|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
613-1122 |
2.53e-107 |
|
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: 339.85 E-value: 2.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 613 PIGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKDLNmIENKEAVKKVGGRIVTRIEFLRALQFTYELRKLFIELIT 692
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAEL-ASDYPTERRIGGREVSRSELQRSNQFVYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 693 SKSSSVHPSSVLTYLALipltldqvksgtssvmdlsssrelsnlnersitidpraeeqaqgleqeqgqdeakspaeqsss 772
Cdd:cd02666 80 SNTRSVTPSKELAYLAL--------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 773 vnlidfpmantngesqtqphyfevseeeinssmdlgRQQDVLECIDHVLFQLEASLGRISN-----SEDRLGSDNDLIRR 847
Cdd:cd02666 97 ------------------------------------RQQDVTECIDNVLFQLEVALEPISNafagpDTEDDKEQSDLIKR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 848 LFSGKLKQTLNDASQG----VRSNYEIFSHLIVDLFE---------EKQTLYDALDGVFETVNIdmgsetaqrslciTEL 914
Cdd:cd02666 141 LFSGKTKQQLVPESMGnqpsVRTKTERFLSLLVDVGKkgreivvllEPKDLYDALDRYFDYDSL-------------TKL 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 915 PIILQLQIQrvqfdrttgqpfksNAFVEFGKELSMDRYvedtdgkmapllqrywdlkreiinlqkrqqlllttnsNLMSS 994
Cdd:cd02666 208 PQRSQVQAQ--------------LAQPLQRELISMDRY-------------------------------------ELPSS 236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 995 VDTLSILSKWAAQQQDSRLPinpklpdilqeeinnvvaevdMLKKQEASLKEERTHLFDNYISHSYDLLAVFVHRGQASF 1074
Cdd:cd02666 237 IDDIDELIREAIQSESSLVR---------------------QAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEASS 295
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 19115120 1075 GHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADTTGNNANPYMLTYI 1122
Cdd:cd02666 296 GHYWVYIKDFEENVWRKYNDETVTVVPASEVFLFTLGNTATPYFLVYV 343
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
614-1121 |
2.11e-25 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 108.30 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 614 IGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKDLNMIENKeavkkvggrivtrieflraLQFTYELRKLFIELits 693
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKD-------------------INLLCALRDLFKAL--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 694 ksssvhpssvltylalipltldQVKSGTSSVmdlsssrelsnlnersitidpraeeqaqgleqeqgqdeakspaeqsssv 773
Cdd:pfam00443 59 ----------------------QKNSKSSSV------------------------------------------------- 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 774 nlidfpmantngesqtQPHYFEVSEEEINSSMDLGRQQDVLECIDHVLFQLEASLGRISNSEDrlgsdNDLIRRLFSGKL 853
Cdd:pfam00443 68 ----------------SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTEN-----ESLITDLFRGQL 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 854 KQTLND-ASQGVRSNYEIFSHLIVDLFEEKQTLYDA-------LDGVFETVNIDM--------GSETAQRSLCITELPII 917
Cdd:pfam00443 127 KSRLKClSCGEVSETFEPFSDLSLPIPGDSAELKTAslqicflQFSKLEELDDEEkyycdkcgCKQDAIKQLKISRLPPV 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 918 LQLQIQRVQFDRTTgqPFKSNAFVEFGKELSMDRYVEDTDGKMAPLLQrywdlkreiinlqkrqqlllttnsnlmssvdt 997
Cdd:pfam00443 207 LIIHLKRFSYNRST--WEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-------------------------------- 252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 998 lsilskwaaqqqdsrlpinpklpdilqeeinnvvaevdmlkkqeaslkeerthlfdnyishSYDLLAVFVHRGQASFGHY 1077
Cdd:pfam00443 253 -------------------------------------------------------------DYRLVAVVVHSGSLSSGHY 271
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19115120 1078 WTYIHDFENNVYRKYNDEYVTVVDEseifaDTTGNNANPYMLTY 1121
Cdd:pfam00443 272 IAYIKAYENNRWYKFDDEKVTEVDE-----ETAVLSSSAYILFY 310
|
|
| RPT |
pfam13446 |
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating ... |
538-597 |
7.11e-15 |
|
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating proteins. It's exact function is not known although it is likely to be involved in the binding of the Ubps in the complex with Rsp5 and Rup1.
Pssm-ID: 463882 Cd Length: 59 Bit Score: 69.83 E-value: 7.11e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 538 DEDLAYNTLGVqDRALSDDVLINVYGFAVEDHPEQSDTLRAALKCIGEVRNSRLITHYLE 597
Cdd:pfam13446 1 DVEQAYKLLGI-DEDTDDDFIITAYQVKVEDAPSQKDLLRRALKVIAEERNSELLRNFLE 59
|
|
| RPT |
pfam13446 |
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating ... |
467-521 |
3.55e-11 |
|
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating proteins. It's exact function is not known although it is likely to be involved in the binding of the Ubps in the complex with Rsp5 and Rup1.
Pssm-ID: 463882 Cd Length: 59 Bit Score: 59.43 E-value: 3.55e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115120 467 TVNEAYQWLGIKSNTEDAMVASVALVKFED---DSDKAIEAVKWIAEERNSSILYDFL 521
Cdd:pfam13446 1 DVEQAYKLLGIDEDTDDDFIITAYQVKVEDapsQKDLLRRALKVIAEERNSELLRNFL 58
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1058-1141 |
9.53e-08 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 56.42 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1058 HSYDLLAVFVHRGQASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADTTGNN----------------ANPYMLTY 1121
Cdd:COG5077 429 AVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGDhpykdkirdhsgikrfMSAYMLVY 508
|
90 100 110
....*....|....*....|....*....|....
gi 19115120 1122 IRKEY--------------RHIIECVHREHNLLL 1141
Cdd:COG5077 509 LRKSMlddllnpvaavdipPHVEEVLSEEIDKTE 542
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
613-1122 |
2.53e-107 |
|
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: 339.85 E-value: 2.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 613 PIGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKDLNmIENKEAVKKVGGRIVTRIEFLRALQFTYELRKLFIELIT 692
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAEL-ASDYPTERRIGGREVSRSELQRSNQFVYELRSLFNDLIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 693 SKSSSVHPSSVLTYLALipltldqvksgtssvmdlsssrelsnlnersitidpraeeqaqgleqeqgqdeakspaeqsss 772
Cdd:cd02666 80 SNTRSVTPSKELAYLAL--------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 773 vnlidfpmantngesqtqphyfevseeeinssmdlgRQQDVLECIDHVLFQLEASLGRISN-----SEDRLGSDNDLIRR 847
Cdd:cd02666 97 ------------------------------------RQQDVTECIDNVLFQLEVALEPISNafagpDTEDDKEQSDLIKR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 848 LFSGKLKQTLNDASQG----VRSNYEIFSHLIVDLFE---------EKQTLYDALDGVFETVNIdmgsetaqrslciTEL 914
Cdd:cd02666 141 LFSGKTKQQLVPESMGnqpsVRTKTERFLSLLVDVGKkgreivvllEPKDLYDALDRYFDYDSL-------------TKL 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 915 PIILQLQIQrvqfdrttgqpfksNAFVEFGKELSMDRYvedtdgkmapllqrywdlkreiinlqkrqqlllttnsNLMSS 994
Cdd:cd02666 208 PQRSQVQAQ--------------LAQPLQRELISMDRY-------------------------------------ELPSS 236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 995 VDTLSILSKWAAQQQDSRLPinpklpdilqeeinnvvaevdMLKKQEASLKEERTHLFDNYISHSYDLLAVFVHRGQASF 1074
Cdd:cd02666 237 IDDIDELIREAIQSESSLVR---------------------QAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEASS 295
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 19115120 1075 GHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADTTGNNANPYMLTYI 1122
Cdd:cd02666 296 GHYWVYIKDFEENVWRKYNDETVTVVPASEVFLFTLGNTATPYFLVYV 343
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
809-1122 |
1.43e-31 |
|
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: 124.52 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 809 RQQDVLECIDHVLFQLEASLGRISNSEDRLGSDNDLIRRLFSGKLKQTLNDASQG---VRSNYEIFSHLIVDLFEEKQ-T 884
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGhesVSTEPELFLSLPLPVKGLPQvS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 885 LYDALDGVFETVNID---------MGSETAQRSLCITELPIILQLQIQRVQFDRTtGQPFKSNAFVEFGKELSMDRYVEd 955
Cdd:cd02257 101 LEDCLEKFFKEEILEgdncykcekKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLELDLSPYLS- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 956 tdgkmapllqrywdlkreiinlqkrqqlllttnsnlmssvdtlsilskwaaqqqdsrlpinpklpdilqeeinnvvaevd 1035
Cdd:cd02257 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1036 mlkkqeaslkEERTHLFDNYISHSYDLLAVFVHRGQ-ASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADtTGNNA 1114
Cdd:cd02257 179 ----------EGEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF-GSLSS 247
|
....*...
gi 19115120 1115 NPYMLTYI 1122
Cdd:cd02257 248 SAYILFYE 255
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
614-1121 |
2.11e-25 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 108.30 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 614 IGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKDLNMIENKeavkkvggrivtrieflraLQFTYELRKLFIELits 693
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKD-------------------INLLCALRDLFKAL--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 694 ksssvhpssvltylalipltldQVKSGTSSVmdlsssrelsnlnersitidpraeeqaqgleqeqgqdeakspaeqsssv 773
Cdd:pfam00443 59 ----------------------QKNSKSSSV------------------------------------------------- 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 774 nlidfpmantngesqtQPHYFEVSEEEINSSMDLGRQQDVLECIDHVLFQLEASLGRISNSEDrlgsdNDLIRRLFSGKL 853
Cdd:pfam00443 68 ----------------SPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTEN-----ESLITDLFRGQL 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 854 KQTLND-ASQGVRSNYEIFSHLIVDLFEEKQTLYDA-------LDGVFETVNIDM--------GSETAQRSLCITELPII 917
Cdd:pfam00443 127 KSRLKClSCGEVSETFEPFSDLSLPIPGDSAELKTAslqicflQFSKLEELDDEEkyycdkcgCKQDAIKQLKISRLPPV 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 918 LQLQIQRVQFDRTTgqPFKSNAFVEFGKELSMDRYVEDTDGKMAPLLQrywdlkreiinlqkrqqlllttnsnlmssvdt 997
Cdd:pfam00443 207 LIIHLKRFSYNRST--WEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ-------------------------------- 252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 998 lsilskwaaqqqdsrlpinpklpdilqeeinnvvaevdmlkkqeaslkeerthlfdnyishSYDLLAVFVHRGQASFGHY 1077
Cdd:pfam00443 253 -------------------------------------------------------------DYRLVAVVVHSGSLSSGHY 271
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19115120 1078 WTYIHDFENNVYRKYNDEYVTVVDEseifaDTTGNNANPYMLTY 1121
Cdd:pfam00443 272 IAYIKAYENNRWYKFDDEKVTEVDE-----ETAVLSSSAYILFY 310
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-1125 |
3.00e-20 |
|
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: 93.48 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 614 IGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDEnkdlnmIENKEAVKKVggrivtrieflralqfTYELRKLFIELits 693
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPP------TEDDDDNKSV----------------PLALQRLFLFL--- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 694 ksssvhpssvltYLALIPLtldQVKSGTSSVmdlsssrelsnlneRSITIDPraeeqaqgleqeqgqdeakspaeqsssv 773
Cdd:cd02659 58 ------------QLSESPV---KTTELTDKT--------------RSFGWDS---------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 774 nlidfpmantngesqtqphyfevseeeinssMDLGRQQDVLE-CIdhVLF-QLEASLGRISNSedrlgsdnDLIRRLFSG 851
Cdd:cd02659 81 -------------------------------LNTFEQHDVQEfFR--VLFdKLEEKLKGTGQE--------GLIKNLFGG 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 852 KLKQtlNDASQGVRSNY---EIFSHLIVDLFEeKQTLYDALDGVFETVNIDmGSE-----------TAQRSLCITELPII 917
Cdd:cd02659 120 KLVN--YIICKECPHESereEYFLDLQVAVKG-KKNLEESLDAYVQGETLE-GDNkyfcekcgkkvDAEKGVCFKKLPPV 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 918 LQLQIQRVQFDRTTGQPFKSNAFVEFGKELSMDRYVEDTDGKmapllqrywdlkreiinlqkrqqlllttnsnlmssvdt 997
Cdd:cd02659 196 LTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAK-------------------------------------- 237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 998 lsilskwaaqqqdsrlpinpklpdilqeeinnvvAEVDMLKKQEASLKeerthlfdnyishsYDLLAVFVHRGQASFGHY 1077
Cdd:cd02659 238 ----------------------------------KEGDSEKKDSESYI--------------YELHGVLVHSGDAHGGHY 269
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115120 1078 WTYIHDFENNVYRKYNDEYVTVVDESEIFADTTG------------------NNAnpYMLTYIRKE 1125
Cdd:cd02659 270 YSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGgeetqktydsgprafkrtTNA--YMLFYERKS 333
|
|
| RPT |
pfam13446 |
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating ... |
538-597 |
7.11e-15 |
|
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating proteins. It's exact function is not known although it is likely to be involved in the binding of the Ubps in the complex with Rsp5 and Rup1.
Pssm-ID: 463882 Cd Length: 59 Bit Score: 69.83 E-value: 7.11e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 538 DEDLAYNTLGVqDRALSDDVLINVYGFAVEDHPEQSDTLRAALKCIGEVRNSRLITHYLE 597
Cdd:pfam13446 1 DVEQAYKLLGI-DEDTDDDFIITAYQVKVEDAPSQKDLLRRALKVIAEERNSELLRNFLE 59
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1058-1122 |
8.58e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 69.12 E-value: 8.58e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115120 1058 HSYDLLAVFVHRGQASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADT--TGNNANPYMLTYI 1122
Cdd:cd02665 162 VPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgGGRNPSAYCLMYI 228
|
|
| RPT |
pfam13446 |
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating ... |
467-521 |
3.55e-11 |
|
A repeated domain in UCH-protein; This is a repeated domain found in de-ubiquitinating proteins. It's exact function is not known although it is likely to be involved in the binding of the Ubps in the complex with Rsp5 and Rup1.
Pssm-ID: 463882 Cd Length: 59 Bit Score: 59.43 E-value: 3.55e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115120 467 TVNEAYQWLGIKSNTEDAMVASVALVKFED---DSDKAIEAVKWIAEERNSSILYDFL 521
Cdd:pfam13446 1 DVEQAYKLLGIDEDTDDDFIITAYQVKVEDapsQKDLLRRALKVIAEERNSELLRNFL 58
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
801-1122 |
7.92e-11 |
|
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: 63.46 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 801 INSSMD--LGRQQDVLECIDHVLfqleaslgrisnseDRLGSdndLIRRLFSGKLKQTLNDASQGVRSN-YEIFSHLIVD 877
Cdd:cd02674 11 MNSILQclSADQQDAQEFLLFLL--------------DGLHS---IIVDLFQGQLKSRLTCLTCGKTSTtFEPFTYLSLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 878 LFEE-----KQTLYDALDGVFETVNID---------MGSET-AQRSLCITELPIILQLQIQRVQFDRTTGQpfKSNAFVE 942
Cdd:cd02674 74 IPSGsgdapKVTLEDCLRLFTKEETLDgdnawkcpkCKKKRkATKKLTISRLPKVLIIHLKRFSFSRGSTR--KLTTPVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 943 FgkelsmdryvedtdgkmaPLlqrywdlkreiinlqkrQQLLLTTNSnlmssvdtlsilskwaaqqqDSRLPINPKLpdi 1022
Cdd:cd02674 152 F------------------PL-----------------NDLDLTPYV--------------------DTRSFTGPFK--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1023 lqeeinnvvaevdmlkkqeaslkeerthlfdnyishsYDLLAVFVHRGQASFGHYWTYIHDFENNVYRKYNDEYVTVVDE 1102
Cdd:cd02674 174 -------------------------------------YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSE 216
|
330 340
....*....|....*....|
gi 19115120 1103 SEIfadttgNNANPYMLTYI 1122
Cdd:cd02674 217 SSV------VSSSAYILFYE 230
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
615-957 |
2.25e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 60.51 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 615 GLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKDLNMIENKEAVKKVGGRIVtrieflralqftYELRKLFIELitsk 694
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTII------------DQLQLIFAQL---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 695 sssvhpssvltylalipltldqvksgtssvmdlsssrelsNLNERSItIDPRAEEQAQGLeqeqgqdeakspaeqsssvn 774
Cdd:cd02668 65 ----------------------------------------QFGNRSV-VDPSGFVKALGL-------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 775 lidfpmantngesqtqphyfevseeeinssmDLGRQQDVLECidHVLFQ--LEASLGRISNSEDRlgsdnDLIRRLFSGK 852
Cdd:cd02668 84 -------------------------------DTGQQQDAQEF--SKLFLslLEAKLSKSKNPDLK-----NIVQDLFRGE 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 853 LKQTlNDASQGVRSN------YEIfsHLIVDLFEekqTLYDALDGVFETVNID---------MGSET-AQRSLCITELPI 916
Cdd:cd02668 126 YSYV-TQCSKCGRESslpskfYEL--ELQLKGHK---TLEECIDEFLKEEQLTgdnqyfcesCNSKTdATRRIRLTTLPP 199
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 19115120 917 ILQLQIQRVQFDRTTGQPFKSNAFVEFGKELSMDRYVEDTD 957
Cdd:cd02668 200 TLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESD 240
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1058-1141 |
9.53e-08 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 56.42 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1058 HSYDLLAVFVHRGQASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADTTGNN----------------ANPYMLTY 1121
Cdd:COG5077 429 AVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGDhpykdkirdhsgikrfMSAYMLVY 508
|
90 100 110
....*....|....*....|....*....|....
gi 19115120 1122 IRKEY--------------RHIIECVHREHNLLL 1141
Cdd:COG5077 509 LRKSMlddllnpvaavdipPHVEEVLSEEIDKTE 542
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1004-1124 |
1.43e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 51.34 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1004 WAAQQQDSRLPINPKLPDIL-------------QEEINNVVAEVDMLKKQEASLKEERTHLfdnyishsYDLLAVFVHRG 1070
Cdd:COG5533 164 LEVQAKQEYEVSFVKLPKILtiqlkrfanlggnQKIDTEVDEKFELPVKHDQILNIVKETY--------YDLVGFVLHQG 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 19115120 1071 QASFGHYWTYIHdfENNVYRKYNDEYVTVVDESEIFADttgNNANPYMLTYIRK 1124
Cdd:COG5533 236 SLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAINE---KAKNAYLYFYERI 284
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
810-1122 |
4.94e-06 |
|
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: 50.06 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 810 QQDVLECIDHVLFQLEASLGRISNSEDRLGSDNDLIRRLFSGKLKQTLN-DASQGVRSNYEIFSHLIVDLFEEKQ----- 883
Cdd:cd02660 88 QQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTcQRCGGVSTTVDPFLDLSLDIPNKSTpswal 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 884 ---------TLYDALDgvFETVNIDMGS-----------ETAQRSLCITELPIILQLQIQRVQFDrTTGQPFKSNAFVEF 943
Cdd:cd02660 168 gesgvsgtpTLSDCLD--RFTRPEKLGDfaykcsgcgstQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 944 GKELSMDRYvedtdgkmapllqrywdlkreiinlqkrqqlllttnsnlmssvdtlsiLSKWAAQQQDSrlpiNPKLPDIL 1023
Cdd:cd02660 245 PLELNMTPY------------------------------------------------TSSSIGDTQDS----NSLDPDYT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1024 qeeinnvvaevdmlkkqeaslkeerthlfdnyishsYDLLAVFVHRGQASFGHYWTYIHDfENNVYRKYNDEYVTVVDES 1103
Cdd:cd02660 273 ------------------------------------YDLFAVVVHKGTLDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEE 315
|
330
....*....|....*....
gi 19115120 1104 EIFadttgnNANPYMLTYI 1122
Cdd:cd02660 316 EVL------KSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1060-1122 |
2.24e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 47.66 E-value: 2.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115120 1060 YDLLAVFVHRG-QASFGHYWTYIHDFENNVYRkYNDEYVTVVDESEIFadttgnNANPYMLTYI 1122
Cdd:cd02661 248 YKLYAVLVHSGfSPHSGHYYCYVKSSNGKWYN-MDDSKVSPVSIETVL------SQKAYILFYI 304
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1060-1124 |
2.64e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 48.34 E-value: 2.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115120 1060 YDLLAVFVHRGQASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEIFADTTgnnanpYMLTYIRK 1124
Cdd:COG5560 764 YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSA------YVLFYRRK 822
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1055-1105 |
9.28e-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 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: 45.78 E-value: 9.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19115120 1055 YISHS--YDLLAVFVHRGQ-ASFGHYWTYIHDFENNVYRKYNDEYVTVVDESEI 1105
Cdd:cd02657 234 LCTPSgyYELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDI 287
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1018-1121 |
6.98e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 39.66 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115120 1018 KLPDILQEEINNVV--AEVDMLKKQEA-SLKEERTHLfdnyishSYDLLAVFVHRGQASFGHYWTYIH------DFENNV 1088
Cdd:cd02662 125 RLPQILCIHLSRSVfdGRGTSTKNSCKvSFPERLPKV-------LYRLRAVVVHYGSHSSGHYVCYRRkplfskDKEPGS 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19115120 1089 YRKYN--------------DEYVTVVDESEIFAdttgnNANPYMLTY 1121
Cdd:cd02662 198 FVRMRegpsstshpwwrisDTTVKEVSESEVLE-----QKSAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
614-650 |
7.02e-03 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 40.62 E-value: 7.02e-03
10 20 30
....*....|....*....|....*....|....*..
gi 19115120 614 IGLENTGNLCYLNSLIQYYFIIKPLRNAILDIDENKD 650
Cdd:COG5077 194 VGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHP 230
|
|
|