|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
159-508 |
1.15e-76 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 243.89 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 159 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDSNVSLVEEFRKTLCALWQGSQ-TAF 237
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 238 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 317
Cdd:pfam00443 68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 318 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 398 FWIQKLPKALCLHLKRFHWTAYLRNKVDTYVQFPLRgLDMKCYLLEPENSG-PDSCLYDLAAVVVHHGSgVGSGHYTAYA 476
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYI 275
|
330 340 350
....*....|....*....|....*....|....*
gi 21450103 477 VH--EGRWFHFNDSTVTVTDEETVGKAK-AYILFY 508
Cdd:pfam00443 276 KAyeNNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-509 |
7.24e-73 |
|
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: 234.57 E-value: 7.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLsnieqfccyfkeLPAVELRNGKTAGRRTYHTRSQgDSNVSLVEEFRKTLCALWQ-GSQTAFS 238
Cdd:cd02660 2 GLINLGATCFMNVILQAL------------LHNPLLRNYFLSDRHSCTCLSC-SPNSCLSCAMDEIFQEFYYsGDRSPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 239 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNkcCIngastvVTAIFGGIL 318
Cdd:cd02660 69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN---------EANDESHCN--CI------IHQTFSGSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 319 QNEVNCLICGTESRKFDPFLDLSLDIPSQ-FRSKRSKNQENGPVCSLRDCLRSFTDLEELDETElYMCHKCKKKQKSTKK 397
Cdd:cd02660 132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKsTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 398 FWIQKLPKALCLHLKRF-HWTAYLRNKVDTYVQFPLRgLDMKCYL------LEPENSGPDSCLYDLAAVVVHHGSgVGSG 470
Cdd:cd02660 211 LSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLE-LNMTPYTsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 21450103 471 HYTAYA-VHEGRWFHFNDSTVTVTDEETVGKAKAYILFYV 509
Cdd:cd02660 289 HYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
158-509 |
2.25e-63 |
|
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: 209.05 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 158 ATGLRNLGNTCFMNAILQSLSNIEQFCCYFkelpavelrngktagRRTYHTRSQGDSNVSLVEEFRKTLCALWQGSQTAF 237
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYL---------------LSREHSKDCCNEGFCMMCALEAHVERALASSGPGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 238 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrSAILQENSTLSASNKccINGASTVVTAIFGGI 317
Cdd:cd02661 66 APRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ------------KACLDRFKKLKAVDP--SSQETTLVQQIFGGY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 318 LQNEVNCLICGTESRKFDPFLDLSLDIPSqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:cd02661 132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 398 FWIQKLPKALCLHLKRFhwTAYLRNKVDTYVQFPLRgLDMKCYLLEPENSgpdSCLYDLAAVVVHHGSGVGSGHYTAYA- 476
Cdd:cd02661 198 LTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMSQPNDG---PLKYKLYAVLVHSGFSPHSGHYYCYVk 271
|
330 340 350
....*....|....*....|....*....|...
gi 21450103 477 VHEGRWFHFNDSTVTVTDEETVGKAKAYILFYV 509
Cdd:cd02661 272 SSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
2.87e-62 |
|
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: 203.29 E-value: 2.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdsnvslveefrktlcalwqgsqtafsp 239
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGILQ 319
Cdd:cd02674 21 -----------------DQQDAQEFLLFLLDGLH----------------------------------SIIVDLFQGQLK 49
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02674 50 SRLTCLTCGKTSTTFEPFTYLSLPIP--------SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFHWTAYLRNKVDTYVQFPLRGLDMKCYLLEPENSGPDscLYDLAAVVVHHGSgVGSGHYTAYA--V 477
Cdd:cd02674 122 ISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPF--KYDLYAVVNHYGS-LNGGHYTAYCknN 198
|
330 340 350
....*....|....*....|....*....|.
gi 21450103 478 HEGRWFHFNDSTVTVTDEETVGKAKAYILFY 508
Cdd:cd02674 199 ETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
160-509 |
7.03e-62 |
|
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: 203.48 E-value: 7.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdsnvslveefrktlcalwqgsqtafsp 239
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILqenstlsasnkccingaSTVVTAIFGGILQ 319
Cdd:cd02257 21 -----------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------KSLIHDLFGGKLE 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIPSQfrskrsknqeNGPVCSLRDCLRSFTDLEELDETELYMChKCKKKQKSTKKFW 399
Cdd:cd02257 67 STIVCLECGHESVSTEPELFLSLPLPVK----------GLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFHWT-AYLRNKVDTYVQFPLRgLDMKCYLLE---PENSGPDSCLYDLAAVVVHHGSGVGSGHYTAY 475
Cdd:cd02257 136 IKKLPPVLIIHLKRFSFNeDGTKEKLNTKVSFPLE-LDLSPYLSEgekDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21450103 476 A--VHEGRWFHFNDSTVTVTDEETV-----GKAKAYILFYV 509
Cdd:cd02257 215 VkdPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
6.84e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 164.48 E-value: 6.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelrngktagrrtyhtrsqgdsnvslveefrktlcalwqgsqtafSP 239
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------------------TP 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDhlhlelqggfngvsrsailqenstlsasnkccinGASTVVTAIFGGILQ 319
Cdd:cd02667 33 KELFSQVCRKAPQFKGYQQQDSHELLRYLLD----------------------------------GLRTFIDSIFGGELT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkfw 399
Cdd:cd02667 79 STIMCESCGTVSLVYEPFLDLSLPRS----------DEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYL--- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFHWTAYLR-NKVDTYVQFPLRgLDMKCYLLEPENS--GPDSCLYDLAAVVVHHGSgVGSGHYTAYA 476
Cdd:cd02667 146 ISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFPEI-LDLAPFCDPKCNSseDKSSVLYRLYGVVEHSGT-MRSGHYVAYV 223
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21450103 477 -----------------------VHEGRWFHFNDSTVTVTDEETVGKAKAYILFY 508
Cdd:cd02667 224 kvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
7.70e-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: 165.18 E-value: 7.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFCCyFKELpavelrngktagrrtYHTRSQGDSNVSLVeefrktlcalwqgsqtafSP 239
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLTC-LKDL---------------FESISEQKKRTGVI------------------SP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCcingastvVTAIFGGILQ 319
Cdd:cd02663 47 KKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW--------VHEIFQGILT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknqengPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02663 119 NETRCLTCETVSSRDETFLDLSIDVE--------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFHWT-AYLRN-KVDTYVQFPlrgLDMKCYLLEPENSGPDScLYDLAAVVVHHGSGVGSGHYTAYAV 477
Cdd:cd02663 185 IKKLPKILALHLKRFKYDeQLNRYiKLFYRVVFP---LELRLFNTTDDAENPDR-LYELVAVVVHIGGGPNHGHYVSIVK 260
|
330 340 350
....*....|....*....|....*....|....*....
gi 21450103 478 HEGRWFHFNDSTVTVTDEETV--------GKAKAYILFY 508
Cdd:cd02663 261 SHGGWLLFDDETVEKIDENAVeeffgdspNQATAYVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-509 |
1.86e-38 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 143.55 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLsnieqfccYFKelPavELRNGKTAGRRTYhtRSQGDSNVSLVEEFRKTLCALWQGSQTAFSP 239
Cdd:cd02659 4 GLKNQGATCYMNSLLQQL--------YMT--P--EFRNAVYSIPPTE--DDDDNKSVPLALQRLFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 ESLFYVVWKiMPNfRGYQQQDAHEFMRYLLDHLHLELQGgfngvsrsaILQENStlsasnkccingastvVTAIFGGILQ 319
Cdd:cd02659 70 TDKTRSFGW-DSL-NTFEQHDVQEFFRVLFDKLEEKLKG---------TGQEGL----------------IKNLFGGKLV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02659 123 NYIICKECPHESEREEYFLDLQVAV------KGKKN--------LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVC 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFH--WTAYLRNKVDTYVQFPLRgLDMKCYL--------LEPENSGPDSCLYDLAAVVVHHGsGVGS 469
Cdd:cd02659 189 FKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLE-LDMEPYTekglakkeGDSEKKDSESYIYELHGVLVHSG-DAHG 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21450103 470 GHYTAY--AVHEGRWFHFNDSTVTVTDEETVGKA----------------------KAYILFYV 509
Cdd:cd02659 267 GHYYSYikDRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYE 330
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-490 |
1.42e-33 |
|
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: 129.85 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHtrsqgdSNVSLVEEFRKtLCALWQGSQTAFSP 239
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPH------EPQTIIDQLQL-IFAQLQFGNRSVVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 ESLFYVVWKIMPNfrgyQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqenstlsasnkcciNGASTVVTAIFGGILQ 319
Cdd:cd02668 74 PSGFVKALGLDTG----QQQDAQEFSKLFLSLLEAKLSKSKN----------------------PDLKNIVQDLFRGEYS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKnqengpvcSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02668 128 YVTQCSKCGRESSLPSKFYELELQL------KGHK--------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKR--FHWTAYLRNKVDTYVQFPLRgLDMKCYLLEpenSGPDSCLYDLAAVVVHHGSGVGSGHYTA--Y 475
Cdd:cd02668 194 LTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEI-LDMGEYLAE---SDEGSYVYELSGVLIHQGVSAYSGHYIAhiK 269
|
330
....*....|....*
gi 21450103 476 AVHEGRWFHFNDSTV 490
Cdd:cd02668 270 DEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
7.40e-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: 124.91 E-value: 7.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFkelpaveLRngktagrrtYHTRSQGDSNVSLVEEfrKTLCALWQGSQTAFS- 238
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQV-------LS---------LNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEa 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 239 -PESLFYVVWKimPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGI 317
Cdd:cd02664 63 pPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLH----------------------------------TLIEKMFGGK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 318 LQNEVNCLICGTESRKFDPFLDLSLDipsqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:cd02664 107 LSTTIRCLNCNSTSARTERFRDLDLS-----------------FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 398 FWIQKLPKALCLHLKRF------HWTAYLRNKV--DTYVQFPLR-----GLDMKCYLLEPENSGPDSC----LYDLAAVV 460
Cdd:cd02664 170 MKVTGAPEYLILTLLRFsydqktHVREKIMDNVsiNEVLSLPVRvesksSESPLEKKEEESGDDGELVtrqvHYRLYAVV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21450103 461 VHHGSGVGSGHYTAYAVH----------------------EGRWFHFNDSTVTVTDEETV-------GKAKAYILFY 508
Cdd:cd02664 250 VHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
8.37e-30 |
|
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: 119.23 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLsnieQFCCYFKElpavelrngktagrrTYHTRSQGDSNVSLVEEFRKTLCALWQGSQTAFSP 239
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL----YFCPGFKH---------------GLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 ESLFYVVWKIMPNFRGYQQQDAHEFMrylldhlhlelqggfngvsrsailqenstlsasnKCCINGASTVVTAIFGGILQ 319
Cdd:cd02671 87 RRLLNALREVNPMYEGYLQHDAQEVL----------------------------------QCILGNIQELVEKDFQGQLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGP-----VCSLRDCLRSFTDLEELDETELYMCHKCKKKQKS 394
Cdd:cd02671 133 LRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 395 TKKFWIQKLPKALCLHLKRFHWTAYLRN------KVDTYVQFPLrglDMKCyllEPENSGPDSCLYDLAAVVVHHGSGVG 468
Cdd:cd02671 213 ERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTPL---KLSL---EEWSTKPKNDVYRLFAVVMHSGATIS 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 21450103 469 SGHYTAYAvhegRWFHFNDSTVTVTDEE---------TVGKAKAYILFY 508
Cdd:cd02671 287 SGHYTAYV----RWLLFDDSEVKVTEEKdflealspnTSSTSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-508 |
7.52e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 118.58 E-value: 7.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 29 CSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQipllnhkrsekqekaqHTVCMDCSSYSTYC----YRCDDFVVN 104
Cdd:cd02669 19 CSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDN----------------HHVFLNLETLKFYClpdnYEIIDSSLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 105 DTKLGLvqkvrehlqnleNSAFTadrhrkRKLLENSSLNSKLLK-VNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQF 183
Cdd:cd02669 83 DIKYVL------------NPTYT------KEQISDLDRDPKLSRdLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 184 CCYF--KELPAVELRNGKTAGRRtyhtrsqgdsnvsLVEEFRKtlcaLWqgSQTAF----SP-ESLFYVVWKIMPNFRGY 256
Cdd:cd02669 145 RNFFllYENYENIKDRKSELVKR-------------LSELIRK----IW--NPRNFkghvSPhELLQAVSKVSKKKFSIT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 257 QQQDAHEFMRYLLDHLHLELQGgfngvsrsailqenstlsaSNKCcingASTVVTAIFGGILQNEVNCLI----CGTESR 332
Cdd:cd02669 206 EQSDPVEFLSWLLNTLHKDLGG-------------------SKKP----NSSIIHDCFQGKVQIETQKIKphaeEEGSKD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 333 KFD-----------PFLDLSLDIPSQ--FRSKRSKNQEngPVCSLRDCLRSFTdleELDETELymchkckkkQKSTKKFW 399
Cdd:cd02669 263 KFFkdsrvkktsvsPFLLLTLDLPPPplFKDGNEENII--PQVPLKQLLKKYD---GKTETEL---------KDSLKRYL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFHWTAYLRNKVDTYVQFPLRGLDMKCYLLEPENSGPDSCLYDLAAVVVHHGSGVGSGHYTAYAVHE 479
Cdd:cd02669 329 ISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHK 408
|
490 500 510
....*....|....*....|....*....|.
gi 21450103 480 GR--WFHFNDSTVTVTDEETVGKAKAYILFY 508
Cdd:cd02669 409 STnkWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
1.33e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 109.72 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKEL----------PA-------VELRNGKTAGRrTYHTRSQGDSNVslveef 222
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLenkfpsdvvdPAndlncqlIKLADGLLSGR-YSKPASLKSEND------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 223 rktlcalwqGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailQENSTLSASNkcc 302
Cdd:cd02658 74 ---------PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD----------------RESFKNLGLN--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 303 ingastvVTAIFGGILQNEVNCLICGteSRKFDPFLD--LSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDET 380
Cdd:cd02658 126 -------PNDLFKFMIEDRLECLSCK--KVKYTSELSeiLSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 381 elymCHKCKKKQKSTKKFWIQKLPKALCLHLKRF----HWTAylrNKVDTYVQFPLRGLDMKcyllepensgpdsclYDL 456
Cdd:cd02658 197 ----CSTCKEKTTATKTTGFKTFPDYLVINMKRFqlleNWVP---KKLDVPIDVPEELGPGK---------------YEL 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 21450103 457 AAVVVHHGSGVGSGHYTAY----AVHEGRWFHFNDSTVTVTDEETVGKAKAYILFY 508
Cdd:cd02658 255 IAFISHKGTSVHSGHYVAHikkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
159-511 |
2.00e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 113.82 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 159 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelRNGKTAGRRTYHTRSQGdsnvSLVEEFRKTLCALWQGSQTAFS 238
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLS------DEYEESINEENPLGMHG----SVASAYADLIKQLYDGNLHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 239 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGG--------------------------------------- 279
Cdd:COG5560 336 PSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIikkpytskpdlspgddvvvkkkakecwwehlkrndsiit 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 280 --FNGVSRSA----------------------------------ILQENST-------LSASNK---------------- 300
Cdd:COG5560 416 dlFQGMYKSTltcpgcgsvsitfdpfmdltlplpvsmvwkhtivVFPESGRrqplkieLDASSTirglkklvdaeygklg 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 301 ------CCI--NGASTVVTAIFGGILQ-------------NEVNCLIC---------GTESRKF-DPFLDLSLDIPSQFR 349
Cdd:COG5560 496 cfeikvMCIyyGGNYNMLEPADKVLLQdipqtdfvylyetNDNGIEVPvvhlriekgYKSKRLFgDPFLQLNVLIKASIY 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 350 SK--------------------------RSKNQENGP--------------------------------VC--------- 362
Cdd:COG5560 576 DKlvkefeellvlvemkktdvdlvseqvRLLREESSPsswlkleteidtkreeqveeegqmnfndavviSCeweekryls 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 363 --------------------SLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKALCLHLKRFHWTAYLRN 422
Cdd:COG5560 656 lfsydplwtireigaaertiTLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRD 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 423 KVDTYVQFPLRGLDMKCYLLEPENSgpdSCLYDLAAVVVHHGsGVGSGHYTAYA--VHEGRWFHFNDSTVTVTDEETVGK 500
Cdd:COG5560 736 KIDDLVEYPIDDLDLSGVEYMVDDP---RLIYDLYAVDNHYG-GLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVT 811
|
570
....*....|.
gi 21450103 501 AKAYILFYVER 511
Cdd:COG5560 812 SSAYVLFYRRK 822
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
8.17e-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: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLsnieqfccyfKELPAV--ELRNGKTAGRRTYHtrsqgdSNVSLVEEFRKTLCALwQGSQTAF 237
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL----------RSVPELrdALKNYNPARRGANQ------SSDNLTNALRDLFDTM-DKKQEPV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 238 SPESLFYVVWKIMPNF------RGYQQQDAHEFMRYLLDHLHLELQGGfnGVSRSailqenstlsasnkccingastVVT 311
Cdd:cd02657 64 PPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKLPGA--GSKGS----------------------FID 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 312 AIFGGILQNEVNCLICGT-ESRKFDPFLDLSLDIPSQFrskrsknqengPVCSLRDCLrsftdLEELDETELYMCHKCKK 390
Cdd:cd02657 120 QLFGIELETKMKCTESPDeEEVSTESEYKLQCHISITT-----------EVNYLQDGL-----KKGLEEEIEKHSPTLGR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 391 KQKSTKKFWIQKLPKALCLHLKRFHW--TAYLRNKVDTYVQFPLRgLDMKCYLLEpensgpdSCLYDLAAVVVHHGSGVG 468
Cdd:cd02657 184 DAIYTKTSRISRLPKYLTVQFVRFFWkrDIQKKAKILRKVKFPFE-LDLYELCTP-------SGYYELVAVITHQGRSAD 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 21450103 469 SGHYTAY--AVHEGRWFHFNDSTVTVTDEETVGKAK-------AYILFY 508
Cdd:cd02657 256 SGHYVAWvrRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
160-509 |
1.58e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 100.26 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSnieqfcCYFKELPAVELRNGKTAgrRTYHTRSQGDSNVSLVEEFRKTLCALWQGSQTAFSP 239
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA------LYLPKLDELLDDLSKEL--KVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 EslfyvvwkimpnFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNKccingastvVTAIFGGILQ 319
Cdd:COG5533 73 I------------PPMGSQEDAHELLGKLLDELKLDLVNSFT---------IRIFKTTKDK---------KKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 NEVNCLI--CGTESRKFDPFLD-LSLDIPSQFRSKRSKNQEngpvcslrdclrsftdLEELDETELYMChkckkkqkstk 396
Cdd:COG5533 123 IIIELPDqtWVNNLKTLQEFIDnMEELVDDETGVKAKENEE----------------LEVQAKQEYEVS----------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 397 kfwIQKLPKALCLHLKRFhwtAYL--RNKVDTYVQFPLrglDMKcylLEPENSGPD--SCLYDLAAVVVHHGSgVGSGHY 472
Cdd:COG5533 176 ---FVKLPKILTIQLKRF---ANLggNQKIDTEVDEKF---ELP---VKHDQILNIvkETYYDLVGFVLHQGS-LEGGHY 242
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 21450103 473 TAYAVHEGRWFHFNDSTVT---VTDEETVGKAKAYILFYV 509
Cdd:COG5533 243 IAYVKKGGKWEKANDSDVTpvsEEEAINEKAKNAYLYFYE 282
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
1.64e-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: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFccyfkelpavelrngktagrrtyhtrsqgdsnVSLVEEFRktlcalwqgsqtafsp 239
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSL--------------------------------IEYLEEFL---------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSrsailqenstlsasnkccingASTVVtaifggilq 319
Cdd:cd02662 33 -----------------EQQDAHELFQVLLETLEQLLKFPFDGLL---------------------ASRIV--------- 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 320 nevnCLICGTESR-KFDPFLDLSLDIPsqfrskrskNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCkkkqkstkkf 398
Cdd:cd02662 66 ----CLQCGESSKvRYESFTMLSLPVP---------NQSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQTV---------- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 399 wIQKLPKALCLHLKRFHWTA---YLRNKvdTYVQFPLRgLDMKcyllepensgpdscLYDLAAVVVHHGSgVGSGHYTAY 475
Cdd:cd02662 123 -IVRLPQILCIHLSRSVFDGrgtSTKNS--CKVSFPER-LPKV--------------LYRLRAVVVHYGS-HSSGHYVCY 183
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 21450103 476 ----------------------AVHEGRWFHFNDSTVTVTDEETVGKAK-AYILFY 508
Cdd:cd02662 184 rrkplfskdkepgsfvrmregpSSTSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
160-491 |
6.37e-19 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 90.70 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDSNVSLVEEFRKTlcalwqgsQTAFSP 239
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-------------TDHPRGRDSVALALQRLFYNL--------QTGEEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 240 -ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLhlelqggfngvsrsailqENSTlsasNKCCINGAstvVTAIFGGIL 318
Cdd:COG5077 254 vDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNL------------------EKSM----RGTVVENA---LNGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 319 QNEVNCLICGTESRKFDPFLDLsldipsQFRSKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKF 398
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDI------QLNVKGMKN--------LQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 399 WiQKLPKALCLHLKRFHWTaYLRN---KVDTYVQFPLRgLDMKCYL----LEPENSgpdSCLYDLAAVVVHHGSgVGSGH 471
Cdd:COG5077 375 F-ESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDLLPFLdrdaDKSENS---DAVYVLYGVLVHSGD-LHEGH 447
|
330 340
....*....|....*....|..
gi 21450103 472 YTAY--AVHEGRWFHFNDSTVT 491
Cdd:COG5077 448 YYALlkPEKDGRWYKFDDTRVT 469
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
29-105 |
1.49e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.53 E-value: 1.49e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21450103 29 CSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYedaqipllnhkrsekqEKAQHTVCMDCSSYSTYCYRCDDFVVND 105
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHY----------------EETGHPLAVNLSTLTVYCYPCDDYVHDP 61
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
264-490 |
8.80e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 66.14 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 264 FMRYLLDHLHLElqggfngvsrsailqENSTLSASNkccinGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLD 343
Cdd:pfam13423 102 FNRFLLDQLSSE---------------ENSTPPNPS-----PAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 344 IPSQFrskrSKNQENGPVCSLRDCLRSFTDLEELDETelyMCHKCKKKQKSTKKFWIQKLPKALCLHLKRFhwTAYLRNK 423
Cdd:pfam13423 162 YPRKP----SSNNKKPPNQTFSSILKSSLERETTTKA---WCEKCKRYQPLESRRTVRNLPPVLSLNAALT--NEEWRQL 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450103 424 VDTYVQFPLRgldMKCYLLEPENSGPDSCLYDLAAVVVHHGSGVGSGHYTAY---------AVHEGRWFHFNDSTV 490
Cdd:pfam13423 233 WKTPGWLPPE---IGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFvkvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-509 |
1.40e-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: 59.81 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 159 TGLRNLGNTCFMNAILQSLSNIE-------QFCCYFKELPAVELRNGKTAGRRTyhTRSQGDSNVSLVEEFRKTLCALWQ 231
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKplrdlvlNFDESKAELASDYPTERRIGGREV--SRSELQRSNQFVYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 232 GSQTAFSPES-LFYVVwkimpnFRgyqQQDAHEFMRYLLDHLHLEL-QGGFNGVSRSAILQenstlsasnkcciNGASTV 309
Cdd:cd02666 80 SNTRSVTPSKeLAYLA------LR---QQDVTECIDNVLFQLEVALePISNAFAGPDTEDD-------------KEQSDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 310 VTAIF-GGILQNEVNCLICGTESRKFDPFLDLSLDIPSqFRSKRSKNQENGPvCSLRDCL-RSF-----TDLEELDETEL 382
Cdd:cd02666 138 IKRLFsGKTKQQLVPESMGNQPSVRTKTERFLSLLVDV-GKKGREIVVLLEP-KDLYDALdRYFdydslTKLPQRSQVQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 383 YMCHKCKKKQKSTKKFWIQKLpKALCLHLKRfhWTAYLRNKVDTYVQFPLRGLDMKcylLEPENSGPDSCLYDLAAVVVH 462
Cdd:cd02666 216 QLAQPLQRELISMDRYELPSS-IDDIDELIR--EAIQSESSLVRQAQNELAELKHE---IEKQFDDLKSYGYRLHAVFIH 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21450103 463 HGSgVGSGHYTAYA--VHEGRWFHFNDSTVT-VTDEETVGK-----AKAYILFYV 509
Cdd:cd02666 290 RGE-ASSGHYWVYIkdFEENVWRKYNDETVTvVPASEVFLFtlgntATPYFLVYV 343
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-68 |
1.58e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.52 E-value: 1.58e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 21450103 29 CSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQIPL 68
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPL 41
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
257-509 |
2.28e-07 |
|
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: 51.79 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 257 QQQDAHEFMRYLLDHLHLELQGGFNGVS-RSAILQENSTLsasnkccINGASTVVTAIFGGILQNevnCLICGtesrkfd 335
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAAAEAISpGEKSKNPMVQL-------FYGTFLTEGVLEGKPFCN---CETFG------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 336 pfldlslDIPSQFRSKRSknqengpvcsLRDCLRSFT---DLEELDETELYMCHKCKkkqkstkkfWIQKLPKALCLHLK 412
Cdd:cd02665 84 -------QYPLQVNGYGN----------LHECLEAAMfegEVELLPSDHSVKSGQER---------WFTELPPVLTFELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 413 RFHWTAYLRNKVDTYVQFPlrgldmKCYLLEPensgpdsclYDLAAVVVHHGSgVGSGHYTAYAV--HEGRWFHFNDSTV 490
Cdd:cd02665 138 RFEFNQGRPEKIHDKLEFP------QIIQQVP---------YELHAVLVHEGQ-ANAGHYWAYIYkqSRQEWEKYNDISV 201
|
250 260
....*....|....*....|....*..
gi 21450103 491 TVTDEETVGK--------AKAYILFYV 509
Cdd:cd02665 202 TESSWEEVERdsfgggrnPSAYCLMYI 228
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
400-508 |
1.57e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 43.29 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 400 IQKLPKALCLHLKRFhwtaYLRNKVDTYVQfpLRGLDMKCYLLEPENsgpdsclYDLAAVVVHHGSGVGSGHYTAYA--- 476
Cdd:cd02673 143 IMTFPECLSINLKRY----KLRIATSDYLK--KNEEIMKKYCGTDAK-------YSLVAVICHLGESPYDGHYIAYTkel 209
|
90 100 110
....*....|....*....|....*....|....*
gi 21450103 477 VHEGRWFHFNDSTVTVTDEETVGKA---KAYILFY 508
Cdd:cd02673 210 YNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
301-508 |
7.68e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 41.34 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 301 CCINGASTVVTAIFGGILQNEVNC------LICGTESRKFDPFLDLSLDIPSQFRSKRSknqengpvcSLRDCLRSFTDL 374
Cdd:cd02672 59 CELGYLFSTLIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPLGSTKTSKES---------TFLQLLKRSLDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450103 375 EELDETElymCHKCKKKQKSTKKFWIQKLP----KALCLHLKRFH------WTAYLRNKVD-TYVQFPlrglDMKCYLLE 443
Cdd:cd02672 130 EKVTKAW---CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNgefddiNVVLPSGKVMqNKVSPK----AIDHDKLV 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21450103 444 PENSGPDSCLYDLAAVVVHHGSGVGSGHY-TAYAVHE-----GRWFHFNDSTVTVTDEetvgkaKAYILFY 508
Cdd:cd02672 203 KNRGQESIYKYELVGYVCEINDSSRGQHNvVFVIKVNeesthGRWYLFNDFLVTPVSE------LAYILLY 267
|
|
| |
