|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
0e+00 |
|
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: 511.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFcvpfreqlleyytsnksvadaeENLMTCLADLFSQISSQKKKTGVIAPKRFVQRLKKQNE 103
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF----------------------ENLLTCLKDLFESISEQKKRTGVISPKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 LFRSYMHQDAHEFLNYLLNEVVDILEKEAKATKTEHETssssspekianglkvpqaNGVVHKEPIVTWVHNIFQGILTNE 183
Cdd:cd02663 59 LFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKL------------------NNNNNAEPQPTWVHEIFQGILTNE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 184 TRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFK 263
Cdd:cd02663 121 TRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 264 YIEQLGRYKKLSYRVVFPLELKLSNTVE--PYADVEYSLFAVVVHVGSGPNHGHYVSLVKSHNHWLFFDDENVEMIEESA 341
Cdd:cd02663 201 YDEQLNRYIKLFYRVVFPLELRLFNTTDdaENPDRLYELVAVVVHIGGGPNHGHYVSIVKSHGGWLLFDDETVEKIDENA 280
|
330 340
....*....|....*....|....
gi 18420557 342 VQTFFGssqeYSSNTDHGYILFYE 365
Cdd:cd02663 281 VEEFFG----DSPNQATAYVLFYQ 300
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
23-364 |
1.67e-88 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 269.31 E-value: 1.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 23 FGFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEE-NLMTCLADLFSQISSQKKKTGvIAPKRFVQRLKKQ 101
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDiNLLCALRDLFKALQKNSKSSS-VSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 102 NELFRSYMHQDAHEFLNYLLNEVVDILEKeakatktehetssssspekianglkvpqangvVHKEPIVTWVHNIFQGILT 181
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------------NHSTENESLITDLFRGQLK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 182 NETRCLRCETVTARDETFLDLSLDIEQNSSITS------CLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHIL 255
Cdd:pfam00443 128 SRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 256 VIHLKRFKYieQLGRYKKLSYRVVFPLELKLSNTVEPYAD------VEYSLFAVVVHVGSgPNHGHYVSLVKS--HNHWL 327
Cdd:pfam00443 208 IIHLKRFSY--NRSTWEKLNTEVEFPLELDLSRYLAEELKpktnnlQDYRLVAVVVHSGS-LSSGHYIAYIKAyeNNRWY 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 18420557 328 FFDDENVEMIEEsavqtffgssqEYSSNTDHGYILFY 364
Cdd:pfam00443 285 KFDDEKVTEVDE-----------ETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
24-365 |
1.42e-67 |
|
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: 213.50 E-value: 1.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFcvpfreqlleyytsnksvadaeenlmtcladlfsqissqkkktgviapkrfvqrlkkqne 103
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 lfrsyMHQDAHEFLNYLLNEVVDILEKEAKATKtehetssssspekianglkvpqangvvHKEPIVTWVHNIFQGILTNE 183
Cdd:cd02257 21 -----EQQDAHEFLLFLLDKLHEELKKSSKRTS---------------------------DSSSLKSLIHDLFGGKLEST 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 184 TRCLRC--ETVTARDETFLDLSLDIEQ--NSSITSCLKNFSSTETLHAEDKFFCDKCcSLQEAQKRMKIKKPPHILVIHL 259
Cdd:cd02257 69 IVCLECghESVSTEPELFLSLPLPVKGlpQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 260 KRFKYIEQlGRYKKLSYRVVFPLELKLSNTVEPYA--------DVEYSLFAVVVHVGSGPNHGHYVSLVKSHNH--WLFF 329
Cdd:cd02257 148 KRFSFNED-GTKEKLNTKVSFPLELDLSPYLSEGEkdsdsdngSYKYELVAVVVHSGTSADSGHYVAYVKDPSDgkWYKF 226
|
330 340 350
....*....|....*....|....*....|....*.
gi 18420557 330 DDENVEMIEESAVQTFFGSSQEyssntdhGYILFYE 365
Cdd:cd02257 227 NDDKVTEVSEEEVLEFGSLSSS-------AYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-364 |
4.91e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 190.56 E-value: 4.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEY-YTSNKSVADAeenLMTCLADLFSQISSQKKKTGvIAPKRFVQRLKKQN 102
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSReHSKDCCNEGF---CMMCALEAHVERALASSGPG-SAPRIFSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 103 ELFRSYMHQDAHEFLNYLLnevvDILEKEAkatktehetssssSPEKIANGLKVPQANGVvhkepivTWVHNIFQGILTN 182
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLL----DAMQKAC-------------LDRFKKLKAVDPSSQET-------TLVQQIFGGYLRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 183 ETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRF 262
Cdd:cd02661 135 QVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 263 KYIeqlgRYKKLSYRVVFPLELKLSntvePYA------DVEYSLFAVVVHVGSGPNHGHYVSLVK-SHNHWLFFDDENVE 335
Cdd:cd02661 215 SNF----RGGKINKQISFPETLDLS----PYMsqpndgPLKYKLYAVLVHSGFSPHSGHYYCYVKsSNGKWYNMDDSKVS 286
|
330 340
....*....|....*....|....*....
gi 18420557 336 MIEESAVQtffgsSQEyssntdhGYILFY 364
Cdd:cd02661 287 PVSIETVL-----SQK-------AYILFY 303
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
21-365 |
5.02e-55 |
|
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: 183.61 E-value: 5.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 21 RYFGFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEENLMTCLADLFSQISSQKKKTGVIAPKRFVQRLKK 100
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 101 QNelfrSYMHQDAHEFLNYLLnevvDILEKEAKATKTEHEtssssspekianglkvpqangvvhkepivtwVHNIFQGIL 180
Cdd:cd02659 81 LN----TFEQHDVQEFFRVLF----DKLEEKLKGTGQEGL-------------------------------IKNLFGGKL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 181 TNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLK 260
Cdd:cd02659 122 VNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 261 RFKYIEQLGRYKKLSYRVVFPLELKLSNTVEPYA-------------DVEYSLFAVVVHvgSGPNH-GHYVSLVKS--HN 324
Cdd:cd02659 202 RFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLakkegdsekkdseSYIYELHGVLVH--SGDAHgGHYYSYIKDrdDG 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18420557 325 HWLFFDDENV-EMIEESAVQTFFGSSQEYSSN---------TDHGYILFYE 365
Cdd:cd02659 280 KWYKFNDDVVtPFDPNDAEEECFGGEETQKTYdsgprafkrTTNAYMLFYE 330
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-364 |
7.08e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 164.85 E-value: 7.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEENLMTC-LADLFSQISSQKKKTGVIaPKRFVQRLKKQN 102
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCaMDEIFQEFYYSGDRSPYG-PINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 103 ELFRSYMHQDAHEFLNYLLNEVvdilekeakatkteHEtssssspekiANGLKVPQANGVVHKEPIVtwvHNIFQGILTN 182
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQL--------------HT----------HYGGDKNEANDESHCNCII---HQTFSGSLQS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 183 ETRCLRCETVTARDETFLDLSLDIEQNS---------------SITSCLKNFSSTETLhAEDKFFCDKCCSLQEAQKRMK 247
Cdd:cd02660 134 SVTCQRCGGVSTTVDPFLDLSLDIPNKStpswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 248 IKKPPHILVIHLKRFKYiEQLGRYKKLSYRVVFPLELKLSN-----------TVEPYADVEYSLFAVVVHVGSgPNHGHY 316
Cdd:cd02660 213 IKKLPPVLCFQLKRFEH-SLNKTSRKIDTYVQFPLELNMTPytsssigdtqdSNSLDPDYTYDLFAVVVHKGT-LDTGHY 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18420557 317 VSLVKSHN-HWLFFDDENVEMIEESAVQtffgSSQeyssntdhGYILFY 364
Cdd:cd02660 291 TAYCRQGDgQWFKFDDAMITRVSEEEVL----KSQ--------AYLLFY 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
7.41e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 159.38 E-value: 7.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALyfcvpfreqlleyytsnksvadaeenlmtcladlfsqissqkkktgviapkrfvqrlkkqne 103
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 lfrSYMHQDAHEFLNYLLNevvdilekeakatktehetssssspekianglkvpqangvvhkepivtWVHNI----FQGI 179
Cdd:cd02674 19 ---SADQQDAQEFLLFLLD------------------------------------------------GLHSIivdlFQGQ 47
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 180 LTNETRCLRCETVTARDETFLDLSLDIEQNS------SITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPH 253
Cdd:cd02674 48 LKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPK 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 254 ILVIHLKRFKYieQLGRYKKLSYRVVFPLEL----KLSNTVEPYADVEYSLFAVVVHVGSGpNHGHYVSLVKS--HNHWL 327
Cdd:cd02674 128 VLIIHLKRFSF--SRGSTRKLTTPVTFPLNDldltPYVDTRSFTGPFKYDLYAVVNHYGSL-NGGHYTAYCKNneTNDWY 204
|
330 340 350
....*....|....*....|....*....|....*...
gi 18420557 328 FFDDENVEMIEESavqtffgssqeySSNTDHGYILFYE 365
Cdd:cd02674 205 KFDDSRVTKVSES------------SVVSSSAYILFYE 230
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-364 |
1.30e-44 |
|
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: 156.59 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVadaeENLMTCLADLFSQISSQKKKTgviAPKRFVQRLKKQNE 103
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSV----EQLQSSFLLNPEKYNDELANQ---APRRLLNALREVNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 LFRSYMHQDAHEFLNYLLNEVVDILEKeakatktehetssssspekianglkvpqangvvhkepivtwvhnIFQGILTNE 183
Cdd:cd02671 99 MYEGYLQHDAQEVLQCILGNIQELVEK--------------------------------------------DFQGQLVLR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 184 TRCLRCETVTARDETFLDLSLDI--------EQNSSITSCLK-----------NFSSTETLHAEDKFFCDKCCSLQEAQK 244
Cdd:cd02671 135 TRCLECETFTERREDFQDISVPVqeselsksEESSEISPDPKtemktlkwaisQFASVERIVGEDKYFCENCHHYTEAER 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 245 RMKIKKPPHILVIHLKRF----KYIEQLGRYKKLSYRVVFPLELKLSNTVEPYADVEYSLFAVVVHVGSGPNHGHYVSLV 320
Cdd:cd02671 215 SLLFDKLPEVITIHLKCFaangSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISSGHYTAYV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 18420557 321 KshnhWLFFDDENVEMIEEsavQTFFGSSQEYSSNTDHGYILFY 364
Cdd:cd02671 295 R----WLLFDDSEVKVTEE---KDFLEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
1.76e-43 |
|
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: 152.16 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYytsnksvadaeenlmtcLADLFSQISSQkkktgviAPKrfvqrlkkqne 103
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-----------------PKELFSQVCRK-------APQ----------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 lFRSYMHQDAHEFLNYLLNEvvdilekeakatktehetssssspekianglkvpqangvvhkepIVTWVHNIFQGILTNE 183
Cdd:cd02667 46 -FKGYQQQDSHELLRYLLDG--------------------------------------------LRTFIDSIFGGELTST 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 184 TRCLRCETVTARDETFLDLSL----DIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCslqEAQKRMKIKKPPHILVIHL 259
Cdd:cd02667 81 IMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 260 KRFKYiEQLGRYKKLSYRVVFPLELKLS-------NTVEPYADVEYSLFAVVVHVGSgPNHGHYVSLVKSHNHWLFFDDE 332
Cdd:cd02667 158 KRFQQ-PRSANLRKVSRHVSFPEILDLApfcdpkcNSSEDKSSVLYRLYGVVEHSGT-MRSGHYVAYVKVRPPQQRLSDL 235
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 18420557 333 NVEMIEESAVQTffGSSQEYSSNTDH-------------GYILFYE 365
Cdd:cd02667 236 TKSKPAADEAGP--GSGQWYYISDSDvrevsleevlkseAYLLFYE 279
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
1.73e-42 |
|
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: 150.65 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLL--------EYYTSNKSVADAEENLMTCLADLFSQISSQKKKtgVIAPKRFV 95
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstedaELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRS--VVDPSGFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 96 QRLKKQNELfrsymHQDAHEFLNYLLNEVVDILEKeakatktehetssssspekianglkvpQANGVVhkepiVTWVHNI 175
Cdd:cd02668 79 KALGLDTGQ-----QQDAQEFSKLFLSLLEAKLSK---------------------------SKNPDL-----KNIVQDL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 176 FQGILTNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHIL 255
Cdd:cd02668 122 FRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 256 VIHLKRFKYIEQLGRYKKLSYRVVFPLELKLSNTVEPY--ADVEYSLFAVVVHVGSGPNHGHYVSLVKSHNH--WLFFDD 331
Cdd:cd02668 202 NFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLAESdeGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTgeWYKFND 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 18420557 332 ENVEMI----------EESAVQTFFGSSQEYSSNTDhGYILFYE 365
Cdd:cd02668 282 EDVEEMpgkplklgnsEDPAKPRKSEIKKGTHSSRT-AYMLVYK 324
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
7.22e-38 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 138.39 E-value: 7.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAeenLMTCLADLFSQISSQKKKTGVIAPKRFVQRLKkqnE 103
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS---VMKKLQLLQAHLMHTQRRAEAPPDYFLEASRP---P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 LFRSYMHQDAHEFLNYLLnevvDILEkeakatktehetssssspekianglkvpqangvvhkepivTWVHNIFQGILTNE 183
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLL----DRLH----------------------------------------TLIEKMFGGKLSTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 184 TRCLRCETVTARDETFLDLSLDIeqnSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFK 263
Cdd:cd02664 111 IRCLNCNSTSARTERFRDLDLSF---PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFS 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 264 YIEQLGRYKKLSYRVVFPLELKL------SNTVEPYAD---------------VEYSLFAVVVHVGSGPNHGHYVSLVK- 321
Cdd:cd02664 188 YDQKTHVREKIMDNVSINEVLSLpvrvesKSSESPLEKkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTYARd 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18420557 322 -----SHNH----------------WLFFDDENVemiEESAVQTFFGSSQEYSSNTdhGYILFYE 365
Cdd:cd02664 268 qtdadSTGQecpepkdaeendesknWYLFNDSRV---TFSSFESVQNVTSRFPKDT--PYILFYE 327
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
1.20e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 126.67 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYYTS-NKSVADAEENL---MTCLADLF---------SQISSQKKKTGVIA 90
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfPSDVVDPANDLncqLIKLADGLlsgryskpaSLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 91 PKRFVQRLKKQNELFRSYMHQDAHEFLNYLLnevvDILEKEAKATKTehetssssspekianglkvpqangvvhKEPIvt 170
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLI----DKLDRESFKNLG---------------------------LNPN-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 171 wvhNIFQGILTNETRCLRCETVTARDETFLDLSLDIE--------------QNSSITSCLKNFSSTETLhaedKFFCDKC 236
Cdd:cd02658 128 ---DLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPkdeatekeegelvyEPVPLEDCLKAYFAPETI----EDFCSTC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 237 CSLQEAQKRMKIKKPPHILVIHLKRFKYIEQlGRYKKLSYRVVFPLELklsntvepyADVEYSLFAVVVHVGSGPNHGHY 316
Cdd:cd02658 201 KEKTTATKTTGFKTFPDYLVINMKRFQLLEN-WVPKKLDVPIDVPEEL---------GPGKYELIAFISHKGTSVHSGHY 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 18420557 317 VSLVK----SHNHWLFFDDENVemieesavqtffGSSQEYSSNTDHGYILFYE 365
Cdd:cd02658 271 VAHIKkeidGEGKWVLFNDEKV------------VASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
1.42e-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 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: 120.90 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEENLMTCLADLFSQISsqkKKTGVIAPKRFVQRLKKQNE 103
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMD---KKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 LFRS------YMHQDAHEFLNYLLNEVVDILEKEAKATKtehetssssspekianglkvpqangvvhkepivtWVHNIFQ 177
Cdd:cd02657 78 QFAEkqnqggYAQQDAEECWSQLLSVLSQKLPGAGSKGS----------------------------------FIDQLFG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 178 GILTNETRCL---RCETVTARDETFLDLSLDIEQ--NSSITSCLKNFSSTETLHAEdkffcdkccSLQ-EA--QKRMKIK 249
Cdd:cd02657 124 IELETKMKCTespDEEEVSTESEYKLQCHISITTevNYLQDGLKKGLEEEIEKHSP---------TLGrDAiyTKTSRIS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 250 KPPHILVIHLKRFKYIEQLGRYKKLSYRVVFPLELKLSNTVEPYAdvEYSLFAVVVHVGSGPNHGHYVSLVKS--HNHWL 327
Cdd:cd02657 195 RLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLYELCTPSG--YYELVAVITHQGRSADSGHYVAWVRRknDGKWI 272
|
330 340 350
....*....|....*....|....*....|....*...
gi 18420557 328 FFDDENVEMIEESAVQTFFGSSqEYSSntdhGYILFYE 365
Cdd:cd02657 273 KFDDDKVSEVTEEDILKLSGGG-DWHI----AYILLYK 305
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
22-347 |
1.48e-26 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 111.50 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 22 YFGFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKsvaDAEENLMTCLADLFSQISSQKKKTGVIapkrfvqRLKKQ 101
Cdd:COG5077 193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHP---RGRDSVALALQRLFYNLQTGEEPVDTT-------ELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 102 N--ELFRSYMHQDAHEFlnyllNEVV-DILEKEAKATKTEHEtssssspekianglkvpqangvvhkepivtwVHNIFQG 178
Cdd:COG5077 263 FgwDSDDSFMQHDIQEF-----NRVLqDNLEKSMRGTVVENA-------------------------------LNGIFVG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 179 ILTNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKcCSLQEAQKRMKIKKPPHILVIH 258
Cdd:COG5077 307 KMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 259 LKRFKYIEQLGRYKKLSYRVVFPLELKLSNTVEPYA------DVEYSLFAVVVHVGSGPNhGHYVSLVKSH--NHWLFFD 330
Cdd:COG5077 386 LKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDAdksensDAVYVLYGVLVHSGDLHE-GHYYALLKPEkdGRWYKFD 464
|
330
....*....|....*...
gi 18420557 331 DENV-EMIEESAVQTFFG 347
Cdd:COG5077 465 DTRVtRATEKEVLEENFG 482
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-365 |
1.38e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 100.52 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREqlleyytsnksvadaeenlmtcladlfsqissqkkktgviapkrFVQRLKKQne 103
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIE--------------------------------------------YLEEFLEQ-- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 104 lfrsymhQDAHEFLNYLLNEvvdiLEKEAKatktehetssssspekianglkvpqangvvhkepivtwvhNIFQGILTNE 183
Cdd:cd02662 35 -------QDAHELFQVLLET----LEQLLK----------------------------------------FPFDGLLASR 63
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 184 TRCLRCETVTA-RDETFLDLSLDIEQNSSIT-----SCLKNFSSTETLhaeDKFFCDKCcslqeaqkRMKIKKPPHILVI 257
Cdd:cd02662 64 IVCLQCGESSKvRYESFTMLSLPVPNQSSGSgttleHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCI 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 258 HLKRFKYIEQlGRYKKLSYRVVFPLELKlsntvepyaDVEYSLFAVVVHVGSgPNHGHYVSLVKS--------------- 322
Cdd:cd02662 133 HLSRSVFDGR-GTSTKNSCKVSFPERLP---------KVLYRLRAVVVHYGS-HSSGHYVCYRRKplfskdkepgsfvrm 201
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 18420557 323 -------HNHWLFFDDENVEMIEESAVQTffGSSqeyssntdhGYILFYE 365
Cdd:cd02662 202 regpsstSHPWWRISDTTVKEVSESEVLE--QKS---------AYMLFYE 240
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
215-365 |
3.79e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 98.03 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 215 CLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFKYieQLGRYKKLSYRVVFPL-ELKLSNTVEPY 293
Cdd:COG5560 680 CLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSS--VRSFRDKIDDLVEYPIdDLDLSGVEYMV 757
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18420557 294 ADVE--YSLFAVVVHVGsGPNHGHYVSLVK--SHNHWLFFDDENVEMIEESavqtffgssqeySSNTDHGYILFYE 365
Cdd:COG5560 758 DDPRliYDLYAVDNHYG-GLSGGHYTAYARnfANNGWYLFDDSRITEVDPE------------DSVTSSAYVLFYR 820
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
24-365 |
5.98e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 91.40 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVP-FREQLLEYYTSNKSVADA----EENLMTCLAD-LFSQISSQKKKtgviapkrfvqr 97
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkLDELLDDLSKELKVLKNVirkpEPDLNQEEALkLFTALWSSKEH------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 98 lkKQNELFRSYMHQDAHEFLNYLLNEVvdilekEAKATKTEHETSSSSSPEKIANGLKvpQANGVVHKEPIVTWVHNifq 177
Cdd:COG5533 69 --KVGWIPPMGSQEDAHELLGKLLDEL------KLDLVNSFTIRIFKTTKDKKKTSTG--DWFDIIIELPDQTWVNN--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 178 giltnetrclrcetvtarDETFLDLsLDIEQNSSITSCLKNFSSTETLHAEDKffcdkccslqeAQKRMKIKKPPHILVI 257
Cdd:COG5533 136 ------------------LKTLQEF-IDNMEELVDDETGVKAKENEELEVQAK-----------QEYEVSFVKLPKILTI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 258 HLKRFKYieqLGRYKKLSYRVVFPLELKLSnTVEPYADVE---YSLFAVVVHVGSgPNHGHYVSLVKSHNHWLFFDDENV 334
Cdd:COG5533 186 QLKRFAN---LGGNQKIDTEVDEKFELPVK-HDQILNIVKetyYDLVGFVLHQGS-LEGGHYIAYVKKGGKWEKANDSDV 260
|
330 340 350
....*....|....*....|....*....|.
gi 18420557 335 EMIEEsavqtffgsSQEYSSNTDHGYILFYE 365
Cdd:COG5533 261 TPVSE---------EEAINEKAKNAYLYFYE 282
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
24-331 |
2.06e-20 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 90.41 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNksvaDAEENLMTC--------LAD-------------LFSQISsQ 82
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATE----CLKEHCLLCelgflfdmLEKakgkncqasnflrALSSIP-E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 83 KKKTGVIApkrfvQRLKKQNELFRSYMHQDAHEFLnyllnevVDILEKEAKATKTehetssssspekianglkvpqangv 162
Cdd:pfam13423 77 ASALGLLD-----EDRETNSAISLSSLIQSFNRFL-------LDQLSSEENSTPP------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 163 vHKEPIVTWVHNIFQGILTNETRCLRCETVTARDETFLDLSLDI----------EQNSSITSCLKNFSSTETLHaedKFF 232
Cdd:pfam13423 120 -NPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYprkpssnnkkPPNQTFSSILKSSLERETTT---KAW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 233 CDKCCSLQEAQKRMKIKKPPHILVIHLKRFKYiEQLGRYKKLSYrvvFPLELKLSNTVEPYAD---VEYSLFAVVVHVGS 309
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNE-EWRQLWKTPGW---LPPEIGLTLSDDLQGDneiVKYELRGVVVHIGD 271
|
330 340 350
....*....|....*....|....*....|.
gi 18420557 310 GPNHGHYVSLVK---------SHNHWLFFDD 331
Cdd:pfam13423 272 SGTSGHLVSFVKvadseledpTESQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
26-365 |
3.89e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 88.35 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 26 ENFGNTCYCNSVLQALyfcvpfreqlleyytsnksvadaeenlmtcladlfsqiSSqkkktgviapkrfvqrLKKQNELF 105
Cdd:cd02673 3 VNTGNSCYFNSTMQAL--------------------------------------SS----------------IGKINTEF 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 106 RSYMHQDAHEFLNYLLNEVVDILEKEAKatktehetssssspekiangLKVPQANGVVHKEPIVTWVHNIfqgiltnETR 185
Cdd:cd02673 29 DNDDQQDAHEFLLTLLEAIDDIMQVNRT--------------------NVPPSNIEIKRLNPLEAFKYTI-------ESS 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 186 --CLRC---ETVTARDeTFLDLSLDIEQNSSITSCLKNFSSTETLHAEdkffCDKCcSLQEAQKRMKIKKPPHILVIHLK 260
Cdd:cd02673 82 yvCIGCsfeENVSDVG-NFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSC-KCESAISSERIMTFPECLSINLK 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 261 RFKYIEQLGRYKKLSYRVVFPLELKLSNtvepyadveYSLFAVVVHVGSGPNHGHYVSLVKS---HNHWLFFDDENVEMI 337
Cdd:cd02673 156 RYKLRIATSDYLKKNEEIMKKYCGTDAK---------YSLVAVICHLGESPYDGHYIAYTKElynGSSWLYCSDDEIRPV 226
|
330 340
....*....|....*....|....*...
gi 18420557 338 EESAVQTFFGSSqeyssntdhGYILFYE 365
Cdd:cd02673 227 SKNDVSTNARSS---------GYLIFYD 245
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
6-339 |
1.91e-17 |
|
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: 83.14 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 6 SKLEKAL-GDQFPEGerYFGFENFGNTCYCNSVLQALYFCVPFREQLLEYYTSNKSVADAEEnLMTCLADLFSQISSQKK 84
Cdd:cd02669 104 PKLSRDLdGKPYLPG--FVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSE-LVKRLSELIRKIWNPRN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 85 KTGVIAPKRFVQRLKKQNELFRSYMHQ-DAHEFLNYLLNEVVDILEKEAKatktehetssssspekianglkvpqangvv 163
Cdd:cd02669 181 FKGHVSPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSKK------------------------------ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 164 hkePIVTWVHNIFQGILTNETRCLRCETVTA---------------RDETFLDLSLD-----IEQNSSITSCLKNFSSTE 223
Cdd:cd02669 231 ---PNSSIIHDCFQGKVQIETQKIKPHAEEEgskdkffkdsrvkktSVSPFLLLTLDlppppLFKDGNEENIIPQVPLKQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 224 TLhaeDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRF-KYIEQLGRYKKLsyrVVFPLE-LKLSNTVEPYAD-----V 296
Cdd:cd02669 308 LL---KKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFsKNNFFKEKNPTI---VNFPIKnLDLSDYVHFDKPslnlsT 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18420557 297 EYSLFAVVVHVGSGPNHGHYVSLV--KSHNHWLFFDDENVEMIEE 339
Cdd:cd02669 382 KYNLVANIVHEGTPQEDGTWRVQLrhKSTNKWFEIQDLNVKEVLP 426
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
24-206 |
6.61e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 79.16 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQALYFCvpfrEQLLEYYTSNKSVADAEEN--------LMTCLADLFSQISSQKKKTgvIAPKRFV 95
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHT----WELRDYFLSDEYEESINEEnplgmhgsVASAYADLIKQLYDGNLHA--FTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 96 QRLKKQNELFRSYMHQDAHEFLNYLLNEVVDILEKEAKATKTEHETSSSSSPEKIAnglKVPQANGVVHKEPIVTWVHNI 175
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVK---KKAKECWWEHLKRNDSIITDL 417
|
170 180 190
....*....|....*....|....*....|.
gi 18420557 176 FQGILTNETRCLRCETVTARDETFLDLSLDI 206
Cdd:COG5560 418 FQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
24-364 |
2.12e-08 |
|
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: 55.19 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 24 GFENFGNTCYCNSVLQaLYFCV-PFREQLLEYYTSNKSVADAEEnlmtcladlfsqissQKKKTG--------VIAPKRF 94
Cdd:cd02666 3 GLDNIGNTCYLNSLLQ-YFFTIkPLRDLVLNFDESKAELASDYP---------------TERRIGgrevsrseLQRSNQF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 95 VQRLKkqnELFRSYMHQDAH-----EFLNYL------LNEVVD-ILEKEAKATKTEHETSSSSSPE--KIANGLkVPQAN 160
Cdd:cd02666 67 VYELR---SLFNDLIHSNTRsvtpsKELAYLalrqqdVTECIDnVLFQLEVALEPISNAFAGPDTEddKEQSDL-IKRLF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 161 GVVHKEPIVTWVHNIFQGILTNETRCLRCeTVTARDETflDLSLDIEQNSSITSCL-KNF--SSTETLHAEDKFFCDKCC 237
Cdd:cd02666 143 SGKTKQQLVPESMGNQPSVRTKTERFLSL-LVDVGKKG--REIVVLLEPKDLYDALdRYFdyDSLTKLPQRSQVQAQLAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 238 SLQEAQKRMKIKKPPHI--LVIHLKRFKYIEQLGRYKKLSYRVVfPLELKLSNTVEPYADVEYSLFAVVVHVGSGpNHGH 315
Cdd:cd02666 220 PLQRELISMDRYELPSSidDIDELIREAIQSESSLVRQAQNELA-ELKHEIEKQFDDLKSYGYRLHAVFIHRGEA-SSGH 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18420557 316 YVSLVKSH--NHWLFFDDENVEMIEESAVQTFfgssqeYSSNTDHGYILFY 364
Cdd:cd02666 298 YWVYIKDFeeNVWRKYNDETVTVVPASEVFLF------TLGNTATPYFLVY 342
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
248-365 |
1.42e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 51.76 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 248 IKKPPHILVIHLKRFKYIEqlGRYKKLSYRVVFPLELKLSNTVEP---------------YADVEY---------SLFAV 303
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTE--GKAQKMFKKILIPDEIDIPDFVADdpracskcqlecrvcYDDKDFsptcgkfklSLCSA 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18420557 304 VVHVGSGPNHGHYVSLVKS-------------HNHWLFFDDenveMIEESAVQTffGSSQEYSSNTDHGYILFYE 365
Cdd:cd02670 173 VCHRGTSLETGHYVAFVRYgsysltetdneayNAQWVFFDD----MADRDGVSN--GFNIPAARLLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
172-342 |
1.41e-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: 45.97 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 172 VHNIFQGILTNETRC-----LRCETVTARDETF---LDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQ 243
Cdd:cd02672 68 LIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLlytLSLPLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 244 KRMKIKKPPHI----LVIHLKRFKYIE-----QLGRYKKLSYRVVFPLE--LKLSNTVEPYADVEYSLFAVVVHVGSGPN 312
Cdd:cd02672 148 QTTSIRHLPDIlllvLVINLSVTNGEFddinvVLPSGKVMQNKVSPKAIdhDKLVKNRGQESIYKYELVGYVCEINDSSR 227
|
170 180 190
....*....|....*....|....*....|....*.
gi 18420557 313 HGHYVSLV------KSHNHWLFFDDENVEMIEESAV 342
Cdd:cd02672 228 GQHNVVFVikvneeSTHGRWYLFNDFLVTPVSELAY 263
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
243-334 |
3.67e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 41.39 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420557 243 QKRMKIKKPPhILVIHLKRFKYIEqlGRYKKLSYRVVFPLELKlsntvepyaDVEYSLFAVVVHVGSGpNHGHYVS--LV 320
Cdd:cd02665 121 QERWFTELPP-VLTFELSRFEFNQ--GRPEKIHDKLEFPQIIQ---------QVPYELHAVLVHEGQA-NAGHYWAyiYK 187
|
90
....*....|....
gi 18420557 321 KSHNHWLFFDDENV 334
Cdd:cd02665 188 QSRQEWEKYNDISV 201
|
|
| |
