|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
159-508 |
4.55e-79 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 250.05 E-value: 4.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 159 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQ-TAF 237
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIS-------------PLSEDSRYNKDINLLCALRDLFKALQKNSKsSSV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 238 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQggfngvsrsailQENSTLSASNkccingastvVTAIFGGI 317
Cdd:pfam00443 68 SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLN------------GNHSTENESL----------ITDLFRGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 318 LQNEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:pfam00443 126 LKSRLKCLSCGEVSETFEPFSDLSLPIP--------GDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 398 FWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRgLDMKCYLLEPENSG-PESCLYDLAAVVVHHGSgVGSGHYTAY- 475
Cdd:pfam00443 198 LKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKtNNLQDYRLVAVVVHSGS-LSSGHYIAYi 275
|
330 340 350
....*....|....*....|....*....|....*
gi 55770886 476 -ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 508
Cdd:pfam00443 276 kAYENNRWYKFDDEKVTEVDEETAVLSSsAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-509 |
2.57e-74 |
|
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: 238.43 E-value: 2.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLsnieqfccyfkeLPAVELRNGKTAGRRTYHTRSQGDNNvSLVEEFRKTLCALWQ-GSQTAFS 238
Cdd:cd02660 2 GLINLGATCFMNVILQAL------------LHNPLLRNYFLSDRHSCTCLSCSPNS-CLSCAMDEIFQEFYYsGDRSPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 239 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNkcCIngastvVTAIFGGIL 318
Cdd:cd02660 69 PINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN---------EANDESHCN--CI------IHQTFSGSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 319 QNEVNCLICGTESRKFDPFLDLSLDIPSQ-FRSKRSKNQENGPVCSLRDCLRSFTDLEELDETElYMCHKCKKKQKSTKK 397
Cdd:cd02660 132 QSSVTCQRCGGVSTTVDPFLDLSLDIPNKsTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 398 FWIQKLPKVLCLHLKRF-HWTAYLRNKVDTYVEFPLRgLDMKCYL------LEPENSGPESCLYDLAAVVVHHGSgVGSG 470
Cdd:cd02660 211 LSIKKLPPVLCFQLKRFeHSLNKTSRKIDTYVQFPLE-LNMTPYTsssigdTQDSNSLDPDYTYDLFAVVVHKGT-LDTG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 55770886 471 HYTAYA-THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 509
Cdd:cd02660 289 HYTAYCrQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
158-509 |
5.05e-66 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 215.99 E-value: 5.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 158 ATGLRNLGNTCFMNAILQSLSNIEQFCCYFkelpavelrngktagRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAF 237
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYL---------------LSREHSKDCCNEGFCMMCALEAHVERALASSGPGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 238 SPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrSAILQENSTLSASNKccINGASTVVTAIFGGI 317
Cdd:cd02661 66 APRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ------------KACLDRFKKLKAVDP--SSQETTLVQQIFGGY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 318 LQNEVNCLICGTESRKFDPFLDLSLDIPSqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:cd02661 132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 398 FWIQKLPKVLCLHLKRFhwTAYLRNKVDTYVEFPLRgLDMKCYLLEPENsgpESCLYDLAAVVVHHGSGVGSGHYTAYA- 476
Cdd:cd02661 198 LTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMSQPND---GPLKYKLYAVLVHSGFSPHSGHYYCYVk 271
|
330 340 350
....*....|....*....|....*....|...
gi 55770886 477 THEGRWFHFNDSTVTLTDEETVVKAKAYILFYV 509
Cdd:cd02661 272 SSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
2.27e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 206.37 E-value: 2.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 239
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGILQ 319
Cdd:cd02674 21 -----------------DQQDAQEFLLFLLDGLH----------------------------------SIIVDLFQGQLK 49
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02674 50 SRLTCLTCGKTSTTFEPFTYLSLPIP--------SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPEscLYDLAAVVVHHGSgVGSGHYTAYA--T 477
Cdd:cd02674 122 ISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPF--KYDLYAVVNHYGS-LNGGHYTAYCknN 198
|
330 340 350
....*....|....*....|....*....|.
gi 55770886 478 HEGRWFHFNDSTVTLTDEETVVKAKAYILFY 508
Cdd:cd02674 199 ETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
160-509 |
5.39e-63 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 206.18 E-value: 5.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNieqfccyfkelpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafsp 239
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILqenstlsasnkccingaSTVVTAIFGGILQ 319
Cdd:cd02257 21 -----------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------KSLIHDLFGGKLE 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLICGTESRKFDPFLDLSLDIPSQfrskrsknqeNGPVCSLRDCLRSFTDLEELDETELYMChKCKKKQKSTKKFW 399
Cdd:cd02257 67 STIVCLECGHESVSTEPELFLSLPLPVK----------GLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFHWT-AYLRNKVDTYVEFPLRgLDMKCYLLE---PENSGPESCLYDLAAVVVHHGSGVGSGHYTAY 475
Cdd:cd02257 136 IKKLPPVLIIHLKRFSFNeDGTKEKLNTKVSFPLE-LDLSPYLSEgekDSDSDNGSYKYELVAVVVHSGTSADSGHYVAY 214
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 55770886 476 A--THEGRWFHFNDSTVTLTDEETVVK-----AKAYILFYV 509
Cdd:cd02257 215 VkdPSDGKWYKFNDDKVTEVSEEEVLEfgslsSSAYILFYE 255
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
1.99e-48 |
|
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: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelrngktagrrtyhtrsqgdnnvslveefrktlcalwqgsqtafSP 239
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------------------TP 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDhlhlelqggfngvsrsailqenstlsasnkccinGASTVVTAIFGGILQ 319
Cdd:cd02667 33 KELFSQVCRKAPQFKGYQQQDSHELLRYLLD----------------------------------GLRTFIDSIFGGELT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKkfw 399
Cdd:cd02667 79 STIMCESCGTVSLVYEPFLDLSLPRS----------DEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYL--- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFHWTAYLR-NKVDTYVEFPLRgLDMKCYLLEPENS--GPESCLYDLAAVVVHHGSgVGSGHYTAYA 476
Cdd:cd02667 146 ISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFPEI-LDLAPFCDPKCNSseDKSSVLYRLYGVVEHSGT-MRSGHYVAYV 223
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 55770886 477 -----------------------THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 508
Cdd:cd02667 224 kvrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
6.19e-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: 6.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFCCyFKELpavelrngktagrrtYHtrsqgdnnvSLVEEFRKTlcalwqGSqtaFSP 239
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLTC-LKDL---------------FE---------SISEQKKRT------GV---ISP 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCcingastvVTAIFGGILQ 319
Cdd:cd02663 47 KKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW--------VHEIFQGILT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLICGTESRKFDPFLDLSLDIPsqfrskrsknqengPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02663 119 NETRCLTCETVSSRDETFLDLSIDVE--------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFHWT-AYLRN-KVDTYVEFPlrgLDMKCYLLEPENSGPEScLYDLAAVVVHHGSGVGSGHYTAYAT 477
Cdd:cd02663 185 IKKLPKILALHLKRFKYDeQLNRYiKLFYRVVFP---LELRLFNTTDDAENPDR-LYELVAVVVHIGGGPNHGHYVSIVK 260
|
330 340 350
....*....|....*....|....*....|....*....
gi 55770886 478 HEGRWFHFNDSTVTLTDEETVVK--------AKAYILFY 508
Cdd:cd02663 261 SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-509 |
1.04e-40 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 149.72 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLsnieqfccYFKelPavELRNGktagRRTYHTRSQGDNNVSLVEEFRK--TLCALWQGSQTAF 237
Cdd:cd02659 4 GLKNQGATCYMNSLLQQL--------YMT--P--EFRNA----VYSIPPTEDDDDNKSVPLALQRlfLFLQLSESPVKTT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 238 SPESLFYVVWKiMPNfRGYQQQDAHEFMRYLLDHLHLELQGgfngvsrsaILQENStlsasnkccingastvVTAIFGGI 317
Cdd:cd02659 68 ELTDKTRSFGW-DSL-NTFEQHDVQEFFRVLFDKLEEKLKG---------TGQEGL----------------IKNLFGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 318 LQNEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:cd02659 121 LVNYIICKECPHESEREEYFLDLQVAV------KGKKN--------LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 398 FWIQKLPKVLCLHLKRFH--WTAYLRNKVDTYVEFPLRgLDMKCYL--------LEPENSGPESCLYDLAAVVVHHGsGV 467
Cdd:cd02659 187 VCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLE-LDMEPYTekglakkeGDSEKKDSESYIYELHGVLVHSG-DA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55770886 468 GSGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKA----------------------KAYILFYV 509
Cdd:cd02659 265 HGGHYYSYikDRDDGKWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYE 330
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-490 |
5.29e-34 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 131.00 E-value: 5.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKtLCALWQGSQTAFSP 239
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPH------EPQTIIDQLQL-IFAQLQFGNRSVVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 ESLFYVVWKIMPNfrgyQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqenstlsasnkcciNGASTVVTAIFGGILQ 319
Cdd:cd02668 74 PSGFVKALGLDTG----QQQDAQEFSKLFLSLLEAKLSKSKN----------------------PDLKNIVQDLFRGEYS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLICGTESRKFDPFLDLSLDIpsqfrsKRSKnqengpvcSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFW 399
Cdd:cd02668 128 YVTQCSKCGRESSLPSKFYELELQL------KGHK--------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKR--FHWTAYLRNKVDTYVEFPLRgLDMKCYLLEpenSGPESCLYDLAAVVVHHGSGVGSGHYTA--Y 475
Cdd:cd02668 194 LTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFPEI-LDMGEYLAE---SDEGSYVYELSGVLIHQGVSAYSGHYIAhiK 269
|
330
....*....|....*
gi 55770886 476 ATHEGRWFHFNDSTV 490
Cdd:cd02668 270 DEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
7.33e-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: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFkelpaveLRngktagrrtYHTRSQGDNNVSLVEEfrKTLCALWQGSQTAFS- 238
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQV-------LS---------LNLPRLGDSQSVMKKL--QLLQAHLMHTQRRAEa 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 239 -PESLFYVVWKimPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailqenstlsasnkccingasTVVTAIFGGI 317
Cdd:cd02664 63 pPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLH----------------------------------TLIEKMFGGK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 318 LQNEVNCLICGTESRKFDPFLDLSLDipsqfrskrsknqengpVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKK 397
Cdd:cd02664 107 LSTTIRCLNCNSTSARTERFRDLDLS-----------------FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 398 FWIQKLPKVLCLHLKRF------HWTAYLRNKV--DTYVEFPLR-----GLDMKCYLLEPENSGPESC----LYDLAAVV 460
Cdd:cd02664 170 MKVTGAPEYLILTLLRFsydqktHVREKIMDNVsiNEVLSLPVRvesksSESPLEKKEEESGDDGELVtrqvHYRLYAVV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770886 461 VHHGSGVGSGHYTAYATH----------------------EGRWFHFNDSTVTLTDEETV-------VKAKAYILFY 508
Cdd:cd02664 250 VHSGYSSESGHYFTYARDqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
8.13e-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: 116.53 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLsnieQFCCYFKElpavelrngktagrrTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 239
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL----YFCPGFKH---------------GLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 ESLFYVVWKIMPNFRGYQQQDAHEFMrylldhlhlelqggfngvsrsailqenstlsasnKCCINGASTVVTAIFGGILQ 319
Cdd:cd02671 87 RRLLNALREVNPMYEGYLQHDAQEVL----------------------------------QCILGNIQELVEKDFQGQLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGP-----VCSLRDCLRSFTDLEELDETELYMCHKCKKKQKS 394
Cdd:cd02671 133 LRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 395 TKKFWIQKLPKVLCLHLKRFHWTAYLRN------KVDTYVEFPLrglDMKCyllEPENSGPESCLYDLAAVVVHHGSGVG 468
Cdd:cd02671 213 ERSLLFDKLPEVITIHLKCFAANGSEFDcygglsKVNTPLLTPL---KLSL---EEWSTKPKNDVYRLFAVVMHSGATIS 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 55770886 469 SGHYTAYAthegRWFHFNDSTVTLTDEE---------TVVKAKAYILFY 508
Cdd:cd02671 287 SGHYTAYV----RWLLFDDSEVKVTEEKdflealspnTSSTSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-508 |
1.22e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 118.19 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 29 CSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQvpltnhkksekqdkvqHTVCMDCSSYSTYC----YRCDDFVVN 104
Cdd:cd02669 19 CSVSLSNLNVYACLVCGKYFQGRGKGSHAYTHSLEDN----------------HHVFLNLETLKFYClpdnYEIIDSSLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 105 DTKLGLvqkvrehlqnleNSAFTadrhkkRKLLENSTLNSKLLK-VNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQF 183
Cdd:cd02669 83 DIKYVL------------NPTYT------KEQISDLDRDPKLSRdLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 184 CCYF--KELPAVELRNGKTAGRRtyhtrsqgdnnvsLVEEFRKtlcaLWqgSQTAF----SP-ESLFYVVWKIMPNFRGY 256
Cdd:cd02669 145 RNFFllYENYENIKDRKSELVKR-------------LSELIRK----IW--NPRNFkghvSPhELLQAVSKVSKKKFSIT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 257 QQQDAHEFMRYLLDHLHLELQGgfngvsrsailqenstlsaSNKCcingASTVVTAIFGGILQNEVNCLI----CGTESR 332
Cdd:cd02669 206 EQSDPVEFLSWLLNTLHKDLGG-------------------SKKP----NSSIIHDCFQGKVQIETQKIKphaeEEGSKD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 333 KFD-----------PFLDLSLDIPSQ--FRSKRSKNQEngPVCSLRDCLRSFTdleELDETELymchkckkkQKSTKKFW 399
Cdd:cd02669 263 KFFkdsrvkktsvsPFLLLTLDLPPPplFKDGNEENII--PQVPLKQLLKKYD---GKTETEL---------KDSLKRYL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHE 479
Cdd:cd02669 329 ISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTPQEDGTWRVQLRHK 408
|
490 500 510
....*....|....*....|....*....|.
gi 55770886 480 GR--WFHFNDSTVTLTDEETVVKAKAYILFY 508
Cdd:cd02669 409 STnkWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
353-508 |
6.64e-28 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 118.45 E-value: 6.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 353 SKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPL 432
Cdd:COG5560 666 REIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770886 433 RGLDMKCYLLEPENSgpeSCLYDLAAVVVHHGsGVGSGHYTAYA--THEGRWFHFNDSTVTLTDEETVVKAKAYILFY 508
Cdd:COG5560 746 DDLDLSGVEYMVDDP---RLIYDLYAVDNHYG-GLSGGHYTAYArnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
1.06e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 112.80 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKEL----------PA-------VELRNGKTAGRrTYHTRSQGDNNVslveef 222
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLenkfpsdvvdPAndlncqlIKLADGLLSGR-YSKPASLKSEND------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 223 rktlcalwqGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHlelqggfngvsrsailQENSTLSASNkcc 302
Cdd:cd02658 74 ---------PYQVGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLD----------------RESFKNLGLN--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 303 ingastvVTAIFGGILQNEVNCLICGteSRKFDPFLD--LSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDET 380
Cdd:cd02658 126 -------PNDLFKFMIEDRLECLSCK--KVKYTSELSeiLSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIEDF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 381 elymCHKCKKKQKSTKKFWIQKLPKVLCLHLKRF----HWTAylrNKVDTYVEFPLRGLDMKcyllepensgpesclYDL 456
Cdd:cd02658 197 ----CSTCKEKTTATKTTGFKTFPDYLVINMKRFqlleNWVP---KKLDVPIDVPEELGPGK---------------YEL 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 55770886 457 AAVVVHHGSGVGSGHYTAY----ATHEGRWFHFNDSTVTLTDEETVVKAKAYILFY 508
Cdd:cd02658 255 IAFISHKGTSVHSGHYVAHikkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
160-509 |
1.19e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSnieqfcCYFKELPAVELRNGKTAgrRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSP 239
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA------LYLPKLDELLDDLSKEL--KVLKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 EslfyvvwkimpnFRGYQQQDAHEFMRYLLDHLHLELQGGFNgvsrsailqENSTLSASNKccingastvVTAIFGGILQ 319
Cdd:COG5533 73 I------------PPMGSQEDAHELLGKLLDELKLDLVNSFT---------IRIFKTTKDK---------KKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 NEVNCLI--CGTESRKFDPFLD-LSLDIPSQFRSKRSKNQEngpvcslrdclrsftdLEELDETELYMChkckkkqkstk 396
Cdd:COG5533 123 IIIELPDqtWVNNLKTLQEFIDnMEELVDDETGVKAKENEE----------------LEVQAKQEYEVS----------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 397 kfwIQKLPKVLCLHLKRFhwtAYL--RNKVDTYVEFPLrglDMKCYLLEPENSGPEScLYDLAAVVVHHGSgVGSGHYTA 474
Cdd:COG5533 176 ---FVKLPKILTIQLKRF---ANLggNQKIDTEVDEKF---ELPVKHDQILNIVKET-YYDLVGFVLHQGS-LEGGHYIA 244
|
330 340 350
....*....|....*....|....*....|....*...
gi 55770886 475 YATHEGRWFHFNDSTVTLTDEETVVKAK---AYILFYV 509
Cdd:COG5533 245 YVKKGGKWEKANDSDVTPVSEEEAINEKaknAYLYFYE 282
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
4.90e-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: 105.11 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLsnieqfccyfKELPAV--ELRNGKTAGRRTYHtrsqgdNNVSLVEEFRKTLCALwQGSQTAF 237
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCL----------RSVPELrdALKNYNPARRGANQ------SSDNLTNALRDLFDTM-DKKQEPV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 238 SPESLFYVVWKIMPNF------RGYQQQDAHEFMRYLLDHLHLELQGGfngvsrsaiLQENStlsasnkccingastVVT 311
Cdd:cd02657 64 PPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQLLSVLSQKLPGA---------GSKGS---------------FID 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 312 AIFGGILQNEVNCLICGT-ESRKFDPFLDLSLDIPSQFrskrsknqengPVCSLRDCLrsftdLEELDETELYMCHKCKK 390
Cdd:cd02657 120 QLFGIELETKMKCTESPDeEEVSTESEYKLQCHISITT-----------EVNYLQDGL-----KKGLEEEIEKHSPTLGR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 391 KQKSTKKFWIQKLPKVLCLHLKRFHW--TAYLRNKVDTYVEFPLRgLDMKCYLlepensgPESCLYDLAAVVVHHGSGVG 468
Cdd:cd02657 184 DAIYTKTSRISRLPKYLTVQFVRFFWkrDIQKKAKILRKVKFPFE-LDLYELC-------TPSGYYELVAVITHQGRSAD 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 55770886 469 SGHYTAY--ATHEGRWFHFNDSTVTLTDEETVVKAK-------AYILFY 508
Cdd:cd02657 256 SGHYVAWvrRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
160-508 |
2.97e-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: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFccyfkelpavelrngktagrrtyhtrsqgdnnVSLVEEFRktlcalwqgsqtafsp 239
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSL--------------------------------IEYLEEFL---------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 eslfyvvwkimpnfrgyQQQDAHEFMRYLLDHLHLELQGGFNGVSrsailqenstlsasnkccingASTVVtaifggilq 319
Cdd:cd02662 33 -----------------EQQDAHELFQVLLETLEQLLKFPFDGLL---------------------ASRIV--------- 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 320 nevnCLICGTESR-KFDPFLDLSLDIPsqfrskrskNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCkkkqkstkkf 398
Cdd:cd02662 66 ----CLQCGESSKvRYESFTMLSLPVP---------NQSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQTV---------- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 399 wIQKLPKVLCLHLKRFHWT---AYLRNKvdTYVEFPLRgLDMKcyllepensgpescLYDLAAVVVHHGSgVGSGHYTAY 475
Cdd:cd02662 123 -IVRLPQILCIHLSRSVFDgrgTSTKNS--CKVSFPER-LPKV--------------LYRLRAVVVHYGS-HSSGHYVCY 183
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 55770886 476 ----------------------ATHEGRWFHFNDSTVTLTDEETVVKAK-AYILFY 508
Cdd:cd02662 184 rrkplfskdkepgsfvrmregpSSTSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
160-491 |
1.72e-20 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 95.71 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 160 GLRNLGNTCFMNAILQSLSNIEQFCCYFKELPavelrngktagrrTYHtrSQGDNNVSLVeefrktLCALWQGSQTAFSP 239
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP-------------TDH--PRGRDSVALA------LQRLFYNLQTGEEP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 240 -ESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLhlelqggfngvsrsailqENSTlsasNKCCINGAstvVTAIFGGIL 318
Cdd:COG5077 254 vDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNL------------------EKSM----RGTVVENA---LNGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 319 QNEVNCLICGTESRKFDPFLDLsldipsQFRSKRSKNqengpvcsLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKF 398
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDI------QLNVKGMKN--------LQESFRRYIQVETLDGDNRYNAEKHGLQDAKKGVI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 399 WiQKLPKVLCLHLKRFHWTaYLRN---KVDTYVEFPLRgLDMKCYL----LEPENSgpeSCLYDLAAVVVHHGSgVGSGH 471
Cdd:COG5077 375 F-ESLPPVLHLQLKRFEYD-FERDmmvKINDRYEFPLE-IDLLPFLdrdaDKSENS---DAVYVLYGVLVHSGD-LHEGH 447
|
330 340
....*....|....*....|..
gi 55770886 472 YTAYATHE--GRWFHFNDSTVT 491
Cdd:COG5077 448 YYALLKPEkdGRWYKFDDTRVT 469
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
159-345 |
1.08e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 89.56 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 159 TGLRNLGNTCFMNAILQSLSNIEQFCCYFKElpavelRNGKTAGRRTYHTRSQGdnnvSLVEEFRKTLCALWQGSQTAFS 238
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLS------DEYEESINEENPLGMHG----SVASAYADLIKQLYDGNLHAFT 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 239 PESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNG--VSRSAILQENSTL--SASNKCC---INGASTVVT 311
Cdd:COG5560 336 PSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKpyTSKPDLSPGDDVVvkKKAKECWwehLKRNDSIIT 415
|
170 180 190
....*....|....*....|....*....|....
gi 55770886 312 AIFGGILQNEVNCLICGTESRKFDPFLDLSLDIP 345
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLP 449
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
29-105 |
2.29e-17 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 76.15 E-value: 2.29e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770886 29 CSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEdaqvpltnhkksekqdKVQHTVCMDCSSYSTYCYRCDDFVVND 105
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYE----------------ETGHPLAVNLSTLTVYCYPCDDYVHDP 61
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
264-490 |
4.41e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 69.99 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 264 FMRYLLDHLHLElqggfngvsrsailqENSTLSASNkccinGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLD 343
Cdd:pfam13423 102 FNRFLLDQLSSE---------------ENSTPPNPS-----PAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 344 IPSQFrskrSKNQENGPVCSLRDCLRSFTDLEELDETelyMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFhwTAYLRNK 423
Cdd:pfam13423 162 YPRKP----SSNNKKPPNQTFSSILKSSLERETTTKA---WCEKCKRYQPLESRRTVRNLPPVLSLNAALT--NEEWRQL 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55770886 424 VDTYVEFPLRgldMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAY---------ATHEGRWFHFNDSTV 490
Cdd:pfam13423 233 WKTPGWLPPE---IGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFvkvadseleDPTESQWYLFNDFLV 305
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-509 |
1.71e-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: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 159 TGLRNLGNTCFMNAILQSLSNIE-------QFCCYFKELPAVELRNGKTAGRRTyhTRSQGDNNVSLVEEFRKTLCALWQ 231
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKplrdlvlNFDESKAELASDYPTERRIGGREV--SRSELQRSNQFVYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 232 GSQTAFSPES-LFYVVwkimpnFRgyqQQDAHEFMRYLLDHLHLEL-QGGFNGVSRSAILQenstlsasnkcciNGASTV 309
Cdd:cd02666 80 SNTRSVTPSKeLAYLA------LR---QQDVTECIDNVLFQLEVALePISNAFAGPDTEDD-------------KEQSDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 310 VTAIF-GGILQNEVNCLICGTESRKFDPFLDLSLDIPSqFRSKRSKNQENGPvCSLRDCL-RSF-----TDLEELDETEL 382
Cdd:cd02666 138 IKRLFsGKTKQQLVPESMGNQPSVRTKTERFLSLLVDV-GKKGREIVVLLEP-KDLYDALdRYFdydslTKLPQRSQVQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 383 YMCHKCKKKQKSTKKFWIQKLPKVLcLHLKRfhWTAYLRNKVDTYVEFPLRGLDMKcylLEPENSGPESCLYDLAAVVVH 462
Cdd:cd02666 216 QLAQPLQRELISMDRYELPSSIDDI-DELIR--EAIQSESSLVRQAQNELAELKHE---IEKQFDDLKSYGYRLHAVFIH 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 55770886 463 HGSgVGSGHYTAYATH--EGRWFHFNDSTVTLTDEETVV------KAKAYILFYV 509
Cdd:cd02666 290 RGE-ASSGHYWVYIKDfeENVWRKYNDETVTVVPASEVFlftlgnTATPYFLVYV 343
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-68 |
1.84e-09 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 53.52 E-value: 1.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 55770886 29 CSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQVPL 68
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPL 41
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
257-509 |
7.21e-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: 56.41 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 257 QQQDAHEFMRYLLDHLHLELQGGFNGVS-RSAILQENSTLsasnkccINGASTVVTAIFGGILQNevnCLICGtesrkfd 335
Cdd:cd02665 21 QQQDVSEFTHLLLDWLEDAFQAAAEAISpGEKSKNPMVQL-------FYGTFLTEGVLEGKPFCN---CETFG------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 336 pfldlslDIPSQFRSKRSknqengpvcsLRDCLRSFT---DLEELDETELYMCHKCKkkqkstkkfWIQKLPKVLCLHLK 412
Cdd:cd02665 84 -------QYPLQVNGYGN----------LHECLEAAMfegEVELLPSDHSVKSGQER---------WFTELPPVLTFELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 413 RFHWTAYLRNKVDTYVEFPlrgldmKCYLLEPensgpesclYDLAAVVVHHGSgVGSGHYTAYA--THEGRWFHFNDSTV 490
Cdd:cd02665 138 RFEFNQGRPEKIHDKLEFP------QIIQQVP---------YELHAVLVHEGQ-ANAGHYWAYIykQSRQEWEKYNDISV 201
|
250 260
....*....|....*....|....*..
gi 55770886 491 TLTDEETVVK--------AKAYILFYV 509
Cdd:cd02665 202 TESSWEEVERdsfgggrnPSAYCLMYI 228
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
400-508 |
6.07e-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: 44.83 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFhwtaYLRNKVDTYVEfpLRGLDMKCYLLEPENsgpesclYDLAAVVVHHGSGVGSGHYTAYA--- 476
Cdd:cd02673 143 IMTFPECLSINLKRY----KLRIATSDYLK--KNEEIMKKYCGTDAK-------YSLVAVICHLGESPYDGHYIAYTkel 209
|
90 100 110
....*....|....*....|....*....|....*
gi 55770886 477 THEGRWFHFNDSTVTLTDEETVVKA---KAYILFY 508
Cdd:cd02673 210 YNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
301-508 |
1.10e-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: 44.04 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 301 CCINGASTVVTAIFGGILQNEVNC------LICGTESRKFDPFLDLSLDIPSQFRSKRSknqengpvcSLRDCLRSFTDL 374
Cdd:cd02672 59 CELGYLFSTLIQNFTRFLLETISQdqlgtpFSCGTSRNSVSLLYTLSLPLGSTKTSKES---------TFLQLLKRSLDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 375 EELDETElymCHKCKKKQKSTKKFWIQKLP----KVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLE---PENS 447
Cdd:cd02672 130 EKVTKAW---CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNGEFDDINVVLPSGKVMQNKVSPKAIDHDklvKNRG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770886 448 GPESCLYDLAAVVVH--HGSG-----VGSGHYTAYATHeGRWFHFNDSTVTLTDEetvvkaKAYILFY 508
Cdd:cd02672 207 QESIYKYELVGYVCEinDSSRgqhnvVFVIKVNEESTH-GRWYLFNDFLVTPVSE------LAYILLY 267
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
400-508 |
6.96e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 38.28 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770886 400 IQKLPKVLCLHLKRFHWTAYLRNKVDTYVeFPLRGLDMKcYLLEPENSGPESCLYD--------------------LAAV 459
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQKMFKKI-LIPDEIDIP-DFVADDPRACSKCQLEcrvcyddkdfsptcgkfklsLCSA 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55770886 460 VVHHGSGVGSGHYTAYA-------------THEGRWFHFNDstvtLTDEETV-----VKAK-----AYILFY 508
Cdd:cd02670 173 VCHRGTSLETGHYVAFVrygsysltetdneAYNAQWVFFDD----MADRDGVsngfnIPAArlledPYMLFY 240
|
|
| |
