|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
50-346 |
1.34e-145 |
|
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: 418.22 E-value: 1.34e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 50 GCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHTHSGDVMKP-SQNLT---SA 125
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIfSSNLKqisKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 126 FHKRKQEDAHEFLMFTLETMHESCLQVHRQSE---PTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISS 202
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 203 VQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFLDLKPYLSQ 282
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099263640 283 PTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYV 346
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
51-345 |
3.95e-96 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 292.04 E-value: 3.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCK--MCAMEAHVtQSLLHTHSGDVMKPSQNLTSA--- 125
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDInlLCALRDLF-KALQKNSKSSSVSPKMFKKSLgkl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 126 ---FHKRKQEDAHEFLMFTLETMHESCLQVHrqsepTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISS 202
Cdd:pfam00443 80 npdFSGYKQQDAQEFLLFLLDGLHEDLNGNH-----STENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 203 VQSVK------QALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFS--GSMGKKLDRKVSYPEFL 274
Cdd:pfam00443 155 DSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLEL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1099263640 275 DLKPYLSQPTGGPLP----YALYAVLVHEGaTCHSGHYFCCVKA-GHGKWYKMDDTKVTSCDV-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 |
1.07e-70 |
|
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: 227.26 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTC--CSPEGCKMCAME---------AHVTQ----SLLHThsgdVM 116
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAMDeifqefyysGDRSPygpiNLLYL----SW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 117 KPSQNLTSAfhkrKQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDI 196
Cdd:cd02660 78 KHSRNLAGY----SQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 197 PLDI-----------SSVQSVKQALQ---DTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRF---SGS 259
Cdd:cd02660 154 SLDIpnkstpswalgESGVSGTPTLSdclDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 260 MGKKLDRKVSYPEFLDLKPYLSQPTGGPLP---------YALYAVLVHEGaTCHSGHYFCCVKAGHGKWYKMDDTKVTSC 330
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRV 312
|
330
....*....|....*.
gi 1099263640 331 DVTSVLNENAYVLFYV 346
Cdd:cd02660 313 SEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
52-346 |
2.78e-69 |
|
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: 221.20 E-value: 2.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHtppladymlsqehsqtccspegckmcameahvtqsllhthsgdvmkpsqnltsafhkrKQ 131
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS----------------------------------------------------------EQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 132 EDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPF----LDIPLDISSVQSVK 207
Cdd:cd02257 23 QDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPElflsLPLPVKGLPQVSLE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 208 QALQDTEKAEELCGENSYYCGRCRqKKPASKTLKLYSAPKVLMLVLKRFS---GSMGKKLDRKVSYPEFLDLKPYLSQPT 284
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099263640 285 ------GGPLPYALYAVLVHEGATCHSGHYFCCVK-AGHGKWYKMDDTKVTSCDVTSVL-----NENAYVLFYV 346
Cdd:cd02257 182 kdsdsdNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.14e-52 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 177.09 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHtppladymlsqehsqtccspegckmcameahvtqsllhthsgdvmkpsqnltsafhkrKQ 131
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA----------------------------------------------------------DQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 132 EDAHEFLMFTLETMHesclqvhrqseptsedsSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSV--KQA 209
Cdd:cd02674 23 QDAQEFLLFLLDGLH-----------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDapKVT 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 210 LQDT----EKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFS--GSMGKKLDRKVSYP-EFLDLKPYL-S 281
Cdd:cd02674 86 LEDClrlfTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSfsRGSTRKLTTPVTFPlNDLDLTPYVdT 165
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1099263640 282 QPTGGPLPYALYAVLVHEGaTCHSGHYFCCVKAGH-GKWYKMDDTKVTSCDVTSVLNENAYVLFY 345
Cdd:cd02674 166 RSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
51-350 |
7.81e-51 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 175.52 E-value: 7.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 51 CGLQNTGNSCYLNAALQCLTHTPPL--ADYMLSQEHSQTCCSPEGCKM--CAMEAHVTQSLLHTHSGDVMKPSQNLTSAf 126
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDDDNKSVPLALqrLFLFLQLSESPVKTTELTDKTRSFGWDSL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 127 HKRKQEDAHEFLMFTLETMHESclqvhrqSEPTSEDSSpIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSV 206
Cdd:cd02659 82 NTFEQHDVQEFFRVLFDKLEEK-------LKGTGQEGL-IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 207 KQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRF-----SGSMgKKLDRKVSYPEFLDLKPYLS 281
Cdd:cd02659 154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeTMMR-IKINDRFEFPLELDMEPYTE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 282 Q----PTGGPLP-------YALYAVLVHEGaTCHSGHYFCCVK-AGHGKWYKMDDTKVTSCDVTSVLNE----------- 338
Cdd:cd02659 233 KglakKEGDSEKkdsesyiYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqkty 311
|
330 340
....*....|....*....|...
gi 1099263640 339 -----------NAYVLFYVQQND 350
Cdd:cd02659 312 dsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.41e-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: 160.55 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHT---PPLADYMlsqeHSQTCCSPegckmcameahvtqsllhthSGDVMKPSQNLT----- 123
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEnllTCLKDLF----ESISEQKK--------------------RTGVISPKKFITrlkre 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 124 -SAFHKRKQEDAHEFLMFTLETMHEsCLQVHRQSEPTSEDSSP----------IHDIFGGWWRSQIKCHHCQGTSYSYDP 192
Cdd:cd02663 57 nELFDNYMHQDAHEFLNFLLNEIAE-ILDAERKAEKANRKLNNnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDET 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 193 FLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRF--SGSMGK--KLDRKV 268
Cdd:cd02663 136 FLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQLNRyiKLFYRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 269 SYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAgHGKWYKMDDTKVTSCDVTSVLN--------ENA 340
Cdd:cd02663 216 VFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKS-HGGWLLFDDETVEKIDENAVEEffgdspnqATA 294
|
....*
gi 1099263640 341 YVLFY 345
Cdd:cd02663 295 YVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
9.60e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 147.15 E-value: 9.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSqehsqtccSPEGckmcaMEAHVTQsllhthsgdvmKPSQnltsaFHKRKQ 131
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------TPKE-----LFSQVCR-----------KAPQ-----FKGYQQ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 132 EDAHEFLMFTLETMhesclqvhrqseptsedSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPL----DISSVQSVK 207
Cdd:cd02667 52 QDSHELLRYLLDGL-----------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 208 QALQDTEKAEELCGENSYYCGRCRQkkpASKTLKLYSAPKVLMLVLKRFSG---SMGKKLDRKVSYPEFLDLKPYLSQPT 284
Cdd:cd02667 115 SCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQprsANLRKVSRHVSFPEILDLAPFCDPKC 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 285 GGP-----LPYALYAVLVHEGaTCHSGHYFCCVKAGH----------------------GKWYKMDDTKVTSCDVTSVLN 337
Cdd:cd02667 192 NSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVLK 270
|
....*...
gi 1099263640 338 ENAYVLFY 345
Cdd:cd02667 271 SEAYLLFY 278
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
4.12e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 144.17 E-value: 4.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLS-QEHSQTCCSPEGCKMcameaHVTQSLLHTHSGDVMKP-----SQNLTSA 125
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSlNLPRLGDSQSVMKKL-----QLLQAHLMHTQRRAEAPpdyflEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 126 FHKRKQEDAHEFLMFTLETMHesclqvhrqseptsedsSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQS 205
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 206 VkqaLQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFS-----GSMGKKLDrKVSYPEFLDLKPYL 280
Cdd:cd02664 139 L---LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqktHVREKIMD-NVSINEVLSLPVRV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 281 SQPTGGP-------------------LPYALYAVLVHEGATCHSGHYFC-------CVKAGH--------------GKWY 320
Cdd:cd02664 215 ESKSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTyardqtdADSTGQecpepkdaeendesKNWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 1099263640 321 KMDDTKVTSCDVTSVLN-------ENAYVLFY 345
Cdd:cd02664 295 LFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-327 |
5.74e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 141.02 E-value: 5.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSqtcCSPEGCKMCAMEAHVTQS----------LLHTHSGDVMKPSqN 121
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNST---EDAELKNMPPDKPHEPQTiidqlqlifaQLQFGNRSVVDPS-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 122 LTSAFH--KRKQEDAHEFLMFTLETMhESCLQVHRQSEPtsedSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLD 199
Cdd:cd02668 77 FVKALGldTGQQQDAQEFSKLFLSLL-EAKLSKSKNPDL----KNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 200 ISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRF-----SGSMgKKLDRKVSYPEFL 274
Cdd:cd02668 152 LKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrkTGAK-KKLNASISFPEIL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1099263640 275 DLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGH-GKWYKMDDTKV 327
Cdd:cd02668 231 DMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDV 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
2.44e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 133.22 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCC--SPEGCKMCAMeAHVTQSLLhthSGDVMKPSQNLTSA---- 125
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLL---SGRYSKPASLKSENdpyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 126 ------------------FHKRKQEDAHEFLMFTLETMHESCLQVHrQSEPTsedsspihDIFGGWWRSQIKCHHCQGTS 187
Cdd:cd02658 77 vgikpsmfkaligkghpeFSTMRQQDALEFLLHLIDKLDRESFKNL-GLNPN--------DLFKFMIEDRLECLSCKKVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 188 YSYDP--FLDIPLDIsSVQSVKQalQDTEKAEEL----CGEN-------SYYCGRCRQKKPASKTLKLYSAPKVLMLVLK 254
Cdd:cd02658 148 YTSELseILSLPVPK-DEATEKE--EGELVYEPVpledCLKAyfapetiEDFCSTCKEKTTATKTTGFKTFPDYLVINMK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 255 RF---SGSMGKKLDRKVSYPEFLdlkpylsqptgGPLPYALYAVLVHEGATCHSGHYFCCVK---AGHGKWYKMDDTKVT 328
Cdd:cd02658 225 RFqllENWVPKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
|
330
....*....|....*..
gi 1099263640 329 SCDVTSVLNENAYVLFY 345
Cdd:cd02658 294 ASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
52-380 |
4.29e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 109.19 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLAD--YMLSQEHSQTCCS-PEGCKMCAMEAHVTQSLLHTHSGDVMKPSQNLTSaFHk 128
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSvALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDS-FM- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 129 rkQEDAHEF---LMFTLEtmhesclqvhrQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQS 205
Cdd:COG5077 273 --QHDIQEFnrvLQDNLE-----------KSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 206 VKQALQDTEKAEELCGENSYYCgrcrQK---KPASKTLKLYSAPKVLMLVLKRFS----GSMGKKLDRKVSYPEFLDLKP 278
Cdd:COG5077 340 LQESFRRYIQVETLDGDNRYNA----EKhglQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLLP 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 279 YLS----QPTGGPLPYALYAVLVHEGaTCHSGHYFCCVKAG-HGKWYKMDDTKVTSCDVTSVLNEN-------------- 339
Cdd:COG5077 416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEENfggdhpykdkirdh 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1099263640 340 --------AYVLFYVQQ---NDL--KKGSINMPEgRIHEVLDAKYQLKKSGEKK 380
Cdd:COG5077 495 sgikrfmsAYMLVYLRKsmlDDLlnPVAAVDIPP-HVEEVLSEEIDKTEVRCKE 547
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
1.70e-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 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: 100.48 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQehsqtccSPEGCKMCAMEAHVTQSLLHTH-----SGDVMKPS---QNLT 123
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNY-------NPARRGANQSSDNLTNALRDLFdtmdkKQEPVPPIeflQLLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 124 SAF---------HKRKQEDAHEFLMftletmheSCLQVHRQS-EPTSEDSSPIHDIFGGWWRSQIKCHHCQG---TSYSY 190
Cdd:cd02657 74 MAFpqfaekqnqGGYAQQDAEECWS--------QLLSVLSQKlPGAGSKGSFIDQLFGIELETKMKCTESPDeeeVSTES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 191 DPFLDIPLDISSVQS-----VKQALQDT-EKAEELCGENSYYcgrcrqkkpaSKTLKLYSAPKVLMLVLKRFS--GSMGK 262
Cdd:cd02657 146 EYKLQCHISITTEVNylqdgLKKGLEEEiEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRFFwkRDIQK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 263 KLD--RKVSYPEFLDLKPYLSqPTGgplPYALYAVLVHEGATCHSGHYFCCVK-AGHGKWYKMDDTKVTSCDVTSVLN-- 337
Cdd:cd02657 216 KAKilRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDILKls 291
|
330
....*....|...
gi 1099263640 338 -----ENAYVLFY 345
Cdd:cd02657 292 gggdwHIAYILLY 304
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
210-349 |
1.95e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 103.81 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 210 LQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSG--SMGKKLDRKVSYPEF-LDLKPYLSQPTGG 286
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSvrSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099263640 287 PLPYALYAVLVHEGATcHSGHYFCCVK-AGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQN 349
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
49-345 |
2.32e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 94.57 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 49 PGCGLQNTGNSCYLNAALQCLTHTP-------PLADYMLSQEHSQTCC--SPEgckmcameaHVTQSLLHTHSGDVMKPS 119
Cdd:cd02671 23 PFVGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSSFllNPE---------KYNDELANQAPRRLLNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 120 QNLTSAFHKRKQEDAHEFLMFTLETMHE-----------------SCLQVHRQSEPTSEDSSPIHDifggwwrsqikchh 182
Cdd:cd02671 94 REVNPMYEGYLQHDAQEVLQCILGNIQElvekdfqgqlvlrtrclECETFTERREDFQDISVPVQE-------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 183 cQGTSYSYDPFLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGK 262
Cdd:cd02671 160 -SELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 263 --------KLDRKVSYPEFLDLKPYLSQPTGGplPYALYAVLVHEGATCHSGHYFCCVkaghgKWYKMDDTKV------- 327
Cdd:cd02671 239 fdcygglsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYV-----RWLLFDDSEVkvteekd 311
|
330 340
....*....|....*....|
gi 1099263640 328 --TSCDVTSVLNENAYVLFY 345
Cdd:cd02671 312 flEALSPNTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
51-205 |
1.27e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 95.34 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 51 CGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHT-HSGDV--MKPSQ------N 121
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQlYDGNLhaFTPSGfkktigS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 122 LTSAFHKRKQEDAHEFLMFTLETMHE--SCLQVHRQSE-PTSEDSSPIH---------------------DIFGGWWRSQ 177
Cdd:COG5560 346 FNEEFSGYDQQDSQEFIAFLLDGLHEdlNRIIKKPYTSkPDLSPGDDVVvkkkakecwwehlkrndsiitDLFQGMYKST 425
|
170 180 190
....*....|....*....|....*....|
gi 1099263640 178 IKCHHCQGTSYSYDPFLDI--PLDISSVQS 205
Cdd:COG5560 426 LTCPGCGSVSITFDPFMDLtlPLPVSMVWK 455
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
52-347 |
4.03e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 81.39 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLT-HTPPLADYM---------LSQEHSQtccSPEGCKMCAMEAHVTQSLLHTHSGDVMKPSQN 121
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTALWSSKEHKVGWIPPMG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 122 ltsafhkrKQEDAHEFLMFTLETMHESCL-QVHRQSEPTSEDSSpiHDIFGGWwrSQIKCHHCQGTSYSYDPFLDIPLD- 199
Cdd:COG5533 78 --------SQEDAHELLGKLLDELKLDLVnSFTIRIFKTTKDKK--KTSTGDW--FDIIIELPDQTWVNNLKTLQEFIDn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 200 ----ISSVQSVKQALQDTEKAeelcgensyycgRCRQKKPASKTlklySAPKVLMLVLKRFSGSMGK-KLDRKVSYPEFL 274
Cdd:COG5533 146 meelVDDETGVKAKENEELEV------------QAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKFEL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1099263640 275 DLKPylsQPTGGPLP---YALYAVLVHEGaTCHSGHYFCCVKAGhGKWYKMDDTKVTSCDVTSVLN---ENAYVLFYVQ 347
Cdd:COG5533 210 PVKH---DQILNIVKetyYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-345 |
4.67e-17 |
|
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: 80.49 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMlsqehsqtccspegckmcameahvtqsllhthsgdvmkpsQNLTSafhkrkQ 131
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL----------------------------------------EEFLE------Q 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 132 EDAHEFLMFTLETMHESClqvhrqseptsedSSPIHDIFGgwwrSQIKCHHCQGTSY-SYDPFLDIPLdissvqSVKQAL 210
Cdd:cd02662 35 QDAHELFQVLLETLEQLL-------------KFPFDGLLA----SRIVCLQCGESSKvRYESFTMLSL------PVPNQS 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 211 QDTEKAEELCGE--------NSYYCGRCRqkkpasktLKLYSAPKVLMLVLKR--FSGSMG-KKLDRKVSYPEFldLKPY 279
Cdd:cd02662 92 SGSGTTLEHCLDdflsteiiDDYKCDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTsTKNSCKVSFPER--LPKV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 280 LsqptggplpYALYAVLVHEGaTCHSGHYFC---------------------CVKAGHGKWYKMDDTKVTSCDVTSVLNE 338
Cdd:cd02662 162 L---------YRLRAVVVHYG-SHSSGHYVCyrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQ 231
|
....*...
gi 1099263640 339 -NAYVLFY 345
Cdd:cd02662 232 kSAYMLFY 239
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
49-330 |
2.95e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 80.83 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 49 PGC-GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQ---TCCSPEGCKMC----------AMEAHVT-QSLLHThsg 113
Cdd:cd02669 117 PGFvGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYEnikDRKSELVKRLSelirkiwnprNFKGHVSpHELLQA--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 114 dVMKPSQNltsAFHKRKQEDAHEFLMFTLETMHeSCLQVHRQSeptseDSSPIHDIFGGWWR---SQIKCHHCQGT---- 186
Cdd:cd02669 194 -VSKVSKK---KFSITEQSDPVEFLSWLLNTLH-KDLGGSKKP-----NSSIIHDCFQGKVQietQKIKPHAEEEGskdk 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 187 ----SYSYD----PFLDIPLDI------SSVQSVKQALQdtEKAEELCgeNSYYCGRCRQKKPASKTLKLYSAPKVLMLV 252
Cdd:cd02669 264 ffkdSRVKKtsvsPFLLLTLDLpppplfKDGNEENIIPQ--VPLKQLL--KKYDGKTETELKDSLKRYLISRLPKYLIFH 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 253 LKRFSGSMGKKlDRK---VSYP-EFLDLKPYLSQPTGGPLP---YALYAVLVHEGATCHSGHYFCCV-KAGHGKWYKMDD 324
Cdd:cd02669 340 IKRFSKNNFFK-EKNptiVNFPiKNLDLSDYVHFDKPSLNLstkYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
....*.
gi 1099263640 325 TKVTSC 330
Cdd:cd02669 419 LNVKEV 424
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
52-327 |
9.36e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 74.61 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLadYMLSQEHSQTCCSPEGCKMCAM----------------------------EAHV 103
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPL--RNLALSHLATECLKEHCLLCELgflfdmlekakgkncqasnflralssipEASA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 104 TQSLLHTHSGDVMKPSQNLTSAFHKrkqedaheFLmftLETMHESCLqvhRQSEPTSEDSSPIHDIFGGWWRSQIKCHHC 183
Cdd:pfam13423 80 LGLLDEDRETNSAISLSSLIQSFNR--------FL---LDQLSSEEN---STPPNPSPAESPLEQLFGIDAETTIRCSNC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 184 ------QGTSYSYDpfLDIP------------LDISSV--QSVKQalQDTEKAeelcgensyYCGRCRQKKPASKTLKLY 243
Cdd:pfam13423 146 ghesvrESSTHVLD--LIYPrkpssnnkkppnQTFSSIlkSSLER--ETTTKA---------WCEKCKRYQPLESRRTVR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 244 SAPKVLMLVLKRFSgSMGKKLDRKVSY--PEFldlKPYLSQPTGGPLP---YALYAVLVHEGATCHSGHYFCCVKAGH-- 316
Cdd:pfam13423 213 NLPPVLSLNAALTN-EEWRQLWKTPGWlpPEI---GLTLSDDLQGDNEivkYELRGVVVHIGDSGTSGHLVSFVKVADse 288
|
330
....*....|....*..
gi 1099263640 317 ------GKWYKMDDTKV 327
Cdd:pfam13423 289 ledpteSQWYLFNDFLV 305
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
53-345 |
3.57e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 63.32 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 53 LQNTGNSCYLNAALQCLThtppladymlsqehsqtccspegckmcameahvtqSLlhthsGDVMKpsqnltsAFHKRKQE 132
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS-----------------------------------SI-----GKINT-------EFDNDDQQ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 133 DAHEFLMFTLETMhESCLQVHRQSEPTSEDS----SPIHDIfggwwRSQIK-CHHCQG-----TSYSYDPFLD---IPLD 199
Cdd:cd02673 35 DAHEFLLTLLEAI-DDIMQVNRTNVPPSNIEikrlNPLEAF-----KYTIEsSYVCIGcsfeeNVSDVGNFLDvsmIDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 200 ISSVQSVKQALQDTEKAEELCGENSYycgrcrqkKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFldlKPY 279
Cdd:cd02673 109 LDIDELLISNFKTWSPIEKDCSSCKC--------ESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEIM---KKY 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1099263640 280 LSQPTGgplpYALYAVLVHEGATCHSGHYFCCVKAGHG--KWYKMDDT---KVTSCDVTSVLNENAYVLFY 345
Cdd:cd02673 178 CGTDAK----YSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDeirPVSKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
52-346 |
2.69e-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: 61.74 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 52 GLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPE--------GCKMCAMEAHVTQS-----------LLHTHS 112
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterrigGREVSRSELQRSNQfvyelrslfndLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 113 GDVmKPSQNLT-SAFhkrKQEDAHEFL---MFTLE--TMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQI-------- 178
Cdd:cd02666 83 RSV-TPSKELAyLAL---RQQDVTECIdnvLFQLEvaLEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLvpesmgnq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 179 ------------------KCHHCQGTSYS----YDPfLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPA 236
Cdd:cd02666 159 psvrtkterflsllvdvgKKGREIVVLLEpkdlYDA-LDRYFDYDSLTKLPQRSQVQAQLAQPLQRELISMDRYELPSSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 237 SKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYpEFLDLKPYlsqptggplPYALYAVLVHEGATCHsGHYFCCVKAGH 316
Cdd:cd02666 238 DDIDELIREAIQSESSLVRQAQNELAELKHEIEK-QFDDLKSY---------GYRLHAVFIHRGEASS-GHYWVYIKDFE 306
|
330 340 350
....*....|....*....|....*....|....*..
gi 1099263640 317 GK-WYKMDDTKVTSCDVTSVLNE------NAYVLFYV 346
Cdd:cd02666 307 ENvWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
245-345 |
3.69e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 45.21 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 245 APKVLMLVLKRFSGSMGK--KLDRKVSYPEFLDLKPYL----------------------SQPTGGPLPYALYAVLVHEG 300
Cdd:cd02670 98 APSCLIICLKRYGKTEGKaqKMFKKILIPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCHRG 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1099263640 301 ATCHSGHYFCCVKAGHG------------KWYK---MDDTKVTSCDV---TSVLNENAYVLFY 345
Cdd:cd02670 178 TSLETGHYVAFVRYGSYsltetdneaynaQWVFfddMADRDGVSNGFnipAARLLEDPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
131-346 |
5.83e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 44.47 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 131 QEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGwwRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSVKQAL 210
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYG--TFLTEGVLEGKPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099263640 211 QDTEKAEELCGENSYYCGRCRQKKpasktlkLYSA-PKVLMLVLKRFSGSMGK--KLDRKVSYPEFLDlkpylsqptggP 287
Cdd:cd02665 100 EAAMFEGEVELLPSDHSVKSGQER-------WFTElPPVLTFELSRFEFNQGRpeKIHDKLEFPQIIQ-----------Q 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1099263640 288 LPYALYAVLVHEGATcHSGHYFCCV-KAGHGKWYKMDDTKVTSCDVTSV--------LNENAYVLFYV 346
Cdd:cd02665 162 VPYELHAVLVHEGQA-NAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVerdsfgggRNPSAYCLMYI 228
|
|
| |
