|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-346 |
3.95e-146 |
|
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: 421.68 E-value: 3.95e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 50 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKLCAMEALVTQSLLHSHSGDVMKP----SHILTSA 125
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfssnLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 126 FHKHQQEDAHEFLMFTLETMHESCLQVHRQSK---PTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISS 202
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 203 AQSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSAFTGNKLDRKVSYPEFLDLKPYLSE 282
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1302630 283 PTGGPLPYALYAVLVHDGATSHSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYV 346
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
51-345 |
1.10e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 305.91 E-value: 1.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCK--LCAMEALVtQSLLHSHSGDVMKPSHILTSA--- 125
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInlLCALRDLF-KALQKNSKSSSVSPKMFKKSLgkl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 126 ---FHKHQQEDAHEFLMFTLETMHESCLQVHrqskpTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISS 202
Cdd:pfam00443 80 npdFSGYKQQDAQEFLLFLLDGLHEDLNGNH-----STENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 203 AQSVK------QALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFS--AFTGNKLDRKVSYPEFL 274
Cdd:pfam00443 155 DSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1302630 275 DLKPYLSEPTGGPLP----YALYAVLVHDGaTSHSGHYFCCVKA-GHGKWYKMDDTKVTRCDV-TSVLNENAYVLFY 345
Cdd:pfam00443 235 DLSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEeTAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-346 |
8.03e-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: 224.17 E-value: 8.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTC--CSPEGCKLCAMEALVtQSLLHSHSGDVMKPSHILTSAFHK- 128
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAMDEIF-QEFYYSGDRSPYGPINLLYLSWKHs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 129 -----HQQEDAHEFLMFTLETMHESCLQVHRQSKPTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSA 203
Cdd:cd02660 81 rnlagYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 204 QSVKQALW--------------DTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRF---SAFTGNKLDR 266
Cdd:cd02660 161 STPSWALGesgvsgtptlsdclDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKIDT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 267 KVSYPEFLDLKPYLSEPTGGPLP---------YALYAVLVHDGaTSHSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLN 337
Cdd:cd02660 241 YVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLK 319
|
....*....
gi 1302630 338 ENAYVLFYV 346
Cdd:cd02660 320 SQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
52-346 |
8.88e-68 |
|
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: 218.89 E-value: 8.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHtppladymlsqehsqtccspegcklcamealvtqsllhshsgdvmkpshiltsafhkhQQ 131
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS----------------------------------------------------------EQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 132 EDAHEFLMFTLETMHESCLQVHRQSKPTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRF----LDIPLDISSAQSVK 207
Cdd:cd02257 23 QDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPElflsLPLPVKGLPQVSLE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 208 QALWDTEKSEELCGDNAYYCGKCRqKMPASKTLHVHIAPKVLMVVLNRFS---AFTGNKLDRKVSYPEFLDLKPYLSEPT 284
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1302630 285 ------GGPLPYALYAVLVHDGATSHSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVL-----NENAYVLFYV 346
Cdd:cd02257 182 kdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
4.12e-51 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 174.40 E-value: 4.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHtppladymlsqehsqtccspegcklcamealvtqsllhshsgdvmkpshiltsafhkhQQ 131
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA----------------------------------------------------------DQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 132 EDAHEFLMFTLETMHesclqvhrqskptsedsSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSAQ------S 205
Cdd:cd02674 23 QDAQEFLLFLLDGLH-----------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvT 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 206 VKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSA--FTGNKLDRKVSYP-EFLDLKPYL-S 281
Cdd:cd02674 86 LEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFsrGSTRKLTTPVTFPlNDLDLTPYVdT 165
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1302630 282 EPTGGPLPYALYAVLVHDGATShSGHYFCCVKAGH-GKWYKMDDTKVTRCDVTSVLNENAYVLFY 345
Cdd:cd02674 166 RSFTGPFKYDLYAVVNHYGSLN-GGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
51-348 |
4.55e-49 |
|
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: 172.06 E-value: 4.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 51 CGLQNTGNSCYLNAALQCLTHTPPL--ADYMLSQEHSQTccsPEGCKLCAMEALVTQSLLHSHSGDVMKPSHiLTSAFHK 128
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDD---DNKSVPLALQRLFLFLQLSESPVKTTELTD-KTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 129 -----HQQEDAHEFLMFTLETMHESclqvhrqSKPTSEDSSpIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSA 203
Cdd:cd02659 79 dslntFEQHDVQEFFRVLFDKLEEK-------LKGTGQEGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 204 QSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSaF-----TGNKLDRKVSYPEFLDLKP 278
Cdd:cd02659 151 KNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE-FdfetmMRIKINDRFEFPLELDMEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 279 YLSE----PTGGPLP-------YALYAVLVHDGaTSHSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVLNE-------- 338
Cdd:cd02659 230 YTEKglakKEGDSEKkdsesyiYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetq 308
|
330 340
....*....|....*....|....
gi 1302630 339 --------------NAYVLFYVQQ 348
Cdd:cd02659 309 ktydsgprafkrttNAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
6.44e-45 |
|
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: 160.17 E-value: 6.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHtpplaDYMLSqehsqtccspegCKLCAMEALVTQSLLhshsGDVMKPSHILT------SA 125
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------------CLKDLFESISEQKKR----TGVISPKKFITrlkrenEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 126 FHKHQQEDAHEFLMFTLETMHEsCLQVHRQSKPTSEDSSP----------IHDIFGGWWRSQIKCLLCQGTSDTYDRFLD 195
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIAE-ILDAERKAEKANRKLNNnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 196 IPLDISSAQSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFsAFTGN-----KLDRKVSY 270
Cdd:cd02663 139 LSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF-KYDEQlnryiKLFYRVVF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 271 PEFLDLKPYLSEPTGGPLPYALYAVLVHDGATSHSGHYFCCVKAgHGKWYKMDDTKVTRCDVTSVLN--------ENAYV 342
Cdd:cd02663 218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENAVEEffgdspnqATAYV 296
|
...
gi 1302630 343 LFY 345
Cdd:cd02663 297 LFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
3.02e-39 |
|
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: 144.07 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqehsqtccSPEG-----CKLCamealvtqsllhshsgdvmkpshiltSAF 126
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------TPKElfsqvCRKA--------------------------PQF 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 127 HKHQQEDAHEFLMFTLETMhesclqvhrqskptsedSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPL----DISS 202
Cdd:cd02667 47 KGYQQQDSHELLRYLLDGL-----------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 203 AQSVKQALWDTEKSEELCGDNAYYCGKCRQkmpASKTLHVHIAPKVLMVVLNRFSA---FTGNKLDRKVSYPEFLDLKPY 279
Cdd:cd02667 110 ECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQprsANLRKVSRHVSFPEILDLAPF 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 280 LSEPTGGP-----LPYALYAVLVHDGaTSHSGHYFCCVKAGH----------------------GKWYKMDDTKVTRCDV 332
Cdd:cd02667 187 CDPKCNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSL 265
|
330
....*....|...
gi 1302630 333 TSVLNENAYVLFY 345
Cdd:cd02667 266 EEVLKSEAYLLFY 278
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.11e-38 |
|
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: 144.17 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqEHSQTccspEGCKLCAMEALVTQ--SLLHSHSGDVMKPSHILTSA---- 125
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS-LNLPR----LGDSQSVMKKLQLLqaHLMHTQRRAEAPPDYFLEASrppw 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 126 FHKHQQEDAHEFLMFTLETMHesclqvhrqskptsedsSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSAQS 205
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 206 VkqaLWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFS--AFTGN--KLDRKVSYPEFLDLKPYLS 281
Cdd:cd02664 139 L---LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVreKIMDNVSINEVLSLPVRVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 282 ------------EPTGG-------PLPYALYAVLVHDGATSHSGHYFC-------CVKAGH--------------GKWYK 321
Cdd:cd02664 216 skssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTyardqtdADSTGQecpepkdaeendesKNWYL 295
|
330 340 350
....*....|....*....|....*....|.
gi 1302630 322 MDDTKVTRCDVTSVLN-------ENAYVLFY 345
Cdd:cd02664 296 FNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-327 |
4.01e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 134.09 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqehsqtCCSPEGCKLCAMEALVTQS-------------LLHSHSGDVMKP 118
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE------CNSTEDAELKNMPPDKPHEpqtiidqlqlifaQLQFGNRSVVDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 119 SH-ILTSAFHKHQQEDAHEFLMFTLETMhESCLQVHRQSKPtsedSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIP 197
Cdd:cd02668 75 SGfVKALGLDTGQQQDAQEFSKLFLSLL-EAKLSKSKNPDL----KNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 198 LDISSAQSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSaF---TGN--KLDRKVSYPE 272
Cdd:cd02668 150 LQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkKLNASISFPE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1302630 273 FLDLKPYLSEPTGGPLPYALYAVLVHDGATSHSGHYFCCVKAGH-GKWYKMDDTKV 327
Cdd:cd02668 229 ILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDV 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
5.49e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 125.13 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCC--SPEGCKLCAMEALVtQSLLhshSGDVMKPS---------- 119
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQLIKLA-DGLL---SGRYSKPAslksendpyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 120 -HILTSAF-----HKHQ------QEDAHEFLMFTLETMHESCLQVHrQSKPTsedsspihDIFGGWWRSQIKCLLCQ--G 185
Cdd:cd02658 77 vGIKPSMFkaligKGHPefstmrQQDALEFLLHLIDKLDRESFKNL-GLNPN--------DLFKFMIEDRLECLSCKkvK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 186 TSDTYDRFLDIPLDISSA-QSVKQALWDTEKSEELCGDN-------AYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFS 257
Cdd:cd02658 148 YTSELSEILSLPVPKDEAtEKEEGELVYEPVPLEDCLKAyfapetiEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 258 A---FTGNKLDRKVSYPEFLdlkpylseptgGPLPYALYAVLVHDGATSHSGHYFCCVK---AGHGKWYKMDDTKVTRCD 331
Cdd:cd02658 228 LlenWVPKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQ 296
|
330
....*....|....
gi 1302630 332 VTSVLNENAYVLFY 345
Cdd:cd02658 297 DPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
3.04e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 111.65 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQehsqtccSPEGCKLCAMEALVTQSLLH-----SHSGDVMKPShILTSAF 126
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNY-------NPARRGANQSSDNLTNALRDlfdtmDKKQEPVPPI-EFLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 127 HKH-------------QQEDAHEFLMftletmheSCLQVHRQS-KPTSEDSSPIHDIFGGWWRSQIKCL---LCQGTSDT 189
Cdd:cd02657 73 RMAfpqfaekqnqggyAQQDAEECWS--------QLLSVLSQKlPGAGSKGSFIDQLFGIELETKMKCTespDEEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 190 YDRFLDIPLDISSA-----QSVKQALWDT-EKSEELCGDNAYYcgkcrqkmpaSKTLHVHIAPKVLMVVLNRF----SAF 259
Cdd:cd02657 145 SEYKLQCHISITTEvnylqDGLKKGLEEEiEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRFfwkrDIQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 260 TGNKLDRKVSYPEFLDLKPYLSePTGgplPYALYAVLVHDGATSHSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVLN- 337
Cdd:cd02657 215 KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDILKl 290
|
330
....*....|....
gi 1302630 338 ------ENAYVLFY 345
Cdd:cd02657 291 sgggdwHIAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
52-373 |
9.49e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 111.89 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLAD--YMLSQEHSQtccsPEGCKLCAMEALVTQSLLHSHSGDVMK--PSHILTSAFH 127
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQRLFYNLQTGEEPVDTTEltRSFGWDSDDS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 128 KHQQeDAHEF---LMFTLEtmhesclqvhrQSKPTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSAQ 204
Cdd:COG5077 271 FMQH-DIQEFnrvLQDNLE-----------KSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 205 SVKQALWDTEKSEELCGDNAYYCGKcRQKMPASKTLHVHIAPKVLMVVLNRFSA--FTGN--KLDRKVSYPEFLDLKPYL 280
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYdfERDMmvKINDRYEFPLEIDLLPFL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 281 SEPT----GGPLPYALYAVLVHDGaTSHSGHYFCCVKAG-HGKWYKMDDTKVTRCDVTSVLNEN---------------- 339
Cdd:COG5077 418 DRDAdkseNSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEENfggdhpykdkirdhsg 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1302630 340 ------AYVLFYVQQANLKQV-----SIDMPEgRINEVLDPEYQL 373
Cdd:COG5077 497 ikrfmsAYMLVYLRKSMLDDLlnpvaAVDIPP-HVEEVLSEEIDK 540
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
49-345 |
1.06e-23 |
|
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: 101.89 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 49 PGCGLQNTGNSCYLNAALQCLTHTP-------PLADYMLSQEHSQTCC--SPEgcklcameaLVTQSLLHSHSGDVMKPS 119
Cdd:cd02671 23 PFVGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSSFllNPE---------KYNDELANQAPRRLLNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 120 HILTSAFHKHQQEDAHEFLMFTLETMHESclqvhrqskptsedsspIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDI--P 197
Cdd:cd02671 94 REVNPMYEGYLQHDAQEVLQCILGNIQEL-----------------VEKDFQGQLVLRTRCLECETFTERREDFQDIsvP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 198 LDISSAQSV--------------KQALWDTEK---SEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSAfT 260
Cdd:cd02671 157 VQESELSKSeesseispdpktemKTLKWAISQfasVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAA-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 261 GNKLD-----RKVSYPEFLDLKPYLSEPTGGPLP--YALYAVLVHDGATSHSGHYFCCVkaghgKWYKMDDTKV---TRC 330
Cdd:cd02671 236 GSEFDcygglSKVNTPLLTPLKLSLEEWSTKPKNdvYRLFAVVMHSGATISSGHYTAYV-----RWLLFDDSEVkvtEEK 310
|
330 340
....*....|....*....|.
gi 1302630 331 DVTSVLNENA------YVLFY 345
Cdd:cd02671 311 DFLEALSPNTsststpYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
214-345 |
6.63e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.49 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 214 EKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSAFTG--NKLDRKVSYPEF-LDLKPYLSEPTGGPLPY 290
Cdd:COG5560 685 SKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPIDdLDLSGVEYMVDDPRLIY 764
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1302630 291 ALYAVLVHDGATShSGHYFCCVK-AGHGKWYKMDDTKVTRCDVTSVLNENAYVLFY 345
Cdd:COG5560 765 DLYAVDNHYGGLS-GGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
8.09e-20 |
|
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: 88.58 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMlsqehsqtccspegcklcamealvtQSLLhshsgdvmkpshiltsafhkhQQ 131
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-------------------------EEFL---------------------EQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 132 EDAHEFLMFTLETMHESClqvhrqskptsedSSPIHDIFGgwwrSQIKCLLCQGTS-DTYDRFLDIPLdissaqSVKQAL 210
Cdd:cd02662 35 QDAHELFQVLLETLEQLL-------------KFPFDGLLA----SRIVCLQCGESSkVRYESFTMLSL------PVPNQS 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 211 WDTEKSEELC--GDNA------YYCGKCrqkmpasKTLHVHiAPKVLMVVLNRFSaFTGN----KLDRKVSYPEFldLKP 278
Cdd:cd02662 92 SGSGTTLEHCldDFLSteiiddYKCDRC-------QTVIVR-LPQILCIHLSRSV-FDGRgtstKNSCKVSFPER--LPK 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 279 YLseptggplpYALYAVLVHDGaTSHSGHYFC---------------------CVKAGHGKWYKMDDTKVTRCDVTSVLN 337
Cdd:cd02662 161 VL---------YRLRAVVVHYG-SHSSGHYVCyrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLE 230
|
....*....
gi 1302630 338 E-NAYVLFY 345
Cdd:cd02662 231 QkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
51-200 |
1.12e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 93.02 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKLCAMEALVTQSLLHS-HSGDV--MKPSHI------ 121
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQlYDGNLhaFTPSGFkktigs 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 122 LTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQ---SKPTSEDSSPIH---------------------DIFGGWWRSQ 177
Cdd:COG5560 346 FNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKpytSKPDLSPGDDVVvkkkakecwwehlkrndsiitDLFQGMYKST 425
|
170 180
....*....|....*....|...
gi 1302630 178 IKCLLCQGTSDTYDRFLDIPLDI 200
Cdd:COG5560 426 LTCPGCGSVSITFDPFMDLTLPL 448
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
52-347 |
1.32e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 89.09 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLT-HTPPLADYM---------LSQEHSQtccSPEGCKLCAMEALVTQSLLHSHsgdvmkpsHI 121
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTALWSSKE--------HK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 122 LTSAFHKHQQEDAHEFLMFTLETMHESCL-QVHRQSKPTSEDSSpiHDIFGGWwrSQIKCLLCQGTSD----TYDRFLD- 195
Cdd:COG5533 70 VGWIPPMGSQEDAHELLGKLLDELKLDLVnSFTIRIFKTTKDKK--KTSTGDW--FDIIIELPDQTWVnnlkTLQEFIDn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 196 IPLDISSAQSVKqalWDTEKSEELCGDNAYYCGKCRqkmpasktlhvhiAPKVLMVVLNRFSAFTGN-KLDRKVSYPEFL 274
Cdd:COG5533 146 MEELVDDETGVK---AKENEELEVQAKQEYEVSFVK-------------LPKILTIQLKRFANLGGNqKIDTEVDEKFEL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1302630 275 DLKPylsEPTGGPLP---YALYAVLVHDGATShSGHYFCCVKAGhGKWYKMDDTKVTRCDVTSVLN---ENAYVLFYVQ 347
Cdd:COG5533 210 PVKH---DQILNIVKetyYDLVGFVLHQGSLE-GGHYIAYVKKG-GKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
52-327 |
1.32e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 74.61 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLadYMLSQEHSQTCCSPEGCKLCAM----------------------------EAlV 103
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPL--RNLALSHLATECLKEHCLLCELgflfdmlekakgkncqasnflralssipEA-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 104 TQSLL--HSHSGDVMKPSHILTSaFHKhqqedaheFLmftLETMHESCLqvhRQSKPTSEDSSPIHDIFGGWWRSQIKCL 181
Cdd:pfam13423 79 ALGLLdeDRETNSAISLSSLIQS-FNR--------FL---LDQLSSEEN---STPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 182 LCQGTSDTYDRFLDIPLDISSAQSVKQA-------LWDTEKSeeLCGDNAY--YCGKCRQKMPASKTLHVHIAPKVLMvv 252
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYPRKPSSNNKkppnqtfSSILKSS--LERETTTkaWCEKCKRYQPLESRRTVRNLPPVLS-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 253 LNrfSAFTGNKLDRKVSYPEFL--DLKPYLSEPTGGPLP---YALYAVLVHDGATSHSGHYFCCVKAGH--------GKW 319
Cdd:pfam13423 220 LN--AALTNEEWRQLWKTPGWLppEIGLTLSDDLQGDNEivkYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQW 297
|
....*...
gi 1302630 320 YKMDDTKV 327
Cdd:pfam13423 298 YLFNDFLV 305
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
49-330 |
1.28e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 72.74 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 49 PGC-GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEhsqtccSPEGCKLCAMEALVTQSLL----------------HSH 111
Cdd:cd02669 117 PGFvGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE------NYENIKDRKSELVKRLSELirkiwnprnfkghvspHEL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 112 SGDVMKPSHiltSAFHKHQQEDAHEFLMFTLETMHeSCLQvhrqsKPTSEDSSPIHDIFGGWWR--------------SQ 177
Cdd:cd02669 191 LQAVSKVSK---KKFSITEQSDPVEFLSWLLNTLH-KDLG-----GSKKPNSSIIHDCFQGKVQietqkikphaeeegSK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 178 IKCLLCQGTSDTYD-RFLDIPLDI---------SSAQSVKQ-ALWD-----TEKSEELCGDNayycgkcrqkmpaSKTLH 241
Cdd:cd02669 262 DKFFKDSRVKKTSVsPFLLLTLDLpppplfkdgNEENIIPQvPLKQllkkyDGKTETELKDS-------------LKRYL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 242 VHIAPKVLMVVLNRFS--AFTGNKLDRKVSYP-EFLDLKPYLSEPTGGPLP---YALYAVLVHDGATSHSGHYFCCV-KA 314
Cdd:cd02669 329 ISRLPKYLIFHIKRFSknNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSLNLstkYNLVANIVHEGTPQEDGTWRVQLrHK 408
|
330
....*....|....*.
gi 1302630 315 GHGKWYKMDDTKVTRC 330
Cdd:cd02669 409 STNKWFEIQDLNVKEV 424
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
53-345 |
1.30e-12 |
|
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: 67.55 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 53 LQNTGNSCYLNAALQCLthtppladymlsqehsqtccspegcklcamealvtqsllhSHSGDVMKpshiltsAFHKHQQE 132
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL----------------------------------------SSIGKINT-------EFDNDDQQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 133 DAHEFLMFTLETMhESCLQVHRQSKPTSEDS----SPIHDIfggwwRSQIK-CLLCQGTSD-----TYDRFLD---IPLD 199
Cdd:cd02673 35 DAHEFLLTLLEAI-DDIMQVNRTNVPPSNIEikrlNPLEAF-----KYTIEsSYVCIGCSFeenvsDVGNFLDvsmIDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 200 ISSAQSVKQALWDTEKSEELcgdnayyCGKCRQKMPASKTLHVHIaPKVLMVVLNRFSAFTGNKLDRKVSYPEFldlKPY 279
Cdd:cd02673 109 LDIDELLISNFKTWSPIEKD-------CSSCKCESAISSERIMTF-PECLSINLKRYKLRIATSDYLKKNEEIM---KKY 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1302630 280 LSEPTGgplpYALYAVLVHDGATSHSGHYFCCVKAGHG--KWYKMDDT---KVTRCDVTSVLNENAYVLFY 345
Cdd:cd02673 178 CGTDAK----YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDeirPVSKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-346 |
2.46e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 62.12 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPE--------GCKLCAMEALVTQS-----------LLHSHS 112
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterrigGREVSRSELQRSNQfvyelrslfndLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 113 GDVmKPSHILT-SAFhkhQQEDAHEFL---MFTLE--TMHESCLQVHRQSKPTSEDSSPIHDIFGGWWRSQI---KCLLC 183
Cdd:cd02666 83 RSV-TPSKELAyLAL---RQQDVTECIdnvLFQLEvaLEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLvpeSMGNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 184 QGTSDTYDRFLDIPLDI----------SSAQSVKQAL----------------WDTEKSEELCGDNAYYCGkcRQKMPAS 237
Cdd:cd02666 159 PSVRTKTERFLSLLVDVgkkgreivvlLEPKDLYDALdryfdydsltklpqrsQVQAQLAQPLQRELISMD--RYELPSS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 238 KTLhVHIAPKVLMVVLNRFSAFTGNKLDRKVSYPE--FLDLKPYlseptggplPYALYAVLVHDGATSHsGHYFCCVKAG 315
Cdd:cd02666 237 IDD-IDELIREAIQSESSLVRQAQNELAELKHEIEkqFDDLKSY---------GYRLHAVFIHRGEASS-GHYWVYIKDF 305
|
330 340 350
....*....|....*....|....*....|....*...
gi 1302630 316 HGK-WYKMDDTKVTRCDVTSVLNE------NAYVLFYV 346
Cdd:cd02666 306 EENvWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
246-346 |
1.26e-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: 46.40 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 246 PKVLMVVLNRFS--AFTGNKLDRKVSYPEFLDlkpylseptggPLPYALYAVLVHDGaTSHSGHYFCCV-KAGHGKWYKM 322
Cdd:cd02665 129 PPVLTFELSRFEfnQGRPEKIHDKLEFPQIIQ-----------QVPYELHAVLVHEG-QANAGHYWAYIyKQSRQEWEKY 196
|
90 100 110
....*....|....*....|....*....|..
gi 1302630 323 DDTKVTRCDVTSV--------LNENAYVLFYV 346
Cdd:cd02665 197 NDISVTESSWEEVerdsfgggRNPSAYCLMYI 228
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-345 |
2.62e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 39.82 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1302630 245 APKVLMVVLNRFSAFTGN--KLDRKVSYPEFLDLKPYL----------------------SEPTGGPLPYALYAVLVHDG 300
Cdd:cd02670 98 APSCLIICLKRYGKTEGKaqKMFKKILIPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCHRG 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1302630 301 ATSHSGHYFCCVKAGHG------------KWYKMDDTKVTRCDV------TSVLNENAYVLFY 345
Cdd:cd02670 178 TSLETGHYVAFVRYGSYsltetdneaynaQWVFFDDMADRDGVSngfnipAARLLEDPYMLFY 240
|
|
| |
