|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
110-410 |
0e+00 |
|
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: 552.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 110 GAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARH 189
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 190 FRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKA 266
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 267 AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQ 346
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530385056 347 PNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
111-409 |
5.70e-81 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 260.84 E-value: 5.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFC--MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIA 187
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 188 RHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAA 267
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 268 QSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLD 339
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530385056 340 IRPYMSQPNGEPIV----YVLYAVLVHTGfNCHAGHYFCYIKA-SNGLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 409
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-410 |
2.41e-71 |
|
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: 235.73 E-value: 2.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQALSNPGDVIK--PMFVINEMRRIA 187
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSpnSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 188 RHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIK-- 265
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 266 ------AAQSVNKA-------LEQFVKPEQLdGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGG---KIA 329
Cdd:cd02660 161 stpswaLGESGVSGtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 330 KDVKYPEYLDIRPYMSQPNGEP---------IVYVLYAVLVHTGfNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVL 400
Cdd:cd02660 240 TYVQFPLELNMTPYTSSSIGDTqdsnsldpdYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
|
330
....*....|
gi 530385056 401 SQQAYVLFYI 410
Cdd:cd02660 319 KSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
112-410 |
1.48e-70 |
|
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: 231.22 E-value: 1.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 191
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 FGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI----KAA 267
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 268 QSVNKALEQFVKPEQLDGENSYKCSKCKKmVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDVKYPEYLDIRPYM 344
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530385056 345 SQP------NGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL-----SQQAYVLFYI 410
Cdd:cd02257 178 SEGekdsdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-410 |
1.83e-53 |
|
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: 184.41 E-value: 1.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 191
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 FGNQEDAHEFLQYTVDAMqkaclngsnkldrHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI------K 265
Cdd:cd02674 19 SADQQDAQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 266 AAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFaNFTGG---KIAKDVKYP-EYLDIR 341
Cdd:cd02674 82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530385056 342 PY-MSQPNGEPIVYVLYAVLVHTG-FNChaGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYGsLNG--GHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-412 |
1.25e-51 |
|
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: 182.84 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMMcTMQAHITQALSNPGDVIKPMfvinemrriARH 189
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLAL-QRLFLFLQLSESPVKTTELT---------DKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 190 FRFG-------NQEDAHEFLQYTVDAMQkaclNGSNKLDRHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL 262
Cdd:cd02659 74 RSFGwdslntfEQHDVQEFFRVLFDKLE----EKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 263 EIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGGKIAKD---VKYPEYL 338
Cdd:cd02659 146 AVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMMRIKIndrFEFPLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 339 DIRPYMSQPNG-----------EPIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQ--- 403
Cdd:cd02659 226 DMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfgg 304
|
330 340
....*....|....*....|....*...
gi 530385056 404 -------------------AYVLFYIRS 412
Cdd:cd02659 305 eetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
1.28e-50 |
|
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: 178.35 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmctmqahitqalsNPgdviKPMFviNEMRRIARHFR 191
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------------------------TP----KELF--SQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 FGNQEDAHEFLQYTVDAMQkaclngsnkldrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL----EIKAA 267
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 268 QSVNKALEQFVKPEQLDGENSYKCSKCKKmvpASKRFTIHRSSNVLTLSLKRF-----ANFTggKIAKDVKYPEYLDIRP 342
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 343 YMSQPN-----GEPIVYVLYAVLVHTGfNCHAGHYFCYIKASN----------------------GLWYQMNDSIVSTSD 395
Cdd:cd02667 186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 530385056 396 IRSVLSQQAYVLFY 409
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
1.91e-44 |
|
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: 161.71 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYtpplaNYMLshehskTCHAEGFCMMctmqahITQALSnpGDVIKPMFVINEMRRIARHFR 191
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLL------TCLKDLFESI------SEQKKR--TGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 FGNQEDAHEFLQY-------TVDAMQKACL---NGSNKLDRHTQaTTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT 261
Cdd:cd02663 62 NYMHQDAHEFLNFllneiaeILDAERKAEKanrKLNNNNNAEPQ-PTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 262 LEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnFTGG-----KIAKDVKYPE 336
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK-YDEQlnryiKLFYRVVFPL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 337 YLdiRPYMSQPNGEP--IVYVLYAVLVHTGFNCHAGHYFCYIKaSNGLWYQMNDSIVSTSDIRSVL--------SQQAYV 406
Cdd:cd02663 220 EL--RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeffgdspnQATAYV 296
|
...
gi 530385056 407 LFY 409
Cdd:cd02663 297 LFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
4.57e-41 |
|
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: 152.96 E-value: 4.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFR 191
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 FGN-------------------QEDAHEFLQYTVDAMQkACLNGSNKLDrhtqATTLVCQIFGGYLRSRVKCLNCKGVSD 252
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKSKNPD----LKNIVQDLFRGEYSYVTQCSKCGRESS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 253 TFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnF---TGG--K 327
Cdd:cd02668 141 LPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 328 IAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL------ 400
Cdd:cd02668 220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKlgnsed 299
|
330 340
....*....|....*....|....
gi 530385056 401 ---------------SQQAYVLFY 409
Cdd:cd02668 300 pakprkseikkgthsSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
2.21e-35 |
|
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: 136.85 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKT--CHAEGFCM-MCTMQAHITQALSNPgdviKPMFVINEMRriAR 188
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLgdSQSVMKKLqLLQAHLMHTQRRAEA----PPDYFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 189 HFRFGNQEDAHEFLQYTVDamqkaclngsnKLDrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLeikAAQ 268
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 269 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGG---KIAKDVKYPEYLD--IRP 342
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 343 YMS----------QPNGE-------PIVYVLYAVLVHTGFNCHAGHYFCYI---------------------KASNGLWY 384
Cdd:cd02664 215 ESKssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 530385056 385 QMNDSIVS---TSDIRSVLS----QQAYVLFY 409
Cdd:cd02664 295 LFNDSRVTfssFESVQNVTSrfpkDTPYILFY 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
8.85e-27 |
|
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: 111.26 E-value: 8.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQAL-----SNPGDV----------I 174
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQL-IKLADGLlsgrySKPASLksendpyqvgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 175 KP-MF--VI---NEMrriarhFRFGNQEDAHEFLQYTVDAMQKACLNgsnkldRHTQATTlvcQIFGGYLRSRVKCLNCK 248
Cdd:cd02658 80 KPsMFkaLIgkgHPE------FSTMRQQDALEFLLHLIDKLDRESFK------NLGLNPN---DLFKFMIEDRLECLSCK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 249 GVSDTFD---------PYLDIT-----LEIKAAQSVNKALEQFVKPEQLDgensYKCSKCKKMVPASKRFTIHRSSNVLT 314
Cdd:cd02658 145 KVKYTSElseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 315 LSLKRFA---NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGFNCHAGHYFCYIK---ASNGLWYQMND 388
Cdd:cd02658 221 INMKRFQlleNWVPKKLDVPIDVPEELGPGKYE-----------LIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFND 289
|
330 340
....*....|....*....|.
gi 530385056 389 SIVSTSDIRSVLSQQAYVLFY 409
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
112-411 |
9.55e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.81 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMM-CTMQahiTQALSNPGDVIKpmFVINEMRRIAR 188
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALALQrLFYN---LQTGEEPVDTTE--LTRSFGWDSDD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 189 HFrfgNQEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQ 268
Cdd:COG5077 270 SF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 269 SVNKALEQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYM 344
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 345 S----QPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------- 402
Cdd:COG5077 418 DrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsg 496
|
330
....*....|....
gi 530385056 403 -----QAYVLFYIR 411
Cdd:COG5077 497 ikrfmSAYMLVYLR 510
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-409 |
2.73e-25 |
|
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: 107.67 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 111 AGLQNLGNTCFANAALQCLTYTPPLAN---YMLSHEHSKTCHAEGFCMMCTM--QAHITQAlsnpgdvikPMFVINEMRR 185
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSFLLNPEKynDELANQA---------PRRLLNALRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 186 IARHFRFGNQEDAHEFLQYTVDAMQKaclngsnkldrhtqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT---- 261
Cdd:cd02671 96 VNPMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISvpvq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 262 ------------------LEIKAAQsvnKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-- 321
Cdd:cd02671 159 eselskseesseispdpkTEMKTLK---WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAan 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 322 ----NFTGG--KIAKDVKYPEYLDIRPYMSQPNGEpiVYVLYAVLVHTGFNCHAGHYFCYIKasnglWYQMNDS---IVS 392
Cdd:cd02671 236 gsefDCYGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSevkVTE 308
|
330 340
....*....|....*....|...
gi 530385056 393 TSDIRSVLSQQA------YVLFY 409
Cdd:cd02671 309 EKDFLEALSPNTsststpYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
112-411 |
7.23e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 102.19 E-value: 7.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLT-YTPPLANYM---------LSHEHSKTCHAEGFCMMctmqahiTQALSNpgdvikpmFVIN 181
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRKPEPDLNQEEA-------LKLFTA--------LWSS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 182 EMRRIARHFRFGNQEDAHEFLQYTVDAMqkaclngsnKLDRHTQATTLVCQIFGGYLRSrvkclnckgvsdTFDPYLDIT 261
Cdd:COG5533 66 KEHKVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKT------------STGDWFDII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 262 LEIKAAQSVN--KALEQFVKP--EQLD-------GENSYKCSKCKKMVPASKRftihRSSNVLTLSLKRFANFTGG-KIA 329
Cdd:COG5533 125 IELPDQTWVNnlKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKID 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 330 KDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKaSNGLWYQMNDSIVST---SDIRSVLSQQAYV 406
Cdd:COG5533 201 TEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPvseEEAINEKAKNAYL 278
|
....*
gi 530385056 407 LFYIR 411
Cdd:COG5533 279 YFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
8.59e-24 |
|
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: 102.41 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPP----LANYMLSHEHSktchaegfcmmctMQAHIT---------QALSNPGDVIKPMF 178
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGA-------------NQSSDNltnalrdlfDTMDKKQEPVPPIE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 179 VINEMRriaRHF-RFGNQEDAHEFLQytvdamQKA--CLNG-----SNKLDRHTQATTLVCQIFGGYLRSRVKCL-NCKG 249
Cdd:cd02657 68 FLQLLR---MAFpQFAEKQNQGGYAQ------QDAeeCWSQllsvlSQKLPGAGSKGSFIDQLFGIELETKMKCTeSPDE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 250 VSDTFDP------YLDITLEIKAAQS-VNKALEQFVK--PEQLDGENSYkcskckkmvpaSKRFTIHRSSNVLTLSLKRF 320
Cdd:cd02657 139 EEVSTESeyklqcHISITTEVNYLQDgLKKGLEEEIEkhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 321 -----ANfTGGKIAKDVKYPEYLDIRPYMSqPNGepiVYVLYAVLVHTGFNCHAGHYFCYIKASN-GLWYQMND---SIV 391
Cdd:cd02657 208 fwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDdkvSEV 282
|
330 340
....*....|....*....|...
gi 530385056 392 STSDIRSvLS-----QQAYVLFY 409
Cdd:cd02657 283 TEEDILK-LSgggdwHIAYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-409 |
7.23e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 95.13 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYmlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvINemrriarhfR 191
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-----------------------------------------LE---------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 FGNQEDAHEFLQYTVDAMQKACLNgsnkldrhtqattlvcqIFGGYLRSRVKCLNCKGVS-DTFDPYLDITLEIKAAQSV 270
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSSG 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 271 NKA-----LEQFVKPEQLDGensYKCSKCK-KMVPASKRFTIH--RSS-NVLTLSLKRFANftggkiakdVKYPEYLdiR 341
Cdd:cd02662 94 SGTtlehcLDDFLSTEIIDD---YKCDRCQtVIVRLPQILCIHlsRSVfDGRGTSTKNSCK---------VSFPERL--P 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 342 PYMsqpngepivYVLYAVLVHTGFnCHAGHYFCY--------------------IKASNGL-WYQMNDSIVSTSDIRSVL 400
Cdd:cd02662 160 KVL---------YRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHpWWRISDTTVKEVSESEVL 229
|
330
....*....|
gi 530385056 401 SQ-QAYVLFY 409
Cdd:cd02662 230 EQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
269-413 |
1.11e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 97.26 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 269 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYP-EYLDIRPYMS 345
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530385056 346 QPNGEPIVYVLYAVLVHTGFnCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSH 413
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
112-264 |
6.67e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 78.77 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSnpgDVIKPMFVINEMRRIARHFR 191
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN---PLGMHGSVASAYA---DLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 192 F----------GN-QEDAHEFLQYTVDAMQKAcLN------------------------GSNKLDRHTQAT-TLVCQIFG 235
Cdd:COG5560 341 KtigsfneefsGYdQQDSQEFIAFLLDGLHED-LNriikkpytskpdlspgddvvvkkkAKECWWEHLKRNdSIITDLFQ 419
|
170 180
....*....|....*....|....*....
gi 530385056 236 GYLRSRVKCLNCKGVSDTFDPYLDITLEI 264
Cdd:COG5560 420 GMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
111-391 |
4.16e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 70.76 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSH-------EHS-----------------KTCHAEGFC-MMCTMQAHITQ 165
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHlateclkEHCllcelgflfdmlekakgKNCQASNFLrALSSIPEASAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 166 ALSNPGDVIKPmfVINEMRRIARHFRFGNQEDAHEFLQYTvdamqkaclngsnklDRHTQATTLVCQIFGGYLRSRVKCL 245
Cdd:pfam13423 81 GLLDEDRETNS--AISLSSLIQSFNRFLLDQLSSEENSTP---------------PNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 246 NCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQ-----LDGENSYK--CSKCKKMVPASKRFTIHRSSNVLTLSlk 318
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLN-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 319 rfANFTGGKIAKDVKYPEYL--DIRPYMS---QPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASN--------GLWYQ 385
Cdd:pfam13423 222 --AALTNEEWRQLWKTPGWLppEIGLTLSddlQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYL 299
|
....*.
gi 530385056 386 MNDSIV 391
Cdd:pfam13423 300 FNDFLV 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-388 |
2.00e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 66.57 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMqAHITQALSNPGD---VIKPMFVINE-MRRIA 187
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPRNfkgHVSPHELLQAvSKVSK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 188 RHFRFGNQEDAHEFLQYTVDAMqKACLNGSNKldrhtQATTLVCQIFGGYLR--------------SRVKCLNCKGVSDT 253
Cdd:cd02669 200 KKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 254 FD-PYLDITLEIKAA---QSVNKA--LEQfVKPEQLdgENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRF--ANFTG 325
Cdd:cd02669 274 SVsPFLLLTLDLPPPplfKDGNEEniIPQ-VPLKQL--LKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFskNNFFK 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530385056 326 GKIAKDVKYP-EYLDIRPYMSQP---NGEPIVYVLYAVLVHTGFNCHAGHYFCYI-KASNGLWYQMND 388
Cdd:cd02669 351 EKNPTIVNFPiKNLDLSDYVHFDkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
113-409 |
1.33e-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 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: 50.22 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 113 LQNLGNTCFANAALQcltytpplanymlshehsktchaegfcmmctmqahitqALSNPGDVIKpmfvinemrriarHFRF 192
Cdd:cd02673 2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------------EFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 193 GNQEDAHEFLQYTVDAMQKAC-LNGSNKLDRHTQATTL-VCQIFGGYLRSRVKCLNCKGVSDTFDpyLDITLEIKAAQSV 270
Cdd:cd02673 31 DDQQDAHEFLLTLLEAIDDIMqVNRTNVPPSNIEIKRLnPLEAFKYTIESSYVCIGCSFEENVSD--VGNFLDVSMIDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 271 NKALEQFVKPEQLDGENSYKCSKCK-KMVPASKRFTihRSSNVLTLSLKRFANFTGgkIAKDVKypeylDIRPYMSQPNG 349
Cdd:cd02673 109 LDIDELLISNFKTWSPIEKDCSSCKcESAISSERIM--TFPECLSINLKRYKLRIA--TSDYLK-----KNEEIMKKYCG 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530385056 350 EPIVYVLYAVLVHTGFNCHAGHYFCYIKAS--NGLWYQMNDSI---VSTSDIRSVLSQQAYVLFY 409
Cdd:cd02673 180 TDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-392 |
1.36e-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 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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSNpGDVIKPMFVINEMRRIARHF 190
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASD---YPTERRIGGREVSR-SELQRSNQFVYELRSLFNDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 191 RFGN----------------QEDAHEFLQYTVDAMQKACLNGSN-----KLDRHTQATTLVCQIF-GGYLRSRVKCLNCK 248
Cdd:cd02666 78 IHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVALEPISNafagpDTEDDKEQSDLIKRLFsGKTKQQLVPESMGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 249 GVSD---------TFDPYLDITLEIKA---AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASK------RFTIHRSS 310
Cdd:cd02666 158 QPSVrtkterflsLLVDVGKKGREIVVllePKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRelismdRYELPSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 311 NVlTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGE-PIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMND 388
Cdd:cd02666 238 DD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLkSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYND 315
|
....
gi 530385056 389 SIVS 392
Cdd:cd02666 316 ETVT 319
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
312-410 |
2.23e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 43.32 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 312 VLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGfNCHAGHYFCYI-KASNGLWYQMND 388
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 530385056 389 SIVSTSDIRSVLSQ--------QAYVLFYI 410
Cdd:cd02665 199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-298 |
1.52e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 40.96 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 111 AGLQNLGNTCFANAALQCLTYTPPLANYMLsheHSKTCHAEGFCMMC-------TMQAHITQALSN--PGDVIKPMFVIN 181
Cdd:cd02672 16 AGLENHITNSYCNSLLQLLYFIPPFRNFTA---IILVACPKESCLLCelgylfsTLIQNFTRFLLEtiSQDQLGTPFSCG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385056 182 EMRR-------IARHFRFGNQEDAHEFLQytvdamqkaCLNGSNKLDRHTQATTLVCQifggYLRSRVKCLNCKGVSDTF 254
Cdd:cd02672 93 TSRNsvsllytLSLPLGSTKTSKESTFLQ---------LLKRSLDLEKVTKAWCDTCC----KYQPLEQTTSIRHLPDIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530385056 255 DPYLDITLEiKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMV 298
Cdd:cd02672 160 LLVLVINLS-VTNGEFDDINVVLPSGKVMQNKVSPKAIDHDKLV 202
|
|
| |
