|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-373 |
9.10e-158 |
|
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: 451.34 E-value: 9.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 79 GAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQP------SQALAAG 152
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 153 FHRGKQEDAHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 230 AQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQ 309
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379030599 310 TNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
80-372 |
1.84e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 248.51 E-value: 1.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGC--MLCTMQAHITRALHNPGH-VIQPSQALAA----- 151
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSsSVSPKMFKKSlgkln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 152 -GFHRGKQEDAHEFLMFTVDAMKKACLPghkqvDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:pfam00443 81 pDFSGYKQQDAQEFLLFLLDGLHEDLNG-----NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 231 QSV------QQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-DV-TGNKIAKNVQYPECLD 302
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSyNRsTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379030599 303 MQPYMSQTNTGPLV----YVLYAVLVHAGwSCHNGHYFSYVKAQE-GQWYKMDDAEVTASS-ITSVLSQQAYVLFY 372
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAYEnNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-373 |
1.10e-69 |
|
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: 226.49 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRH--KGCMLCTMqAHITRALHNPGHVIQ--PSQALAAGFHRG 156
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCspNSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 157 K------QEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQ-- 228
Cdd:cd02660 81 RnlagysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 229 -------------AAQSVQQALEQLVKPEELnGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRF---SDVTGNKIA 292
Cdd:cd02660 161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 293 KNVQYPECLDMQPYM---------SQTNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVL 363
Cdd:cd02660 240 TYVQFPLELNMTPYTsssigdtqdSNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
|
330
....*....|
gi 379030599 364 SQQAYVLFYI 373
Cdd:cd02660 319 KSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
81-373 |
7.38e-67 |
|
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: 216.58 E-value: 7.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLtytpplanymlsrehsqtchrhkgcmlctmqahitralhnpghviqpsqalaagFHRgkQED 160
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL------------------------------------------------------FSE--QQD 24
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 161 AHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQ----AAQSVQQA 236
Cdd:cd02257 25 AHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPvkglPQVSLEDC 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 237 LEQLVKPEELNGENAYHCGVClQRAPASKTLTLHTSAKVLILVLKRFS---DVTGNKIAKNVQYPECLDMQPYM------ 307
Cdd:cd02257 105 LEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLsegekd 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379030599 308 SQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEVTASSITSVL-----SQQAYVLFYI 373
Cdd:cd02257 184 SDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-373 |
1.78e-52 |
|
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: 177.86 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLtytpplanymlsrehsqtCHRhkgcmlctmqahitralhnpghviqpsqalaagfhrgkQED 160
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------SAD--------------------------------------QQD 24
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 161 AHEFLMFTVDAMkkaclpghkqvdhHSkdttLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDI------QAAQSVQ 234
Cdd:cd02674 25 AQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLE 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 235 QALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS--DVTGNKIAKNVQYP-ECLDMQPY-MSQT 310
Cdd:cd02674 88 DCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSfsRGSTRKLTTPVTFPlNDLDLTPYvDTRS 167
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379030599 311 NTGPLVYVLYAVLVHAGwSCHNGHYFSYVK-AQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02674 168 FTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-376 |
2.39e-52 |
|
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: 180.92 E-value: 2.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTCHRHKGCML----CTMQAHITRAL-HNPGHVIQ--PSQALAA 151
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLALqrlfLFLQLSESPVKtTELTDKTRsfGWDSLNT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 152 GfhrgKQEDAHEFLMFTVDAMKKaCLPGHKQVDhhskdttLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ 231
Cdd:cd02659 84 F----EQHDVQEFFRVLFDKLEE-KLKGTGQEG-------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 232 SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-D-VTGNKIAKNVQY--PECLDMQPYM 307
Cdd:cd02659 152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDfETMMRIKINDRFefPLELDMEPYT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 308 SQTN-----------TGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQE-GQWYKMDDAEVTASSITSVLSQQ--------- 366
Cdd:cd02659 232 EKGLakkegdsekkdSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEECfggeetqkt 310
|
330 340
....*....|....*....|...
gi 379030599 367 -------------AYVLFYIQKS 376
Cdd:cd02659 311 ydsgprafkrttnAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-372 |
2.58e-47 |
|
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: 166.02 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREH---SQTCHRHkgcmlctmqahitralhnpghviqpSQalaagFHRGK 157
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKelfSQVCRKA-------------------------PQ-----FKGYQ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 158 QEDAHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL----DIQAAQSV 233
Cdd:cd02667 51 QQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 234 QQALEQLVKPEELNGENAYHCGVCLQrapASKTLTLHTSAKVLILVLKRF---SDVTGNKIAKNVQYPECLDMQPYMSQT 310
Cdd:cd02667 114 ESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqpRSANLRKVSRHVSFPEILDLAPFCDPK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 311 NTGP-----LVYVLYAVLVHAGwSCHNGHYFSYVKAQ----------------------EGQWYKMDDAEVTASSITSVL 363
Cdd:cd02667 191 CNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRppqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVL 269
|
....*....
gi 379030599 364 SQQAYVLFY 372
Cdd:cd02667 270 KSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-372 |
2.47e-42 |
|
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: 153.23 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCL----TYTPpLANYMlsreHSQTCHRHKGcmlctmqahitralhnpgHVIQPS---QAL--AA 151
Cdd:cd02663 1 GLENFGNTCYCNSVLQALyfenLLTC-LKDLF----ESISEQKKRT------------------GVISPKkfiTRLkrEN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 152 GFHRGK-QEDAHEFLMF-------TVDAMKKACLPGHKQVDHHSKD--TTLIHQIFGGYWRSQIKCLHCHGISDTFDPYL 221
Cdd:cd02663 58 ELFDNYmHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAEpqPTWVHEIFQGILTNETRCLTCETVSSRDETFL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 222 DIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS---DVTGN-KIAKNVQY 297
Cdd:cd02663 138 DLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKydeQLNRYiKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 298 PECLDMQPYMSQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQeGQWYKMDDAEVTA---SSITSVL-----SQQAYV 369
Cdd:cd02663 218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKideNAVEEFFgdspnQATAYV 296
|
...
gi 379030599 370 LFY 372
Cdd:cd02663 297 LFY 299
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-372 |
2.74e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 151.11 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSRehsqTCHRHKGC-----MLCTMQAHitrALHNPGHVIQP-----SQALA 150
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL----NLPRLGDSqsvmkKLQLLQAH---LMHTQRRAEAPpdyflEASRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 151 AGFHRGKQEDAHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALdiqAA 230
Cdd:cd02664 74 PWFTPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 231 QSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDV--TGN--KIAKNVQYPECLDMQPY 306
Cdd:cd02664 134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDqkTHVreKIMDNVSINEVLSLPVR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 307 MSQTNTGP-------------------LVYVLYAVLVHAGWSCHNGHYFSYVKAQ---------------------EGQW 346
Cdd:cd02664 214 VESKSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaeendeSKNW 293
|
330 340 350
....*....|....*....|....*....|...
gi 379030599 347 YKMDDAEVTASS------ITSVLSQQ-AYVLFY 372
Cdd:cd02664 294 YLFNDSRVTFSSfesvqnVTSRFPKDtPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-354 |
3.09e-36 |
|
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: 137.17 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLS--------REHSQTCHRHKGCMLCTMQAHITRALHNPG-HVIQPSQ-ALA 150
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrSVVDPSGfVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 151 AGFHRGKQEDAHEFLMFTVDAMKkACLPGHKqvdhHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLE-AKLSKSK----NPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 231 QSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS--DVTGN--KIAKNVQYPECLDMQPY 306
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdRKTGAkkKLNASISFPEILDMGEY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 379030599 307 MSQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02668 236 LAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
81-410 |
4.41e-28 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 119.20 E-value: 4.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTchrhKGCMLCTMQahitRALHNPGHVIQPSQAL--------- 149
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRG----RDSVALALQ----RLFYNLQTGEEPVDTTeltrsfgwd 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 150 -AAGFHrgkQEDAHEFLMFTVDAMKKAclpghkqvdhhSKDTTL---IHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL 225
Cdd:COG5077 267 sDDSFM---QHDIQEFNRVLQDNLEKS-----------MRGTVVenaLNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 226 DIQAAQSVQQALEQLVKPEELNGENAYHC-GVCLQRapASKTLTLHTSAKVLILVLKRFS-DV-TGN--KIAKNVQYPEC 300
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAeKHGLQD--AKKGVIFESLPPVLHLQLKRFEyDFeRDMmvKINDRYEFPLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 301 LDMQPYMS----QTNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQ-EGQWYKMDDAEVTASSITSVLSQ---------- 365
Cdd:COG5077 411 IDLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 379030599 366 ------------QAYVLFYIQKSEWERHSESVSRGREPRALgAEDTDRRAKQGELKR 410
Cdd:COG5077 490 kirdhsgikrfmSAYMLVYLRKSMLDDLLNPVAAVDIPPHV-EEVLSEEIDKTEVRC 545
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
80-372 |
4.25e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 108.83 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 80 AGLQNMGNTCYVNASLQCLTYTP-------PLANYMLSREHSQTChrhkgCMLCTMQAHITRALHNPGHVIQPSQALAAG 152
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSS-----FLLNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 153 FHRGKQEDAHEFLMftvdamkkaCLPGHKQvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ- 231
Cdd:cd02671 100 YEGYLQHDAQEVLQ---------CILGNIQ--------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 232 ------------------SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS------DVT 287
Cdd:cd02671 163 skseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAangsefDCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 288 GNKIAKNVQYPECLDMQPYMSQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKaqegqWYKMDDAEV---------TASS 358
Cdd:cd02671 243 GGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvteekdflEALS 317
|
330
....*....|....
gi 379030599 359 ITSVLSQQAYVLFY 372
Cdd:cd02671 318 PNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
81-375 |
9.14e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 98.34 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLT-YTPPLANYM---------LSREHSQtchRHKGCMLCTMQAHITRAlhnpghVIQPSQALA 150
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTAL------WSSKEHKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 151 AGFHRGKQEDAHEFLMFTVDAMKkacLPGHKQVdhhskdTTLIHQIFGGYWRsqikclhcHGISDTFDpyLDIALDIQAA 230
Cdd:COG5533 72 WIPPMGSQEDAHELLGKLLDELK---LDLVNSF------TIRIFKTTKDKKK--------TSTGDWFD--IIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 231 QSVQQALEQLvkPEELNGENAYHCGVCLQ-------RAPASKTLTLHTSAKVLILVLKRFS-DVTGNKIAKNVQYPECLD 302
Cdd:COG5533 133 VNNLKTLQEF--IDNMEELVDDETGVKAKeneelevQAKQEYEVSFVKLPKILTIQLKRFAnLGGNQKIDTEVDEKFELP 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379030599 303 MQPYMSQTNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKaQEGQWYKMDDAEVTASSITSVL---SQQAYVLFYIQK 375
Cdd:COG5533 211 VKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAInekAKNAYLYFYERI 284
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-372 |
2.64e-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 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: 97.40 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPP----LANYMLSREHS-QTCHRhkgcmlctmqahITRALHN-------------PGHV 142
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGAnQSSDN------------LTNALRDlfdtmdkkqepvpPIEF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 143 IQ------PSQALAAGFHRGKQEDAHEFLMFTVDAMkKACLPGhkqvdhHSKDTTLIHQIFGGYWRSQIKC--------- 207
Cdd:cd02657 69 LQllrmafPQFAEKQNQGGYAQQDAEECWSQLLSVL-SQKLPG------AGSKGSFIDQLFGIELETKMKCtespdeeev 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 208 -------LHCHgISDTFD-PYLDIALDiqaaqsvQQALEQLVKPEELNGENAYHcgvclqrapaSKTLTLHTSAKVLILV 279
Cdd:cd02657 142 steseykLQCH-ISITTEvNYLQDGLK-------KGLEEEIEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 280 LKRF----SDVTGNKIAKNVQYPECLDMQPYMsqTNTGplVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02657 204 FVRFfwkrDIQKKAKILRKVKFPFELDLYELC--TPSG--YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKV 279
|
330 340
....*....|....*....|....*
gi 379030599 355 TASSITSVL-------SQQAYVLFY 372
Cdd:cd02657 280 SEVTEEDILklsgggdWHIAYILLY 304
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-372 |
1.39e-21 |
|
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: 95.47 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCH--RHKGCMLCTMqAHITRAL--------------HNPGHV-I 143
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLlsgryskpaslkseNDPYQVgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 144 QPSQ--ALAAGFHR----GKQEDAHEFLMFTVDAMKKAClpghkqvdhHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTF 217
Cdd:cd02658 80 KPSMfkALIGKGHPefstMRQQDALEFLLHLIDKLDRES---------FKNLGLNPNDLFKFMIEDRLECLSCKKVKYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 218 DPYLDIALDIQAA--------------QSVQQALEQLVKPEELngenAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRF 283
Cdd:cd02658 151 ELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 284 ---SDVTGNKIAKNVQYPECLdmqpymsqtntGPLVYVLYAVLVHAGWSCHNGHYFSYVK---AQEGQWYKMDDAEVTAS 357
Cdd:cd02658 227 qllENWVPKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVAS 295
|
330
....*....|....*
gi 379030599 358 SITSVLSQQAYVLFY 372
Cdd:cd02658 296 QDPPEMKKLGYIYFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
232-376 |
1.79e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 95.34 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 232 SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTG--NKIAKNVQYP-ECLDMQPYMS 308
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379030599 309 QTNTGPLVYVLYAVLVHAGWScHNGHYFSYVK-AQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKS 376
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
70-227 |
1.06e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 86.48 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 70 LSSRRPAAVGaGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHR--HKGCM--LCTMQAHITRALHNPG-HVIQ 144
Cdd:COG5560 257 RSINKEAGTC-GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEenPLGMHgsVASAYADLIKQLYDGNlHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 145 PSQ------ALAAGFHRGKQEDAHEFLMFTVDAM--------------KKACLPGHKQV----------DHHSKDTTLIH 194
Cdd:COG5560 336 PSGfkktigSFNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytsKPDLSPGDDVVvkkkakecwwEHLKRNDSIIT 415
|
170 180 190
....*....|....*....|....*....|...
gi 379030599 195 QIFGGYWRSQIKCLHCHGISDTFDPYLDIALDI 227
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-372 |
8.95e-15 |
|
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: 73.94 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYmlsrehsqtchrhkgcmlctmqahITRALhnpghviqpsqalaagfhrgKQED 160
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY------------------------LEEFL--------------------EQQD 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 161 AHEFLmftvdamkkaclpghkqvdHHSkdTTLIHQIFGGYWR----SQIKCLHCHGIS-DTFDPYLDIALDIQAAQSVQ- 234
Cdd:cd02662 37 AHELF-------------------QVL--LETLEQLLKFPFDgllaSRIVCLQCGESSkVRYESFTMLSLPVPNQSSGSg 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 235 QALEQLV----KPEELNGENAYHCGVCLQRAPasKTLTLHtsakvlilvLKRFS---DVTGNKIAKNVQYPECLdmQPYM 307
Cdd:cd02662 96 TTLEHCLddflSTEIIDDYKCDRCQTVIVRLP--QILCIH---------LSRSVfdgRGTSTKNSCKVSFPERL--PKVL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 308 sqtntgplvYVLYAVLVHAGwSCHNGHYFSYVKAQE---------------------GQWYKMDDAEVTASSITSVLSQ- 365
Cdd:cd02662 163 ---------YRLRAVVVHYG-SHSSGHYVCYRRKPLfskdkepgsfvrmregpsstsHPWWRISDTTVKEVSESEVLEQk 232
|
....*..
gi 379030599 366 QAYVLFY 372
Cdd:cd02662 233 SAYMLFY 239
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-355 |
1.60e-14 |
|
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: 75.82 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMqAHITRALHNP----GHV-----IQPSQALAA 151
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPrnfkGHVsphelLQAVSKVSK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 152 G-FHRGKQEDAHEFLMFTVDAMkkaclpgHKQVDHHSKD-TTLIHQIFGG--------------YWRSQIKCLHCHGISD 215
Cdd:cd02669 200 KkFSITEQSDPVEFLSWLLNTL-------HKDLGGSKKPnSSIIHDCFQGkvqietqkikphaeEEGSKDKFFKDSRVKK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 216 TFD-PYLDIALDI---------QAAQSVQQ-ALEQLVKpeELNGENAYHCGvclqraPASKTLTLHTSAKVLILVLKRFS 284
Cdd:cd02669 273 TSVsPFLLLTLDLpppplfkdgNEENIIPQvPLKQLLK--KYDGKTETELK------DSLKRYLISRLPKYLIFHIKRFS 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379030599 285 DVTGNKiAKN---VQYP-ECLDMQPYMSQTNTGPLVYVLY---AVLVHAGWSCHNGHYFSYV-KAQEGQWYKMDDAEVT 355
Cdd:cd02669 345 KNNFFK-EKNptiVNFPiKNLDLSDYVHFDKPSLNLSTKYnlvANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
80-351 |
2.38e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.84 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSreHSQTCHRHKGCMLCTM---------------QA-------------- 130
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELgflfdmlekakgkncQAsnflralssipeas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 131 --------HITRALHNPGHVIQpsqalaaGFHRgkqedaheFLMftvdamKKACLPGHKQVDHHSKDTTLIHQIFGGYWR 202
Cdd:pfam13423 79 alglldedRETNSAISLSSLIQ-------SFNR--------FLL------DQLSSEENSTPPNPSPAESPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 203 SQIKCLHCHGISDTFDPYLDIALDI----------QAAQSVQQALEQLVKPEELNgeNAyHCGVCLQRAPASKTLTLHTS 272
Cdd:pfam13423 138 TTIRCSNCGHESVRESSTHVLDLIYprkpssnnkkPPNQTFSSILKSSLERETTT--KA-WCEKCKRYQPLESRRTVRNL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 273 AKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYM-SQTNTGPLVYVLYAVLVHAGWSCHNGHYFSYVK--------AQE 343
Cdd:pfam13423 215 PPVLSLNAALTNEEWRQLWKTPGWLPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTE 294
|
....*...
gi 379030599 344 GQWYKMDD 351
Cdd:pfam13423 295 SQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
82-372 |
7.96e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 59.46 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 82 LQNMGNTCYVNASLQcltytpplanymlsrehsqtchrhkgcmlctmqahitrALHNPGHVIQpsqalaaGFHRGKQEDA 161
Cdd:cd02673 2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------EFDNDDQQDA 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 162 HEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQI--FGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQalEQ 239
Cdd:cd02673 37 HEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLeaFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNKLDID--EL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 240 LVKPEELNGENAYHCGVC-LQRAPASKTLTlhTSAKVLILVLKRF--SDVTGNKIAKNvqypeCLDMQPYMSQTNTgplv 316
Cdd:cd02673 115 LISNFKTWSPIEKDCSSCkCESAISSERIM--TFPECLSINLKRYklRIATSDYLKKN-----EEIMKKYCGTDAK---- 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379030599 317 YVLYAVLVHAGWSCHNGHYFSYVK--AQEGQWYKMDDAEVTASSITSVL---SQQAYVLFY 372
Cdd:cd02673 184 YSLVAVICHLGESPYDGHYIAYTKelYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
80-355 |
7.98e-07 |
|
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: 51.34 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLS-----REHSQTCHRHK--GCMLCTMQ--------AHITRAL-----HNP 139
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeskAELASDYPTERriGGREVSRSelqrsnqfVYELRSLfndliHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 140 GHVIQPSQALA-AGFhrgKQEDAHEFL---MFTVDAMKKAclPGHKQVDHHSKD----TTLIHQIF-GGYWRSQIKCLHC 210
Cdd:cd02666 82 TRSVTPSKELAyLAL---RQQDVTECIdnvLFQLEVALEP--ISNAFAGPDTEDdkeqSDLIKRLFsGKTKQQLVPESMG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 211 HGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILV-------LKRF 283
Cdd:cd02666 157 NQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryeLPSS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 284 SDVTGNKIAKNVQ--YPECLDMQPYMSQTNT---------GPLVYVLYAVLVHAGWSCHnGHYFSYVK-AQEGQWYKMDD 351
Cdd:cd02666 237 IDDIDELIREAIQseSSLVRQAQNELAELKHeiekqfddlKSYGYRLHAVFIHRGEASS-GHYWVYIKdFEENVWRKYND 315
|
....
gi 379030599 352 AEVT 355
Cdd:cd02666 316 ETVT 319
|
|
| HABP4_PAI-RBP1 |
pfam04774 |
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding ... |
417-454 |
1.81e-05 |
|
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding proteins, and the PAI-1 mRNA-binding protein, PAI-RBP1. HABP4 has been observed to bind hyaluronan (a glucosaminoglycan), but it is not known whether this is its primary role in vivo. It has also been observed to bind RNA, but with a lower affinity than that for hyaluronan. PAI-1 mRNA-binding protein specifically binds the mRNA of type-1 plasminogen activator inhibitor (PAI-1), and is thought to be involved in regulation of mRNA stability. However, in both cases, the sequence motifs predicted to be important for ligand binding are not conserved throughout the family, so it is not known whether members of this family share a common function.
Pssm-ID: 461421 Cd Length: 108 Bit Score: 43.90 E-value: 1.81e-05
10 20 30
....*....|....*....|....*....|....*...
gi 379030599 417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRK 454
Cdd:pfam04774 68 AAAEEEEKEPNEDKEMTLDEYKKVQEEKRALPAFNIRK 105
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
275-373 |
9.64e-05 |
|
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: 44.09 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 275 VLILVLKRFS--DVTGNKIAKNVQYPECLDMQPYMsqtntgplvyvLYAVLVHAGwSCHNGHYFSYVKAQEGQ-WYKMDD 351
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIYKQSRQeWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 379030599 352 AEVTASSITSVLSQ--------QAYVLFYI 373
Cdd:cd02665 199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
214-372 |
4.35e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 42.13 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 214 SDTFDPYLDIALDIQAAQ--------SVQQALEQLVKPEELNGENAYhCGVCLQRAPASKTLTLHTSakVLILVLKRFSD 285
Cdd:cd02670 35 DKLLMPLLEPKVDIIHGGkkdqdddkLVNERLLQIPVPDDDDGGGIT-LEQCLEQYFNNSVFAKAPS--CLIICLKRYGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030599 286 VTGN--KIAKNVQYPECLDMQPYMSQTNT----------------------GPLVYVLYAVLVHAGWSCHNGHYFSYVK- 340
Cdd:cd02670 112 TEGKaqKMFKKILIPDEIDIPDFVADDPRacskcqlecrvcyddkdfsptcGKFKLSLCSAVCHRGTSLETGHYVAFVRy 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 379030599 341 -----------AQEGQWYKMDD-----AEVTASSITSVLSQQ-AYVLFY 372
Cdd:cd02670 192 gsysltetdneAYNAQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
|