|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-474 |
4.58e-84 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 259.22 E-value: 4.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 122
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 202
Cdd:cd02662 35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 203 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 282
Cdd:cd02662 61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 283 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 362
Cdd:cd02662 120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 363 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 436
Cdd:cd02662 159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2217291606 437 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 474
Cdd:cd02662 196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
43-473 |
1.01e-39 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 145.66 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 122
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 202
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 203 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 278
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 279 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 358
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 359 gaptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsar 438
Cdd:pfam00443 240 ----------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY---- 278
|
410 420 430
....*....|....*....|....*....|....*.
gi 2217291606 439 nplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 473
Cdd:pfam00443 279 ----ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
238-475 |
8.71e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 51.81 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 238 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 314
Cdd:COG5560 675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 315 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 394
Cdd:COG5560 739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 395 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 474
Cdd:COG5560 763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
.
gi 2217291606 475 R 475
Cdd:COG5560 821 R 821
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
43-239 |
5.71e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 45.64 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 121
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 122 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 196
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217291606 197 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 239
Cdd:COG5560 417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-149 |
2.43e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 43.34 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 35 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 112
Cdd:cd02671 16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 2217291606 113 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 149
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 ... |
43-474 |
4.58e-84 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 259.22 E-value: 4.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 122
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLEQ---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 myrwqissfeeQDAHELFHVITSSLEderdrqprvthlfdvhsleqqseitpkqitcrtrgsphptsnhWKSQHPFHGRL 202
Cdd:cd02662 35 -----------QDAHELFQVLLETLE-------------------------------------------QLLKFPFDGLL 60
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 203 TSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCtkieakgtlngekvehqrttf 282
Cdd:cd02662 61 ASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTLEHCLDDFLSTEIIDDYKCDRC--------------------- 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 283 vkQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmdiykyhllghkpsqhnpklnknpgptlelqdgpgapt 362
Cdd:cd02662 120 --QTVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERL--------------------------------------- 158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 363 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPS------ 436
Cdd:cd02662 159 -------------------------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFskdkep 195
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2217291606 437 ------ARNPLSTSNQWLWVSDDTVRKASLQEVL-SSSAYLLFYE 474
Cdd:cd02662 196 gsfvrmREGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFYE 240
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
43-474 |
2.19e-46 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 161.88 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 122
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 myrwqissfEEQDAHELFHVITSSLEDERDRQPRVTHlfdvhsleqqseitpkqitcrtrgspHPTSNHWKSQHPFHGRL 202
Cdd:cd02257 21 ---------EQQDAHEFLLFLLDKLHEELKKSSKRTS--------------------------DSSSLKSLIHDLFGGKL 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 203 TSNMVCKHCEHQSpVRFDTFDSLSLSIPAATWgHPLTLDHCLHHFISSESVRDVVCDNCTKieakgtlngekveHQRTTF 282
Cdd:cd02257 66 ESTIVCLECGHES-VSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILEGDNCYKCEK-------------KKKQEA 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 283 VKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPklnknpgptlelqdgpgapt 362
Cdd:cd02257 131 TKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNGS-------------------- 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 363 pvlnqpgapktqifmngacspsllptlsapmpfplpvvpdyssstYLFRLMAVVVHHGD-MHSGHFVTYRRSPPsarnpl 441
Cdd:cd02257 191 ---------------------------------------------YKYELVAVVVHSGTsADSGHYVAYVKDPS------ 219
|
410 420 430
....*....|....*....|....*....|....*...
gi 2217291606 442 stSNQWLWVSDDTVRKASLQEVL-----SSSAYLLFYE 474
Cdd:cd02257 220 --DGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
43-473 |
1.01e-39 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 145.66 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEeftsQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLR 122
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLL----RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 MYRWQISSFEEQDAHELFHVITSSLEDErdrqprvthLFDVHSLEQQSEITpkqitcrtrgsphptsnhwksqHPFHGRL 202
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHED---------LNGNHSTENESLIT----------------------DLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 203 TSNMVCKHCEHQSpVRFDTFDSLSLSIP-AATWGHPLTLDHCLHHFISSESVRDVV---CDNCTkieakgtlngekvEHQ 278
Cdd:pfam00443 127 KSRLKCLSCGEVS-ETFEPFSDLSLPIPgDSAELKTASLQICFLQFSKLEELDDEEkyyCDKCG-------------CKQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 279 RTTfvKQLKLGKLPQCLCIHLQRLSWSShGTPLKRHEHVQFNEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 358
Cdd:pfam00443 193 DAI--KQLKISRLPPVLIIHLKRFSYNR-STWEKLNTEVEFPLELDLSRY------------------------------ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 359 gaptpvlnqpgapktqifmngaCSPSLLPtlsapmpfPLPVVPDYssstylfRLMAVVVHHGDMHSGHFVTYRRSPpsar 438
Cdd:pfam00443 240 ----------------------LAEELKP--------KTNNLQDY-------RLVAVVVHSGSLSSGHYIAYIKAY---- 278
|
410 420 430
....*....|....*....|....*....|....*.
gi 2217291606 439 nplsTSNQWLWVSDDTVRKASLQ-EVLSSSAYLLFY 473
Cdd:pfam00443 279 ----ENNRWYKFDDEKVTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-474 |
1.33e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 125.58 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLeeftsqysrdqKEPPSHqylsltllhllkalscqevtddevldascLLDVLR 122
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----------SETPKE-----------------------------LFSQVC 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 MYRWQISSFEEQDAHELFHVITSSLEDERDRQprvthlfdvhsleqqseitpkqitcrtrgsphptsnhwksqhpFHGRL 202
Cdd:cd02667 41 RKAPQFKGYQQQDSHELLRYLLDGLRTFIDSI-------------------------------------------FGGEL 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 203 TSNMVCKHCEHQSPVRFdTFDSLSLSIPAATWGhPLTLDHCLHHFISSESVRD---VVCDNCTKieAKgtlngekvehqr 279
Cdd:cd02667 78 TSTIMCESCGTVSLVYE-PFLDLSLPRSDEIKS-ECSIESCLKQFTEVEILEGnnkFACENCTK--AK------------ 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 280 ttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYhllghkpsqhnpklnknpgptlelqdgpg 359
Cdd:cd02667 142 ----KQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEIL--DLAPF----------------------------- 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 360 aptpvlnqpgapktqifmngaCSPSllptlsapmpfplpVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRR------- 432
Cdd:cd02667 187 ---------------------CDPK--------------CNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqr 231
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2217291606 433 ------SPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 474
Cdd:cd02667 232 lsdltkSKPAADEAGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-473 |
8.00e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 107.84 E-value: 8.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIR-WLEEFTSQYSRDQKEPPShqylsltllhllkaLSCQevTDDEVLDASCLLDV- 120
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSC--------------LSCA--MDEIFQEFYYSGDRs 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 121 ------LRMYRWQIS----SFEEQDAHELFHVITSSLEderdrqprvTHLFDVHSLEQqseiTPKQITCRTrgspHPTsn 190
Cdd:cd02660 66 pygpinLLYLSWKHSrnlaGYSQQDAHEFFQFLLDQLH---------THYGGDKNEAN----DESHCNCII----HQT-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 191 hwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIP----------AATWGHPLTLDHCLHHFISSESVRDVV--C 258
Cdd:cd02660 127 -------FSGSLQSSVTCQRCGGVS-TTVDPFLDLSLDIPnkstpswalgESGVSGTPTLSDCLDRFTRPEKLGDFAykC 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 259 DNCtkieakgtlngekveHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYkyhllghkps 338
Cdd:cd02660 199 SGC---------------GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELNMTPY---------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 339 qhnpklnknpgptlelqdgpgaptpvlnqpgapktqifmngaCSPSLLPTLSAPMPfplpvvpdysSSTYLFRLMAVVVH 418
Cdd:cd02660 254 ------------------------------------------TSSSIGDTQDSNSL----------DPDYTYDLFAVVVH 281
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2217291606 419 HGDMHSGHFVTYRRsppsarnplSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFY 473
Cdd:cd02660 282 KGTLDTGHYTAYCR---------QGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-474 |
9.31e-22 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 93.89 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSAcpafirwleeftsqysrdqkeppshqylsltllhllkalscqevtddevldasclldvlr 122
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 123 myrwqissfEEQDAHELFhvitsslederdrqprvTHLFD-VHSLeqqseitpkqITcrtrgsphptsnhwksqHPFHGR 201
Cdd:cd02674 21 ---------DQQDAQEFL-----------------LFLLDgLHSI----------IV-----------------DLFQGQ 47
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 202 LTSNMVCKHCEHQSpVRFDTFDSLSLSIPAA-TWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKgtlngekvehqrT 280
Cdd:cd02674 48 LKSRLTCLTCGKTS-TTFEPFTYLSLPIPSGsGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKK------------R 114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 281 TFVKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRHEHVQF--NEFLMMDIYkyhllghkpsqhnpklnknpgptlelqdgp 358
Cdd:cd02674 115 KATKKLTISRLPKVLIIHLKRFS-FSRGSTRKLTTPVTFplNDLDLTPYV------------------------------ 163
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 359 gaptpvlnqpgapktqifmngacspsllPTLSAPMPFplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYRRSPpsar 438
Cdd:cd02674 164 ----------------------------DTRSFTGPF-------------KYDLYAVVNHYGSLNGGHYTAYCKNN---- 198
|
410 420 430
....*....|....*....|....*....|....*.
gi 2217291606 439 nplsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 474
Cdd:cd02674 199 ----ETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
42-473 |
1.21e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 89.26 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 42 PGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 121
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 122 RMYRwqissfeEQDAHELFHVITSSLE----DERDRQPRVTHLFDVHSLeqqseitpkqitcrtrgsphptsnhwkSQHP 197
Cdd:cd02661 82 RIGR-------QEDAHEFLRYLLDAMQkaclDRFKKLKAVDPSSQETTL---------------------------VQQI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 198 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngeK 274
Cdd:cd02661 128 FGGYLRSQVKCLNCKHVSN-TYDPFLDLSLDIKGAD-----SLEDALEQFTKPEQLDGenkYKCERCKK----------K 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 275 VEHQrttfvKQLKLGKLPQCLCIHLQRLSWSSHGTPLKrheHVQFNEflmmdiykyhllghkpsqhnpklnknpgpTLEL 354
Cdd:cd02661 192 VKAS-----KQLTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPE-----------------------------TLDL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 355 QDgpgaptpvlnqpgapktqiFMNGACSPSLLptlsapmpfplpvvpdyssstylFRLMAVVVHHG-DMHSGHFVTYRRS 433
Cdd:cd02661 235 SP-------------------YMSQPNDGPLK-----------------------YKLYAVLVHSGfSPHSGHYYCYVKS 272
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2217291606 434 PPsarnplstsNQWLWVSDDTVRKASLQEVLSSSAYLLFY 473
Cdd:cd02661 273 SN---------GKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-476 |
1.04e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 81.15 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 39 GLVpGLVNLGNTCFMNSLLQGLSACPAF----IRWLEEftsqysrDQKEPPSH---QYLSLTLLHLLKALSCQEVTDdev 111
Cdd:cd02659 1 GYV-GLKNQGATCYMNSLLQQLYMTPEFrnavYSIPPT-------EDDDDNKSvplALQRLFLFLQLSESPVKTTEL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 112 ldasclLDVLRMYRWQ-ISSFEEQDAHELFHVitsslederdrqprvthLFDvhSLEQQSEITP-KQITCRTrgsphpts 189
Cdd:cd02659 70 ------TDKTRSFGWDsLNTFEQHDVQEFFRV-----------------LFD--KLEEKLKGTGqEGLIKNL-------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 190 nhwksqhpFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAATwghplTLDHCLHHFISSEsvrdvVCDNCTKIEAKGT 269
Cdd:cd02659 117 --------FGGKLVNYIICKECPHES-EREEYFLDLQVAVKGKK-----NLEESLDAYVQGE-----TLEGDNKYFCEKC 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 270 lnGEKVEHqrttfVKQLKLGKLPQCLCIHLQRLswsshgtplkrhehvQFNeFLMMDIYKYhllghkpsqhN-----P-K 343
Cdd:cd02659 178 --GKKVDA-----EKGVCFKKLPPVLTLQLKRF---------------EFD-FETMMRIKI----------NdrfefPlE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 344 LNKNP--GPTLELQDGPGAPTPvlnqpgapktqifmngacspsllptlsapmpfplpvvpdysSSTYLFRLMAVVVHHGD 421
Cdd:cd02659 225 LDMEPytEKGLAKKEGDSEKKD-----------------------------------------SESYIYELHGVLVHSGD 263
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217291606 422 MHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL----------------------SSSAYLLFYERV 476
Cdd:cd02659 264 AHGGHYYSYIKD--------RDDGKWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-340 |
1.59e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 62.34 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPP---------------SHQYLSLTLLHLLKAlSCQEVt 107
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAndlncqlikladgllSGRYSKPASLKSEND-PYQVG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 108 ddevLDASCLLDVLRMYRWQISSFEEQDAHELFhvitsslederdrqprvTHLFDVhsLEQQseitpkqitCRTRGSPHP 187
Cdd:cd02658 79 ----IKPSMFKALIGKGHPEFSTMRQQDALEFL-----------------LHLIDK--LDRE---------SFKNLGLNP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 188 TSNhwksqhpFHGRLTSNMVCKHCEHqspVRFDTFDS--LSLSIPAATWGH---------PLTLDHCLHHFISSESVRDV 256
Cdd:cd02658 127 NDL-------FKFMIEDRLECLSCKK---VKYTSELSeiLSLPVPKDEATEkeegelvyePVPLEDCLKAYFAPETIEDF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 257 VCDNCTKieakgtlngekvehqrTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLmmDIYKYHLLG-- 334
Cdd:cd02658 197 CSTCKEK----------------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKLDVPIDVPEEL--GPGKYELIAfi 258
|
....*...
gi 2217291606 335 -HK-PSQH 340
Cdd:cd02658 259 sHKgTSVH 266
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
410-474 |
2.26e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 57.92 E-value: 2.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217291606 410 FRLMAVVVHHGDM-HSGHFVTYRRSppsarnpLSTSNQWLWVSDDTVRKASLQEVL---SSSAYLLFYE 474
Cdd:cd02673 184 YSLVAVICHLGESpYDGHYIAYTKE-------LYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFYD 245
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-474 |
4.24e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSA-----CPAFIrwLEEFTSQYSRDQKEPPSHqylsltllhllkalscqevtddevldascL 117
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFenlltCLKDL--FESISEQKKRTGVISPKK-----------------------------F 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 118 LDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRqprvthlfdvhslEQQSEITPKQITCRTRGSPHPTsnhWKSQHp 197
Cdd:cd02663 50 ITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDA-------------ERKAEKANRKLNNNNNAEPQPT---WVHEI- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 198 FHGRLTSNMVCKHCEHQSPvRFDTFDSLSLSIPAATwghplTLDHCLHHFISSESVRD---VVCDNC-TKIEAKgtlnge 273
Cdd:cd02663 113 FQGILTNETRCLTCETVSS-RDETFLDLSIDVEQNT-----SITSCLRQFSATETLCGrnkFYCDECcSLQEAE------ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 274 kvehqrttfvKQLKLGKLPQCLCIHLQRlswsshgtplkrhehvqfneflmmdiYKYhllghkpsqhNPKLNKNpgptle 353
Cdd:cd02663 181 ----------KRMKIKKLPKILALHLKR--------------------------FKY----------DEQLNRY------ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 354 lqdgpgaptpvlnqpgapktqifmngacspsllPTLSAPMPFPLPVVP-----DYSSSTYLFRLMAVVVHHGD-MHSGHF 427
Cdd:cd02663 209 ---------------------------------IKLFYRVVFPLELRLfnttdDAENPDRLYELVAVVVHIGGgPNHGHY 255
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2217291606 428 VTYRRsppsarnplsTSNQWLWVSDDTVRK---ASLQEVL-----SSSAYLLFYE 474
Cdd:cd02663 256 VSIVK----------SHGGWLLFDDETVEKideNAVEEFFgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-328 |
1.53e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 56.27 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKE-PPSHQYLSLTLLHLLKALSCQ-EVTDDEVLDASCLLDV 120
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 121 LRmyrwqISSFEEQDAHELFHVITSSLEDErdrqprvthlfdvhsLEQQSEITPKQITcrtrgsphptsnhwksQHPFHG 200
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEAK---------------LSKSKNPDLKNIV----------------QDLFRG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 201 RLTSNMVCKHCEHQSPVRfDTFDSLSLSIPaatwGHpLTLDHCLHHFISSESVRD---VVCDNCTKieakgtlngekveh 277
Cdd:cd02668 125 EYSYVTQCSKCGRESSLP-SKFYELELQLK----GH-KTLEECIDEFLKEEQLTGdnqYFCESCNS-------------- 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217291606 278 qRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKR-HEHVQFNEFLMMDIY 328
Cdd:cd02668 185 -KTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILDMGEY 235
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-474 |
2.03e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 55.80 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSqySRDQKEPPSHQYLSLTLLHLLKALSCQE-VTDDEvldascLLDVL 121
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP--ARRGANQSSDNLTNALRDLFDTMDKKQEpVPPIE------FLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 122 RMYRWQISSFEE------QDAHE----LFHVITSSLederdrqprvthlfdvhsleqqseitpkqitcrtrgsPHPTSNH 191
Cdd:cd02657 73 RMAFPQFAEKQNqggyaqQDAEEcwsqLLSVLSQKL-------------------------------------PGAGSKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 192 WKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATwgHPLTLDHCLHHFISSEsvrdvvcdnctkIEAKGTLN 271
Cdd:cd02657 116 SFIDQLFGIELETKMKCTESPDEEEVSTESEYKLQCHISITT--EVNYLQDGLKKGLEEE------------IEKHSPTL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 272 GEKVEHQRTTFVKQlklgkLPQCLCIHLQRLSW-SSHGTPLKRHEHVQFNefLMMDIYKYhllghkpsqhnpklnknpgp 350
Cdd:cd02657 182 GRDAIYTKTSRISR-----LPKYLTVQFVRFFWkRDIQKKAKILRKVKFP--FELDLYEL-------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 351 tlelqdgpgaptpvlnqpgapktqifmngaCSPSllptlsapmpfplpvvpdyssstYLFRLMAVVVHHG-DMHSGHFVT 429
Cdd:cd02657 235 ------------------------------CTPS-----------------------GYYELVAVITHQGrSADSGHYVA 261
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2217291606 430 YRRSPpsarnplsTSNQWLWVSDDTVRKASLQEVL-------SSSAYLLFYE 474
Cdd:cd02657 262 WVRRK--------NDGKWIKFDDDKVSEVTEEDILklsgggdWHIAYILLYK 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
238-475 |
8.71e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 51.81 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 238 LTLDHCLHHFISSESV---RDVVCDNCTkieakgtlngekvEHQRTTfvKQLKLGKLPQCLCIHLQRLSwSSHGTPLKRH 314
Cdd:COG5560 675 ITLQDCLNEFSKPEQLglsDSWYCPGCK-------------EFRQAS--KQMELWRLPMILIIHLKRFS-SVRSFRDKID 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 315 EHVQFneflmmdiykyhllghkpsqhnpklnknpgptlelqdgpgaptpvlnqpgaPKTQIFMNGACSPSLLPTLsapmp 394
Cdd:COG5560 739 DLVEY---------------------------------------------------PIDDLDLSGVEYMVDDPRL----- 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 395 fplpvvpdyssstyLFRLMAVVVHHGDMHSGHFVTYrrsppsARNPlsTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYE 474
Cdd:COG5560 763 --------------IYDLYAVDNHYGGLSGGHYTAY------ARNF--ANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
.
gi 2217291606 475 R 475
Cdd:COG5560 821 R 821
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
394-475 |
2.92e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 45.95 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 394 PFPLPVVPDYSSS---TYLFRLMAVVVHHGDMHSGHFVTYRRsppsarnplsTSNQWLWVSDDTVRKASLQEVL---SSS 467
Cdd:COG5533 206 KFELPVKHDQILNivkETYYDLVGFVLHQGSLEGGHYIAYVK----------KGGKWEKANDSDVTPVSEEEAInekAKN 275
|
....*...
gi 2217291606 468 AYLLFYER 475
Cdd:COG5533 276 AYLYFYER 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
43-239 |
5.71e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 45.64 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIRWleeFTS-QYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVL 121
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDY---FLSdEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 122 RMYRWQISSFEEQDAHELFHVITSSLEDERDR---QPRVTH--LFDVHSLEQQSeitpkqiTCRTRGSPHPTSNHWKSQH 196
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRiikKPYTSKpdLSPGDDVVVKK-------KAKECWWEHLKRNDSIITD 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217291606 197 PFHGRLTSNMVCKHCEHQSpVRFDTFDSLSLSIPAAT-WGHPLT 239
Cdd:COG5560 417 LFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPLPVSMvWKHTIV 459
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-149 |
2.43e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 43.34 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217291606 35 KRRKGLVP--GLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSrdQKEppSHQylsltllhlLKALSCQEVTDDEVL 112
Cdd:cd02671 16 EKRENLLPfvGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS--SVE--QLQ---------SSFLLNPEKYNDELA 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 2217291606 113 D--ASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLED 149
Cdd:cd02671 83 NqaPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-68 |
2.74e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 42.86 E-value: 2.74e-04
10 20
....*....|....*....|....*.
gi 2217291606 43 GLVNLGNTCFMNSLLQGLSACPAFIR 68
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRR 26
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
394-464 |
2.80e-04 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 43.71 E-value: 2.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217291606 394 PFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSppsarnplSTSNQWLWVSDDTVRKASLQEVL 464
Cdd:COG5077 415 PFLDRDADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKP--------EKDGRWYKFDDTRVTRATEKEVL 477
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
43-60 |
4.97e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 42.10 E-value: 4.97e-04
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
412-474 |
3.20e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 39.43 E-value: 3.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217291606 412 LMAVVVHHG-DMHSGHFVTYRRSPPSARNPLS---TSNQWLWVSDDTVRKASLQEV------LSSSAYLLFYE 474
Cdd:cd02670 169 LCSAVCHRGtSLETGHYVAFVRYGSYSLTETDneaYNAQWVFFDDMADRDGVSNGFnipaarLLEDPYMLFYQ 241
|
|
| |
