGGKLVNYIICKECPHES-EREEYFLDLQVAVKGKK-----NLEESLDAYVQGE-----TLEGDNKYFCEKC 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 296 lnGEKVEHqrttfVKQLKLGKLPQCLCIHLQRLswsshgtplkrhehvQFNEFLMMDIykyhllghkpsqhnpKLNknpg 375
Cdd:cd02659   178 --GKKVDA-----EKGVCFKKLPPVLTLQLKRF---------------EFDFETMMRI---------------KIN---- 216

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 376 ptlelqdgpgaptpgvcargadaagifsteksslasppsgSLMTgaqgLYNVLNqpgapktqifMNGACSPSLLPTLSAP 455
Cdd:cd02659   217 ----------------------------------------DRFE----FPLELD----------MEPYTEKGLAKKEGDS 242

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 456 MPFPlpvvpdysSSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL-------- 527
Cdd:cd02659   243 EKKD--------SESYIYELHGVLVHSGDAHGGHYYSYIKD--------RDDGKWYKFNDDVVTPFDPNDAEeecfggee 306

                         490       500
                  ....*....|....*....|....*.
gi 2462535088 528 --------------SSSAYLLFYERV 539
Cdd:cd02659   307 tqktydsgprafkrTTNAYMLFYERK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-366 5.01e-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: 63.88  E-value: 5.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPP---------------SHQYLSLTLLHLLKAlSCQEVt 133
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladgllSGRYSKPASLKSEND-PYQVG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 134 ddevLDASCLLDVLRMYRWQISSFEEQDAHELFhvitsslederdrqprvTHLFDVhsLEQQseitpkqitCRTRGSPHP 213
Cdd:cd02658    79 ----IKPSMFKALIGKGHPEFSTMRQQDALEFL-----------------LHLIDK--LDRE---------SFKNLGLNP 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 214 TSNhwksqhpFHGRLTSNMVCKHCEHqspVRFDTFDS--LSLSIPAATWGH---------PLTLDHCLHHFISSESVRDV 282
Cdd:cd02658   127 NDL-------FKFMIEDRLECLSCKK---VKYTSELSeiLSLPVPKDEATEkeegelvyePVPLEDCLKAYFAPETIEDF 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 283 VCDNCTKieakgtlngekvehqrTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYHLLG-- 360
Cdd:cd02658   197 CSTCKEK----------------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--GPGKYELIAfi 258


                  ....*...
gi 2462535088 361 -HK-PSQH 366
Cdd:cd02658   259 sHKgTSVH 266
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 473-537 1.67e-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: 58.69  E-value: 1.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535088 473 FRLMAVVVHHGDM-HSGHFVTYRRSppsarnpLSTSNQWLWVSDDTVRKASLQEVL---SSSAYLLFYE 537
Cdd:cd02673   184 YSLVAVICHLGESpYDGHYIAYTKE-------LYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFYD 245
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-327 4.49e-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: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSA-----CPAFIrwLEEFTSQYSRDQKEPPSHqylsltllhllkalscqevtddevldascL 143
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFenlltCLKDL--FESISEQKKRTGVISPKK-----------------------------F 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 144 LDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRqprvthlfdvhslEQQSEITPKQITCRTRGSPHPTsnhWKSQHp 223
Cdd:cd02663    50 ITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDA-------------ERKAEKANRKLNNNNNAEPQPT---WVHEI- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 224 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNC-TKIEAKgtlnge 299
Cdd:cd02663   113 FQGILTNETRCLTCETVSS-RDETFLDLSIDVEQNT-----SITSCLRQFSATETLCGrnkFYCDECcSLQEAE------ 180

                         250       260
                  ....*....|....*....|....*...
gi 2462535088 300 kvehqrttfvKQLKLGKLPQCLCIHLQR 327
Cdd:cd02663   181 ----------KRMKIKKLPKILALHLKR 198
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-354 6.43e-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: 57.82  E-value: 6.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKE-PPSHQYLSLTLLHLLKALSCQ-EVTDDEVLDASCLLDV 146
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlQFGNRSVVDPSGFVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 147 LRmyrwqISSFEEQDAHELFHVITSSLEDErdrqprvthlfdvhsLEQQSEITPKQITcrtrgsphptsnhwksQHPFHG 226
Cdd:cd02668    81 LG-----LDTGQQQDAQEFSKLFLSLLEAK---------------LSKSKNPDLKNIV----------------QDLFRG 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 227 RLTSNMVCKHCEHQSPVRfDTFDSLSLSIPaatwGHpLTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngekveh 303
Cdd:cd02668   125 EYSYVTQCSKCGRESSLP-SKFYELELQLK----GH-KTLEECIDEFLKEEQLTGdnqYFCESCNS-------------- 184

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462535088 304 qRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKR-HEHVQFNEFLMMDIY 354
Cdd:cd02668   185 -KTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILDMGEY 235
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
466-538 8.27e-07

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 51.81  E-value: 8.27e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535088 466 YSSSTYLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYER 538
Cdd:COG5560   757 VDDPRLIYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-356 1.32e-06

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 50.41  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSqySRDQKEPPSHQYLSLTLLHLLKALSCQE-VTDDEvldascLLDVL 147
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP--ARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIE------FLQLL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 148 RMYRWQISSFEE------QDAHE----LFHVITSSLederdrqprvthlfdvhsleqqseitpkqitcrtrgsPHPTSNH 217
Cdd:cd02657    73 RMAFPQFAEKQNqggyaqQDAEEcwsqLLSVLSQKL-------------------------------------PGAGSKG 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 218 WKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATwgHPLTLDHCLHHFISSEsvrdvvcdnctkIEAKGTLN 297
Cdd:cd02657   116 SFIDQLFGIELETKMKCTESPDEEEVSTESEYKLQCHISITT--EVNYLQDGLKKGLEEE------------IEKHSPTL 181

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 298 GEKVEHQRTTFVKQlklgkLPQCLCIHLQRLSW-SSHGTPLKRHEHVQFNefLMMDIYKY 356
Cdd:cd02657   182 GRDAIYTKTSRISR-----LPKYLTVQFVRFFWkRDIQKKAKILRKVKFP--FELDLYEL 234
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-265 2.78e-05

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 47.19  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 147
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 148 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 222
Cdd:COG5560   344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462535088 223 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 265
Cdd:COG5560   417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
457-538 3.45e-05

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 45.95  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 457 PFPLPVVPDYSSS---TYLFRLMAVVVHHGDMHSGHFVTYRRsppsarnplsTSNQWLWVSDDTVRKASLQEVL---SSS 530
Cdd:COG5533   206 KFELPVKHDQILNivkETYYDLVGFVLHQGSLEGGHYIAYVK----------KGGKWEKANDSDVTPVSEEEAInekAKN 275


                  ....*...
gi 2462535088 531 AYLLFYER 538
Cdd:COG5533   276 AYLYFYER 283
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 457-537 1.61e-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 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: 43.86  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 457 PFPLPVVpDYSSSTYLFRLMAVVVHHG-DMHSGHFVTYRRSPpsarnplsTSNQWLWVSDDTVRKASLQEVL-------S 528
Cdd:cd02657   226 PFELDLY-ELCTPSGYYELVAVITHQGrSADSGHYVAWVRRK--------NDGKWIKFDDDKVSEVTEEDILklsgggdW 296


                  ....*....
gi 2462535088 529 SSAYLLFYE 537
Cdd:cd02657   297 HIAYILLYK 305
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 61-175 1.63e-04

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 44.11  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088  61 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 138
Cdd:cd02671    16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462535088 139 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 175
Cdd:cd02671    83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 457-527 2.10e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 44.48  E-value: 2.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535088  457 PFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL 527
Cdd:COG5077    415 PFLDRDADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKP--------EKDGRWYKFDDTRVTRATEKEVL 477
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 69-94 2.36e-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: 2.36e-04
                          10        20
                  ....*....|....*....|....*.
gi 2462535088  69 GLVNLGNTCFMNSLLQGLSACPAFIR 94
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRR 26
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
69-86 5.84e-04

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 42.10  E-value: 5.84e-04
                          10
                  ....*....|....*...
gi 2462535088  69 GLVNLGNTCFMNSLLQGL 86
Cdd:COG5533     1 GLPNLGNTCFMNSVLQIL 18
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 475-537 2.14e-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: 39.82  E-value: 2.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535088 475 LMAVVVHHG-DMHSGHFVTYRRSPPSARNPLS---TSNQWLWVSDDTVRKASLQEV------LSSSAYLLFYE 537
Cdd:cd02670   169 LCSAVCHRGtSLETGHYVAFVRYGSYSLTETDneaYNAQWVFFDDMADRDGVSNGFnipaarLLEDPYMLFYQ 241
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 469-537 4.47e-03

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 39.40  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535088 469 STYLFRLMAVVVHHG-DMHSGHFVTYRRSP------------PSARNPLSTSNQWLWVSDDTVRKASLQEVL-------S 528
Cdd:cd02664   239 RQVHYRLYAVVVHSGySSESGHYFTYARDQtdadstgqecpePKDAEENDESKNWYLFNDSRVTFSSFESVQnvtsrfpK 318


                  ....*....
gi 2462535088 529 SSAYLLFYE 537
Cdd:cd02664   319 DTPYILFYE 327
 
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