|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
106-408 |
5.36e-169 |
|
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: 491.79 E-value: 5.36e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 106 GAGLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKYCHVAGFCALCAIQKHVRTARQANGRILAPKDLVSNLRCISRN 185
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 186 FRNCRQEDAHEYMINLLECMHKCSLPSGVPSESSD--AYRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDISK 263
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDpsSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 264 ADSLQRALSRFTAVELLDNGAKvYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRSEKIDRKVDFTSAIDMKPFVS 343
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENK-YKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18424054 344 GPHEGNLKYTLYGVLVHYGRSSHSGHYACFVRTSSGMWYSLDDNRVVQVSEKTVFNQKAYMLFYV 408
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
107-407 |
1.44e-75 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 248.90 E-value: 1.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 107 AGLQNLGNTCFLNSVLQCLTYTEPLA-ATLQTAAHQKYCHVAGFCAL-CAIQKHVRTAR-QANGRILAPKDLVSNLRCIS 183
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRdYLLRISPLSEDSRYNKDINLlCALRDLFKALQkNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 184 RNFRNCRQEDAHEYMINLLECMHkCSLPSGVPSESSdayrrSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDI-- 261
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENE-----SLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIpg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 262 ----SKADSLQRALSRFTAVELLDNGAKVYqCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRS--EKIDRKVDFTSA 335
Cdd:pfam00443 155 dsaeLKTASLQICFLQFSKLEELDDEEKYY-CDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRStwEKLNTEVEFPLE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18424054 336 IDMKPFVSGP----HEGNLKYTLYGVLVHYGrSSHSGHYACFVR-TSSGMWYSLDDNRVVQVS-EKTVFNQKAYMLFY 407
Cdd:pfam00443 234 LDLSRYLAEElkpkTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKaYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
108-408 |
6.33e-71 |
|
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: 234.30 E-value: 6.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYteplaatlqtaahqkychvagfcalcaiqkhvrtarqangrilapkdlvsnlrcisrnfr 187
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 188 ncRQEDAHEYMINLLECMHKCsLPSGVPSESSDAYRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDISKAD-- 265
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEE-LKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGlp 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 266 --SLQRALSRFTAVELLDnGAKVYQCERCKqKVKAKKQLTVSKAPYVLTVHLKRFEAHRS---EKIDRKVDFTSAIDMKP 340
Cdd:cd02257 98 qvSLEDCLEKFFKEEILE-GDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDgtkEKLNTKVSFPLELDLSP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 341 FVS------GPHEGNLKYTLYGVLVHYGRSSHSGHYACFVR-TSSGMWYSLDDNRVVQVSEKTVF-----NQKAYMLFYV 408
Cdd:cd02257 176 YLSegekdsDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-408 |
2.61e-66 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 224.56 E-value: 2.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKYCHVAG--FCALCAIQKHVRTARQANGRilAPKDLVSNLRC---I 182
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSpnSCLSCAMDEIFQEFYYSGDR--SPYGPINLLYLswkH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 183 SRNFRNCRQEDAHEYMINLLECMHKCSLpSGVPSESSDAYRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDI- 261
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYG-GDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 262 --------------SKADSLQRALSRFTAVELLdnGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFE---AHRSE 324
Cdd:cd02660 159 nkstpswalgesgvSGTPTLSDCLDRFTRPEKL--GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 325 KIDRKVDFTSAIDMKPFVSG---------PHEGNLKYTLYGVLVHYGrSSHSGHYACFVRTSSGMWYSLDDNRVVQVSEK 395
Cdd:cd02660 237 KIDTYVQFPLELNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEE 315
|
330
....*....|...
gi 18424054 396 TVFNQKAYMLFYV 408
Cdd:cd02660 316 EVLKSQAYLLFYH 328
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
9.65e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 201.85 E-value: 9.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEPLAATLQTAahqkychvagfcalcaiqkhvrtarqangrilaPKDLVSNLRCISRNFR 187
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET---------------------------------PKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 188 NCRQEDAHEYMINLLECMhkcslpsgvpsessdayrRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSL----DISK 263
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 264 ADSLQRALSRFTAVELLDnGAKVYQCERCKqkvKAKKQLTVSKAPYVLTVHLKRF---EAHRSEKIDRKVDFTSAIDMKP 340
Cdd:cd02667 110 ECSIESCLKQFTEVEILE-GNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFqqpRSANLRKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 341 FVS----GPHEG-NLKYTLYGVLVHYGrSSHSGHYACFVR----------------------TSSGMWYSLDDNRVVQVS 393
Cdd:cd02667 186 FCDpkcnSSEDKsSVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVS 264
|
330
....*....|....
gi 18424054 394 EKTVFNQKAYMLFY 407
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
3.46e-58 |
|
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: 198.67 E-value: 3.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLtyteplaatlqtaahqkyCHvagfcalcaiqkhvrtarqangrilapkdlvsnlrcisrnfr 187
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------SA------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 188 ncRQEDAHEYMINLLECMHkcslpsgvpsessdayrrSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDISKAD-- 265
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLH------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgd 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 266 ----SLQRALSRFTAVELLDNGAKVYqCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHR--SEKIDRKVDF-TSAIDM 338
Cdd:cd02674 81 apkvTLEDCLRLFTKEETLDGDNAWK-CPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgsTRKLTTPVTFpLNDLDL 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18424054 339 KPFVSGPH-EGNLKYTLYGVLVHYGrSSHSGHYACFVRTSS-GMWYSLDDNRVVQVSEKTVFNQKAYMLFY 407
Cdd:cd02674 160 TPYVDTRSfTGPFKYDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-412 |
5.35e-49 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 176.68 E-value: 5.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKY----CHVagfcaLCAIQKhVRTARQangriLAPKDLVS-NLRCI 182
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDdddnKSV-----PLALQR-LFLFLQ-----LSESPVKTtELTDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 183 SRNFRNC-----RQEDAHEYMINLLECMHKCSLPSGVPSessdayrrsLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDL 257
Cdd:cd02659 73 TRSFGWDslntfEQHDVQEFFRVLFDKLEEKLKGTGQEG---------LIKNLFGGKLVNYIICKECPHESEREEYFLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 258 SLDISKADSLQRALSRFTAVELLDnGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFE----AHRSEKIDRKVDFT 333
Cdd:cd02659 144 QVAVKGKKNLEESLDAYVQGETLE-GDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdfeTMMRIKINDRFEFP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 334 SAIDMKPFV----------SGPH-EGNLKYTLYGVLVHYGrSSHSGHYACFVR-TSSGMWYSLDDNRVVQVSEKTVFNQ- 400
Cdd:cd02659 223 LELDMEPYTekglakkegdSEKKdSESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEEc 301
|
330 340 350
....*....|....*....|....*....|...
gi 18424054 401 ---------------------KAYMLFYVRDRQ 412
Cdd:cd02659 302 fggeetqktydsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
5.44e-45 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 164.02 E-value: 5.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLtYTEPLAATLQTAAHqkychvagfcalCAIQKHVRTArqangrILAPKDLVSNLRCISRNFR 187
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL-YFENLLTCLKDLFE------------SISEQKKRTG------VISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 188 NCRQEDAHE---YMIN----LLECMHKCSLPSGVPSESSDA-YRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSL 259
Cdd:cd02663 62 NYMHQDAHEflnFLLNeiaeILDAERKAEKANRKLNNNNNAePQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 260 DISKADSLQRALSRFTAVELLdNGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFE----AHRSEKIDRKVDFTSA 335
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETL-CGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKydeqLNRYIKLFYRVVFPLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 336 IDMKPFVSGPHEGNLKYTLYGVLVHYGRSSHSGHYACFVRTSSGmWYSLDDNRVVQVSEKTVF-------NQK-AYMLFY 407
Cdd:cd02663 221 LRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGG-WLLFDDETVEKIDENAVEeffgdspNQAtAYVLFY 299
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
1.91e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 143.40 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYT-----EPLAATLQTAAHqkyCHVAGFcALCAIQKHVRTARQANGrilAPKDLVSNlRCI 182
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAkdfrrQVLSLNLPRLGD---SQSVMK-KLQLLQAHLMHTQRRAE---APPDYFLE-ASR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 183 SRNFRNCRQEDAHEYMINLLECMHkcslpsgvpsessdayrrSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDIS 262
Cdd:cd02664 73 PPWFTPGSQQDCSEYLRYLLDRLH------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 263 kadSLQRALSRFTAVELLDnGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRF----EAHRSEKIDRKVDFTSAIDM 338
Cdd:cd02664 135 ---SVQDLLNYFLSPEKLT-GDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFsydqKTHVREKIMDNVSINEVLSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 339 K-----PFVSGPHEGNLK--------------YTLYGVLVHYGRSSHSGHYACFVRTSSGM------------------- 380
Cdd:cd02664 211 PvrvesKSSESPLEKKEEesgddgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARDQTDAdstgqecpepkdaeendes 290
|
330 340 350
....*....|....*....|....*....|....*.
gi 18424054 381 --WYSLDDNRVVQVSEKTVFN-------QKAYMLFY 407
Cdd:cd02664 291 knWYLFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
1.13e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 141.02 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEPL-----------AATLQTAAHQKYCHVAGFCAlcAIQKHVRTARQANGRILAPKDLV 176
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFrkavyecnsteDAELKNMPPDKPHEPQTIID--QLQLIFAQLQFGNRSVVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 177 SNLRCISRNfrncrQEDAHEYMINLLecmhkcSLPSGVPSESSDAYRRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLD 256
Cdd:cd02668 79 KALGLDTGQ-----QQDAQEFSKLFL------SLLEAKLSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 257 LSLDISKADSLQRALSRFTAVELLDnGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRS----EKIDRKVDF 332
Cdd:cd02668 148 LELQLKGHKTLEECIDEFLKEEQLT-GDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKtgakKKLNASISF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 333 TSAIDMKPFVSGPHEGNLKYTLYGVLVHYGRSSHSGHYACFVRTSS-GMWYSLDDNRVVQ---------VSEKTVFNQK- 401
Cdd:cd02668 227 PEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDVEEmpgkplklgNSEDPAKPRKs 306
|
330
....*....|....*..
gi 18424054 402 -----------AYMLFY 407
Cdd:cd02668 307 eikkgthssrtAYMLVY 323
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
5.54e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 113.23 E-value: 5.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQcltyteplaatlqtaahqkychvagfcALCAIqkhvrtarqangrilapKDLVSNLRcisrnfR 187
Cdd:cd02662 1 GLVNLGNTCFMNSVLQ---------------------------ALASL-----------------PSLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 188 NCRQEDAHEYMINLLECMH-KCSLPsgvpsessdayrrslvhkiFGGSLRSQVKCEQCSHCSN-KFDPFLDLSLDISKAD 265
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEqLLKFP-------------------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQS 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 266 -----SLQRALSRFTAVELLDNgakvYQCERCkqkvkakkQLTVSKAPYVLTVHLKRFEAHRSEKIDR---KVDFTSAID 337
Cdd:cd02662 92 sgsgtTLEHCLDDFLSTEIIDD----YKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKnscKVSFPERLP 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 338 MKpfvsgphegnlKYTLYGVLVHYGrSSHSGHYACFVRTSSGM---------------------WYSLDDNRVVQVSEKT 396
Cdd:cd02662 160 KV-----------LYRLRAVVVHYG-SHSSGHYVCYRRKPLFSkdkepgsfvrmregpsstshpWWRISDTTVKEVSESE 227
|
330
....*....|..
gi 18424054 397 VFNQK-AYMLFY 407
Cdd:cd02662 228 VLEQKsAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
108-421 |
3.99e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 112.27 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEPLAAT---LQTAAHQKYCHVAgfCALCAIQKHVRTARQAngriLAPKDLVSNLrcISR 184
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDvygIPTDHPRGRDSVA--LALQRLFYNLQTGEEP----VDTTELTRSF--GWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 185 NFRNCRQEDAHEY----MINLLECMHkcslpsGVPSESSdayrrslVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLD 260
Cdd:COG5077 267 SDDSFMQHDIQEFnrvlQDNLEKSMR------GTVVENA-------LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 261 ISKADSLQRALSRFTAVELLDnGAKVYQCERcKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRSE----KIDRKVDFTSAI 336
Cdd:COG5077 334 VKGMKNLQESFRRYIQVETLD-GDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERdmmvKINDRYEFPLEI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 337 DMKPFVS----GPHEGNLKYTLYGVLVHYGrSSHSGHYACFVRTS-SGMWYSLDDNRVVQVSEKTVFNQ----------- 400
Cdd:COG5077 412 DLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdk 490
|
330 340 350
....*....|....*....|....*....|....*..
gi 18424054 401 -----------KAYMLFYVRDRQ-----NAVPKNSVP 421
Cdd:COG5077 491 irdhsgikrfmSAYMLVYLRKSMlddllNPVAAVDIP 527
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
107-407 |
8.66e-25 |
|
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: 106.52 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 107 AGLQNLGNTCFLNSVLQCLTYteplAATLQTAAHQKYCHVAGFCALCAIQKHVRTARQANGRILAPKDLVSNLRCISRNF 186
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYF----CPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAPRRLLNALREVNPMY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 187 RNCRQEDAHEYMINLLECMhkcslpsgvpsessdayrRSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDI----- 261
Cdd:cd02671 101 EGYLQHDAQEVLQCILGNI------------------QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVqesel 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 262 SKADS--------------LQRALSRFTAVELLdNGAKVYQCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRS---- 323
Cdd:cd02671 163 SKSEEsseispdpktemktLKWAISQFASVERI-VGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSefdc 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 324 ----EKIDRKVdfTSAIDMKPFVSGPHEGNLKYTLYGVLVHYGRSSHSGHYACFVRtssgmWYSLDDNRVVQVSEKTVFN 399
Cdd:cd02671 242 ygglSKVNTPL--LTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLE 314
|
330
....*....|....*..
gi 18424054 400 ---------QKAYMLFY 407
Cdd:cd02671 315 alspntsstSTPYLLFY 331
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
1.11e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 105.48 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKYCHVAG--FCALCAIQKhVRTARQAnGRILAPKDLVSNL------ 179
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIK-LADGLLS-GRYSKPASLKSENdpyqvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 180 -------RCISRN---FRNCRQEDAHEYMINLLECMHKCSLPSGV--PSEssdayrrslvhkIFGGSLRSQVKCEQCSHC 247
Cdd:cd02658 79 ikpsmfkALIGKGhpeFSTMRQQDALEFLLHLIDKLDRESFKNLGlnPND------------LFKFMIEDRLECLSCKKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 248 SNKFDPFLDLSLDISKAD--------------SLQRALSRFTAVELLDngakvYQCERCKQKVKAKKQLTVSKAPYVLTV 313
Cdd:cd02658 147 KYTSELSEILSLPVPKDEatekeegelvyepvPLEDCLKAYFAPETIE-----DFCSTCKEKTTATKTTGFKTFPDYLVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 314 HLKRFEAhRSEKIDRKVDFtsAIDMkPFVSGPHegnlKYTLYGVLVHYGRSSHSGHYACFVR---TSSGMWYSLDDNRVV 390
Cdd:cd02658 222 NMKRFQL-LENWVPKKLDV--PIDV-PEELGPG----KYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
|
330
....*....|....*..
gi 18424054 391 QVSEKTVFNQKAYMLFY 407
Cdd:cd02658 294 ASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
2.84e-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 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: 104.34 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCL-TYTEPLAATLQ-TAAHQKYCHVAGfcALCAIQKHVRTARQANGRILAPKDLVSNLRCISRN 185
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLrSVPELRDALKNyNPARRGANQSSD--NLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 186 F------RNCRQEDAHEYMINLLEcmhkcSLPSGVPSESSDayrRSLVHKIFGGSLRSQVKC-EQCSHCSNKFDPFLDLS 258
Cdd:cd02657 79 FaekqnqGGYAQQDAEECWSQLLS-----VLSQKLPGAGSK---GSFIDQLFGIELETKMKCtESPDEEEVSTESEYKLQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 259 LDISKAdslqralsrfTAVELLDNGAKvyqcERCKQKVKA-----------KKQLTVSKAPYVLTVHLKRFEAHRSE--- 324
Cdd:cd02657 151 CHISIT----------TEVNYLQDGLK----KGLEEEIEKhsptlgrdaiyTKTSRISRLPKYLTVQFVRFFWKRDIqkk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 325 -KIDRKVDFTSAIDMKPFVSgpHEGNlkYTLYGVLVHYGRSSHSGHYACFVRTSS-GMWYSLDDNRVVQVSEKTVFN--- 399
Cdd:cd02657 217 aKILRKVKFPFELDLYELCT--PSGY--YELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKlsg 292
|
330
....*....|..
gi 18424054 400 ----QKAYMLFY 407
Cdd:cd02657 293 ggdwHIAYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
108-409 |
1.18e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 99.11 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEP-LAATLQTAAHQkychvagfcaLCAIQKHVRTARQANGRILAPKDL----VSNLRCI 182
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkLDELLDDLSKE----------LKVLKNVIRKPEPDLNQEEALKLFtalwSSKEHKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 183 SRNFRNCRQEDAHEYMINLLECMhkcslpsgvpsESSDAYRRSLVHKIFGGSLRSQVKceqcshcsnkfDPFLDL----- 257
Cdd:COG5533 71 GWIPPMGSQEDAHELLGKLLDEL-----------KLDLVNSFTIRIFKTTKDKKKTST-----------GDWFDIiielp 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 258 ---SLDISKadSLQRALSRFTavELLDNGAKVYQCERCKQKVKAKKQLTVS--KAPYVLTVHLKRFeAHR--SEKIDRKV 330
Cdd:COG5533 129 dqtWVNNLK--TLQEFIDNME--ELVDDETGVKAKENEELEVQAKQEYEVSfvKLPKILTIQLKRF-ANLggNQKIDTEV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 331 DFTSAIDMKPFVSGPHEGNLKYTLYGVLVHYGrSSHSGHYACFVRTsSGMWYSLDDNRVVQVSEKTVFNQK---AYMLFY 407
Cdd:COG5533 204 DEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVKK-GGKWEKANDSDVTPVSEEEAINEKaknAYLYFY 281
|
..
gi 18424054 408 VR 409
Cdd:COG5533 282 ER 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
266-409 |
6.81e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 98.42 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 266 SLQRALSRFTAVELLDNGAKVYqCERCKQKVKAKKQLTVSKAPYVLTVHLKRFEAHRS--EKIDRKVDF-TSAIDMKPFV 342
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWY-CPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYpIDDLDLSGVE 754
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18424054 343 SGPHEGNLKYTLYGVLVHYGRSShSGHYACFVR-TSSGMWYSLDDNRVVQVSEKTVFNQKAYMLFYVR 409
Cdd:COG5560 755 YMVDDPRLIYDLYAVDNHYGGLS-GGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
107-375 |
2.27e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 86.94 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 107 AGLQNLGNTCFLNSVLQCLTYTEPLAATLQtaAHQKYCHVAGFCALC-------AIQKhvrtarqANGRILAPkdlvSNL 179
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCelgflfdMLEK-------AKGKNCQA----SNF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 180 rciSRNFRNCRQ--------EDAHEY-------MI-----NLLECMHKCSLPSGVPSESSDayrrSLVHKIFGGSLRSQV 239
Cdd:pfam13423 68 ---LRALSSIPEasalglldEDRETNsaislssLIqsfnrFLLDQLSSEENSTPPNPSPAE----SPLEQLFGIDAETTI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 240 KCEQCSHCSNKFDPFLDLSLDIS-KADSLQRALSRFTAVELLDNGAKVYQ-----CERCKQKVKAKKQLTVSKAPYVLTV 313
Cdd:pfam13423 141 RCSNCGHESVRESSTHVLDLIYPrKPSSNNKKPPNQTFSSILKSSLERETttkawCEKCKRYQPLESRRTVRNLPPVLSL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18424054 314 HLKRFEAhRSEKIDRKVDFTS---AIDMKPFVSGPHEGNlKYTLYGVLVHYGRSSHSGHYACFVR 375
Cdd:pfam13423 221 NAALTNE-EWRQLWKTPGWLPpeiGLTLSDDLQGDNEIV-KYELRGVVVHIGDSGTSGHLVSFVK 283
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
109-407 |
2.80e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 67.55 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 109 LQNLGNTCFLNSVLQcltyteplaatlqtaahqkychvagfcALCAIQKhvrtarqangrilapkdlvsnlrcISRNFRN 188
Cdd:cd02673 2 LVNTGNSCYFNSTMQ---------------------------ALSSIGK------------------------INTEFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 189 CRQEDAHEYMINLLECMH---KCSLPSGVPSESSDAYRRSLvhKIFGGSLRSQVKCEQCSHCSNKFDP--FLDLSLDISK 263
Cdd:cd02673 31 DDQQDAHEFLLTLLEAIDdimQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVgnFLDVSMIDNK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 264 ADSLQRALSRFTAVELLDNgakvyQCERCKQKVKAKKQlTVSKAPYVLTVHLKRFEAHRSEKIDRKvdfTSAIDMKPFVS 343
Cdd:cd02673 109 LDIDELLISNFKTWSPIEK-----DCSSCKCESAISSE-RIMTFPECLSINLKRYKLRIATSDYLK---KNEEIMKKYCG 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18424054 344 GPHegnlKYTLYGVLVHYGRSSHSGHYACFVRTSSG--MWYSLDDNRVVQVSEKTVFNQ---KAYMLFY 407
Cdd:cd02673 180 TDA----KYSLVAVICHLGESPYDGHYIAYTKELYNgsSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
108-407 |
2.80e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 69.65 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 108 GLQNLGNTCFLNSVLQCLTYTEP------LAATLQTAAHQKYCHVAGFCALcaIQKhvrtarQANGRIL----APKDLVS 177
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPirnfflLYENYENIKDRKSELVKRLSEL--IRK------IWNPRNFkghvSPHELLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 178 NL-RCISRNFRNCRQEDAHEYMINLLECMHKCSlpsgvpsESSDAYRRSLVHKIFGGSLrsQVKCEQCSHCSNKFD---- 252
Cdd:cd02669 193 AVsKVSKKKFSITEQSDPVEFLSWLLNTLHKDL-------GGSKKPNSSIIHDCFQGKV--QIETQKIKPHAEEEGskdk 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 253 -------------PFLDLSLD-----ISKADSLQRALSRFTAVELLDNgakvYQCERCKQKVKAKKQLTVSKAPYVLTVH 314
Cdd:cd02669 264 ffkdsrvkktsvsPFLLLTLDlppppLFKDGNEENIIPQVPLKQLLKK----YDGKTETELKDSLKRYLISRLPKYLIFH 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 315 LKRFEAHR--SEKIDRKVDFTSAI-DMKPFVSGPHEGN---LKYTLYGVLVHYGRSSHSGHYACFVR-TSSGMWYSLDDN 387
Cdd:cd02669 340 IKRFSKNNffKEKNPTIVNFPIKNlDLSDYVHFDKPSLnlsTKYNLVANIVHEGTPQEDGTWRVQLRhKSTNKWFEIQDL 419
|
330 340
....*....|....*....|
gi 18424054 388 RVVQVSEKTVFNQKAYMLFY 407
Cdd:cd02669 420 NVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
247-407 |
2.27e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 64.86 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 247 CSNKFDPFLDLSLDIS---KADSLQRALSRFTAVELL---DNGAKVYQCERCKQKVKAKKQLtvSKAPYVLTVHLKRF-- 318
Cdd:cd02670 34 TDKLLMPLLEPKVDIIhggKKDQDDDKLVNERLLQIPvpdDDDGGGITLEQCLEQYFNNSVF--AKAPSCLIICLKRYgk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 319 EAHRSEKIDRKVDFTSAIDMKPFV----------------------SGPHEGNLKYTLYGVLVHYGRSSHSGHYACFVRT 376
Cdd:cd02670 112 TEGKAQKMFKKILIPDEIDIPDFVaddpracskcqlecrvcyddkdFSPTCGKFKLSLCSAVCHRGTSLETGHYVAFVRY 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18424054 377 SSGM------------WYSLDD----NRVVQVSEKTV-FNQK-AYMLFY 407
Cdd:cd02670 192 GSYSltetdneaynaqWVFFDDmadrDGVSNGFNIPAaRLLEdPYMLFY 240
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
82-261 |
9.82e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 65.67 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 82 PDSSDLL---EHGFEPDLTFSIT-------FRKIGA-GLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQK---YCHVA 147
Cdd:COG5560 230 EDRSVLLlskITRNPDWLVDSIVddhnrsiNKEAGTcGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEEsinEENPL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 148 GFCALCA-----IQKHVRTARQANgriLAPKDLVSNLRCISRNFRNCRQEDAHEYMINLLECMHK----------CSLPS 212
Cdd:COG5560 310 GMHGSVAsayadLIKQLYDGNLHA---FTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpyTSKPD 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18424054 213 GVPSESSDAYR-------------RSLVHKIFGGSLRSQVKCEQCSHCSNKFDPFLDLSLDI 261
Cdd:COG5560 387 LSPGDDVVVKKkakecwwehlkrnDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
107-408 |
8.32e-09 |
|
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: 58.27 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 107 AGLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQKYchvagfcalcAIQKHVRTARQANGRILAPKDLV---------- 176
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSELQrsnqfvyelr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 177 --------SNLRCI--SRNFRNC--RQEDAHEYMINLLECMHKCSLPSGVPSESSDAYRRS----LVHKIFGGSLRSQ-V 239
Cdd:cd02666 72 slfndlihSNTRSVtpSKELAYLalRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKeqsdLIKRLFSGKTKQQlV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 240 KCEQCSHCSNKFDPFLDLSLDISKADSLQRALSRFTAVELLDNGAKVYQCERcKQKVKAKKQLTVSKAPyVLTVHL---K 316
Cdd:cd02666 152 PESMGNQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDLYDALDRYFDYDS-LTKLPQRSQVQAQLAQ-PLQRELismD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 317 RFEAH----RSEKIDRKV--DFTSAIDMKPFVSGP----------HEGNLKYTLYGVLVHYGRSSHsGHYACFVRT-SSG 379
Cdd:cd02666 230 RYELPssidDIDELIREAiqSESSLVRQAQNELAElkheiekqfdDLKSYGYRLHAVFIHRGEASS-GHYWVYIKDfEEN 308
|
330 340 350
....*....|....*....|....*....|....*
gi 18424054 380 MWYSLDDNRVVQVSEKTVFNQK------AYMLFYV 408
Cdd:cd02666 309 VWRKYNDETVTVVPASEVFLFTlgntatPYFLVYV 343
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
306-408 |
7.34e-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: 47.94 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 306 KAPYVLTVHLKRFE--AHRSEKIDRKVDFTSAIDMKPfvsgphegnlkYTLYGVLVHYGRsSHSGHYACFV-RTSSGMWY 382
Cdd:cd02665 127 ELPPVLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVP-----------YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWE 194
|
90 100 110
....*....|....*....|....*....|....
gi 18424054 383 SLDDNRVVQVS----EKTVF----NQKAYMLFYV 408
Cdd:cd02665 195 KYNDISVTESSweevERDSFgggrNPSAYCLMYI 228
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
91-407 |
8.07e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 48.28 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 91 GFEpDLTFSITFRKIGAGLQNLGNTCFLNSVLQCLTYTEPLAATLQTAAHQkyCHvAGFCALCAIqkhvrtarqanGRIL 170
Cdd:cd02672 1 GTE-DFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNFTAIILVA--CP-KESCLLCEL-----------GYLF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 171 APkdLVSNLRCISRNFRNCRQ---EDAHEYMINLLECMHKCSLP-SGVPSESSDAYRRSLVHkifgGSLRSQVKCEQCSH 246
Cdd:cd02672 66 ST--LIQNFTRFLLETISQDQlgtPFSCGTSRNSVSLLYTLSLPlGSTKTSKESTFLQLLKR----SLDLEKVTKAWCDT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 247 CsNKFDPFLdlsldiskadsLQRALSRFTAVELLdngakvyqcerckqkvkakkqltvskapyVLTVHLKRFEAHRSeki 326
Cdd:cd02672 140 C-CKYQPLE-----------QTTSIRHLPDILLL-----------------------------VLVINLSVTNGEFD--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424054 327 DRKVDFTSAIDMKPFVSgPHEGNL-------------KYTLYGVLVHYGRSSHSGHYACFVR-----TSSGMWYSLDDNR 388
Cdd:cd02672 176 DINVVLPSGKVMQNKVS-PKAIDHdklvknrgqesiyKYELVGYVCEINDSSRGQHNVVFVIkvneeSTHGRWYLFNDFL 254
|
330
....*....|....*....
gi 18424054 389 VVQVSEktvfnqKAYMLFY 407
Cdd:cd02672 255 VTPVSE------LAYILLY 267
|
|
| |
