|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-373 |
1.81e-157 |
|
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: 450.57 E-value: 1.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 79 GAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQP------SQALAAG 152
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 153 FHRGKQEDAHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 230 AQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQ 309
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217521328 310 QNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
80-372 |
2.92e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 248.13 E-value: 2.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGC--MLCTMQAHITRALHNPGH-VIQPSQALAA----- 151
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSsSVSPKMFKKSlgkln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 152 -GFHRGKQEDAHEFLMFTVDAMKKACLPghkqvDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:pfam00443 81 pDFSGYKQQDAQEFLLFLLDGLHEDLNG-----NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 231 QSV------QQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-DV-TGNKIAKNVQYPECLD 302
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSyNRsTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217521328 303 MQPYMSQQNTGPLV----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 |
1.12e-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: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRH--KGCMLCTMqAHITRALHNPGHVIQ--PSQALAAGFHRG 156
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCspNSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 157 K------QEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQ-- 228
Cdd:cd02660 81 RnlagysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 229 -------------AAQSVQQALEQLVKPEELnGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRF---SDVTGNKIA 292
Cdd:cd02660 161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 293 KNVQYPECLDMQPYM---------SQQNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVL 363
Cdd:cd02660 240 TYVQFPLELNMTPYTsssigdtqdSNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
|
330
....*....|
gi 2217521328 364 SQQAYVLFYI 373
Cdd:cd02660 319 KSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
81-373 |
8.84e-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: 8.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLtytpplanymlsrehsqtchrhkgcmlctmqahitralhnpghviqpsqalaagFHRgkQED 160
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL------------------------------------------------------FSE--QQD 24
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 161 AHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQ----AAQSVQQA 236
Cdd:cd02257 25 AHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPvkglPQVSLEDC 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 237 LEQLVKPEELNGENAYHCGVClQRAPASKTLTLHTSAKVLILVLKRFS---DVTGNKIAKNVQYPECLDMQPYMSQQ--- 310
Cdd:cd02257 105 LEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGekd 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217521328 311 ---NTGPLVYVLYAVLVHAGWSCHNGHYFSYVK-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 |
7.52e-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: 179.02 E-value: 7.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLtytpplanymlsrehsqtCHRhkgcmlctmqahitralhnpghviqpsqalaagfhrgkQED 160
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------SAD--------------------------------------QQD 24
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 161 AHEFLMFTVDAMkkaclpghkqvdhHSkdttLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDI------QAAQSVQ 234
Cdd:cd02674 25 AQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLE 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 235 QALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS--DVTGNKIAKNVQYP-ECLDMQPY-MSQQ 310
Cdd:cd02674 88 DCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSfsRGSTRKLTTPVTFPlNDLDLTPYvDTRS 167
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217521328 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 |
3.44e-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: 180.53 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTCHRHKGCML----CTMQAHITRAL-HNPGHVIQ--PSQALAA 151
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLALqrlfLFLQLSESPVKtTELTDKTRsfGWDSLNT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 152 GfhrgKQEDAHEFLMFTVDAMKKaCLPGHKQVDhhskdttLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ 231
Cdd:cd02659 84 F----EQHDVQEFFRVLFDKLEE-KLKGTGQEG-------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 232 SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-D-VTGNKIAKNVQY--PECLDMQPYM 307
Cdd:cd02659 152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDfETMMRIKINDRFefPLELDMEPYT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 308 SQ-----------QNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQE-GQWYKMDDAEVTASSITSVLSQQ--------- 366
Cdd:cd02659 232 EKglakkegdsekKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEECfggeetqkt 310
|
330 340
....*....|....*....|...
gi 2217521328 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 |
2.63e-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: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREH---SQTCHRHkgcmlctmqahitralhnpghviqpSQalaagFHRGK 157
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKelfSQVCRKA-------------------------PQ-----FKGYQ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 158 QEDAHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL----DIQAAQSV 233
Cdd:cd02667 51 QQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 234 QQALEQLVKPEELNGENAYHCGVCLQrapASKTLTLHTSAKVLILVLKRF---SDVTGNKIAKNVQYPECLDMQPYMSQQ 310
Cdd:cd02667 114 ESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqpRSANLRKVSRHVSFPEILDLAPFCDPK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 311 NTGP-----LVYVLYAVLVHAGwSCHNGHYFSYVKAQ----------------------EGQWYKMDDAEVTASSITSVL 363
Cdd:cd02667 191 CNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRppqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVL 269
|
....*....
gi 2217521328 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 |
3.72e-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: 152.85 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCL----TYTPpLANYMlsreHSQTCHRHKGcmlctmqahitralhnpgHVIQPS---QAL--AA 151
Cdd:cd02663 1 GLENFGNTCYCNSVLQALyfenLLTC-LKDLF----ESISEQKKRT------------------GVISPKkfiTRLkrEN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 152 GFHRGK-QEDAHEFLMF-------TVDAMKKACLPGHKQVDHHSKD--TTLIHQIFGGYWRSQIKCLHCHGISDTFDPYL 221
Cdd:cd02663 58 ELFDNYmHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAEpqPTWVHEIFQGILTNETRCLTCETVSSRDETFL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 222 DIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS---DVTGN-KIAKNVQY 297
Cdd:cd02663 138 DLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKydeQLNRYiKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 298 PECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQeGQWYKMDDAEVTA---SSITSVL-----SQQAYV 369
Cdd:cd02663 218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKideNAVEEFFgdspnQATAYV 296
|
...
gi 2217521328 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 |
2.52e-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: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSRehsqTCHRHKGC-----MLCTMQAHitrALHNPGHVIQP-----SQALA 150
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL----NLPRLGDSqsvmkKLQLLQAH---LMHTQRRAEAPpdyflEASRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 151 AGFHRGKQEDAHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALdiqAA 230
Cdd:cd02664 74 PWFTPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 231 QSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDV--TGN--KIAKNVQYPECLDMQPY 306
Cdd:cd02664 134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDqkTHVreKIMDNVSINEVLSLPVR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 307 MSQQNTGP-------------------LVYVLYAVLVHAGWSCHNGHYFSYVKAQ---------------------EGQW 346
Cdd:cd02664 214 VESKSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaeendeSKNW 293
|
330 340 350
....*....|....*....|....*....|...
gi 2217521328 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 |
6.98e-37 |
|
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: 139.09 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLS--------REHSQTCHRHKGCMLCTMQAHITRALHNPG-HVIQPSQ-ALA 150
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrSVVDPSGfVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 151 AGFHRGKQEDAHEFLMFTVDAMKkACLPGHKqvdhHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:cd02668 81 LGLDTGQQQDAQEFSKLFLSLLE-AKLSKSK----NPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 231 QSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS--DVTGN--KIAKNVQYPECLDMQPY 306
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdRKTGAkkKLNASISFPEILDMGEY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2217521328 307 MSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02668 236 LAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
81-376 |
5.67e-28 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 118.82 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTchrhKGCMLCTMQahitRALHNPGHVIQPSQAL--------- 149
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRG----RDSVALALQ----RLFYNLQTGEEPVDTTeltrsfgwd 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 150 -AAGFHrgkQEDAHEFLMFTVDAMKKAclpghkqvdhhSKDTTL---IHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL 225
Cdd:COG5077 267 sDDSFM---QHDIQEFNRVLQDNLEKS-----------MRGTVVenaLNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 226 DIQAAQSVQQALEQLVKPEELNGENAYHC-GVCLQRapASKTLTLHTSAKVLILVLKRFS-DV-TGN--KIAKNVQYPEC 300
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAeKHGLQD--AKKGVIFESLPPVLHLQLKRFEyDFeRDMmvKINDRYEFPLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 301 LDMQPYMS----QQNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQ-EGQWYKMDDAEVTASSITSVLSQ---------- 365
Cdd:COG5077 411 IDLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489
|
330 340
....*....|....*....|...
gi 2217521328 366 ------------QAYVLFYIQKS 376
Cdd:COG5077 490 kirdhsgikrfmSAYMLVYLRKS 512
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
80-372 |
8.84e-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: 108.06 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 80 AGLQNMGNTCYVNASLQCLTYTP-------PLANYMLSREHSQTChrhkgCMLCTMQAHITRALHNPGHVIQPSQALAAG 152
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSS-----FLLNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 153 FHRGKQEDAHEFLMftvdamkkaCLPGHKQvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ- 231
Cdd:cd02671 100 YEGYLQHDAQEVLQ---------CILGNIQ--------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 232 ------------------SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS------DVT 287
Cdd:cd02671 163 skseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAangsefDCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 288 GNKIAKNVQYPECLDMQPY-MSQQNTGPlVYVLYAVLVHAGWSCHNGHYFSYVKaqegqWYKMDDAEV---------TAS 357
Cdd:cd02671 243 GGLSKVNTPLLTPLKLSLEeWSTKPKND-VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvteekdflEAL 316
|
330
....*....|....*
gi 2217521328 358 SITSVLSQQAYVLFY 372
Cdd:cd02671 317 SPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
81-375 |
8.07e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 98.34 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLT-YTPPLANYM---------LSREHSQtchRHKGCMLCTMQAHITRAlhnpghVIQPSQALA 150
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTAL------WSSKEHKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 151 AGFHRGKQEDAHEFLMFTVDAMKkacLPGHKQVdhhskdTTLIHQIFGGYWRsqikclhcHGISDTFDpyLDIALDIQAA 230
Cdd:COG5533 72 WIPPMGSQEDAHELLGKLLDELK---LDLVNSF------TIRIFKTTKDKKK--------TSTGDWFD--IIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 231 QSVQQALEQLvkPEELNGENAYHCGVCLQ-------RAPASKTLTLHTSAKVLILVLKRFS-DVTGNKIAKNVQYPECLD 302
Cdd:COG5533 133 VNNLKTLQEF--IDNMEELVDDETGVKAKeneelevQAKQEYEVSFVKLPKILTIQLKRFAnLGGNQKIDTEVDEKFELP 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217521328 303 MQPYMSQQNTGPLVYVLYAVLVHAGwSCHNGHYFSYVKaQEGQWYKMDDAEVTASSITSVL---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 |
3.42e-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: 97.02 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPP----LANYMLSREHS-QTCHRhkgcmlctmqahITRALHN-------------PGHV 142
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGAnQSSDN------------LTNALRDlfdtmdkkqepvpPIEF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 143 IQ------PSQALAAGFHRGKQEDAHEFLMFTVDAMkKACLPGhkqvdhHSKDTTLIHQIFGGYWRSQIKC--------- 207
Cdd:cd02657 69 LQllrmafPQFAEKQNQGGYAQQDAEECWSQLLSVL-SQKLPG------AGSKGSFIDQLFGIELETKMKCtespdeeev 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 208 -------LHCHgISDTFD-PYLDIALDiqaaqsvQQALEQLVKPEELNGENAYHcgvclqrapaSKTLTLHTSAKVLILV 279
Cdd:cd02657 142 steseykLQCH-ISITTEvNYLQDGLK-------KGLEEEIEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 280 LKRF----SDVTGNKIAKNVQYPECLDMQPYMSqqNTGplVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02657 204 FVRFfwkrDIQKKAKILRKVKFPFELDLYELCT--PSG--YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKV 279
|
330 340
....*....|....*....|....*
gi 2217521328 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 |
1.46e-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: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCH--RHKGCMLCTMqAHITRAL--------------HNPGHV-I 143
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLlsgryskpaslkseNDPYQVgI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 144 QPSQ--ALAAGFHR----GKQEDAHEFLMFTVDAMKKAClpghkqvdhHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTF 217
Cdd:cd02658 80 KPSMfkALIGKGHPefstMRQQDALEFLLHLIDKLDRES---------FKNLGLNPNDLFKFMIEDRLECLSCKKVKYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 218 DPYLDIALDIQAA--------------QSVQQALEQLVKPEELngenAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRF 283
Cdd:cd02658 151 ELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 284 ---SDVTGNKIAKNVQYPECLdmqpymsqqntGPLVYVLYAVLVHAGWSCHNGHYFSYVK---AQEGQWYKMDDAEVTAS 357
Cdd:cd02658 227 qllENWVPKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVAS 295
|
330
....*....|....*
gi 2217521328 358 SITSVLSQQAYVLFY 372
Cdd:cd02658 296 QDPPEMKKLGYIYFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
232-376 |
1.78e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 95.34 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 232 SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTG--NKIAKNVQYP-ECLDMQPYMS 308
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217521328 309 QQNTGPLVYVLYAVLVHAGWScHNGHYFSYVK-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 2217521328 70 LSSRRPAAVGaGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHR--HKGCM--LCTMQAHITRALHNPG-HVIQ 144
Cdd:COG5560 257 RSINKEAGTC-GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEenPLGMHgsVASAYADLIKQLYDGNlHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 145 PSQ------ALAAGFHRGKQEDAHEFLMFTVDAM--------------KKACLPGHKQV----------DHHSKDTTLIH 194
Cdd:COG5560 336 PSGfkktigSFNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytsKPDLSPGDDVVvkkkakecwwEHLKRNDSIIT 415
|
170 180 190
....*....|....*....|....*....|...
gi 2217521328 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 |
1.09e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 73.55 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYmlsrehsqtchrhkgcmlctmqahITRALhnpghviqpsqalaagfhrgKQED 160
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY------------------------LEEFL--------------------EQQD 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 161 AHEFLMFTVDAMkkaclpghkqvdhHSKDTTLIHQIFGgywrSQIKCLHCHGIS-DTFDPYLDIALDIQAAQSVQ-QALE 238
Cdd:cd02662 37 AHELFQVLLETL-------------EQLLKFPFDGLLA----SRIVCLQCGESSkVRYESFTMLSLPVPNQSSGSgTTLE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 239 QLV----KPEELNGENAYHCGVCLQRAPasKTLTLHtsakvlilvLKRFS---DVTGNKIAKNVQYPECLdmQPYMsqqn 311
Cdd:cd02662 100 HCLddflSTEIIDDYKCDRCQTVIVRLP--QILCIH---------LSRSVfdgRGTSTKNSCKVSFPERL--PKVL---- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 312 tgplvYVLYAVLVHAGwSCHNGHYFSYVKAQE---------------------GQWYKMDDAEVTASSITSVLSQ-QAYV 369
Cdd:cd02662 163 -----YRLRAVVVHYG-SHSSGHYVCYRRKPLfskdkepgsfvrmregpsstsHPWWRISDTTVKEVSESEVLEQkSAYM 236
|
...
gi 2217521328 370 LFY 372
Cdd:cd02662 237 LFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
80-351 |
1.36e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 74.61 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSreHSQTCHRHKGCMLCTM---------------QA-------------- 130
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELgflfdmlekakgkncQAsnflralssipeas 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 131 --------HITRALHNPGHVIQpsqalaaGFHRgkqedaheFLMftvdamKKACLPGHKQVDHHSKDTTLIHQIFGGYWR 202
Cdd:pfam13423 79 alglldedRETNSAISLSSLIQ-------SFNR--------FLL------DQLSSEENSTPPNPSPAESPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 203 SQIKCLHCHGISDTFDPYLDIALDI----------QAAQSVQQALEQLVKPEELNgeNAyHCGVCLQRAPASKTLTLHTS 272
Cdd:pfam13423 138 TTIRCSNCGHESVRESSTHVLDLIYprkpssnnkkPPNQTFSSILKSSLERETTT--KA-WCEKCKRYQPLESRRTVRNL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 273 AKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPL-VYVLYAVLVHAGWSCHNGHYFSYVK--------AQE 343
Cdd:pfam13423 215 PPVLSLNAALTNEEWRQLWKTPGWLPPEIGLTLSDDLQGDNEIvKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTE 294
|
....*...
gi 2217521328 344 GQWYKMDD 351
Cdd:pfam13423 295 SQWYLFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
81-355 |
1.53e-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: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMqAHITRALHNP----GHV-----IQPSQALAA 151
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPrnfkGHVsphelLQAVSKVSK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 152 G-FHRGKQEDAHEFLMFTVDAMkkaclpgHKQVDHHSKD-TTLIHQIFGG--------------YWRSQIKCLHCHGISD 215
Cdd:cd02669 200 KkFSITEQSDPVEFLSWLLNTL-------HKDLGGSKKPnSSIIHDCFQGkvqietqkikphaeEEGSKDKFFKDSRVKK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 216 TFD-PYLDIALDI---------QAAQSVQQ-ALEQLVKpeELNGENAYHCGvclqraPASKTLTLHTSAKVLILVLKRFS 284
Cdd:cd02669 273 TSVsPFLLLTLDLpppplfkdgNEENIIPQvPLKQLLK--KYDGKTETELK------DSLKRYLISRLPKYLIFHIKRFS 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217521328 285 DVTGNKiAKN---VQYP-ECLDMQPYMS--QQNTGPLV-YVLYAVLVHAGWSCHNGHYFSYV-KAQEGQWYKMDDAEVT 355
Cdd:cd02669 345 KNNFFK-EKNptiVNFPiKNLDLSDYVHfdKPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
82-372 |
7.19e-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: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 82 LQNMGNTCYVNASLQcltytpplanymlsrehsqtchrhkgcmlctmqahitrALHNPGHVIQpsqalaaGFHRGKQEDA 161
Cdd:cd02673 2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------EFDNDDQQDA 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 162 HEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQI--FGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQalEQ 239
Cdd:cd02673 37 HEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLeaFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNKLDID--EL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 240 LVKPEELNGENAYHCGVC-LQRAPASKTLTlhTSAKVLILVLKRF--SDVTGNKIAKNvqypeCLDMQPYMSQQNTgplv 316
Cdd:cd02673 115 LISNFKTWSPIEKDCSSCkCESAISSERIM--TFPECLSINLKRYklRIATSDYLKKN-----EEIMKKYCGTDAK---- 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217521328 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 |
9.28e-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: 50.95 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLS-----REHSQTCHRHK--GCMLCTMQ--------AHITRAL-----HNP 139
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeskAELASDYPTERriGGREVSRSelqrsnqfVYELRSLfndliHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 140 GHVIQPSQALA-AGFhrgKQEDAHEFL---MFTVDAMKKAclPGHKQVDHHSKD----TTLIHQIF-GGYWRSQIKCLHC 210
Cdd:cd02666 82 TRSVTPSKELAyLAL---RQQDVTECIdnvLFQLEVALEP--ISNAFAGPDTEDdkeqSDLIKRLFsGKTKQQLVPESMG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 211 HGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILV-------LKRF 283
Cdd:cd02666 157 NQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELismdryeLPSS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 284 SDVTGNKIAKNVQypECLDMQPYMSQQNTGPL-------------VYVLYAVLVHAGWSCHnGHYFSYVK-AQEGQWYKM 349
Cdd:cd02666 237 IDDIDELIREAIQ--SESSLVRQAQNELAELKheiekqfddlksyGYRLHAVFIHRGEASS-GHYWVYIKdFEENVWRKY 313
|
....*.
gi 2217521328 350 DDAEVT 355
Cdd:cd02666 314 NDETVT 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 2217521328 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 |
1.02e-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: 43.70 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 275 VLILVLKRFS--DVTGNKIAKNVQYPECLDMQPYMsqqntgplvyvLYAVLVHAGwSCHNGHYFSYVKAQEGQ-WYKMDD 351
Cdd:cd02665 131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIYKQSRQeWEKYND 198
|
90 100 110
....*....|....*....|....*....|
gi 2217521328 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 |
3.40e-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: 42.51 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 214 SDTFDPYLDIALDIQAAQ--------SVQQALEQLVKPEELNGENAYhCGVCLQRAPASKTLTLHTSakVLILVLKRFSD 285
Cdd:cd02670 35 DKLLMPLLEPKVDIIHGGkkdqdddkLVNERLLQIPVPDDDDGGGIT-LEQCLEQYFNNSVFAKAPS--CLIICLKRYGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217521328 286 VTGN--KIAKNVQYPECLDMQPYMSQQNT----------------------GPLVYVLYAVLVHAGWSCHNGHYFSYVK- 340
Cdd:cd02670 112 TEGKaqKMFKKILIPDEIDIPDFVADDPRacskcqlecrvcyddkdfsptcGKFKLSLCSAVCHRGTSLETGHYVAFVRy 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217521328 341 -----------AQEGQWYKMDD-----AEVTASSITSVLSQQ-AYVLFY 372
Cdd:cd02670 192 gsysltetdneAYNAQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| |
