|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
175-474 |
2.99e-143 |
|
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: 420.14 E-value: 2.99e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 175 GAGLWNLGNSCFLNSVFQCFTHTVPLIESLLSFRYEVpcHCGNEFFCVIRAIRYHIEAALRPERCPIAPYFFFDNLNYFS 254
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSK--DCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 255 PDFQRYQQEDAHEFLQAFLEKLEICGSDR--------TSFRGDITSQDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEI 326
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLDAMQKACLDRfkklkavdPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 327 EDVDTLGSALESFTRVEKLDEQLT--CDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNglYMEKIYKHVKIPLEIDLQP 404
Cdd:cd02661 159 KGADSLEDALEQFTKPEQLDGENKykCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RGGKINKQISFPETLDLSP 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 405 YMRNIQENevSTKYHLYALVEHFGYSVAYGHYSSYVRSAPKIWHHFDDSKVTRIDEDMVLSQDSYILFYA 474
Cdd:cd02661 237 YMSQPNDG--PLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
176-473 |
7.42e-83 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 264.69 E-value: 7.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 176 AGLWNLGNSCFLNSVFQCFTHTVPLIESLLSFRYEVPCHCGNEFFCVIRAIRYHIEAAL-RPERCPIAPYFFFDNLNYFS 254
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 255 PDFQRYQQEDAHEFLQAFLEKLEICGSDRTSFRGDITSQDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEIEDVDTLGS 334
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 335 ------ALESFTRVEKL--DEQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLYMEKIYKHVKIPLEIDLQPYM 406
Cdd:pfam00443 161 taslqiCFLQFSKLEELddEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18414985 407 -RNIQENEV-STKYHLYALVEHFGySVAYGHYSSYVRSAPK-IWHHFDDSKVTRIDEDM-VLSQDSYILFY 473
Cdd:pfam00443 241 aEELKPKTNnLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
177-473 |
5.15e-56 |
|
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: 191.54 E-value: 5.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHtvpliesllsfryevpchcgneffcvirairyhieaalrpercpiapyfffdnlnyfspd 256
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 257 fqryQQEDAHEFLQAFLEKLEIC---GSDRTSFRGDITS--QDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEIEDVD- 330
Cdd:cd02257 21 ----EQQDAHEFLLFLLDKLHEElkkSSKRTSDSSSLKSliHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGl 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 331 ---TLGSALESFTRVEKLDEQlTCDNCN--EKVSKEKQLLLDKLPLVATFHLKRFK-NNGLYMEKIYKHVKIPLEIDLQP 404
Cdd:cd02257 97 pqvSLEDCLEKFFKEEILEGD-NCYKCEkkKKQEATKRLKIKKLPPVLIIHLKRFSfNEDGTKEKLNTKVSFPLELDLSP 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18414985 405 YM----RNIQENEVSTKYHLYALVEHFGYSVAYGHYSSYVRSAPK-IWHHFDDSKVTRIDEDMVL-----SQDSYILFY 473
Cdd:cd02257 176 YLsegeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDgKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
8.25e-54 |
|
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: 187.97 E-value: 8.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLLSFRYEVPCHCGNEFFCVIRAIRYHIEAALRPE-RCPIAPYfffdNLNYFSP 255
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGdRSPYGPI----NLLYLSW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 256 DFQR----YQQEDAHEFLQAFLEKL-EICGSDRTSFRGD-----ITSQdVFSGRLISGLRCCNCDYVSETYEKSVGLSLE 325
Cdd:cd02660 78 KHSRnlagYSQQDAHEFFQFLLDQLhTHYGGDKNEANDEshcncIIHQ-TFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 326 IEDVD---------------TLGSALESFTRVEKLDE-QLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLYM-E 388
Cdd:cd02660 157 IPNKStpswalgesgvsgtpTLSDCLDRFTRPEKLGDfAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTsR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 389 KIYKHVKIPLEIDLQPYMRNI-------QENEVSTKYHLYALVEHFGySVAYGHYSSYVRSAPKIWHHFDDSKVTRIDED 461
Cdd:cd02660 237 KIDTYVQFPLELNMTPYTSSSigdtqdsNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEE 315
|
330
....*....|..
gi 18414985 462 MVLSQDSYILFY 473
Cdd:cd02660 316 EVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
6.12e-51 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 178.35 E-value: 6.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTvPLIESLLSFRyevpchcgneffcvirairyhieaalrpercpiaPYFFFDNLNYFSPD 256
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQT-PALRELLSET----------------------------------PKELFSQVCRKAPQ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 257 FQRYQQEDAHEFLQAFLEKLeicgsdrtsfrgdITSQD-VFSGRLISGLRCCNCDYVSETYEKSVGLSL----EIEDVDT 331
Cdd:cd02667 46 FKGYQQQDSHELLRYLLDGL-------------RTFIDsIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 332 LGSALESFTRVEKLDEQ--LTCDNCNEKVskeKQLLLDKLPLVATFHLKRFKNNGLY-MEKIYKHVKIPLEIDLQPYM-- 406
Cdd:cd02667 113 IESCLKQFTEVEILEGNnkFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSAnLRKVSRHVSFPEILDLAPFCdp 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 407 -RNIQENEVSTKYHLYALVEHFGySVAYGHYSSYVRSAPK----------------------IWHHFDDSKVTRIDEDMV 463
Cdd:cd02667 190 kCNSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPPqqrlsdltkskpaadeagpgsgQWYYISDSDVREVSLEEV 268
|
330
....*....|
gi 18414985 464 LSQDSYILFY 473
Cdd:cd02667 269 LKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
6.63e-47 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 165.92 E-value: 6.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHtvpliesllsfryevpchcgneffcvirairyhieaalrpercpiapyfffdnlnyfspd 256
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 257 fqryQQEDAHEFLQAFLEKLEicgsdrtSFrgdITsqDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEIEDVD------ 330
Cdd:cd02674 21 ----DQQDAQEFLLFLLDGLH-------SI---IV--DLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkv 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 331 TLGSALESFTRVEKLD--EQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLYMEKIYKHVKIPLEI-DLQPYMR 407
Cdd:cd02674 85 TLEDCLRLFTKEETLDgdNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDlDLTPYVD 164
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18414985 408 NIQENEVsTKYHLYALVEHFGySVAYGHYSSYVRSAPK-IWHHFDDSKVTRIDEDMVLSQDSYILFY 473
Cdd:cd02674 165 TRSFTGP-FKYDLYAVVNHYG-SLNGGHYTAYCKNNETnDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
1.94e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 141.68 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHtvpliESLLSfryevpchCGNEFFCVIRAIRYHIEAalrpercpIAPYFFFDNLNYFSPD 256
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT--------CLKDLFESISEQKKRTGV--------ISPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 257 FQRYQQEDAHEFLQAFLEKL-EICGSDRTSFRGDITS-------------QDVFSGRLISGLRCCNCDYVSETYEKSVGL 322
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIaEILDAERKAEKANRKLnnnnnaepqptwvHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 323 SLEIEDVDTLGSALESFTRVEKL--DEQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKnnglYMEKIYKHVKIPLEI 400
Cdd:cd02663 140 SIDVEQNTSITSCLRQFSATETLcgRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK----YDEQLNRYIKLFYRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 401 DLQPYMRNIQENEVSTK----YHLYALVEHFGYSVAYGHYSSYVRSApKIWHHFDDSKVTRIDEDMVL-------SQDS- 468
Cdd:cd02663 216 VFPLELRLFNTTDDAENpdrlYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKIDENAVEeffgdspNQATa 294
|
....*
gi 18414985 469 YILFY 473
Cdd:cd02663 295 YVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-476 |
8.43e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 140.86 E-value: 8.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLLSF--------RYEVPCHCGNEFfcvirairyhIEAALRPERC----PIAPY 244
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIppteddddNKSVPLALQRLF----------LFLQLSESPVktteLTDKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 245 FFFDN--LNYFspdfqryQQEDAHEFLQAFLEKLEICgSDRTSFRGDItsQDVFSGRLISGLRCCNCDYVSETYEKSVGL 322
Cdd:cd02659 74 RSFGWdsLNTF-------EQHDVQEFFRVLFDKLEEK-LKGTGQEGLI--KNLFGGKLVNYIICKECPHESEREEYFLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 323 SLEIEDVDTLGSALESFTRVEKLD--EQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLYME--KIYKHVKIPL 398
Cdd:cd02659 144 QVAVKGKKNLEESLDAYVQGETLEgdNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMriKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 399 EIDLQPYM---------RNIQENEVSTKYHLYALVEHFGySVAYGHYSSYVRSAPK-IWHHFDDSKVTRIDEDMVLSQD- 467
Cdd:cd02659 224 ELDMEPYTekglakkegDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDgKWYKFNDDVVTPFDPNDAEEECf 302
|
330 340 350
....*....|....*....|....*....|
gi 18414985 468 ---------------------SYILFYARE 476
Cdd:cd02659 303 ggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-474 |
6.32e-31 |
|
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: 123.85 E-value: 6.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 176 AGLWNLGNSCFLNSVFQC------FTHTVPLIESLLSFRYEVpchcgnEFFCVIRAIRYHIEAALRPERCpiapyfFFDN 249
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVlyfcpgFKHGLKHLVSLISSVEQL------QSSFLLNPEKYNDELANQAPRR------LLNA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 250 LNYFSPDFQRYQQEDAHEFLQAFLekleicGSDRTSFRGDitsqdvFSGRLISGLRCCNCDYVSETYEKSVGLSLEIE-- 327
Cdd:cd02671 93 LREVNPMYEGYLQHDAQEVLQCIL------GNIQELVEKD------FQGQLVLRTRCLECETFTERREDFQDISVPVQes 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 328 -----------------DVDTLGSALESFTRVEKL--DEQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLY-- 386
Cdd:cd02671 161 elskseesseispdpktEMKTLKWAISQFASVERIvgEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEfd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 387 ----MEKIYKHVKIPLEIDLQPYmrniQENEVSTKYHLYALVEHFGYSVAYGHYSSYVRsapkiWHHFDDSKV---TRID 459
Cdd:cd02671 241 cyggLSKVNTPLLTPLKLSLEEW----STKPKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvtEEKD 311
|
330 340
....*....|....*....|.
gi 18414985 460 EDMVLSQDS------YILFYA 474
Cdd:cd02671 312 FLEALSPNTsststpYLLFYK 332
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-459 |
1.68e-28 |
|
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: 116.75 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLlsfrYEVPCHCGNEFFCVIRAIRYHIEAALRPERcpiapYFF----FDNLNY 252
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAV----YECNSTEDAELKNMPPDKPHEPQTIIDQLQ-----LIFaqlqFGNRSV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 253 FSPD-------FQRYQQEDAHEFLQAFLEKLEICGSDRTSFRGDITSQDVFSGRLISGLRCCNCDYVSETYEKSVGLSLE 325
Cdd:cd02668 72 VDPSgfvkalgLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 326 IEDVDTLGSALESFTRVEKL--DEQLTCDNCNEKVSKEKQLLLDKLPLVATFHLKR--FKNNGLYMEKIYKHVKIPLEID 401
Cdd:cd02668 152 LKGHKTLEECIDEFLKEEQLtgDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18414985 402 LQPYMrnIQENEVSTKYHLYALVEHFGYSVAYGHYSSYVR-SAPKIWHHFDDSKVTRID 459
Cdd:cd02668 232 MGEYL--AESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMP 288
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
4.97e-28 |
|
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: 115.11 E-value: 4.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLLSFRYEVPCHC---GNEFFCVIRAI-------RYHIEAALRPERCP----IA 242
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVvdpANDLNCQLIKLadgllsgRYSKPASLKSENDPyqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 243 PYFFFDNLNYFSPDFQRYQQEDAHEFLQAFLEKLeicgsDRTSF-RGDITSQDVFSGRLISGLRCCNCDYVSETYEKSVG 321
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKL-----DRESFkNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 322 LSLEIEDVD--------------TLGSALESFTRVEKLDEqlTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKnnglyM 387
Cdd:cd02658 156 LSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIED--FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ-----L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 388 EKIYKHVKIPLEIDlqpymrnIQENEVSTKYHLYALVEHFGYSVAYGHYSSYVRSAPKI---WHHFDDSKVTRIDEDMVL 464
Cdd:cd02658 229 LENWVPKKLDVPID-------VPEELGPGKYELIAFISHKGTSVHSGHYVAHIKKEIDGegkWVLFNDEKVVASQDPPEM 301
|
....*....
gi 18414985 465 SQDSYILFY 473
Cdd:cd02658 302 KKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
177-475 |
6.10e-27 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 111.05 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLL---SFRYEVpchcgneffcVIRAIRYHiEAALRPERcpiAPYFF----FDN 249
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLddlSKELKV----------LKNVIRKP-EPDLNQEE---ALKLFtalwSSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 250 LNYFSPDFQRYQQEDAHEFLQAFLEKLEI----CGSDRTSFrgdITSQDVFSGrlISGLrccNCDYVSETYEKSVGLSLE 325
Cdd:COG5533 67 EHKVGWIPPMGSQEDAHELLGKLLDELKLdlvnSFTIRIFK---TTKDKKKTS--TGDW---FDIIIELPDQTWVNNLKT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 326 IED-VDTLGSALESFTRV-EKLDEQLTCDNCNEKVSKEKqllldKLPLVATFHLKRFKNNGLYmEKIYKHVKIPLEIDLQ 403
Cdd:COG5533 139 LQEfIDNMEELVDDETGVkAKENEELEVQAKQEYEVSFV-----KLPKILTIQLKRFANLGGN-QKIDTEVDEKFELPVK 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18414985 404 PymRNIQENEVSTKYHLYALVEHFGySVAYGHYSSYVRSAPKiWHHFDDSKVTRIDEDMVLSQDS---YILFYAR 475
Cdd:COG5533 213 H--DQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVKKGGK-WEKANDSDVTPVSEEEAINEKAknaYLYFYER 283
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
3.18e-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: 100.87 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFtHTVP-LIESLLSFRYEVPCHCGNEFFCViRAIRyHIEAALRPERCPIAPYFFFDNLNYFSP 255
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL-RSVPeLRDALKNYNPARRGANQSSDNLT-NALR-DLFDTMDKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 256 DFQR------YQQEDAHE----FLQAFLEKLEICGSDRTSFrgditsQDVFSGRLISGLRCC-NCDYVSETYEKSVGLSL 324
Cdd:cd02657 78 QFAEkqnqggYAQQDAEEcwsqLLSVLSQKLPGAGSKGSFI------DQLFGIELETKMKCTeSPDEEEVSTESEYKLQC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 325 EI---EDVDTLGSALEsftrvEKLDEQLT----CDNCNEKVSKEKQllLDKLPLVATFHLKRFknngLYME------KIY 391
Cdd:cd02657 152 HIsitTEVNYLQDGLK-----KGLEEEIEkhspTLGRDAIYTKTSR--ISRLPKYLTVQFVRF----FWKRdiqkkaKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 392 KHVKIPLEIDLQPYMRNiqenevSTKYHLYALVEHFGYSVAYGHYSSYVRSA-PKIWHHFDDSKVTRIDEDMVLSQD--- 467
Cdd:cd02657 221 RKVKFPFELDLYELCTP------SGYYELVAVITHQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSggg 294
|
330
....*....|
gi 18414985 468 ----SYILFY 473
Cdd:cd02657 295 dwhiAYILLY 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
8.93e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 99.87 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLLSfryEVPCHCGNEFFCVIRAIRYHIEAALRPERCPIAPYFFFDNLN--YFS 254
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS---LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRppWFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 255 PdfqRYQQeDAHEFLQAFLEKLeicgsdrtsfrgDITSQDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEiedVDTLGS 334
Cdd:cd02664 78 P---GSQQ-DCSEYLRYLLDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLS---FPSVQD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 335 ALESFTRVEKL--DEQLTCDNC--NEKVSKEKQLLldKLPLVATFHLKRFKNNGLYM--EKIYKHVKIPLEIDLQPY--- 405
Cdd:cd02664 139 LLNYFLSPEKLtgDNQYYCEKCasLQDAEKEMKVT--GAPEYLILTLLRFSYDQKTHvrEKIMDNVSINEVLSLPVRves 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 406 -----MRNIQENEVSTK---------YHLYALVEHFGYSVAYGHYSSYVRS---------------------APKIWHHF 450
Cdd:cd02664 217 kssesPLEKKEEESGDDgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendESKNWYLF 296
|
330 340 350
....*....|....*....|....*....|
gi 18414985 451 DDSKVTRID-EDM-----VLSQDS-YILFY 473
Cdd:cd02664 297 NDSRVTFSSfESVqnvtsRFPKDTpYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
6.69e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 95.13 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQcfthtvplieSLLSfryevpchcgneffcvirairyhieaalrpercpiapyfffdnlnyfSPD 256
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ----------ALAS-----------------------------------------------LPS 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 257 FQRY-----QQEDAHEFLQAFLEKLEIcgSDRTSFRGDITSQdvfsgrlisgLRCCNCDYVSE-TYEKSVGLSL-----E 325
Cdd:cd02662 24 LIEYleeflEQQDAHELFQVLLETLEQ--LLKFPFDGLLASR----------IVCLQCGESSKvRYESFTMLSLpvpnqS 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 326 IEDVDTLGSALESFTRVEKLDEqLTCDNCnekvskekQLLLDKLPLVATFHLKR--FKNNGLYMeKIYKHVKIPLEidLQ 403
Cdd:cd02662 92 SGSGTTLEHCLDDFLSTEIIDD-YKCDRC--------QTVIVRLPQILCIHLSRsvFDGRGTST-KNSCKVSFPER--LP 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 404 PYMrniqenevstkYHLYALVEHFGySVAYGHYSSYVRSAPKI---------------------WHHFDDSKVTRIDEDM 462
Cdd:cd02662 160 KVL-----------YRLRAVVVHYG-SHSSGHYVCYRRKPLFSkdkepgsfvrmregpsstshpWWRISDTTVKEVSESE 227
|
330
....*....|..
gi 18414985 463 VLSQ-DSYILFY 473
Cdd:cd02662 228 VLEQkSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
331-475 |
1.10e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 87.63 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 331 TLGSALESFTRVEKLDEQ--LTCDNCNEKVSKEKQLLLDKLPLVATFHLKRFKNNGLYMEKIYKHVKIPLEiDLQPYMRN 408
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSdsWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPID-DLDLSGVE 754
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414985 409 IQENEVSTKYHLYALVEHFGYsVAYGHYSSYVRSAPKI-WHHFDDSKVTRIDEDMVLSQDSYILFYAR 475
Cdd:COG5560 755 YMVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
177-469 |
1.44e-16 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 84.15 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQC--FTHtvpliesllSFR---YEVPCHCGNEFFCVIRAIRyHIEAALRPERCPIAPYFFFDNLN 251
Cdd:COG5077 195 GLRNQGATCYMNSLLQSlfFIA---------KFRkdvYGIPTDHPRGRDSVALALQ-RLFYNLQTGEEPVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 252 YfsPDFQRYQQEDAHEFLQAFLEKLEicgsdrTSFRGDITS---QDVFSGRLISGLRCCNCDYVSETYEKSVGLSLEIED 328
Cdd:COG5077 265 W--DSDDSFMQHDIQEFNRVLQDNLE------KSMRGTVVEnalNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 329 VDTLGSALESFTRVEKLDEQlTCDNCNEK--VSKEKQLLLDKLPLVATFHLKRFKNNGLY--MEKIYKHVKIPLEIDLQP 404
Cdd:COG5077 337 MKNLQESFRRYIQVETLDGD-NRYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYDFERdmMVKINDRYEFPLEIDLLP 415
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 405 YMRN--IQENEVSTKYHLYALVEHFGySVAYGHYSSYVRsaPKI---WHHFDDSKVTRIDEDMVLsQDSY 469
Cdd:COG5077 416 FLDRdaDKSENSDAVYVLYGVLVHSG-DLHEGHYYALLK--PEKdgrWYKFDDTRVTRATEKEVL-EENF 481
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
176-455 |
8.51e-10 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 60.75 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 176 AGLWNLGNSCFLNSVFQCFTHTVPLIESLLS-------------------FRYEV-----PCHCGNefFCviRAIRYHIE 231
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALShlateclkehcllcelgflFDMLEkakgkNCQASN--FL--RALSSIPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 232 AA---LRPERCPIAPYFFFDNL--NyfspdFQRYqqedaheflqaFLEKLEICGSDRTSFRGDITS--QDVFSGRLISGL 304
Cdd:pfam13423 77 ASalgLLDEDRETNSAISLSSLiqS-----FNRF-----------LLDQLSSEENSTPPNPSPAESplEQLFGIDAETTI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 305 RCCNCDYVSE----------TYEKSVGLSLEIEDVDTLGSALESFTRVEKLdEQLTCDNCNEKVSKEKQLLLDKLPLVAT 374
Cdd:pfam13423 141 RCSNCGHESVressthvldlIYPRKPSSNNKKPPNQTFSSILKSSLERETT-TKAWCEKCKRYQPLESRRTVRNLPPVLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 375 FHLKRFKNNGLYMEKiyKHVKIPLEIDLQPYMRNIQENEVsTKYHLYALVEHFGYSVAYGHYSSYVRSAPKI-------- 446
Cdd:pfam13423 220 LNAALTNEEWRQLWK--TPGWLPPEIGLTLSDDLQGDNEI-VKYELRGVVVHIGDSGTSGHLVSFVKVADSEledptesq 296
|
....*....
gi 18414985 447 WHHFDDSKV 455
Cdd:pfam13423 297 WYLFNDFLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
177-326 |
5.13e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 59.51 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLLSFRYEVPCHCGNEFFC---VIRAIRYHIEAALRPERCPIAPYFFFDNLNYF 253
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMhgsVASAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 254 SPDFQRYQQEDAHEFLQAFLEKL-----EICGSDRTS------------------------FRGDITSQDVFSGRLISGL 304
Cdd:COG5560 347 NEEFSGYDQQDSQEFIAFLLDGLhedlnRIIKKPYTSkpdlspgddvvvkkkakecwwehlKRNDSIITDLFQGMYKSTL 426
|
170 180
....*....|....*....|..
gi 18414985 305 RCCNCDYVSETYEKSVGLSLEI 326
Cdd:COG5560 427 TCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-473 |
2.85e-08 |
|
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: 56.56 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 177 GLWNLGNSCFLNSVFQCFTHTVPLIESLLSFR-YEVPCHCGNEFFCVI----------RAIRYHIeaalrpercpiAPYF 245
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnYENIKDRKSELVKRLselirkiwnpRNFKGHV-----------SPHE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 246 FfdnLNYFS----PDFQRYQQEDAHEFLQAFLEKLEICgSDRTSFRGDITSQDVFSGRL-ISGLRCCNcdyVSETYEKSV 320
Cdd:cd02669 190 L---LQAVSkvskKKFSITEQSDPVEFLSWLLNTLHKD-LGGSKKPNSSIIHDCFQGKVqIETQKIKP---HAEEEGSKD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 321 GLSLEIEDVDTLGS------------ALESFTRVEKLDEQLTC----DNCNEKVSKE-----KQLLLDKLPLVATFHLKR 379
Cdd:cd02669 263 KFFKDSRVKKTSVSpfllltldlpppPLFKDGNEENIIPQVPLkqllKKYDGKTETElkdslKRYLISRLPKYLIFHIKR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 380 FKNNGLYMEKIYKHVKIPLEI-DLQPYMRNIQENE-VSTKYHLYALVEHFGYSVAYGHYSSYVR-SAPKIWHHFDDSKVT 456
Cdd:cd02669 343 FSKNNFFKEKNPTIVNFPIKNlDLSDYVHFDKPSLnLSTKYNLVANIVHEGTPQEDGTWRVQLRhKSTNKWFEIQDLNVK 422
|
330
....*....|....*..
gi 18414985 457 RIDEDMVLSQDSYILFY 473
Cdd:cd02669 423 EVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
256-473 |
1.11e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 50.61 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 256 DFQRYQQEDAHEFLQAFLEKL-EICGSDRTS--FRGDITSQ----DVFSGRLISGLRCCNCDYvsETYEKSVGLSLEIED 328
Cdd:cd02673 27 EFDNDDQQDAHEFLLTLLEAIdDIMQVNRTNvpPSNIEIKRlnplEAFKYTIESSYVCIGCSF--EENVSDVGNFLDVSM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 329 VDTLGSALES-------FTRVEKldeqlTCDNCNEK--VSKEKqllLDKLPLVATFHLKRFKnnglYMEKIYKHVKIPLE 399
Cdd:cd02673 105 IDNKLDIDELlisnfktWSPIEK-----DCSSCKCEsaISSER---IMTFPECLSINLKRYK----LRIATSDYLKKNEE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18414985 400 IdLQPYMRNIqenevsTKYHLYALVEHFGYSVAYGHYSSYVRS--APKIWHHFDDSKVTRIDEDMVL---SQDSYILFY 473
Cdd:cd02673 173 I-MKKYCGTD------AKYSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
261-469 |
4.44e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 48.32 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 261 QQEDAHEFLQAFLEKLEIC-------GSDRTSFRGDITsqDVFSGRLIS-----GLRCCNCdyvsETYEKsvgLSLEIED 328
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAfqaaaeaISPGEKSKNPMV--QLFYGTFLTegvleGKPFCNC----ETFGQ---YPLQVNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 329 VDTLGSALESFTrVEKLDEQLTCDNCNEKVSKEkqlLLDKLPLVATFHLKRFKNNGLYMEKIYKHVKIPLEIDLQPymrn 408
Cdd:cd02665 92 YGNLHECLEAAM-FEGEVELLPSDHSVKSGQER---WFTELPPVLTFELSRFEFNQGRPEKIHDKLEFPQIIQQVP---- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18414985 409 iqenevstkYHLYALVEHFGYSVAyGHYSSYVRSAP-KIWHHFDDSKVTRIDEDMVlSQDSY 469
Cdd:cd02665 164 ---------YELHAVLVHEGQANA-GHYWAYIYKQSrQEWEKYNDISVTESSWEEV-ERDSF 214
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
352-473 |
1.74e-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: 46.75 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 352 DNCNEKVSKEKQLL--------LDKLPLVATFHLKRFKNNGLYMEKIYKHVKIPLEIDLQPYM--------------RNI 409
Cdd:cd02670 73 DDDDGGGITLEQCLeqyfnnsvFAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVaddpracskcqlecRVC 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 410 QENEVST------KYHLYALVEHFGYSVAYGHYSSYVRSAPKI------------WHHFDD-----SKVTRID-EDMVLS 465
Cdd:cd02670 153 YDDKDFSptcgkfKLSLCSAVCHRGTSLETGHYVAFVRYGSYSltetdneaynaqWVFFDDmadrdGVSNGFNiPAARLL 232
|
....*...
gi 18414985 466 QDSYILFY 473
Cdd:cd02670 233 EDPYMLFY 240
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
293-474 |
4.39e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 42.50 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 293 QDVFSGRLISGLRCCNCDYVSETYEKSVGL---SLEIEDVDTLGSALESFTRVEKLDEQlTCDNCNEKVSKEKQL----L 365
Cdd:cd02672 77 LETISQDQLGTPFSCGTSRNSVSLLYTLSLplgSTKTSKESTFLQLLKRSLDLEKVTKA-WCDTCCKYQPLEQTTsirhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414985 366 LDKLPLVATFHLKRFKNNGLYMEKIYKHVKI------PLEIDLqPYMRNIQENEVSTKYHLYALVEHFGYSVAYGHYSSY 439
Cdd:cd02672 156 PDILLLVLVINLSVTNGEFDDINVVLPSGKVmqnkvsPKAIDH-DKLVKNRGQESIYKYELVGYVCEINDSSRGQHNVVF 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18414985 440 VRSAPKI-----WHHFDDSKVTRIDEdmvlsqDSYILFYA 474
Cdd:cd02672 235 VIKVNEEsthgrWYLFNDFLVTPVSE------LAYILLYQ 268
|
|
| |
