|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-466 |
1.42e-164 |
|
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: 467.23 E-value: 1.42e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYgalntkqasssSTSTNRQTGFI 217
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCAMDEIFQEFY-----------YSGDRSPYGPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 YLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLPNakevsRANNKQCECIVHTVFEGSLESSIVCPGCQNNSk 297
Cdd:cd02660 71 NLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNE-----ANDESHCNCIIHQTFSGSLQSSVTCQRCGGVS- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 298 TTIDPFLDLSLDIKDK---------------KKLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQL 362
Cdd:cd02660 145 TTVDPFLDLSLDIPNKstpswalgesgvsgtPTLSDCLDRFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 363 KRFEHLLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVPDIIYELIGIVSHKGTVNEGHYIAFCKISGGQWFKF 442
Cdd:cd02660 225 KRFEHSLNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKF 304
|
330 340
....*....|....*....|....
gi 6323879 443 NDSMVSSISQEEVLKEQAYLLFYT 466
Cdd:cd02660 305 DDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
138-465 |
1.35e-92 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 283.18 E-value: 1.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPYFiRHSMSQIHSNNCKVRSPDKC-FSCALDKIVHELYgalntKQASSSSTSTNRqtgf 216
Cdd:pfam00443 2 GLVNLGNTCYMNSVLQSLFSIPPF-RDYLLRISPLSEDSRYNKDInLLCALRDLFKALQ-----KNSKSSSVSPKM---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 217 iyLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQsyvldlpnakEVSRANNKQCECIVHTVFEGSLESSIVCPGCQNNS 296
Cdd:pfam00443 72 --FKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHE----------DLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 297 KTTiDPFLDLSLDIKDKKK------LYECLDSFHKKEQLK-DFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLL 369
Cdd:pfam00443 140 ETF-EPFSDLSLPIPGDSAelktasLQICFLQFSKLEELDdEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 370 NgSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKvpdiiYELIGIVSHKGTVNEGHYIAFCK-ISGGQWFKFNDSMVS 448
Cdd:pfam00443 219 S-TWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD-----YRLVAVVVHSGSLSSGHYIAYIKaYENNRWYKFDDEKVT 292
|
330
....*....|....*...
gi 6323879 449 SISQE-EVLKEQAYLLFY 465
Cdd:pfam00443 293 EVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
137-465 |
5.87e-75 |
|
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: 237.56 E-value: 5.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 137 SGLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVrsPDKCFSCALDKIVhelygalntKQASSSSTSTNRQTGF 216
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN--EGFCMMCALEAHV---------ERALASSGPGSAPRIF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 217 IYLLTCawkINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLPNAKEVSRAnnKQCECIVHTVFEGSLESSIVCPGCQNNS 296
Cdd:cd02661 71 SSNLKQ---ISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPS--SQETTLVQQIFGGYLRSQVKCLNCKHVS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 297 KTTiDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEhllNGSNRK 375
Cdd:cd02661 146 NTY-DPFLDLSLDIKGADSLEDALEQFTKPEQLDGENkYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS---NFRGGK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 376 LDDFIEFPTYLNMKNYCStkekdkhseNGKVPDIIYELIGIVSHKGTVNE-GHYIAFCKISGGQWFKFNDSMVSSISQEE 454
Cdd:cd02661 222 INKQISFPETLDLSPYMS---------QPNDGPLKYKLYAVLVHSGFSPHsGHYYCYVKSSNGKWYNMDDSKVSPVSIET 292
|
330
....*....|.
gi 6323879 455 VLKEQAYLLFY 465
Cdd:cd02661 293 VLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
138-465 |
3.85e-67 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 215.81 E-value: 3.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNpyfirhsmsqihsnnckvrspdkcfscaldkivhelygalntkqasssststnrqtgfi 217
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 ylltcawkinqnlagysQQDAHEFWQFIINQIHQSYvldlpNAKEVSRANNKQCECIVHTVFEGSLESSIVCPGCQNNSK 297
Cdd:cd02257 22 -----------------QQDAHEFLLFLLDKLHEEL-----KKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 298 TTI-DPFLDLSLDIKD--KKKLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGSNR 374
Cdd:cd02257 80 STEpELFLSLPLPVKGlpQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKE 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 375 KLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVpdiIYELIGIVSHKGT-VNEGHYIAFCK-ISGGQWFKFNDSMVSSISQ 452
Cdd:cd02257 160 KLNTKVSFPLELDLSPYLSEGEKDSDSDNGSY---KYELVAVVVHSGTsADSGHYVAYVKdPSDGKWYKFNDDKVTEVSE 236
|
330
....*....|....*...
gi 6323879 453 EEVLKE-----QAYLLFY 465
Cdd:cd02257 237 EEVLEFgslssSAYILFY 254
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
135-465 |
1.77e-59 |
|
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: 198.25 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 135 GLSGLINMGSTCFMSSILQCLIHNPYFiRHSMSQIHSNNCKvrSPDKCFSCALDKIVHELygalntkQASSSSTSTNRQT 214
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEF-RNAVYSIPPTEDD--DDNKSVPLALQRLFLFL-------QLSESPVKTTELT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 215 GFIYllTCAWKInqnLAGYSQQDAHEFWQFIINQIHQSyvldLPNAKEvsrannkqcECIVHTVFEGSLESSIVCPGCQN 294
Cdd:cd02659 71 DKTR--SFGWDS---LNTFEQHDVQEFFRVLFDKLEEK----LKGTGQ---------EGLIKNLFGGKLVNYIICKECPH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 295 NSkTTIDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEH-LLNGS 372
Cdd:cd02659 133 ES-EREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNkYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdFETMM 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 373 NRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVPDI--IYELIGIVSHKGTVNEGHYIAFCK-ISGGQWFKFNDSMVSS 449
Cdd:cd02659 212 RIKINDRFEFPLELDMEPYTEKGLAKKEGDSEKKDSEsyIYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVTP 291
|
330 340 350
....*....|....*....|....*....|....*...
gi 6323879 450 ISQEEVLKEQ----------------------AYLLFY 465
Cdd:cd02659 292 FDPNDAEEECfggeetqktydsgprafkrttnAYMLFY 329
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-466 |
3.65e-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: 175.94 E-value: 3.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNpyfirhsmsqihsnnckvrspdkcfscaldkivhelygalntkqasssststnrqtgfi 217
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 ylltcawkinqnlagysQQDAHEFWQFIINQIHqSYVLDLpnakevsrannkqcecivhtvFEGSLESSIVCPGCQNNSk 297
Cdd:cd02674 22 -----------------QQDAQEFLLFLLDGLH-SIIVDL---------------------FQGQLKSRLTCLTCGKTS- 61
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 298 TTIDPFLDLSLDIKDKK------KLYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLlN 370
Cdd:cd02674 62 TTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNaWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS-R 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 371 GSNRKLDDFIEFP-TYLNMKNYCSTKekdkhsenGKVPDIIYELIGIVSHKGTVNEGHYIAFCKIS-GGQWFKFNDSMVS 448
Cdd:cd02674 141 GSTRKLTTPVTFPlNDLDLTPYVDTR--------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNeTNDWYKFDDSRVT 212
|
330
....*....|....*...
gi 6323879 449 SISQEEVLKEQAYLLFYT 466
Cdd:cd02674 213 KVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-466 |
3.42e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 170.18 E-value: 3.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLihnpYFirhsmsqihsnnckvrspDKCFSCALDkivheLYGALNTKQASSSSTSTNRqtgFI 217
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL----YF------------------ENLLTCLKD-----LFESISEQKKRTGVISPKK---FI 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 YLLTcawKINQNLAGYSQQDAHEFWQFIINQIhQSYVLDLPNAKEVSRANNKQCEC-----IVHTVFEGSLESSIVCPGC 292
Cdd:cd02663 51 TRLK---RENELFDNYMHQDAHEFLNFLLNEI-AEILDAERKAEKANRKLNNNNNAepqptWVHEIFQGILTNETRCLTC 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 293 QNNSKTTiDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLN- 370
Cdd:cd02663 127 ETVSSRD-ETFLDLSIDVEQNTSITSCLRQFSATETLCGRNkFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 371 GSNRKLDDFIEFPTYLNMKNYCSTKEKdkhsengkvPDIIYELIGIVSHKG-TVNEGHYIAFCKISGGqWFKFNDSMVSS 449
Cdd:cd02663 206 NRYIKLFYRVVFPLELRLFNTTDDAEN---------PDRLYELVAVVVHIGgGPNHGHYVSIVKSHGG-WLLFDDETVEK 275
|
330 340
....*....|....*....|....*
gi 6323879 450 ISQEEVLK--------EQAYLLFYT 466
Cdd:cd02663 276 IDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-465 |
8.71e-44 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 155.24 E-value: 8.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPyfIRHSMSQihsnnckvRSPDKCFSCaldkivhelygalntkqasssststnrqtgfi 217
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP--ALRELLS--------ETPKELFSQ-------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 yllTCAWKINqnLAGYSQQDAHEFWQfiinqihqsYVLDLPNAkevsrannkqcecIVHTVFEGSLESSIVCPGCQNNSK 297
Cdd:cd02667 39 ---VCRKAPQ--FKGYQQQDSHELLR---------YLLDGLRT-------------FIDSIFGGELTSTIMCESCGTVSL 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 298 TtIDPFLDLSL----DIKDKKKLYECLDSFHKKEQLKDFNYHCgeCNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGSN 373
Cdd:cd02667 92 V-YEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFA--CENCTKAKKQYLISKLPPVLVIHLKRFQQPRSANL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 374 RKLDDFIEFPTYLNMKNYCSTKEkdKHSENGKvpDIIYELIGIVSHKGTVNEGHYIAFCK-------------------- 433
Cdd:cd02667 169 RKVSRHVSFPEILDLAPFCDPKC--NSSEDKS--SVLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaade 244
|
330 340 350
....*....|....*....|....*....|....
gi 6323879 434 --ISGGQWFKFNDSMVSSISQEEVLKEQAYLLFY 465
Cdd:cd02667 245 agPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-450 |
1.90e-42 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 152.96 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPYFiRHSMSQIHSN---NCKVRSPDKCFSCalDKIVHELygALNTKQASSSSTSTNRQT 214
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEF-RKAVYECNSTedaELKNMPPDKPHEP--QTIIDQL--QLIFAQLQFGNRSVVDPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 215 GFIYLLtcawkinqNLAGYSQQDAHEFWQFIINQIhqsyvldlpnAKEVSRANNKQCECIVHTVFEGSLESSIVCPGCQN 294
Cdd:cd02668 76 GFVKAL--------GLDTGQQQDAQEFSKLFLSLL----------EAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 295 NSKTTiDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFE-HLLNGS 372
Cdd:cd02668 138 ESSLP-SKFYELELQLKGHKTLEECIDEFLKEEQLTGDNqYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfDRKTGA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 373 NRKLDDFIEFPTYLNMKNYCSTKEKDKHsengkvpdiIYELIGIVSHKGT-VNEGHYIA-FCKISGGQWFKFNDSMVSSI 450
Cdd:cd02668 217 KKKLNASISFPEILDMGEYLAESDEGSY---------VYELSGVLIHQGVsAYSGHYIAhIKDEQTGEWYKFNDEDVEEM 287
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-465 |
1.67e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 142.08 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALNTKQASSSSTSTNRQTGfi 217
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLKSENDPYQVG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 yLLTCAWK--INQNLAGYS---QQDAHEFWQFIINQIHQSYVLDL---PNakevsrannkqcecivhTVFEGSLESSIVC 289
Cdd:cd02658 79 -IKPSMFKalIGKGHPEFStmrQQDALEFLLHLIDKLDRESFKNLglnPN-----------------DLFKFMIEDRLEC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 290 PGCqNNSKTTIDPFLDLSLDI--------KDKKKLY------ECLDSFHKKEQLKDFnyhCGECNSTQDAIKQLGIHKLP 355
Cdd:cd02658 141 LSC-KKVKYTSELSEILSLPVpkdeatekEEGELVYepvpleDCLKAYFAPETIEDF---CSTCKEKTTATKTTGFKTFP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 356 SVLVLQLKRFEHLLNGSNRKLDDFIEfptylnmknycstkekdkhsengkVPDII----YELIGIVSHKGT-VNEGHYIA 430
Cdd:cd02658 217 DYLVINMKRFQLLENWVPKKLDVPID------------------------VPEELgpgkYELIAFISHKGTsVHSGHYVA 272
|
330 340 350
....*....|....*....|....*....|....*...
gi 6323879 431 FCK--ISG-GQWFKFNDSMVSSISQEEVLKEQAYLLFY 465
Cdd:cd02658 273 HIKkeIDGeGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
138-465 |
4.87e-33 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 126.46 E-value: 4.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNpyfirhsmsqihsnnckvrSPdkcfscALDKIVHELYGALNT-KQASSSSTSTNRQTGF 216
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALY-------------------LP------KLDELLDDLSKELKVlKNVIRKPEPDLNQEEA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 217 IYLLTCAW-----KINQNLAGYSQQDAHEFWQFIINQIhqsyvlDLPNAKEVSRAnnkqceciVHTVFEgslessivcpg 291
Cdd:COG5533 56 LKLFTALWsskehKVGWIPPMGSQEDAHELLGKLLDEL------KLDLVNSFTIR--------IFKTTK----------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 292 cqNNSKTTIDPFLDLSLD------IKDKKKLYECLDSFhkKEQLKDfnyHCGECNSTQDAIK-------QLGIHKLPSVL 358
Cdd:COG5533 111 --DKKKTSTGDWFDIIIElpdqtwVNNLKTLQEFIDNM--EELVDD---ETGVKAKENEELEvqakqeyEVSFVKLPKIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 359 VLQLKRFEHllNGSNRKLDDFIEFPTYLNMKnycstkeKDKHSENgkVPDIIYELIGIVSHKGTVNEGHYIAFCKIsGGQ 438
Cdd:COG5533 184 TIQLKRFAN--LGGNQKIDTEVDEKFELPVK-------HDQILNI--VKETYYDLVGFVLHQGSLEGGHYIAYVKK-GGK 251
|
330 340 350
....*....|....*....|....*....|
gi 6323879 439 WFKFNDSMVSSISQEEVLK---EQAYLLFY 465
Cdd:COG5533 252 WEKANDSDVTPVSEEEAINekaKNAYLYFY 281
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
135-458 |
1.01e-28 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 120.36 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 135 GLSGLINMGSTCFMSSILQCLIHNPYFiRHSMSQIHSNNckvRSPDKCFSCALDKIVHELygalNTKQASSSSTSTNRQT 214
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKF-RKDVYGIPTDH---PRGRDSVALALQRLFYNL----QTGEEPVDTTELTRSF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 215 GfiylltcaWkinQNLAGYSQQDAHEFwqfiiNQIHQSyvlDLPNAKEVSRANNKqceciVHTVFEGSLESSIVCPGcQN 294
Cdd:COG5077 264 G--------W---DSDDSFMQHDIQEF-----NRVLQD---NLEKSMRGTVVENA-----LNGIFVGKMKSYIKCVN-VN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 295 NSKTTIDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEH-LLNGSN 373
Cdd:COG5077 319 YESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYdFERDMM 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 374 RKLDDFIEFPTYLNMKNYCStKEKDKhSENgkvPDIIYELIGIVSHKGTVNEGHYIAFCKIS-GGQWFKFNDSMVSSISQ 452
Cdd:COG5077 399 VKINDRYEFPLEIDLLPFLD-RDADK-SEN---SDAVYVLYGVLVHSGDLHEGHYYALLKPEkDGRWYKFDDTRVTRATE 473
|
....*.
gi 6323879 453 EEVLKE 458
Cdd:COG5077 474 KEVLEE 479
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-465 |
1.70e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 112.20 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKcfscaldKIVHELYGALNTKQASSSSTST----NRQ 213
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMK-------KLQLLQAHLMHTQRRAEAPPDYfleaSRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 214 TGFiylltcawkinqnLAGYsQQDAHEFWQFIINQIHQsyvldlpnakevsrannkqcecIVHTVFEGSLESSIVCPGCQ 293
Cdd:cd02664 74 PWF-------------TPGS-QQDCSEYLRYLLDRLHT----------------------LIEKMFGGKLSTTIRCLNCN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 294 NNSKTTiDPFLDLSLDIKDKKKLyecLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLN-G 371
Cdd:cd02664 118 STSART-ERFRDLDLSFPSVQDL---LNYFLSPEKLTGDNqYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKtH 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 372 SNRKLDDFIEFPTYLNMKNYCSTK----------EKDKHSENGKVPDIIYELIGIVSHKGTVNE-GHYIAF--------- 431
Cdd:cd02664 194 VREKIMDNVSINEVLSLPVRVESKssesplekkeEESGDDGELVTRQVHYRLYAVVVHSGYSSEsGHYFTYardqtdads 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 6323879 432 ------------CKISGGQWFKFNDSMVSSISQEEVL-------KEQAYLLFY 465
Cdd:cd02664 274 tgqecpepkdaeENDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
316-465 |
2.05e-27 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 116.14 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 316 LYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLlNGSNRKLDDFIEFP-TYLNMKNYCS 393
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDsWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV-RSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323879 394 TKEKdkhsengkvPDIIYELIGIVSHKGTVNEGHYIAFCK-ISGGQWFKFNDSMVSSISQEEVLKEQAYLLFY 465
Cdd:COG5560 756 MVDD---------PRLIYDLYAVDNHYGGLSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-465 |
6.08e-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: 110.11 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPyfirhSMSQIHSNNCKVRSPDkcfSCALDKIVHELYGALNTKqasssSTSTNRQTGFI 217
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVP-----ELRDALKNYNPARRGA---NQSSDNLTNALRDLFDTM-----DKKQEPVPPIE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 YLLTCAWKINQ-----NLAGYSQQDAHEFWQFIINQIHQSYVLDLPNAKEVSRannkqcecivhtVFEGSLESSIVCPGC 292
Cdd:cd02657 68 FLQLLRMAFPQfaekqNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSFIDQ------------LFGIELETKMKCTES 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 293 QNNSKTTIDPFLDLSLDIKDKKKLYECLDSFHK--KEQLKDFNYHCGecnstQDAI--KQLGIHKLPSVLVLQLKRFEHL 368
Cdd:cd02657 136 PDEEEVSTESEYKLQCHISITTEVNYLQDGLKKglEEEIEKHSPTLG-----RDAIytKTSRISRLPKYLTVQFVRFFWK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 369 LN-GSNRKLDDFIEFPTYLNMKNYCStkekdkhsengkvPDIIYELIGIVSHKG-TVNEGHYIAFCKISG-GQWFKFNDS 445
Cdd:cd02657 211 RDiQKKAKILRKVKFPFELDLYELCT-------------PSGYYELVAVITHQGrSADSGHYVAWVRRKNdGKWIKFDDD 277
|
330 340
....*....|....*....|....*..
gi 6323879 446 MVSSISQEEVLK-------EQAYLLFY 465
Cdd:cd02657 278 KVSEVTEEDILKlsgggdwHIAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-465 |
4.77e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 108.06 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 123 TKTMVPSMerrdglSGLINMGSTCFMSSILQCLIHNPYF---IRHSMSQIHSNNckvrspDKCFSCALDkivHELYGALN 199
Cdd:cd02671 17 KRENLLPF------VGLNNLGNTCYLNSVLQVLYFCPGFkhgLKHLVSLISSVE------QLQSSFLLN---PEKYNDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 200 TKQASSSststnrqtgfiyLLTCAWKINQNLAGYSQQDAHEFWQFIINQIhQSYVLDLPNAKEVSRANNKQCECIVHTVf 279
Cdd:cd02671 82 ANQAPRR------------LLNALREVNPMYEGYLQHDAQEVLQCILGNI-QELVEKDFQGQLVLRTRCLECETFTERR- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 280 EGSLESSIvcPgCQNNSKTTIDPFLDLSLDIK-DKKKLYECLDSFHKKEQLKDFN-YHCGECNSTQDAIKQLGIHKLPSV 357
Cdd:cd02671 148 EDFQDISV--P-VQESELSKSEESSEISPDPKtEMKTLKWAISQFASVERIVGEDkYFCENCHHYTEAERSLLFDKLPEV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 358 LVLQLKRF-----EHLLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDkhsengkvpdiIYELIGIVSHKG-TVNEGHYIAF 431
Cdd:cd02671 225 ITIHLKCFaangsEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKND-----------VYRLFAVVMHSGaTISSGHYTAY 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 6323879 432 CKisggqWFKFNDSMVSSISQEEVLK---------EQAYLLFY 465
Cdd:cd02671 294 VR-----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-465 |
2.34e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 101.29 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQCLIHNPYFIRHsmsqihsnnckvrspdkcfscaLDKIVhelygalntkqasssststnrqtgfi 217
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY----------------------LEEFL-------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 218 ylltcawkinqnlagySQQDAHEFWQFIINQIHQSYVldlpnakevsrannkqcecivhTVFEGSLESSIVCPGCQNNSK 297
Cdd:cd02662 33 ----------------EQQDAHELFQVLLETLEQLLK----------------------FPFDGLLASRIVCLQCGESSK 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 298 TTIDPFLDLSLDIKDKK-----KLYECLDSFHKKEQLKDfnYHCGECnstqdaikQLGIHKLPSVLVLQLKRFEHLLNGS 372
Cdd:cd02662 75 VRYESFTMLSLPVPNQSsgsgtTLEHCLDDFLSTEIIDD--YKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGT 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 373 NRKLDDFIEFPTYLnmknycstkekdkhsengkvPDIIYELIGIVSHKGTVNEGHYIAF--------------------- 431
Cdd:cd02662 145 STKNSCKVSFPERL--------------------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreg 204
|
330 340 350
....*....|....*....|....*....|....*
gi 6323879 432 CKISGGQWFKFNDSMVSSISQEEVLKE-QAYLLFY 465
Cdd:cd02662 205 PSSTSHPWWRISDTTVKEVSESEVLEQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
129-310 |
3.46e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 84.55 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 129 SMERRDGLSGLINMGSTCFMSSILQCLIHNP----YFIRHSM-SQIHSNNckvrspDKCFSCALDKIVHELYGALNTKQA 203
Cdd:COG5560 258 SINKEAGTCGLRNLGNTCYMNSALQCLMHTWelrdYFLSDEYeESINEEN------PLGMHGSVASAYADLIKQLYDGNL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 204 SSSSTSTNRQTgfiylltcAWKINQNLAGYSQQDAHEFWQFIINQIHQ--SYVLDLP-----------------NAKEVS 264
Cdd:COG5560 332 HAFTPSGFKKT--------IGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlNRIIKKPytskpdlspgddvvvkkKAKECW 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6323879 265 RANNKQCECIVHTVFEGSLESSIVCPGCQNNSkTTIDPFLDLSLDI 310
Cdd:COG5560 404 WEHLKRNDSIITDLFQGMYKSTLTCPGCGSVS-ITFDPFMDLTLPL 448
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
225-465 |
3.45e-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: 66.40 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 225 KINQNLAGYSQQDAHEFWQF---IINQIHQS-YVLDLPNAKEVSRANNKQcecivhtVFEGSLESSIVCPGCQNNSkTTI 300
Cdd:cd02673 23 KINTEFDNDDQQDAHEFLLTlleAIDDIMQVnRTNVPPSNIEIKRLNPLE-------AFKYTIESSYVCIGCSFEE-NVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 301 DPFLDLSLDIKDKKKLYECLDSFHKKEQLKdFNYHCGECNStQDAIKQLGIHKLPSVLVLQLKRF-EHLLNGSNRKLDDF 379
Cdd:cd02673 95 DVGNFLDVSMIDNKLDIDELLISNFKTWSP-IEKDCSSCKC-ESAISSERIMTFPECLSINLKRYkLRIATSDYLKKNEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 380 IefptylnMKNYCSTKEKdkhsengkvpdiiYELIGIVSHKG-TVNEGHYIAFCKIS--GGQWFKFNDSMVSSISQEEVL 456
Cdd:cd02673 173 I-------MKKYCGTDAK-------------YSLVAVICHLGeSPYDGHYIAYTKELynGSSWLYCSDDEIRPVSKNDVS 232
|
250
....*....|..
gi 6323879 457 KE---QAYLLFY 465
Cdd:cd02673 233 TNarsSGYLIFY 244
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
137-447 |
4.63e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 66.53 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 137 SGLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNckvrSPDKCFSCALDKIVHELYGALNTK-QAS--SSSTSTNRQ 213
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATEC----LKEHCLLCELGFLFDMLEKAKGKNcQASnfLRALSSIPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 214 TGfiylltcawkiNQNLAGYSQQDAHE---------FWQFIINQIHQSYvldlpnakEVSRANNKQCECIVHTVFEGSLE 284
Cdd:pfam13423 77 AS-----------ALGLLDEDRETNSAislssliqsFNRFLLDQLSSEE--------NSTPPNPSPAESPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 285 SSIVCPGCQNNS-KTTIDPFLDLSLDIKDKKKLY--------ECLDSFHKKEQLKDFnyHCGECNSTQDAIKQLGIHKLP 355
Cdd:pfam13423 138 TTIRCSNCGHESvRESSTHVLDLIYPRKPSSNNKkppnqtfsSILKSSLERETTTKA--WCEKCKRYQPLESRRTVRNLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 356 SVLVLQLKRfehllngSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVpdiiYELIGIVSH-KGTVNEGHYIAFCKI 434
Cdd:pfam13423 216 PVLSLNAAL-------TNEEWRQLWKTPGWLPPEIGLTLSDDLQGDNEIVK----YELRGVVVHiGDSGTSGHLVSFVKV 284
|
330 340
....*....|....*....|.
gi 6323879 435 S--------GGQWFKFNDSMV 447
Cdd:pfam13423 285 AdseledptESQWYLFNDFLV 305
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
46-108 |
2.24e-11 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 59.20 E-value: 2.24e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323879 46 CGTCHeiNSGATFMCLQCGFCGCW--NHSHFLSHSKQIGHIFGINSNNGLLFCFKCEDYIGNIDL 108
Cdd:pfam02148 1 CSLCG--NTSNLWLCLTCGHVGCGryQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
235-465 |
3.36e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 65.03 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 235 QQDAHEFWQFIINQIHQSyvldlpnakevSRANNKQCECIVHTVFEGSLE--------------SSIVCPGCQNNSKTTI 300
Cdd:cd02669 207 QSDPVEFLSWLLNTLHKD-----------LGGSKKPNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKTSV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 301 DPFLDLSLDI------KDKK--------KLYECLDSFHKKEqlkdfnyhcgeCNSTQDAIKQLGIHKLPSVLVLQLKRFE 366
Cdd:cd02669 276 SPFLLLTLDLpppplfKDGNeeniipqvPLKQLLKKYDGKT-----------ETELKDSLKRYLISRLPKYLIFHIKRFS 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 367 HlLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKvpdiiYELIGIVSHKGTVNE-GHYIAF-CKISGGQWFKFND 444
Cdd:cd02669 345 K-NNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTK-----YNLVANIVHEGTPQEdGTWRVQlRHKSTNKWFEIQD 418
|
250 260
....*....|....*....|.
gi 6323879 445 SMVSSISQEEVLKEQAYLLFY 465
Cdd:cd02669 419 LNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
234-465 |
4.38e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 59.88 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 234 SQQDAHEFWQFIINQIHQSYVLDLPNAKEVSRANNKQCECIVHTVF-EGSLESSIVCpgcqnNSKTtidpFLDLSLDIKD 312
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLtEGVLEGKPFC-----NCET----FGQYPLQVNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 313 KKKLYECLDSF---HKKEQLKDFNyhcgECNSTQDAIKQlgihKLPSVLVLQLKRFeHLLNGSNRKLDDFIEFPTYLNmk 389
Cdd:cd02665 92 YGNLHECLEAAmfeGEVELLPSDH----SVKSGQERWFT----ELPPVLTFELSRF-EFNQGRPEKIHDKLEFPQIIQ-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 390 nycstkekdkhsengKVPdiiYELIGIVSHKGTVNEGHYIAFC-KISGGQWFKFNDSMVSSISQEEVLKE--------QA 460
Cdd:cd02665 161 ---------------QVP---YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSA 222
|
....*
gi 6323879 461 YLLFY 465
Cdd:cd02665 223 YCLMY 227
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
45-94 |
8.83e-10 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 54.29 E-value: 8.83e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6323879 45 KCGTCHEINSgaTFMCLQCGFCGCWNH--SHFLSHSKQIGHIFGINSNNGLL 94
Cdd:smart00290 1 RCSVCGTIEN--LWLCLTCGQVGCGRYqnGHALEHFEETGHPLVVKLGTQRV 50
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
353-465 |
1.79e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 49.06 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 353 KLPSVLVLQLKRFEhLLNGSNRKLDDFIEFPTYLNM----------KNYCSTKEKDKHSE---NGKVPDIIYELIGIVSH 419
Cdd:cd02670 97 KAPSCLIICLKRYG-KTEGKAQKMFKKILIPDEIDIpdfvaddpraCSKCQLECRVCYDDkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323879 420 KGT-VNEGHYIAFCKISGG------------QWFKFNDSMVSSISQEEV------LKEQAYLLFY 465
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDMADRDGVSNGFnipaarLLEDPYMLFY 240
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
304-466 |
4.78e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 44.81 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 304 LDLSLDIKDKKKLY---ECLDSFHKKEQlkDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGsnRKLDDFI 380
Cdd:cd02672 104 LSLPLGSTKTSKEStflQLLKRSLDLEK--VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVINLSVTNG--EFDDINV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 381 EFPTYLNMKNYCSTKEKD---KHSENGKVPDIIYELIGIVSH-KGTVNEGHYIAFCKISG-----GQWFKFNDSMVSSIS 451
Cdd:cd02672 180 VLPSGKVMQNKVSPKAIDhdkLVKNRGQESIYKYELVGYVCEiNDSSRGQHNVVFVIKVNeesthGRWYLFNDFLVTPVS 259
|
170
....*....|....*
gi 6323879 452 qeevlkEQAYLLFYT 466
Cdd:cd02672 260 ------ELAYILLYQ 268
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-465 |
2.56e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 138 GLINMGSTCFMSSILQclihnpYF-----IRHSMSQIHSNNckvrspdkcFSCALDKIVHELYGalnTKQASSSSTSTNR 212
Cdd:cd02666 3 GLDNIGNTCYLNSLLQ------YFftikpLRDLVLNFDESK---------AELASDYPTERRIG---GREVSRSELQRSN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 213 QtgFIYLL-----------TCAWKINQNLA--GYSQQDAHEFwqfIINQIHQ--------SYVLDLPNAKEVSRANNkqc 271
Cdd:cd02666 65 Q--FVYELrslfndlihsnTRSVTPSKELAylALRQQDVTEC---IDNVLFQlevalepiSNAFAGPDTEDDKEQSD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 272 ecIVHTVFEGSLESSIV--CPGCQNNSKTTIDPFLDLSLDIKDK----------KKLYECLDSFHKKEQLKD-----FNY 334
Cdd:cd02666 137 --LIKRLFSGKTKQQLVpeSMGNQPSVRTKTERFLSLLVDVGKKgreivvllepKDLYDALDRYFDYDSLTKlpqrsQVQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323879 335 HCGECNSTQDAIKQLGiHKLPSVLvlqlKRFEHLLNGSNRKLDDFIEfptylNMKNYCSTKEKDKHSENGKVPDIIYELI 414
Cdd:cd02666 215 AQLAQPLQRELISMDR-YELPSSI----DDIDELIREAIQSESSLVR-----QAQNELAELKHEIEKQFDDLKSYGYRLH 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323879 415 GIVSHKGTVNEGHYIAFCK-ISGGQWFKFNDSMVSSISQEEVLKE------QAYLLFY 465
Cdd:cd02666 285 AVFIHRGEASSGHYWVYIKdFEENVWRKYNDETVTVVPASEVFLFtlgntaTPYFLVY 342
|
|
| |
