|
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
|
| 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
|
|
| |
