|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1070 |
1.27e-113 |
|
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: 351.20 E-value: 1.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNtprlaeyfnknyyqedinrsnilghkgevaeefgvimkalwsgqyrfisprdfkftigki 819
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 820 ndqfsgfDQQDSQELLLFLMDGLHedlnkradnrkrykeetndhlddykaadlawskhkmlneSIIVALFQGQFKSTVQC 899
Cdd:cd02674 21 -------DQQDAQEFLLFLLDGLH---------------------------------------SIIVDLFQGQLKSRLTC 54
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 900 LTCHKKSRTFEAFMYLSLPLASS----NKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLK 975
Cdd:cd02674 55 LTCGKTSTTFEPFTYLSLPIPSGsgdaPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLK 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 976 RFSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KSNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHEVSDI 1054
Cdd:cd02674 135 RFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKV 214
|
330
....*....|....*.
gi 1993917536 1055 STSSVKSSAAYILFYT 1070
Cdd:cd02674 215 SESSVVSSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
739-1069 |
4.20e-112 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 350.20 E-value: 4.20e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 739 TGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHkgeVAEEFGVIMKALWSG-QYRFISPRDFKFTIG 817
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 818 KINDQFSGFDQQDSQELLLFLMDGLHEDLNKRADNRkrykeetndhlddykaadlawskhkmlNESIIVALFQGQFKSTV 897
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE---------------------------NESLITDLFRGQLKSRL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 898 QCLTCHKKSRTFEAFMYLSLPLASSNKCS----LQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVH 973
Cdd:pfam00443 131 KCLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 974 LKRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----SNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDH 1049
Cdd:pfam00443 211 LKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDE 289
|
330 340
....*....|....*....|.
gi 1993917536 1050 EVSDISTS-SVKSSAAYILFY 1069
Cdd:pfam00443 290 KVTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
740-1069 |
7.63e-74 |
|
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: 244.70 E-value: 7.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNtprlaeyfnknyyqedinrsnilghkgevaeefgvimkalwsgqyrfisprdfkftigki 819
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 820 ndqfsgfDQQDSQELLLFLMDGLHEDLNKRADNrkrykeetndhlddykaadlawSKHKMLNESIIVALFQGQFKSTVQC 899
Cdd:cd02257 21 -------EQQDAHEFLLFLLDKLHEELKKSSKR----------------------TSDSSSLKSLIHDLFGGKLESTIVC 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 900 LTCHKKSRTFEAFMYLSLPL--ASSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKtRRDSTKKIEIWKLPPILLVHLKRF 977
Cdd:cd02257 72 LECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRF 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 978 SYDGRW-KQKLQTSVDFPLEnLDLSQYVIGPKS------NLKKYSLYGVSNHYGGL-DGGHYTAYCKNAIKQRWHKFDDH 1049
Cdd:cd02257 151 SFNEDGtKEKLNTKVSFPLE-LDLSPYLSEGEKdsdsdnGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDD 229
|
330 340
....*....|....*....|....*
gi 1993917536 1050 EVSDISTSSV-----KSSAAYILFY 1069
Cdd:cd02257 230 KVTEVSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
739-1069 |
4.95e-69 |
|
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: 233.32 E-value: 4.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 739 TGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRsnilghkgevaEEFGV-------IMKALWSGQYrFISPRD 811
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGP-GSAPRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 812 FKFTIGKINDQFSGFDQQDSQELLLFLMDGLHedlnkRADNRKRYKEETNDHLddykaadlawSKHKMLNESIivalFQG 891
Cdd:cd02661 70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ-----KACLDRFKKLKAVDPS----------SQETTLVQQI----FGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 892 QFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNkcSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILL 971
Cdd:cd02661 131 YLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 972 VHLKRFSYDGRwkQKLQTSVDFPlENLDLSQYVIGPKSNLKKYSLYGVSNHYGG-LDGGHYTAYCKNAIKqRWHKFDDHE 1050
Cdd:cd02661 209 IHLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNG-KWYNMDDSK 284
|
330
....*....|....*....
gi 1993917536 1051 VSDISTSSVKSSAAYILFY 1069
Cdd:cd02661 285 VSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1070 |
1.04e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 219.17 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTPRLAEYF--NKNYYQEDINRSN--ILGHKGEVAEEFgvimkaLWSGQYRFISPRDFKFT 815
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNscLSCAMDEIFQEF------YYSGDRSPYGPINLLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 816 IGKINDQFSGFDQQDSQELLLFLMDGLHEDLnkradnrKRYKEETNDHLDdykaadlawskhkmlNESIIVALFQGQFKS 895
Cdd:cd02660 76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHY-------GGDKNEANDESH---------------CNCIIHQTFSGSLQS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 896 TVQCLTCHKKSRTFEAFMYLSLPLASSNKCS-------------LQECLKLFSKEEKLTDNNkVLCSHCKTRRDSTKKIE 962
Cdd:cd02660 134 SVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSwalgesgvsgtptLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 963 IWKLPPILLVHLKRFSYD-GRWKQKLQTSVDFPLEnLDLSQYVIG---------PKSNLKKYSLYGVSNHYGGLDGGHYT 1032
Cdd:cd02660 213 IKKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYT 291
|
330 340 350
....*....|....*....|....*....|....*...
gi 1993917536 1033 AYCKNAIKQrWHKFDDHEVSDISTSSVKSSAAYILFYT 1070
Cdd:cd02660 292 AYCRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
2.13e-58 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 202.62 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTPRLAEYFNKNyyqedinrsnilghkgevaeefgvimkalwsgqyrfisPRDFKFTIGKI 819
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------PKELFSQVCRK 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 820 NDQFSGFDQQDSQELLLFLMDGLhedlnkradnrkrykeetndhlddykaadlawskhkmlnESIIVALFQGQFKSTVQC 899
Cdd:cd02667 43 APQFKGYQQQDSHELLRYLLDGL---------------------------------------RTFIDSIFGGELTSTIMC 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 900 LTCHKKSRTFEAFMYLSLPLASSNK--CSLQECLKLFSKEEKLTDNNKVLCSHCKtrrDSTKKIEIWKLPPILLVHLKRF 977
Cdd:cd02667 84 ESCGTVSLVYEPFLDLSLPRSDEIKseCSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRF 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 978 SYDGRWK-QKLQTSVDFPlENLDLSQYViGPKSNLK------KYSLYGVSNHYGGLDGGHYTAYCK-------------- 1036
Cdd:cd02667 161 QQPRSANlRKVSRHVSFP-EILDLAPFC-DPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltks 238
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1993917536 1037 -------NAIKQRWHKFDDHEVSDISTSSVKSSAAYILFY 1069
Cdd:cd02667 239 kpaadeaGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
736-924 |
2.12e-55 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 207.43 E-value: 2.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 736 AALTGLRNLGNTCYMNSILQCLCNTPRLAEYFNKNYYQEDINRSNILGHKGEVAEEFGVIMKALWSGQYRFISPRDFKFT 815
Cdd:COG5560 263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 816 IGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKRAdnRKRYKEETN----DHLDDYKAADLAWSKHKMLNESIIVALFQG 891
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRII--KKPYTSKPDlspgDDVVVKKKAKECWWEHLKRNDSIITDLFQG 420
|
170 180 190
....*....|....*....|....*....|...
gi 1993917536 892 QFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNK 924
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
1.07e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 173.60 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTP--RLAEYFNKNYYQEDINRSNILghkgevaeEFGVIMKALWSGQYRFISPRDFKFTIG 817
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPefRNAVYSIPPTEDDDDNKSVPL--------ALQRLFLFLQLSESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 818 KINDQFSGFDQQDSQELLLFLMDGLHEDLnkradnrkrykeetndhlddyKAADLawskhkmlnESIIVALFQGQFKSTV 897
Cdd:cd02659 76 FGWDSLNTFEQHDVQEFFRVLFDKLEEKL---------------------KGTGQ---------EGLIKNLFGGKLVNYI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 898 QCLTCHKKSRTFEAFmyLSLPLASSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRF 977
Cdd:cd02659 126 ICKECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 978 SYDGR--WKQKLQTSVDFPLEnLDLSQYVI-----GPKSNLKK------YSLYGVSNHYGGLDGGHYTAYCKNAIKQRWH 1044
Cdd:cd02659 204 EFDFEtmMRIKINDRFEFPLE-LDMEPYTEkglakKEGDSEKKdsesyiYELHGVLVHSGDAHGGHYYSYIKDRDDGKWY 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1993917536 1045 KFDDHEVSDISTSSV----------------------KSSAAYILFY 1069
Cdd:cd02659 283 KFNDDVVTPFDPNDAeeecfggeetqktydsgprafkRTTNAYMLFY 329
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1070 |
2.14e-47 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 171.72 E-value: 2.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLcntprlaeYFNKNYYQedinrsnilghkgevaeeFGVIMKALWSGQYRF--ISPRDFKFTIG 817
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL--------YFENLLTC------------------LKDLFESISEQKKRTgvISPKKFITRLK 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 818 KINDQFSGFDQQDSQELLLFLMDGLHEDLNKRADNRKRYKEETNDHLDDykaadlaWSKhkmlneSIIVALFQGQFKSTV 897
Cdd:cd02663 55 RENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAE-------PQP------TWVHEIFQGILTNET 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 898 QCLTCHKKSRTFEAFMYLSLPLasSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRF 977
Cdd:cd02663 122 RCLTCETVSSRDETFLDLSIDV--EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 978 SYDGRWKQ--KLQTSVDFPLEnLDLSQYVIGPKSNLKKYSLYGVSNHYG-GLDGGHYTAYCKnaIKQRWHKFDDHEVSDI 1054
Cdd:cd02663 200 KYDEQLNRyiKLFYRVVFPLE-LRLFNTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKI 276
|
330 340
....*....|....*....|....
gi 1993917536 1055 STSSV-------KSSA-AYILFYT 1070
Cdd:cd02663 277 DENAVeeffgdsPNQAtAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1070 |
3.78e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 171.83 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCL------------CNTPRLAEYFNKNyyqedinrSNILGHKGEVAEEFGVIMKALWSGQYRFI 807
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWfmnlefrkavyeCNSTEDAELKNMP--------PDKPHEPQTIIDQLQLIFAQLQFGNRSVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 808 SPRDFKFTIGKINDQfsgfdQQDSQELLLFLMDGLHEDLNKRADNRKRykeetndhlddykaadlawskhkmlneSIIVA 887
Cdd:cd02668 73 DPSGFVKALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPDLK---------------------------NIVQD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 888 LFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNKcsLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLP 967
Cdd:cd02668 121 LFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 968 PILLVHLKRFSYD--GRWKQKLQTSVDFPlENLDLSQYVIGPKSNLKKYSLYGVSNHYG-GLDGGHYTAYCKNAIKQRWH 1044
Cdd:cd02668 199 PTLNFQLLRFVFDrkTGAKKKLNASISFP-EILDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1993917536 1045 KFDDHEVSDISTSSVK---------------------SSAAYILFYT 1070
Cdd:cd02668 278 KFNDEDVEEMPGKPLKlgnsedpakprkseikkgthsSRTAYMLVYK 324
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
894-1069 |
5.39e-40 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 160.05 E-value: 5.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 894 KSTVQCLtcHKKSRTFEAFMYLSLPL-----ASSNKCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPP 968
Cdd:COG5560 641 AVVISCE--WEEKRYLSLFSYDPLWTireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPM 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 969 ILLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKSNLKKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDD 1048
Cdd:COG5560 719 ILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDD 798
|
170 180
....*....|....*....|.
gi 1993917536 1049 HEVSDISTSSVKSSAAYILFY 1069
Cdd:COG5560 799 SRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
6.06e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 130.69 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLcntprlaeyFNKNYYQEDINRSNILGHKGEVAEEFGVIM-KALWSGQYRFISPRDFKFTIGK 818
Cdd:cd02664 1 GLINLGNTCYMNSVLQAL---------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLlQAHLMHTQRRAEAPPDYFLEAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 819 INDQFSGFDQQDSQELLLFLMDGLHedlnkradnrkrykeetndhlddykaadlawskhkmlneSIIVALFQGQFKSTVQ 898
Cdd:cd02664 72 RPPWFTPGSQQDCSEYLRYLLDRLH---------------------------------------TLIEKMFGGKLSTTIR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 899 CLTCHKKSRTFEAFMYLSLPLassnkCSLQECLKLFSKEEKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFS 978
Cdd:cd02664 113 CLNCNSTSARTERFRDLDLSF-----PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFS 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 979 YD--GRWKQKLQTSVDFPlENLDLSQYVIGPKSNLKK-------------------YSLYGVSNHYG-GLDGGHYTAYCK 1036
Cdd:cd02664 188 YDqkTHVREKIMDNVSIN-EVLSLPVRVESKSSESPLekkeeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTYAR 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 1037 N--------------------AIKQRWHKFDDHEVSDISTSSVK-------SSAAYILFY 1069
Cdd:cd02664 267 DqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
|
|
| USP8_dimer |
pfam08969 |
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ... |
8-116 |
1.18e-31 |
|
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.
Pssm-ID: 462647 Cd Length: 113 Bit Score: 119.71 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 8 LKELYLSTSLGELNKKAEVKPD--KISTRSYVQSACKIFKAAEECRLDRDEEKAYVFYMKFLSVYDLIKKRPDFKQQQDY 85
Cdd:pfam08969 3 LKPLHLSSSLEDLEKLTEKLEVdkNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVKAT 82
|
90 100 110
....*....|....*....|....*....|.
gi 1993917536 86 VMSMLGPTSFKKAIEEAEKLSDSLKLRYEEA 116
Cdd:pfam08969 83 VRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
3.03e-31 |
|
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: 125.13 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTPRLAEYFN--KNYYQEDIN--RSNILGHKGEVAeefgvimKALWSGQYRF--------- 806
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDdlENKFPSDVVdpANDLNCQLIKLA-------DGLLSGRYSKpaslksend 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 807 -----ISPRDFKFTIGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKRADnrkrykEETNDhlddykaadlawskhkmln 881
Cdd:cd02658 74 pyqvgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLG------LNPND------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 882 esiivaLFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNKC------------SLQECLKLFSKEEKLTDNnkvlCS 949
Cdd:cd02658 129 ------LFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATekeegelvyepvPLEDCLKAYFAPETIEDF----CS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 950 HCKTRRDSTKKIEIWKLPPILLVHLKRFSYDGRWKQ-KLQTSVDFPlenldlsqYVIGPksnlKKYSLYGVSNHYG-GLD 1027
Cdd:cd02658 199 TCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP--------EELGP----GKYELIAFISHKGtSVH 266
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1993917536 1028 GGHYTAYCKNAI--KQRWHKFDDHEVSDISTSSVKSSAAYILFY 1069
Cdd:cd02658 267 SGHYVAHIKKEIdgEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
1.97e-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 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: 122.44 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTPRLAEYFnKNYyqeDINRSNILGHKGEVAEEFGVIMKALWSGQYRfISPRDFKFTIGKI 819
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-KNY---NPARRGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 820 NDQFS------GFDQQDSQELLLFLMDGLHEDLNKRADNRkrykeetndhlddykaadlawskhkmlneSIIVALFQGQF 893
Cdd:cd02657 76 FPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKG-----------------------------SFIDQLFGIEL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 894 KSTVQCL-TCHKKSRTFEAFMYLSLPLASSNKCS-LQECLKLFSKEEkLTDNNKVLcshcktRRDS--TKKIEIWKLPPI 969
Cdd:cd02657 127 ETKMKCTeSPDEEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEE-IEKHSPTL------GRDAiyTKTSRISRLPKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 970 LLVHLKRFSydgrWKQKLQT------SVDFPLEnLDLSQYVigpkSNLKKYSLYGVSNHYG-GLDGGHYTAYCKNAIKQR 1042
Cdd:cd02657 200 LTVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWVRRKNDGK 270
|
330 340 350
....*....|....*....|....*....|....
gi 1993917536 1043 WHKFDDHEVSDISTSSVKSSA-------AYILFY 1069
Cdd:cd02657 271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
719-1069 |
3.18e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 116.92 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 719 PTATQIRNLNPvfgglgaaLTGLRNLGNTCYMNSILQCLCNTP----RLAEYFNKNYYQEDINRSNILGHKgevaeefgv 794
Cdd:cd02671 13 TSCEKRENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPgfkhGLKHLVSLISSVEQLQSSFLLNPE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 795 imkaLWSGQYRFISPRDFKFTIGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKradnrkrykeetndhlddykaadlaw 874
Cdd:cd02671 76 ----KYNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK-------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 875 skhkmlnesiivaLFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASSNKCSLQECLKL-----------------FSKE 937
Cdd:cd02671 126 -------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEIspdpktemktlkwaisqFASV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 938 EKLTDNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFSYDGRWK------QKLQTSVDFPLEnLDLSQYVIGPKSNL 1011
Cdd:cd02671 193 ERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993917536 1012 kkYSLYGVSNHYGG-LDGGHYTAYCknaikqRWHKFDDHEV---------SDISTSSVKSSAAYILFY 1069
Cdd:cd02671 272 --YRLFAVVMHSGAtISSGHYTAYV------RWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
1.32e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 109.76 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTPRLAEYFNknyyqedinrsnilghkgevaeefgvimkalwsgqyRFISprdfkftigki 819
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLE------------------------------------EFLE----------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 820 ndqfsgfdQQDSQELLLFLMDGLhedlnkradnrkrykeetndhlddykaadlawskhkmlnESIIVALFQGQFKSTVQC 899
Cdd:cd02662 34 --------QQDAHELFQVLLETL---------------------------------------EQLLKFPFDGLLASRIVC 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 900 LTCHKKSR-TFEAFMYLSLPL---ASSNKCSLQECLKLFSKEEKLTDnnkVLCSHCKTRrdstkkieIWKLPPILLVHLK 975
Cdd:cd02662 67 LQCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLS 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 976 RFSYDGRWK-QKLQTSVDFPLEnldLSQYvigpksnlkKYSLYGVSNHYGGLDGGHYTAY-------------------- 1034
Cdd:cd02662 136 RSVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmre 203
|
330 340 350
....*....|....*....|....*....|....*.
gi 1993917536 1035 CKNAIKQRWHKFDDHEVSDISTSSVK-SSAAYILFY 1069
Cdd:cd02662 204 GPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
740-1069 |
2.85e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 109.89 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLC-NTPRLAEY-----FNKNYYQEDINRSnilgHKGEVAEEFGVIMKALWSGQyrfisprdfK 813
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELlddlsKELKVLKNVIRKP----EPDLNQEEALKLFTALWSSK---------E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 814 FTIGKINDQFSgfdQQDSQELLLFLMDGLheDLNKRADNRKRYKEETNDHLDDYKAadlAWSkhkmlneSIIVALFQGQF 893
Cdd:COG5533 68 HKVGWIPPMGS---QEDAHELLGKLLDEL--KLDLVNSFTIRIFKTTKDKKKTSTG---DWF-------DIIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 894 ---KSTVQCltchkksrTFEAFMYLslplaSSNKCSLQeclklfskeEKLTDNNKVLcshCKTRRDSTKKieiwKLPPIL 970
Cdd:COG5533 133 vnnLKTLQE--------FIDNMEEL-----VDDETGVK---------AKENEELEVQ---AKQEYEVSFV----KLPKIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 971 LVHLKRFSYDGRwKQKLQTSVDfplENLDLSqYVIGPKSNLKK---YSLYGVSNHYGGLDGGHYTAYCKnaIKQRWHKFD 1047
Cdd:COG5533 184 TIQLKRFANLGG-NQKIDTEVD---EKFELP-VKHDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKAN 256
|
330 340
....*....|....*....|....*
gi 1993917536 1048 DHEVSDISTS---SVKSSAAYILFY 1069
Cdd:COG5533 257 DSDVTPVSEEeaiNEKAKNAYLYFY 281
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
740-1052 |
1.76e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 111.12 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTprlaEYFNKNYYQ--EDINRSNilghkGEVAEefgVIMKALWSGQYRFISPRDFKFTIG 817
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFI----AKFRKDVYGipTDHPRGR-----DSVAL---ALQRLFYNLQTGEEPVDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 818 KINDQFSGFDQQDSQELLLFLMDGLhedlnkraDNRKRYKEETNdhlddykaadlawskhkMLNEsiivaLFQGQFKSTV 897
Cdd:COG5077 263 FGWDSDDSFMQHDIQEFNRVLQDNL--------EKSMRGTVVEN-----------------ALNG-----IFVGKMKSYI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 898 QCLTCHKKSRTFEAFMYLSLPLASSNkcSLQECLKLFSKEEKLTDNNKVLCSHcKTRRDSTKKIEIWKLPPILLVHLKRF 977
Cdd:COG5077 313 KCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRF 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 978 SYDGRWKQ--KLQTSVDFPLEnLDLSQYVigPKSNLKK------YSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDH 1049
Cdd:COG5077 390 EYDFERDMmvKINDRYEFPLE-IDLLPFL--DRDADKSensdavYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDT 466
|
...
gi 1993917536 1050 EVS 1052
Cdd:COG5077 467 RVT 469
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-1069 |
7.00e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 106.25 E-value: 7.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 740 GLRNLGNTCYMNSILQCLCNTPRLAEYF--NKNYyqedinrSNILGHKGEVAEEFGVIMKALWS-----GQyrfISPRDF 812
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFllYENY-------ENIKDRKSELVKRLSELIRKIWNprnfkGH---VSPHEL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 813 KFTIGKINDQFSGFDQQ-DSQELLLFLMDGLHEDLNKRADNrkrykeetndhlddykaadlawskhkmlNESIIVALFQG 891
Cdd:cd02669 191 LQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSKKP----------------------------NSSIIHDCFQG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 892 QFKSTVQCLTCHK---------------KSRTFEAFMYLSLPL------ASSNKCSLQECLKLFskeEKLTDNNKVLCSH 950
Cdd:cd02669 243 KVQIETQKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTLDLpppplfKDGNEENIIPQVPLK---QLLKKYDGKTETE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 951 CKTRRdstKKIEIWKLPPILLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKSNLKKYSLYG-VSN--HYGG-L 1026
Cdd:cd02669 320 LKDSL---KRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNlVANivHEGTpQ 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1993917536 1027 DGGHYTAYCKNAIKQRWHKFDDHEVSDISTSSVKSSAAYILFY 1069
Cdd:cd02669 397 EDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
815-1069 |
9.22e-13 |
|
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: 69.48 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 815 TIGKINDQFSGFDQQDSQELLLFLMDGLHEDLNKRADNRKRYKEETNdHLDDYKAadlawskHKMLNESIIValfqgqfk 894
Cdd:cd02673 20 SIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPPSNIEIK-RLNPLEA-------FKYTIESSYV-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 895 stvqCLTCHKKSRTFEAFMYLSLPLASSNKCSLQeclKLFSKEEKLTDNNKVlCSHCKTRRDSTKKiEIWKLPPILLVHL 974
Cdd:cd02673 84 ----CIGCSFEENVSDVGNFLDVSMIDNKLDIDE---LLISNFKTWSPIEKD-CSSCKCESAISSE-RIMTFPECLSINL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 975 KRFsydgrwkqKLQTSVdfpLENLDLSQYVIGP-KSNLKKYSLYGVSNHYG-GLDGGHYTAYCKNAIK-QRWHKFDDHEV 1051
Cdd:cd02673 155 KRY--------KLRIAT---SDYLKKNEEIMKKyCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEI 223
|
250 260
....*....|....*....|.
gi 1993917536 1052 SDISTSSVK---SSAAYILFY 1069
Cdd:cd02673 224 RPVSKNDVStnaRSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
828-1069 |
2.68e-10 |
|
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: 61.81 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 828 QQDSQELLLFLMDGLhedlnKRADNRKRYKEETNDHlddykaadlawSKHKMlnesiiVALFQGQFkSTVQCLTcHKKSR 907
Cdd:cd02665 22 QQDVSEFTHLLLDWL-----EDAFQAAAEAISPGEK-----------SKNPM------VQLFYGTF-LTEGVLE-GKPFC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 908 TFEafMYLSLPLASSNKCSLQECLK--LFSKEEKLTDNNKVLCSHckTRRDSTKkieiwkLPPILLVHLKRFSYDGRWKQ 985
Cdd:cd02665 78 NCE--TFGQYPLQVNGYGNLHECLEaaMFEGEVELLPSDHSVKSG--QERWFTE------LPPVLTFELSRFEFNQGRPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 986 KLQTSVDFPLEnldLSQYvigpksnlkKYSLYGVSNHYGGLDGGHYTAYCKNAIKQRWHKFDDHEVSDISTSSVKSSA-- 1063
Cdd:cd02665 148 KIHDKLEFPQI---IQQV---------PYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfg 215
|
250
....*....|..
gi 1993917536 1064 ------AYILFY 1069
Cdd:cd02665 216 ggrnpsAYCLMY 227
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
837-1048 |
6.60e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 55.35 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 837 FLMDGLHEDLNKRADNRKRykeetndhlddykaadlawskhkmlNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLS 916
Cdd:pfam13423 105 FLLDQLSSEENSTPPNPSP-------------------------AESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 917 L--------PLASSNKCSLQECLKLFSKEEKLTdnnKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKRFSYDgrWKQKLQ 988
Cdd:pfam13423 160 LiyprkpssNNKKPPNQTFSSILKSSLERETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWK 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993917536 989 TSVDFPLE-NLDLSQYVIGPkSNLKKYSLYG-VSNHYGGLDGGHYTAYCKNAIK-------QRWHKFDD 1048
Cdd:pfam13423 235 TPGWLPPEiGLTLSDDLQGD-NEIVKYELRGvVVHIGDSGTSGHLVSFVKVADSeledpteSQWYLFND 302
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
876-1070 |
2.19e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 47.51 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 876 KHKMLNE-----SIIVALFQGQFKSTVQC-----LTCHKKSRTFEAFMY-LSLPLASSNKCSL---QECLKLFSKEEKlt 941
Cdd:cd02672 54 ESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKEstfLQLLKRSLDLEK-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 942 dNNKVLCSHCKTRRDSTKKIEIWKLPPILLVHLKR-----------FSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKSN 1010
Cdd:cd02672 132 -VTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVInlsvtngefddINVVLPSGKVMQNKVSPKAIDHDKLVKNRGQESI 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993917536 1011 lKKYSLYG-VSNHYGGLDGGHYTA----YCKNAIKQRWHKFDDHEVSDISTSsvkssaAYILFYT 1070
Cdd:cd02672 211 -YKYELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFNDFLVTPVSEL------AYILLYQ 268
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
965-1069 |
1.55e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 44.44 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 965 KLPPILLVHLKRFSYDGRWKQKLQTSVDFPLEnLDL----------------------SQYVIGPKSNLKKYSLYGVSNH 1022
Cdd:cd02670 97 KAPSCLIICLKRYGKTEGKAQKMFKKILIPDE-IDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993917536 1023 YG-GLDGGHYTAYCK-----------NAIKQRWHKFDD-------HEVSDISTSSVKSSaAYILFY 1069
Cdd:cd02670 176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
202-311 |
3.48e-03 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 37.85 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993917536 202 VIIMDARSQKDYQESQIqvptQKIISVPEDIIkpgitvnQIEANLPSESREQWKKRGLADYVVLLDWFSSAKDLklgtTL 281
Cdd:pfam00581 6 VVLIDVRPPEEYAKGHI----PGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA----AA 70
|
90 100 110
....*....|....*....|....*....|
gi 1993917536 282 QSLKDALFKwdsqtilrsEPLVLEGGYESW 311
Cdd:pfam00581 71 ALLKALGYK---------NVYVLDGGFEAW 91
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
739-755 |
5.46e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 5.46e-03
|
| |
