|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
115-464 |
3.81e-80 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 251.21 E-value: 3.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 115 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQ-TAF 193
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 194 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 273
Cdd:pfam00443 68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 274 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 353
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 354 FWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRgLDMKCYLLEPENSG-PESCLYDLAAVVVHHGSgVGSGHYTAY- 431
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYi 275
|
330 340 350
....*....|....*....|....*....|....*
gi 375493565 432 -ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 464
Cdd:pfam00443 276 kAYENNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-465 |
1.84e-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: 239.97 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLsnieqfccyfkeLPAVELRNGKTAGRRTYHTRSQGDNNvSLVEEFRKTLCALWQ-GSQTAFS 194
Cdd:cd02660 2 GLINLGATCFMNVILQAL------------LHNPLLRNYFLSDRHSCTCLSCSPNS-CLSCAMDEIFQEFYYsGDRSPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 195 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNkcCIngastvVTAIFGGIL 274
Cdd:cd02660 69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN---------EANDESHCN--CI------IHQTFSGSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 275 QNEVNCLICGTESRKFDPFLDLSLDIPSQ-FRSKRSKNQENGPVCSLRDCLRSFTDLEELDETElYMCHKCKKKQKSTKK 353
Cdd:cd02660 132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKsTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 354 FWIQKLPKVLCLHLKRF-HWTAYLRNKVDTYVEFPLRgLDMKCYL------LEPENSGPESCLYDLAAVVVHHGSgVGSG 426
Cdd:cd02660 211 LSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLE-LNMTPYTsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 375493565 427 HYTAYA-THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 465
Cdd:cd02660 289 HYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
114-465 |
5.64e-67 |
|
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: 217.14 E-value: 5.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 114 ATGLRNLGNTCFMNAILQSLSNIEQFCCYFkelpavelrngktagRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAF 193
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYL---------------LSREHSKDCCNEGFCMMCALEAHVERALASSGPGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 194 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrSAILQENSTLSASNKccINGASTVVTAIFGGI 273
Cdd:cd02661 66 APRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ------------KACLDRFKKLKAVDP--SSQETTLVQQIFGGY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 274 LQNEVNCLICGTESRKFDPFLDLSLDIPSqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 353
Cdd:cd02661 132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 354 FWIQKLPKVLCLHLKRFhwTAYLRNKVDTYVEFPLRgLDMKCYLLEPENsgpESCLYDLAAVVVHHGSGVGSGHYTAYA- 432
Cdd:cd02661 198 LTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMSQPND---GPLKYKLYAVLVHSGFSPHSGHYYCYVk 271
|
330 340 350
....*....|....*....|....*....|...
gi 375493565 433 THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 465
Cdd:cd02661 272 SSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
2.86e-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: 2.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 195
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGILQ 275
Cdd:cd02674 21 -----------------DQQDAQEFLLFLLDGLH----------------------------------SIIVDLFQGQLK 49
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 355
Cdd:cd02674 50 SRLTCLTCGKTSTTFEPFTYLSLPIP--------SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPEscLYDLAAVVVHHGSgVGSGHYTAYA--T 433
Cdd:cd02674 122 ISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPF--KYDLYAVVNHYGS-LNGGHYTAYCknN 198
|
330 340 350
....*....|....*....|....*....|.
gi 375493565 434 HEGRWFHFNDSTVTLTDEETVVKAKAYILFY 464
Cdd:cd02674 199 ETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
116-465 |
3.37e-64 |
|
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: 208.11 E-value: 3.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 195
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILqenstlsasnkccingaSTVVTAIFGGILQ 275
Cdd:cd02257 21 -----------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------KSLIHDLFGGKLE 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLICGTESRKFDPFLDLSLDIPSQfrskrsknqeNGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkFW 355
Cdd:cd02257 67 STIVCLECGHESVSTEPELFLSLPLPVK----------GLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKR-LK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKRFHWT-AYLRNKVDTYVEFPLRgLDMKCYLLE---PENSGPESCLYDLAAVVVHHGSGVGSGHYTAY 431
Cdd:cd02257 136 IKKLPPVLIIHLKRFSFNeDGTKEKLNTKVSFPLE-LDLSPYLSEgekDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 375493565 432 A--THEGRWFHFNDSTVTLTDEETVVK-----AKAYILFYV 465
Cdd:cd02257 215 VkdPSDGKWYKFNDDKVTEVSEEEVLEfgslsSSAYILFYE 255
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
7.69e-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: 168.72 E-value: 7.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafSP 195
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------------------TP 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDhlhlelqggfngvsrsailqenstlsasnkccinGASTVVTAIFGGILQ 275
Cdd:cd02667 33 KELFSQVCRKAPQFKGYQQQDSHELLRYLLD----------------------------------GLRTFIDSIFGGELT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkfw 355
Cdd:cd02667 79 STIMCESCGTVSLVYEPFLDLSLPRS----------DEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYL--- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKRFHWTAYLR-NKVDTYVEFPLRgLDMKCYLLEPENS--GPESCLYDLAAVVVHHGSgVGSGHYTAYA 432
Cdd:cd02667 146 ISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFPEI-LDLAPFCDPKCNSseDKSSVLYRLYGVVEHSGT-MRSGHYVAYV 223
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 375493565 433 -----------------------THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 464
Cdd:cd02667 224 kvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
1.14e-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: 166.33 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCyFKELpavelrngktagrrtYHtrsqgdnnvSLVEEFRKTlcalwqGSqtaFSP 195
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLTC-LKDL---------------FE---------SISEQKKRT------GV---ISP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCcingastvVTAIFGGILQ 275
Cdd:cd02663 47 KKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW--------VHEIFQGILT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknqengPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 355
Cdd:cd02663 119 NETRCLTCETVSSRDETFLDLSIDVE--------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKRFHWT-AYLRN-KVDTYVEFPlrgLDMKCYLLEPENSGPEScLYDLAAVVVHHGSGVGSGHYTAYAT 433
Cdd:cd02663 185 IKKLPKILALHLKRFKYDeQLNRYiKLFYRVVFP---LELRLFNTTDDAENPDR-LYELVAVVVHIGGGPNHGHYVSIVK 260
|
330 340 350
....*....|....*....|....*....|....*....
gi 375493565 434 HEGRWFHFNDSTVTLTDEETVVK--------AKAYILFY 464
Cdd:cd02663 261 SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-465 |
1.60e-41 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 150.87 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLsnieqfccYFKelPavELRNGktagRRTYHTRSQGDNNVSLVEEFRK--TLCALWQGSQTAF 193
Cdd:cd02659 4 GLKNQGATCYMNSLLQQL--------YMT--P--EFRNA----VYSIPPTEDDDDNKSVPLALQRlfLFLQLSESPVKTT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 194 SPESLFYVVWKiMPNfRGYQQQDAHEFMRYLLDHLHLELQGgfngvsrsaILQENStlsasnkccingastvVTAIFGGI 273
Cdd:cd02659 68 ELTDKTRSFGW-DSL-NTFEQHDVQEFFRVLFDKLEEKLKG---------TGQEGL----------------IKNLFGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 274 LQNEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 353
Cdd:cd02659 121 LVNYIICKECPHESEREEYFLDLQVAV------KGKKN--------LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 354 FWIQKLPKVLCLHLKRFH--WTAYLRNKVDTYVEFPLRgLDMKCYL--------LEPENSGPESCLYDLAAVVVHHGsGV 423
Cdd:cd02659 187 VCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLE-LDMEPYTekglakkeGDSEKKDSESYIYELHGVLVHSG-DA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375493565 424 GSGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKA----------------------KAYILFYV 465
Cdd:cd02659 265 HGGHYYSYikDRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYE 330
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-446 |
1.62e-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: 131.77 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKtLCALWQGSQTAFSP 195
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPH------EPQTIIDQLQL-IFAQLQFGNRSVVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 ESLFYVVWKIMPNfrgyQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqenstlsasnkcciNGASTVVTAIFGGILQ 275
Cdd:cd02668 74 PSGFVKALGLDTG----QQQDAQEFSKLFLSLLEAKLSKSKN----------------------PDLKNIVQDLFRGEYS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKnqengpvcSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 355
Cdd:cd02668 128 YVTQCSKCGRESSLPSKFYELELQL------KGHK--------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKR--FHWTAYLRNKVDTYVEFPLRgLDMKCYLLEpenSGPESCLYDLAAVVVHHGSGVGSGHYTA--Y 431
Cdd:cd02668 194 LTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEI-LDMGEYLAE---SDEGSYVYELSGVLIHQGVSAYSGHYIAhiK 269
|
330
....*....|....*
gi 375493565 432 ATHEGRWFHFNDSTV 446
Cdd:cd02668 270 DEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
2.64e-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: 125.68 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCYFkelpaveLRngktagrrtYHTRSQGDNNVSLVEEfrKTLCALWQGSQTAFS- 194
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQV-------LS---------LNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEa 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 195 -PESLFYVVWKimPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGI 273
Cdd:cd02664 63 pPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLH----------------------------------TLIEKMFGGK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 274 LQNEVNCLICGTESRKFDPFLDLSLDipsqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 353
Cdd:cd02664 107 LSTTIRCLNCNSTSARTERFRDLDLS-----------------FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 354 FWIQKLPKVLCLHLKRF------HWTAYLRNKV--DTYVEFPLR-----GLDMKCYLLEPENSGPESC----LYDLAAVV 416
Cdd:cd02664 170 MKVTGAPEYLILTLLRFsydqktHVREKIMDNVsiNEVLSLPVRvesksSESPLEKKEEESGDDGELVtrqvHYRLYAVV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375493565 417 VHHGSGVGSGHYTAYATH----------------------EGRWFHFNDSTVTLTDEETV-------VKAKAYILFY 464
Cdd:cd02664 250 VHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
3.28e-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: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLsnieQFCCYFKElpavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 195
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL----YFCPGFKH---------------GLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 ESLFYVVWKIMPNFRGYQQQDAHEFMrylldhlhlelqggfngvsrsailqenstlsasnKCCINGASTVVTAIFGGILQ 275
Cdd:cd02671 87 RRLLNALREVNPMYEGYLQHDAQEVL----------------------------------QCILGNIQELVEKDFQGQLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGP-----VCSLRDCLRSFTDLEELDETELYMCHKCKKKQKS 350
Cdd:cd02671 133 LRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 351 TKKFWIQKLPKVLCLHLKRFHWTAYLRN------KVDTYVEFPLrglDMKCyllEPENSGPESCLYDLAAVVVHHGSGVG 424
Cdd:cd02671 213 ERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTPL---KLSL---EEWSTKPKNDVYRLFAVVMHSGATIS 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 375493565 425 SGHYTAYAthegRWFHFNDSTVTLTDEE---------TVVKAKAYILFY 464
Cdd:cd02671 287 SGHYTAYV----RWLLFDDSEVKVTEEKdflealspnTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
309-464 |
3.21e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 118.45 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 309 SKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPL 388
Cdd:COG5560 666 REIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493565 389 RGLDMKCYLLEPENSgpeSCLYDLAAVVVHHGsGVGSGHYTAYA--THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 464
Cdd:COG5560 746 DDLDLSGVEYMVDDP---RLIYDLYAVDNHYG-GLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
3.24e-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: 113.96 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCYFKEL----------PA-------VELRNGKTAGRrTYHTRSQGDNNVslveef 178
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLenkfpsdvvdPAndlncqlIKLADGLLSGR-YSKPASLKSEND------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 179 rktlcalwqGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailQENSTLSASNkcc 258
Cdd:cd02658 74 ---------PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD----------------RESFKNLGLN--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 259 ingastvVTAIFGGILQNEVNCLICGteSRKFDPFLD--LSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDET 336
Cdd:cd02658 126 -------PNDLFKFMIEDRLECLSCK--KVKYTSELSeiLSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 337 elymCHKCKKKQKSTKKFWIQKLPKVLCLHLKRF----HWTAylrNKVDTYVEFPLRGLDMKcyllepensgpesclYDL 412
Cdd:cd02658 197 ----CSTCKEKTTATKTTGFKTFPDYLVINMKRFqlleNWVP---KKLDVPIDVPEELGPGK---------------YEL 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 375493565 413 AAVVVHHGSGVGSGHYTAY----ATHEGRWFHFNDSTVTLTDEETVVKAKAYILFY 464
Cdd:cd02658 255 IAFISHKGTSVHSGHYVAHikkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
116-465 |
8.45e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSnieqfcCYFKELPAVELRNGKTAgrRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 195
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA------LYLPKLDELLDDLSKEL--KVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 EslfyvvwkimpnFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNKccingastvVTAIFGGILQ 275
Cdd:COG5533 73 I------------PPMGSQEDAHELLGKLLDELKLDLVNSFT---------IRIFKTTKDK---------KKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 NEVNCLI--CGTESRKFDPFLD-LSLDIPSQFRSKRSKNQEngpvcslrdclrsftdLEELDETELYMChkckkkqkstk 352
Cdd:COG5533 123 IIIELPDqtWVNNLKTLQEFIDnMEELVDDETGVKAKENEE----------------LEVQAKQEYEVS----------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 353 kfwIQKLPKVLCLHLKRFhwtAYL--RNKVDTYVEFPLrglDMKCYLLEPENSGPEScLYDLAAVVVHHGSgVGSGHYTA 430
Cdd:COG5533 176 ---FVKLPKILTIQLKRF---ANLggNQKIDTEVDEKF---ELPVKHDQILNIVKET-YYDLVGFVLHQGS-LEGGHYIA 244
|
330 340 350
....*....|....*....|....*....|....*...
gi 375493565 431 YATHEGRWFHFNDSTVTLTDEETVVKAK---AYILFYV 465
Cdd:COG5533 245 YVKKGGKWEKANDSDVTPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
2.51e-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: 105.49 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLsnieqfccyfKELPAV--ELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKTLCALwQGSQTAF 193
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL----------RSVPELrdALKNYNPARRGANQ------SSDNLTNALRDLFDTM-DKKQEPV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 194 SPESLFYVVWKIMPNF------RGYQQQDAHEFMRYLLDHLHLELQGGfnGVSRSailqenstlsasnkccingastVVT 267
Cdd:cd02657 64 PPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKLPGA--GSKGS----------------------FID 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 268 AIFGGILQNEVNCLICGT-ESRKFDPFLDLSLDIPSQFrskrsknqengPVCSLRDCLrsftdLEELDETELYMCHKCKK 346
Cdd:cd02657 120 QLFGIELETKMKCTESPDeEEVSTESEYKLQCHISITT-----------EVNYLQDGL-----KKGLEEEIEKHSPTLGR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 347 KQKSTKKFWIQKLPKVLCLHLKRFHW--TAYLRNKVDTYVEFPLRgLDMKCYLlepensgPESCLYDLAAVVVHHGSGVG 424
Cdd:cd02657 184 DAIYTKTSRISRLPKYLTVQFVRFFWkrDIQKKAKILRKVKFPFE-LDLYELC-------TPSGYYELVAVITHQGRSAD 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 375493565 425 SGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKAK-------AYILFY 464
Cdd:cd02657 256 SGHYVAWvrRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
1.05e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 106.25 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCYF--KELPAVELRNGKTAGRRtyhtrsqgdnnvsLVEEFRKtlcaLWqgSQTAF 193
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFllYENYENIKDRKSELVKR-------------LSELIRK----IW--NPRNF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 194 ----SP-ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGgfngvsrsailqenstlsaSNKCcingASTVVTA 268
Cdd:cd02669 182 kghvSPhELLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGG-------------------SKKP----NSSIIHD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 269 IFGGILQNEVNCLI----CGTESRKFD-----------PFLDLSLDIPSQ--FRSKRSKNQEngPVCSLRDCLRSFTdle 331
Cdd:cd02669 239 CFQGKVQIETQKIKphaeEEGSKDKFFkdsrvkktsvsPFLLLTLDLPPPplFKDGNEENII--PQVPLKQLLKKYD--- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 332 ELDETELymchkckkkQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYD 411
Cdd:cd02669 314 GKTETEL---------KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYN 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 375493565 412 LAAVVVHHGSGVGSGHYTAYATHEGR--WFHFNDSTVTLTDEETVVKAKAYILFY 464
Cdd:cd02669 385 LVANIVHEGTPQEDGTWRVQLRHKSTnkWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
116-464 |
1.79e-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: 98.59 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFccyfkelpavelrngktagrrtyhtrsqgdnnVSLVEEFRktlcalwqgsqtafsp 195
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSL--------------------------------IEYLEEFL---------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSrsailqenstlsasnkccingASTVVtaifggilq 275
Cdd:cd02662 33 -----------------EQQDAHELFQVLLETLEQLLKFPFDGLL---------------------ASRIV--------- 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 276 nevnCLICGTESR-KFDPFLDLSLDIPsqfrskrskNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCkkkqkstkkf 354
Cdd:cd02662 66 ----CLQCGESSKvRYESFTMLSLPVP---------NQSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQTV---------- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 355 wIQKLPKVLCLHLKRFHWT---AYLRNKvdTYVEFPLRgLDMKcyllepensgpescLYDLAAVVVHHGSgVGSGHYTAY 431
Cdd:cd02662 123 -IVRLPQILCIHLSRSVFDgrgTSTKNS--CKVSFPER-LPKV--------------LYRLRAVVVHYGS-HSSGHYVCY 183
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 375493565 432 ----------------------ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 464
Cdd:cd02662 184 rrkplfskdkepgsfvrmregpSSTSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
116-447 |
6.68e-21 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 96.48 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 116 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHtrSQGDNNVSLVeefrktLCALWQGSQTAFSP 195
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-------------TDH--PRGRDSVALA------LQRLFYNLQTGEEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 196 -ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLhlelqggfngvsrsailqENSTlsasNKCCINGAstvVTAIFGGIL 274
Cdd:COG5077 254 vDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNL------------------EKSM----RGTVVENA---LNGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 275 QNEVNCLICGTESRKFDPFLDLsldipsQFRSKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKF 354
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDI------QLNVKGMKN--------LQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 355 WiQKLPKVLCLHLKRFHWTaYLRN---KVDTYVEFPLRgLDMKCYL----LEPENSgpeSCLYDLAAVVVHHGSgVGSGH 427
Cdd:COG5077 375 F-ESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDLLPFLdrdaDKSENS---DAVYVLYGVLVHSGD-LHEGH 447
|
330 340
....*....|....*....|..
gi 375493565 428 YTAYATHE--GRWFHFNDSTVT 447
Cdd:COG5077 448 YYALLKPEkdGRWYKFDDTRVT 469
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
115-301 |
6.43e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.94 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 115 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelRNGKTAGRRTYHTRSQGdnnvSLVEEFRKTLCALWQGSQTAFS 194
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLS------DEYEESINEENPLGMHG----SVASAYADLIKQLYDGNLHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 195 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNG--VSRSAILQENSTL--SASNKCC---INGASTVVT 267
Cdd:COG5560 336 PSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKpyTSKPDLSPGDDVVvkKKAKECWwehLKRNDSIIT 415
|
170 180 190
....*....|....*....|....*....|....
gi 375493565 268 AIFGGILQNEVNCLICGTESRKFDPFLDLSLDIP 301
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
220-446 |
4.32e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 69.99 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 220 FMRYLLDHLHLElqggfngvsrsailqENSTLSASNkccinGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLD 299
Cdd:pfam13423 102 FNRFLLDQLSSE---------------ENSTPPNPS-----PAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 300 IPSQFrskrSKNQENGPVCSLRDCLRSFTDLEELDETelyMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFhwTAYLRNK 379
Cdd:pfam13423 162 YPRKP----SSNNKKPPNQTFSSILKSSLERETTTKA---WCEKCKRYQPLESRRTVRNLPPVLSLNAALT--NEEWRQL 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375493565 380 VDTYVEFPLRgldMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAY---------ATHEGRWFHFNDSTV 446
Cdd:pfam13423 233 WKTPGWLPPE---IGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFvkvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
115-465 |
1.47e-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: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 115 TGLRNLGNTCFMNAILQSLSNIE-------QFCCYFKELPAVELRNGKTAGRRTyhTRSQGDNNVSLVEEFRKTLCALWQ 187
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKplrdlvlNFDESKAELASDYPTERRIGGREV--SRSELQRSNQFVYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 188 GSQTAFSPES-LFYVVwkimpnFRgyqQQDAHEFMRYLLDHLHLEL-QGGFNGVSRSAILQenstlsasnkcciNGASTV 265
Cdd:cd02666 80 SNTRSVTPSKeLAYLA------LR---QQDVTECIDNVLFQLEVALePISNAFAGPDTEDD-------------KEQSDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 266 VTAIF-GGILQNEVNCLICGTESRKFDPFLDLSLDIPSqFRSKRSKNQENGPvCSLRDCL-RSF-----TDLEELDETEL 338
Cdd:cd02666 138 IKRLFsGKTKQQLVPESMGNQPSVRTKTERFLSLLVDV-GKKGREIVVLLEP-KDLYDALdRYFdydslTKLPQRSQVQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 339 YMCHKCKKKQKSTKKFWIQKLPKVLcLHLKRfhWTAYLRNKVDTYVEFPLRGLDMKcylLEPENSGPESCLYDLAAVVVH 418
Cdd:cd02666 216 QLAQPLQRELISMDRYELPSSIDDI-DELIR--EAIQSESSLVRQAQNELAELKHE---IEKQFDDLKSYGYRLHAVFIH 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 375493565 419 HGSgVGSGHYTAYATH--EGRWFHFNDSTVTLTDEETVV------KAKAYILFYV 465
Cdd:cd02666 290 RGE-ASSGHYWVYIKDfeENVWRKYNDETVTVVPASEVFlftlgnTATPYFLVYV 343
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
213-465 |
4.73e-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: 56.80 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 213 QQQDAHEFMRYLLDHLHLELQGGFNGVS-RSAILQENSTLsasnkccINGASTVVTAIFGGILQNevnCLICGtesrkfd 291
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAAAEAISpGEKSKNPMVQL-------FYGTFLTEGVLEGKPFCN---CETFG------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 292 pfldlslDIPSQFRSKRSknqengpvcsLRDCLRSFT---DLEELDETELYMCHKCKkkqkstkkfWIQKLPKVLCLHLK 368
Cdd:cd02665 84 -------QYPLQVNGYGN----------LHECLEAAMfegEVELLPSDHSVKSGQER---------WFTELPPVLTFELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 369 RFHWTAYLRNKVDTYVEFPlrgldmKCYLLEPensgpesclYDLAAVVVHHGSgVGSGHYTAYA--THEGRWFHFNDSTV 446
Cdd:cd02665 138 RFEFNQGRPEKIHDKLEFP------QIIQQVP---------YELHAVLVHEGQ-ANAGHYWAYIykQSRQEWEKYNDISV 201
|
250 260
....*....|....*....|....*..
gi 375493565 447 TLTDEETVVK--------AKAYILFYV 465
Cdd:cd02665 202 TESSWEEVERdsfgggrnPSAYCLMYI 228
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
356-464 |
3.88e-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: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKRFhwtaYLRNKVDTYVEfpLRGLDMKCYLLEPENsgpesclYDLAAVVVHHGSGVGSGHYTAYA--- 432
Cdd:cd02673 143 IMTFPECLSINLKRY----KLRIATSDYLK--KNEEIMKKYCGTDAK-------YSLVAVICHLGESPYDGHYIAYTkel 209
|
90 100 110
....*....|....*....|....*....|....*
gi 375493565 433 THEGRWFHFNDSTVTLTDEETVVKA---KAYILFY 464
Cdd:cd02673 210 YNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
257-464 |
8.26e-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: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 257 CCINGASTVVTAIFGGILQNEVNC------LICGTESRKFDPFLDLSLDIPSQFRSKRSknqengpvcSLRDCLRSFTDL 330
Cdd:cd02672 59 CELGYLFSTLIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPLGSTKTSKES---------TFLQLLKRSLDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 331 EELDETElymCHKCKKKQKSTKKFWIQKLP----KVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLE---PENS 403
Cdd:cd02672 130 EKVTKAW---CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDklvKNRG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493565 404 GPESCLYDLAAVVVH--HGSG-----VGSGHYTAYATHeGRWFHFNDSTVTLTDEetvvkaKAYILFY 464
Cdd:cd02672 207 QESIYKYELVGYVCEinDSSRgqhnvVFVIKVNEESTH-GRWYLFNDFLVTPVSE------LAYILLY 267
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
29-53 |
8.62e-04 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 37.63 E-value: 8.62e-04
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
356-464 |
4.53e-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: 38.66 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493565 356 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVeFPLRGLDMKcYLLEPENSGPESCLYD--------------------LAAV 415
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQKMFKKI-LIPDEIDIP-DFVADDPRACSKCQLEcrvcyddkdfsptcgkfklsLCSA 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375493565 416 VVHHGSGVGSGHYTAYA-------------THEGRWFHFNDstvtLTDEETV-----VKAK-----AYILFY 464
Cdd:cd02670 173 VCHRGTSLETGHYVAFVrygsysltetdneAYNAQWVFFDD----MADRDGVsngfnIPAArlledPYMLFY 240
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-53 |
7.58e-03 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 34.65 E-value: 7.58e-03
|
| |
