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Conserved domains on  [gi|19115120|ref|NP_594208|]
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ubiquitin hydrolase Ubp2 [Schizosaccharomyces pombe]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10602047)

ubiquitin carboxyl-terminal hydrolase catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin

Graphical summary

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List of domain hits

 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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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