|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
137-486 |
1.89e-79 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 250.44 E-value: 1.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 137 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQ-TAF 215
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 216 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 295
Cdd:pfam00443 68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 296 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 376 FWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRgLDMKCYLLEPENSG-PESCLYDLAAVVVHHGSgVGSGHYTAY- 453
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYi 275
|
330 340 350
....*....|....*....|....*....|....*
gi 1034592453 454 -ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 486
Cdd:pfam00443 276 kAYENNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-487 |
5.62e-75 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 239.20 E-value: 5.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLsnieqfccyfkeLPAVELRNGKTAGRRTYHTRSQGDNNvSLVEEFRKTLCALWQ-GSQTAFS 216
Cdd:cd02660 2 GLINLGATCFMNVILQAL------------LHNPLLRNYFLSDRHSCTCLSCSPNS-CLSCAMDEIFQEFYYsGDRSPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 217 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNkcCIngastvVTAIFGGIL 296
Cdd:cd02660 69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN---------EANDESHCN--CI------IHQTFSGSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 297 QNEVNCLICGTESRKFDPFLDLSLDIPSQ-FRSKRSKNQENGPVCSLRDCLRSFTDLEELDETElYMCHKCKKKQKSTKK 375
Cdd:cd02660 132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKsTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 376 FWIQKLPKVLCLHLKRF-HWTAYLRNKVDTYVEFPLRgLDMKCYL------LEPENSGPESCLYDLAAVVVHHGSgVGSG 448
Cdd:cd02660 211 LSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLE-LNMTPYTsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034592453 449 HYTAYA-THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 487
Cdd:cd02660 289 HYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
136-487 |
1.29e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 216.76 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 136 ATGLRNLGNTCFMNAILQSLSNIEQFCCYFkelpavelrngktagRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAF 215
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYL---------------LSREHSKDCCNEGFCMMCALEAHVERALASSGPGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 216 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrSAILQENSTLSASNKccINGASTVVTAIFGGI 295
Cdd:cd02661 66 APRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ------------KACLDRFKKLKAVDP--SSQETTLVQQIFGGY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 296 LQNEVNCLICGTESRKFDPFLDLSLDIPSqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:cd02661 132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 376 FWIQKLPKVLCLHLKRFhwTAYLRNKVDTYVEFPLRgLDMKCYLLEPENsgpESCLYDLAAVVVHHGSGVGSGHYTAYA- 454
Cdd:cd02661 198 LTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMSQPND---GPLKYKLYAVLVHSGFSPHSGHYYCYVk 271
|
330 340 350
....*....|....*....|....*....|...
gi 1034592453 455 THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 487
Cdd:cd02661 272 SSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
4.81e-64 |
|
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: 207.53 E-value: 4.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 217
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGILQ 297
Cdd:cd02674 21 -----------------DQQDAQEFLLFLLDGLH----------------------------------SIIVDLFQGQLK 49
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 377
Cdd:cd02674 50 SRLTCLTCGKTSTTFEPFTYLSLPIP--------SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPEscLYDLAAVVVHHGSgVGSGHYTAYA--T 455
Cdd:cd02674 122 ISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPF--KYDLYAVVNHYGS-LNGGHYTAYCknN 198
|
330 340 350
....*....|....*....|....*....|.
gi 1034592453 456 HEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02674 199 ETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
138-487 |
2.44e-63 |
|
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: 206.57 E-value: 2.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 217
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILqenstlsasnkccingaSTVVTAIFGGILQ 297
Cdd:cd02257 21 -----------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------KSLIHDLFGGKLE 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLICGTESRKFDPFLDLSLDIPSQfrskrsknqeNGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkFW 377
Cdd:cd02257 67 STIVCLECGHESVSTEPELFLSLPLPVK----------GLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKR-LK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKRFHWT-AYLRNKVDTYVEFPLRgLDMKCYLLE---PENSGPESCLYDLAAVVVHHGSGVGSGHYTAY 453
Cdd:cd02257 136 IKKLPPVLIIHLKRFSFNeDGTKEKLNTKVSFPLE-LDLSPYLSEgekDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034592453 454 A--THEGRWFHFNDSTVTLTDEETVVK-----AKAYILFYV 487
Cdd:cd02257 215 VkdPSDGKWYKFNDDKVTEVSEEEVLEfgslsSSAYILFYE 255
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
7.17e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 169.49 E-value: 7.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafSP 217
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------------------TP 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDhlhlelqggfngvsrsailqenstlsasnkccinGASTVVTAIFGGILQ 297
Cdd:cd02667 33 KELFSQVCRKAPQFKGYQQQDSHELLRYLLD----------------------------------GLRTFIDSIFGGELT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkfw 377
Cdd:cd02667 79 STIMCESCGTVSLVYEPFLDLSLPRS----------DEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYL--- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKRFHWTAYLR-NKVDTYVEFPLRgLDMKCYLLEPENS--GPESCLYDLAAVVVHHGSgVGSGHYTAYA 454
Cdd:cd02667 146 ISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFPEI-LDLAPFCDPKCNSseDKSSVLYRLYGVVEHSGT-MRSGHYVAYV 223
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034592453 455 -----------------------THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02667 224 kvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
4.04e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 165.56 E-value: 4.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFCCyFKELpavelrngktagrrtYHtrsqgdnnvSLVEEFRKTlcalwqGSqtaFSP 217
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLTC-LKDL---------------FE---------SISEQKKRT------GV---ISP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCcingastvVTAIFGGILQ 297
Cdd:cd02663 47 KKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW--------VHEIFQGILT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknqengPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 377
Cdd:cd02663 119 NETRCLTCETVSSRDETFLDLSIDVE--------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKRFHWT-AYLRN-KVDTYVEFPlrgLDMKCYLLEPENSGPEScLYDLAAVVVHHGSGVGSGHYTAYAT 455
Cdd:cd02663 185 IKKLPKILALHLKRFKYDeQLNRYiKLFYRVVFP---LELRLFNTTDDAENPDR-LYELVAVVVHIGGGPNHGHYVSIVK 260
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034592453 456 HEGRWFHFNDSTVTLTDEETVVK--------AKAYILFY 486
Cdd:cd02663 261 SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-487 |
1.55e-40 |
|
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: 148.56 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLsnieqfccYFKelPavELRNGktagRRTYHTRSQGDNNVSLVEEFRK--TLCALWQGSQTAF 215
Cdd:cd02659 4 GLKNQGATCYMNSLLQQL--------YMT--P--EFRNA----VYSIPPTEDDDDNKSVPLALQRlfLFLQLSESPVKTT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 216 SPESLFYVVWKiMPNfRGYQQQDAHEFMRYLLDHLHLELQGgfngvsrsaILQENStlsasnkccingastvVTAIFGGI 295
Cdd:cd02659 68 ELTDKTRSFGW-DSL-NTFEQHDVQEFFRVLFDKLEEKLKG---------TGQEGL----------------IKNLFGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 296 LQNEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:cd02659 121 LVNYIICKECPHESEREEYFLDLQVAV------KGKKN--------LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 376 FWIQKLPKVLCLHLKRFH--WTAYLRNKVDTYVEFPLRgLDMKCYL--------LEPENSGPESCLYDLAAVVVHHGsGV 445
Cdd:cd02659 187 VCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLE-LDMEPYTekglakkeGDSEKKDSESYIYELHGVLVHSG-DA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592453 446 GSGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKA----------------------KAYILFYV 487
Cdd:cd02659 265 HGGHYYSYikDRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYE 330
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-468 |
4.07e-34 |
|
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: 131.00 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKtLCALWQGSQTAFSP 217
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPH------EPQTIIDQLQL-IFAQLQFGNRSVVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 ESLFYVVWKIMPNfrgyQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqenstlsasnkcciNGASTVVTAIFGGILQ 297
Cdd:cd02668 74 PSGFVKALGLDTG----QQQDAQEFSKLFLSLLEAKLSKSKN----------------------PDLKNIVQDLFRGEYS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKnqengpvcSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 377
Cdd:cd02668 128 YVTQCSKCGRESSLPSKFYELELQL------KGHK--------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKR--FHWTAYLRNKVDTYVEFPLRgLDMKCYLLEpenSGPESCLYDLAAVVVHHGSGVGSGHYTA--Y 453
Cdd:cd02668 194 LTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEI-LDMGEYLAE---SDEGSYVYELSGVLIHQGVSAYSGHYIAhiK 269
|
330
....*....|....*
gi 1034592453 454 ATHEGRWFHFNDSTV 468
Cdd:cd02668 270 DEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
4.60e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 125.30 E-value: 4.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFkelpaveLRngktagrrtYHTRSQGDNNVSLVEEfrKTLCALWQGSQTAFS- 216
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQV-------LS---------LNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEa 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 217 -PESLFYVVWKimPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGI 295
Cdd:cd02664 63 pPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLH----------------------------------TLIEKMFGGK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 296 LQNEVNCLICGTESRKFDPFLDLSLDipsqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 375
Cdd:cd02664 107 LSTTIRCLNCNSTSARTERFRDLDLS-----------------FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 376 FWIQKLPKVLCLHLKRF------HWTAYLRNKV--DTYVEFPLR-----GLDMKCYLLEPENSGPESC----LYDLAAVV 438
Cdd:cd02664 170 MKVTGAPEYLILTLLRFsydqktHVREKIMDNVsiNEVLSLPVRvesksSESPLEKKEEESGDDGELVtrqvHYRLYAVV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034592453 439 VHHGSGVGSGHYTAYATH----------------------EGRWFHFNDSTVTLTDEETV-------VKAKAYILFY 486
Cdd:cd02664 250 VHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
3.84e-29 |
|
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: 117.30 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLsnieQFCCYFKElpavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 217
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL----YFCPGFKH---------------GLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 ESLFYVVWKIMPNFRGYQQQDAHEFMrylldhlhlelqggfngvsrsailqenstlsasnKCCINGASTVVTAIFGGILQ 297
Cdd:cd02671 87 RRLLNALREVNPMYEGYLQHDAQEVL----------------------------------QCILGNIQELVEKDFQGQLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGP-----VCSLRDCLRSFTDLEELDETELYMCHKCKKKQKS 372
Cdd:cd02671 133 LRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 373 TKKFWIQKLPKVLCLHLKRFHWTAYLRN------KVDTYVEFPLrglDMKCyllEPENSGPESCLYDLAAVVVHHGSGVG 446
Cdd:cd02671 213 ERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTPL---KLSL---EEWSTKPKNDVYRLFAVVMHSGATIS 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034592453 447 SGHYTAYAthegRWFHFNDSTVTLTDEE---------TVVKAKAYILFY 486
Cdd:cd02671 287 SGHYTAYV----RWLLFDDSEVKVTEEKdflealspnTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
331-486 |
4.03e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 118.45 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 331 SKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPL 410
Cdd:COG5560 666 REIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034592453 411 RGLDMKCYLLEPENSgpeSCLYDLAAVVVHHGsGVGSGHYTAYA--THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:COG5560 746 DDLDLSGVEYMVDDP---RLIYDLYAVDNHYG-GLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
9.91e-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: 112.80 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKEL----------PA-------VELRNGKTAGRrTYHTRSQGDNNVslveef 200
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLenkfpsdvvdPAndlncqlIKLADGLLSGR-YSKPASLKSEND------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 201 rktlcalwqGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailQENSTLSASNkcc 280
Cdd:cd02658 74 ---------PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD----------------RESFKNLGLN--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 281 ingastvVTAIFGGILQNEVNCLICGteSRKFDPFLD--LSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDET 358
Cdd:cd02658 126 -------PNDLFKFMIEDRLECLSCK--KVKYTSELSeiLSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 359 elymCHKCKKKQKSTKKFWIQKLPKVLCLHLKRF----HWTAylrNKVDTYVEFPLRGLDMKcyllepensgpesclYDL 434
Cdd:cd02658 197 ----CSTCKEKTTATKTTGFKTFPDYLVINMKRFqlleNWVP---KKLDVPIDVPEELGPGK---------------YEL 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592453 435 AAVVVHHGSGVGSGHYTAY----ATHEGRWFHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02658 255 IAFISHKGTSVHSGHYVAHikkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
12-486 |
1.22e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 112.03 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 12 SNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQvpltnhkksekqdkvqHTVCMDCSSYSTYC----YRCDDFVVNDTKLG 87
Cdd:cd02669 24 SNLNVYACLVCGKYFQGRGKGSHAYTHSLEDN----------------HHVFLNLETLKFYClpdnYEIIDSSLDDIKYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 88 LvqkvrehlqnleNSAFTadrhkkRKLLENSTLNSKLLK-VNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQFCCYF- 165
Cdd:cd02669 88 L------------NPTYT------KEQISDLDRDPKLSRdLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 166 -KELPAVELRNGKTAGRRtyhtrsqgdnnvsLVEEFRKtlcaLWqgSQTAF----SP-ESLFYVVWKIMPNFRGYQQQDA 239
Cdd:cd02669 150 lYENYENIKDRKSELVKR-------------LSELIRK----IW--NPRNFkghvSPhELLQAVSKVSKKKFSITEQSDP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 240 HEFMRYLLDHLHLELQGgfngvsrsailqenstlsaSNKCcingASTVVTAIFGGILQNEVNCLI----CGTESRKFD-- 313
Cdd:cd02669 211 VEFLSWLLNTLHKDLGG-------------------SKKP----NSSIIHDCFQGKVQIETQKIKphaeEEGSKDKFFkd 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 314 ---------PFLDLSLDIPSQ--FRSKRSKNQEngPVCSLRDCLRSFTdleELDETELymchkckkkQKSTKKFWIQKLP 382
Cdd:cd02669 268 srvkktsvsPFLLLTLDLPPPplFKDGNEENII--PQVPLKQLLKKYD---GKTETEL---------KDSLKRYLISRLP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 383 KVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHEGR--W 460
Cdd:cd02669 334 KYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHKSTnkW 413
|
490 500
....*....|....*....|....*.
gi 1034592453 461 FHFNDSTVTLTDEETVVKAKAYILFY 486
Cdd:cd02669 414 FEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
138-487 |
1.02e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSnieqfcCYFKELPAVELRNGKTAgrRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 217
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA------LYLPKLDELLDDLSKEL--KVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 EslfyvvwkimpnFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNKccingastvVTAIFGGILQ 297
Cdd:COG5533 73 I------------PPMGSQEDAHELLGKLLDELKLDLVNSFT---------IRIFKTTKDK---------KKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 NEVNCLI--CGTESRKFDPFLD-LSLDIPSQFRSKRSKNQEngpvcslrdclrsftdLEELDETELYMChkckkkqkstk 374
Cdd:COG5533 123 IIIELPDqtWVNNLKTLQEFIDnMEELVDDETGVKAKENEE----------------LEVQAKQEYEVS----------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 375 kfwIQKLPKVLCLHLKRFhwtAYL--RNKVDTYVEFPLrglDMKCYLLEPENSGPEScLYDLAAVVVHHGSgVGSGHYTA 452
Cdd:COG5533 176 ---FVKLPKILTIQLKRF---ANLggNQKIDTEVDEKF---ELPVKHDQILNIVKET-YYDLVGFVLHQGS-LEGGHYIA 244
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034592453 453 YATHEGRWFHFNDSTVTLTDEETVVKAK---AYILFYV 487
Cdd:COG5533 245 YVKKGGKWEKANDSDVTPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
5.55e-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 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: 104.72 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLsnieqfccyfKELPAV--ELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKTLCALwQGSQTAF 215
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL----------RSVPELrdALKNYNPARRGANQ------SSDNLTNALRDLFDTM-DKKQEPV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 216 SPESLFYVVWKIMPNF------RGYQQQDAHEFMRYLLDHLHLELQGGfngvsrsaiLQENStlsasnkccingastVVT 289
Cdd:cd02657 64 PPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKLPGA---------GSKGS---------------FID 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 290 AIFGGILQNEVNCLICGT-ESRKFDPFLDLSLDIPSQFrskrsknqengPVCSLRDCLrsftdLEELDETELYMCHKCKK 368
Cdd:cd02657 120 QLFGIELETKMKCTESPDeEEVSTESEYKLQCHISITT-----------EVNYLQDGL-----KKGLEEEIEKHSPTLGR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 369 KQKSTKKFWIQKLPKVLCLHLKRFHW--TAYLRNKVDTYVEFPLRgLDMKCYLlepensgPESCLYDLAAVVVHHGSGVG 446
Cdd:cd02657 184 DAIYTKTSRISRLPKYLTVQFVRFFWkrDIQKKAKILRKVKFPFE-LDLYELC-------TPSGYYELVAVITHQGRSAD 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034592453 447 SGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKAK-------AYILFY 486
Cdd:cd02657 256 SGHYVAWvrRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
138-486 |
1.39e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 99.36 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFccyfkelpavelrngktagrrtyhtrsqgdnnVSLVEEFRktlcalwqgsqtafsp 217
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSL--------------------------------IEYLEEFL---------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSrsailqenstlsasnkccingASTVVtaifggilq 297
Cdd:cd02662 33 -----------------EQQDAHELFQVLLETLEQLLKFPFDGLL---------------------ASRIV--------- 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 298 nevnCLICGTESR-KFDPFLDLSLDIPsqfrskrskNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCkkkqkstkkf 376
Cdd:cd02662 66 ----CLQCGESSKvRYESFTMLSLPVP---------NQSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQTV---------- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 377 wIQKLPKVLCLHLKRFHWT---AYLRNKvdTYVEFPLRgLDMKcyllepensgpescLYDLAAVVVHHGSgVGSGHYTAY 453
Cdd:cd02662 123 -IVRLPQILCIHLSRSVFDgrgTSTKNS--CKVSFPER-LPKV--------------LYRLRAVVVHYGS-HSSGHYVCY 183
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592453 454 ----------------------ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 486
Cdd:cd02662 184 rrkplfskdkepgsfvrmregpSSTSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
138-469 |
2.64e-20 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 94.55 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 138 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHtrSQGDNNVSLVeefrktLCALWQGSQTAFSP 217
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-------------TDH--PRGRDSVALA------LQRLFYNLQTGEEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 218 -ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLhlelqggfngvsrsailqENSTlsasNKCCINGAstvVTAIFGGIL 296
Cdd:COG5077 254 vDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNL------------------EKSM----RGTVVENA---LNGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 297 QNEVNCLICGTESRKFDPFLDLsldipsQFRSKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKF 376
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDI------QLNVKGMKN--------LQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 377 WiQKLPKVLCLHLKRFHWTaYLRN---KVDTYVEFPLRgLDMKCYL----LEPENSgpeSCLYDLAAVVVHHGSgVGSGH 449
Cdd:COG5077 375 F-ESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDLLPFLdrdaDKSENS---DAVYVLYGVLVHSGD-LHEGH 447
|
330 340
....*....|....*....|..
gi 1034592453 450 YTAYATHE--GRWFHFNDSTVT 469
Cdd:COG5077 448 YYALLKPEkdGRWYKFDDTRVT 469
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
137-323 |
8.03e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.94 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 137 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelRNGKTAGRRTYHTRSQGdnnvSLVEEFRKTLCALWQGSQTAFS 216
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLS------DEYEESINEENPLGMHG----SVASAYADLIKQLYDGNLHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 217 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNG--VSRSAILQENSTL--SASNKCC---INGASTVVT 289
Cdd:COG5560 336 PSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKpyTSKPDLSPGDDVVvkKKAKECWwehLKRNDSIIT 415
|
170 180 190
....*....|....*....|....*....|....
gi 1034592453 290 AIFGGILQNEVNCLICGTESRKFDPFLDLSLDIP 323
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
8-83 |
4.17e-16 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 72.68 E-value: 4.17e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592453 8 AVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEdaqvpltnhkksekqdKVQHTVCMDCSSYSTYCYRCDDFVVND 83
Cdd:pfam02148 2 SLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYE----------------ETGHPLAVNLSTLTVYCYPCDDYVHDP 61
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
242-468 |
3.09e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 70.38 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 242 FMRYLLDHLHLElqggfngvsrsailqENSTLSASNkccinGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLD 321
Cdd:pfam13423 102 FNRFLLDQLSSE---------------ENSTPPNPS-----PAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 322 IPSQFrskrSKNQENGPVCSLRDCLRSFTDLEELDETelyMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFhwTAYLRNK 401
Cdd:pfam13423 162 YPRKP----SSNNKKPPNQTFSSILKSSLERETTTKA---WCEKCKRYQPLESRRTVRNLPPVLSLNAALT--NEEWRQL 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034592453 402 VDTYVEFPLRgldMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAY---------ATHEGRWFHFNDSTV 468
Cdd:pfam13423 233 WKTPGWLPPE---IGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFvkvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
137-487 |
1.54e-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: 59.43 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 137 TGLRNLGNTCFMNAILQSLSNIE-------QFCCYFKELPAVELRNGKTAGRRTyhTRSQGDNNVSLVEEFRKTLCALWQ 209
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKplrdlvlNFDESKAELASDYPTERRIGGREV--SRSELQRSNQFVYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 210 GSQTAFSPES-LFYVVwkimpnFRgyqQQDAHEFMRYLLDHLHLEL-QGGFNGVSRSAILQenstlsasnkcciNGASTV 287
Cdd:cd02666 80 SNTRSVTPSKeLAYLA------LR---QQDVTECIDNVLFQLEVALePISNAFAGPDTEDD-------------KEQSDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 288 VTAIF-GGILQNEVNCLICGTESRKFDPFLDLSLDIPSqFRSKRSKNQENGPvCSLRDCL-RSF-----TDLEELDETEL 360
Cdd:cd02666 138 IKRLFsGKTKQQLVPESMGNQPSVRTKTERFLSLLVDV-GKKGREIVVLLEP-KDLYDALdRYFdydslTKLPQRSQVQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 361 YMCHKCKKKQKSTKKFWIQKLPKVLcLHLKRfhWTAYLRNKVDTYVEFPLRGLDMKcylLEPENSGPESCLYDLAAVVVH 440
Cdd:cd02666 216 QLAQPLQRELISMDRYELPSSIDDI-DELIR--EAIQSESSLVRQAQNELAELKHE---IEKQFDDLKSYGYRLHAVFIH 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034592453 441 HGSgVGSGHYTAYATH--EGRWFHFNDSTVTLTDEETVV------KAKAYILFYV 487
Cdd:cd02666 290 RGE-ASSGHYWVYIKDfeENVWRKYNDETVTVVPASEVFlftlgnTATPYFLVYV 343
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
235-487 |
8.57e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 56.03 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 235 QQQDAHEFMRYLLDHLHLELQGGFNGVS-RSAILQENSTLsasnkccINGASTVVTAIFGGILQNevnCLICGtesrkfd 313
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAAAEAISpGEKSKNPMVQL-------FYGTFLTEGVLEGKPFCN---CETFG------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 314 pfldlslDIPSQFRSKRSknqengpvcsLRDCLRSFT---DLEELDETELYMCHKCKkkqkstkkfWIQKLPKVLCLHLK 390
Cdd:cd02665 84 -------QYPLQVNGYGN----------LHECLEAAMfegEVELLPSDHSVKSGQER---------WFTELPPVLTFELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 391 RFHWTAYLRNKVDTYVEFPlrgldmKCYLLEPensgpesclYDLAAVVVHHGSgVGSGHYTAYA--THEGRWFHFNDSTV 468
Cdd:cd02665 138 RFEFNQGRPEKIHDKLEFP------QIIQQVP---------YELHAVLVHEGQ-ANAGHYWAYIykQSRQEWEKYNDISV 201
|
250 260
....*....|....*....|....*..
gi 1034592453 469 TLTDEETVVK--------AKAYILFYV 487
Cdd:cd02665 202 TESSWEEVERdsfgggrnPSAYCLMYI 228
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
9-46 |
6.74e-08 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 48.90 E-value: 6.74e-08
10 20 30
....*....|....*....|....*....|....*...
gi 1034592453 9 VCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQVPL 46
Cdd:smart00290 4 VCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPL 41
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
378-486 |
3.84e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 45.21 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKRFhwtaYLRNKVDTYVEfpLRGLDMKCYLLEPENsgpesclYDLAAVVVHHGSGVGSGHYTAYA--- 454
Cdd:cd02673 143 IMTFPECLSINLKRY----KLRIATSDYLK--KNEEIMKKYCGTDAK-------YSLVAVICHLGESPYDGHYIAYTkel 209
|
90 100 110
....*....|....*....|....*....|....*
gi 1034592453 455 THEGRWFHFNDSTVTLTDEETVVKA---KAYILFY 486
Cdd:cd02673 210 YNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
279-486 |
8.72e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 44.43 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 279 CCINGASTVVTAIFGGILQNEVNC------LICGTESRKFDPFLDLSLDIPSQFRSKRSknqengpvcSLRDCLRSFTDL 352
Cdd:cd02672 59 CELGYLFSTLIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPLGSTKTSKES---------TFLQLLKRSLDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 353 EELDETElymCHKCKKKQKSTKKFWIQKLP----KVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLE---PENS 425
Cdd:cd02672 130 EKVTKAW---CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDklvKNRG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034592453 426 GPESCLYDLAAVVVH--HGSG-----VGSGHYTAYATHeGRWFHFNDSTVTLTDEetvvkaKAYILFY 486
Cdd:cd02672 207 QESIYKYELVGYVCEinDSSRgqhnvVFVIKVNEESTH-GRWYLFNDFLVTPVSE------LAYILLY 267
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
378-486 |
6.01e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 38.28 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034592453 378 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVeFPLRGLDMKcYLLEPENSGPESCLYD--------------------LAAV 437
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQKMFKKI-LIPDEIDIP-DFVADDPRACSKCQLEcrvcyddkdfsptcgkfklsLCSA 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034592453 438 VVHHGSGVGSGHYTAYA-------------THEGRWFHFNDstvtLTDEETV-----VKAK-----AYILFY 486
Cdd:cd02670 173 VCHRGTSLETGHYVAFVrygsysltetdneAYNAQWVFFDD----MADRDGVsngfnIPAArlledPYMLFY 240
|
|
| |
