|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-358 |
6.83e-99 |
|
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: 292.65 E-value: 6.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvvgqyqk 114
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 115 ifrgvDQQDSHEFLTILMDWLHSdlqtlhvprqremisasekawleftkakesMILHLFYGQMKSTVKCVACHKESATYE 194
Cdd:cd02674 21 -----DQQDAQEFLLFLLDGLHS------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTFE 65
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 195 SFSNLSLELPPNS---NVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsnsGS 268
Cdd:cd02674 66 PFTYLSLPIPSGSgdaPKVTLEDCLRLFTKEETLDGDNawkCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR---GS 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 269 YMKKQNYLRFPLENLDMNPYIAraESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVV 348
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVD--TRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV 220
|
330
....*....|
gi 386766198 349 SSAAYILFYT 358
Cdd:cd02674 221 SSSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
34-357 |
5.37e-97 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 290.88 E-value: 5.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 34 TGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKtNGQVIEEVAALIKELW-NGQYKCVASRDLRYVVGQY 112
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK-DINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 113 QKIFRGVDQQDSHEFLTILMDWLHSDLQTLHvprqremisasekawlefTKAKESMILHLFYGQMKSTVKCVACHKESAT 192
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNH------------------STENESLITDLFRGQLKSRLKCLSCGEVSET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 193 YESFSNLSLELPPNSNV---CQLNQCMDMYFSGERIHG---WNCPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADpsns 266
Cdd:pfam00443 142 FEPFSDLSLPIPGDSAElktASLQICFLQFSKLEELDDeekYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 267 GSYMKKQN-YLRFPLEnLDMNPYIAR-AESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDS 344
Cdd:pfam00443 218 RSTWEKLNtEVEFPLE-LDLSRYLAEeLKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDE 296
|
330
....*....|....
gi 386766198 345 SNVV-SSAAYILFY 357
Cdd:pfam00443 297 ETAVlSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
35-357 |
4.84e-74 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 230.06 E-value: 4.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvvgqyqk 114
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 115 ifrgvDQQDSHEFLTILMDWLHSDLQTLHVPRqremisasekawlEFTKAKESMILHLFYGQMKSTVKCVACHKESATYE 194
Cdd:cd02257 21 -----EQQDAHEFLLFLLDKLHEELKKSSKRT-------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTE 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 195 SFSNLSLELPPNSNVCQ-LNQCMDMYFSGERIHGWNCPSC--KTKRDAIKKLDISKLPPVLVVHLKRFYADpsNSGSYMK 271
Cdd:cd02257 83 PELFLSLPLPVKGLPQVsLEDCLEKFFKEEILEGDNCYKCekKKKQEATKRLKIKKLPPVLIIHLKRFSFN--EDGTKEK 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 272 KQNYLRFPLEnLDMNPYIARAESRAVT---PKTYQLYAVSNHYGT-MEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNV 347
Cdd:cd02257 161 LNTKVSFPLE-LDLSPYLSEGEKDSDSdngSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEV 239
|
330
....*....|....*
gi 386766198 348 V-----SSAAYILFY 357
Cdd:cd02257 240 LefgslSSSAYILFY 254
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-358 |
4.07e-64 |
|
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: 207.23 E-value: 4.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYkNYISRSNKTNGQVIEEVAALIKELW----NGQYKCVAsrdLRYVVG 110
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRH-SCTCLSCSPNSCLSCAMDEIFQEFYysgdRSPYGPIN---LLYLSW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 111 QYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVPRQREMISasekawleftkakeSMILH-LFYGQMKSTVKCVACHKE 189
Cdd:cd02660 78 KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHC--------------NCIIHqTFSGSLQSSVTCQRCGGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 190 SATYESFSNLSLELPPNSNVCQ------------LNQCMDMYFSGERI--HGWNCPSCKTKRDAIKKLDISKLPPVLVVH 255
Cdd:cd02660 144 STTVDPFLDLSLDIPNKSTPSWalgesgvsgtptLSDCLDRFTRPEKLgdFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 256 LKRFyaDPSNSGSYMKKQNYLRFPLEnLDMNPYIARA------ESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANyG 329
Cdd:cd02660 224 LKRF--EHSLNKTSRKIDTYVQFPLE-LNMTPYTSSSigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGD-G 299
|
330 340
....*....|....*....|....*....
gi 386766198 330 KWFKFDDQVVSALDSSNVVSSAAYILFYT 358
Cdd:cd02660 300 QWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
34-357 |
7.57e-64 |
|
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: 205.59 E-value: 7.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 34 TGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSnktNGQVIEEVAALIKELWNGQYKCVASRDLRYVVGQYQ 113
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNE---GFCMMCALEAHVERALASSGPGSAPRIFSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 114 KIFRGVDQQDSHEFLTILMDWLHS------DLQTLHVPRQREMisasekawleftkakeSMILHLFYGQMKSTVKCVACH 187
Cdd:cd02661 79 KHFRIGRQEDAHEFLRYLLDAMQKacldrfKKLKAVDPSSQET----------------TLVQQIFGGYLRSQVKCLNCK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 188 KESATYESFSNLSLELPpnsNVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFyadps 264
Cdd:cd02661 143 HVSNTYDPFLDLSLDIK---GADSLEDALEQFTKPEQLDGENkykCERCKKKVKASKQLTIHRAPNVLTIHLKRF----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 265 nSGSYMKKQN-YLRFPlENLDMNPYIARAESravTPKTYQLYAVSNHYGT-MEGGHYTAFCKSANyGKWFKFDDQVVSAL 342
Cdd:cd02661 215 -SNFRGGKINkQISFP-ETLDLSPYMSQPND---GPLKYKLYAVLVHSGFsPHSGHYYCYVKSSN-GKWYNMDDSKVSPV 288
|
330
....*....|....*
gi 386766198 343 DSSNVVSSAAYILFY 357
Cdd:cd02661 289 SIETVLSQKAYILFY 303
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-357 |
4.39e-53 |
|
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: 176.81 E-value: 4.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLTEycisdkyknyisrsnktngqvieevaaLIKELWNGQYKCVASRDLRyvvgqyqk 114
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE---------------------------LLSETPKELFSQVCRKAPQ-------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 115 iFRGVDQQDSHEFLTILMDWLhsdlqtlhvprqremisasekawleftkakESMILHLFYGQMKSTVKCVACHKESATYE 194
Cdd:cd02667 46 -FKGYQQQDSHELLRYLLDGL------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYE 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 195 SFSNLSL-ELPPNSNVCQLNQCMDMYFSGERIHGWNCPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsnSGSYMKKQ 273
Cdd:cd02667 95 PFLDLSLpRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYLISKLPPVLVIHLKRFQQPR--SANLRKVS 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 274 NYLRFPlENLDMNPYI--ARAESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANY---------------------GK 330
Cdd:cd02667 173 RHVSFP-EILDLAPFCdpKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPPqqrlsdltkskpaadeagpgsGQ 251
|
330 340
....*....|....*....|....*..
gi 386766198 331 WFKFDDQVVSALDSSNVVSSAAYILFY 357
Cdd:cd02667 252 WYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
32-357 |
5.10e-51 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 173.21 E-value: 5.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 32 GLTGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYisrsNKTNGQVIEEVAALIKELWNGQYKCVASRDLRYVVGQ 111
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED----DDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 112 YQKIFRGVDQQDSHEFLTILMDWLHSDLQTLhvprqremisasekawleftkAKESMILHLFYGQMKSTVKCVACHKESA 191
Cdd:cd02659 77 GWDSLNTFEQHDVQEFFRVLFDKLEEKLKGT---------------------GQEGLIKNLFGGKLVNYIICKECPHESE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 192 TYESFSNLSLELPPNSNvcqLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsNSGS 268
Cdd:cd02659 136 REEYFLDLQVAVKGKKN---LEESLDAYVQGETLEGDNkyfCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDF-ETMM 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 269 YMKKQNYLRFPLEnLDMNPYIARAESRAVTPKT--------YQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVS 340
Cdd:cd02659 212 RIKINDRFEFPLE-LDMEPYTEKGLAKKEGDSEkkdsesyiYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVT 290
|
330 340 350
....*....|....*....|....*....|....*....
gi 386766198 341 ALDSSNVV----------------------SSAAYILFY 357
Cdd:cd02659 291 PFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFY 329
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
13-357 |
8.28e-51 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 181.62 E-value: 8.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 13 TAPPTYSIYSSIfplrrgrGLTGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNK--TNGQVIEEVAALIK 90
Cdd:COG5560 252 VDDHNRSINKEA-------GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPlgMHGSVASAYADLIK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 91 ELWNGQYKCVASRDLRYVVGQYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVPRQREMISAS-----------EKAWL 159
Cdd:COG5560 325 QLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSpgddvvvkkkaKECWW 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 160 EFTKAKESMILHLFYGQMKSTVKCVACHKESATYESFSNLSLELP-------------PNSN------------------ 208
Cdd:COG5560 405 EHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPvsmvwkhtivvfpESGRrqplkieldasstirglk 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 209 -----VCQLNQC-----MDMYFSGER----------------------------------IHGWNCPSCKTKRD------ 238
Cdd:COG5560 485 klvdaEYGKLGCfeikvMCIYYGGNYnmlepadkvllqdipqtdfvylyetndngievpvVHLRIEKGYKSKRLfgdpfl 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 239 -------------------------AIKKLD------------------------------------------------- 244
Cdd:COG5560 565 qlnvlikasiydklvkefeellvlvEMKKTDvdlvseqvrllreesspsswlkleteidtkreeqveeegqmnfndavvi 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 245 --------------------------------------------------------------------ISKLPPVLVVHL 256
Cdd:COG5560 645 sceweekrylslfsydplwtireigaaertitlqdclnefskpeqlglsdswycpgckefrqaskqmeLWRLPMILIIHL 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 257 KRFYADPSNSgsyMKKQNYLRFPLENLDMNPYIARAESRAVtpkTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDD 336
Cdd:COG5560 725 KRFSSVRSFR---DKIDDLVEYPIDDLDLSGVEYMVDDPRL---IYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDD 798
|
570 580
....*....|....*....|.
gi 386766198 337 QVVSALDSSNVVSSAAYILFY 357
Cdd:COG5560 799 SRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-358 |
1.60e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 155.16 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLTeyCISDKYKnYISRSNKTNGQVieevaalikelwngqykcvASRDLRYVVGQYQK 114
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT--CLKDLFE-SISEQKKRTGVI-------------------SPKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 115 IFRGVDQQDSHEFLTILMDWLHSDLQtlhvpRQREMISASEKAWLEFTKAKESMILH-LFYGQMKSTVKCVACHKESATY 193
Cdd:cd02663 59 LFDNYMHQDAHEFLNFLLNEIAEILD-----AERKAEKANRKLNNNNNAEPQPTWVHeIFQGILTNETRCLTCETVSSRD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 194 ESFSNLSLELPPNSNVcqlNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADpSNSGSYM 270
Cdd:cd02663 134 ETFLDLSIDVEQNTSI---TSCLRQFSATETLCGRNkfyCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD-EQLNRYI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 271 KKQNYLRFPLEnLDMNPYIARAESravTPKTYQLYAVSNHYG-TMEGGHYTAFCKSAnyGKWFKFDDQVVSALDSSNVV- 348
Cdd:cd02663 210 KLFYRVVFPLE-LRLFNTTDDAEN---PDRLYELVAVVVHIGgGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEe 283
|
330
....*....|....*..
gi 386766198 349 -------SSAAYILFYT 358
Cdd:cd02663 284 ffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-358 |
6.84e-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: 149.11 E-value: 6.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCL-SNTP-QLTEY---CISDKYKNYISRSNKTNGQ-VIEEVAALIKELWNGQYKCVAS----RD 104
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWfMNLEfRKAVYecnSTEDAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPsgfvKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 105 LRYVVGQyqkifrgvdQQDSHEFLTILMDWLHSDLQTLHVPrqremisasekawleftKAKeSMILHLFYGQMKSTVKCV 184
Cdd:cd02668 81 LGLDTGQ---------QQDAQEFSKLFLSLLEAKLSKSKNP-----------------DLK-NIVQDLFRGEYSYVTQCS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 185 ACHKESATYESFSNLSLELPPNSnvcQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYA 261
Cdd:cd02668 134 KCGRESSLPSKFYELELQLKGHK---TLEECIDEFLKEEQLTGDNqyfCESCNSKTDATRRIRLTTLPPTLNFQLLRFVF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 262 DpSNSGSYMKKQNYLRFPlENLDMNPYIARAESRAvtpKTYQLYAVSNHYGT-MEGGHYTAFCKSANYGKWFKFDDQVVS 340
Cdd:cd02668 211 D-RKTGAKKKLNASISFP-EILDMGEYLAESDEGS---YVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVE 285
|
330 340 350
....*....|....*....|....*....|....*....
gi 386766198 341 ALDSSNV---------------------VSSAAYILFYT 358
Cdd:cd02668 286 EMPGKPLklgnsedpakprkseikkgthSSRTAYMLVYK 324
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-357 |
1.01e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 138.27 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLTEYcisdkyknyisrsnktngqvIEEVaalikelwngqykcvasrdlryvvgqyqk 114
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY--------------------LEEF----------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 115 ifrgVDQQDSHEFLTILMDWLHSDLQtlhvprqremisasekawleftkakesmilHLFYGQMKSTVKCVAC-HKESATY 193
Cdd:cd02662 32 ----LEQQDAHELFQVLLETLEQLLK------------------------------FPFDGLLASRIVCLQCgESSKVRY 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 194 ESFSNLSLELPPNSNV--CQLNQCMDMYFSGERIHGWNCPSCKTKrdaikkldISKLPPVLVVHLKRFYADPSnsGSYMK 271
Cdd:cd02662 78 ESFTMLSLPVPNQSSGsgTTLEHCLDDFLSTEIIDDYKCDRCQTV--------IVRLPQILCIHLSRSVFDGR--GTSTK 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 272 KQNYLRFPLEnldmnpyiaraesraVTPKTYQLYAVSNHYGTMEGGHYTAF--------------------CKSANYGKW 331
Cdd:cd02662 148 NSCKVSFPER---------------LPKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPW 212
|
330 340
....*....|....*....|....*..
gi 386766198 332 FKFDDQVVSALDSSNVV-SSAAYILFY 357
Cdd:cd02662 213 WRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
32-340 |
2.85e-33 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 131.15 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 32 GLTGLKNLGNTCYMNSILQCLSNTpqlteycisDKYKNYISRSNKTNGQVIEEVA-ALIKELWNGQYKCVASRDLRYVVG 110
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFI---------AKFRKDVYGIPTDHPRGRDSVAlALQRLFYNLQTGEEPVDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 111 QYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVprqremisasekawleftkakESMILHLFYGQMKSTVKCVACHKES 190
Cdd:COG5077 263 FGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVV---------------------ENALNGIFVGKMKSYIKCVNVNYES 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 191 ATYESFSNLSLELPPNSNvcqLNQCMDMYFSGERIHGWNCPSCKTK--RDAIKKLDISKLPPVLVVHLKRFYADpSNSGS 268
Cdd:COG5077 322 ARVEDFWDIQLNVKGMKN---LQESFRRYIQVETLDGDNRYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYD-FERDM 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766198 269 YMKKQNYLRFPLEnLDMNPYIAR-AESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVS 340
Cdd:COG5077 398 MVKINDRYEFPLE-IDLLPFLDRdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVT 469
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-357 |
3.15e-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: 125.51 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKTNGQVIeEVAALIKELWNGQYKCVASRD---------- 104
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANDLNC-QLIKLADGLLSGRYSKPASLKsendpyqvgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 105 ----LRYVVGQYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVprqremisasekawLEFTKakesmilhLFYGQMKST 180
Cdd:cd02658 80 kpsmFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLG--------------LNPND--------LFKFMIEDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 181 VKCVACHKESATYESFSNLSLELPPNSNVCQ-----------LNQCMDMYFSGERIHGwNCPSCKTKRDAIKKLDISKLP 249
Cdd:cd02658 138 LECLSCKKVKYTSELSEILSLPVPKDEATEKeegelvyepvpLEDCLKAYFAPETIED-FCSTCKEKTTATKTTGFKTFP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 250 PVLVVHLKRFYAdpsNSGSYMKKqnylrfplenLDMnpYIARAESRAvtPKTYQLYAVSNHYGT-MEGGHYTAFCK--SA 326
Cdd:cd02658 217 DYLVINMKRFQL---LENWVPKK----------LDV--PIDVPEELG--PGKYELIAFISHKGTsVHSGHYVAHIKkeID 279
|
330 340 350
....*....|....*....|....*....|.
gi 386766198 327 NYGKWFKFDDQVVSALDSSNVVSSAAYILFY 357
Cdd:cd02658 280 GEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-357 |
6.84e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 122.22 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQlteycisdkYKNYISRSNKTNGQviEEVAALIKELW--------NGQYKCVASRDLR 106
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKD---------FRRQVLSLNLPRLG--DSQSVMKKLQLlqahlmhtQRRAEAPPDYFLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 107 YVVGQYqkiFRGVDQQDSHEFLTILMDWLHSdlqtlhvprqremisasekawleftkakesMILHLFYGQMKSTVKCVAC 186
Cdd:cd02664 70 ASRPPW---FTPGSQQDCSEYLRYLLDRLHT------------------------------LIEKMFGGKLSTTIRCLNC 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 187 HKESATYESFSNLSLelppnsNVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADP 263
Cdd:cd02664 117 NSTSARTERFRDLDL------SFPSVQDLLNYFLSPEKLTGDNqyyCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 264 SnSGSYMKKQNYLRFPlENLDMNPYIARAESRAVTPKT----------------YQLYAVSNHYGT-MEGGHYtaFCKSA 326
Cdd:cd02664 191 K-THVREKIMDNVSIN-EVLSLPVRVESKSSESPLEKKeeesgddgelvtrqvhYRLYAVVVHSGYsSESGHY--FTYAR 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 327 N----------------------YGKWFKFDDQVVSALDSS---NVVS----SAAYILFY 357
Cdd:cd02664 267 DqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFEsvqNVTSrfpkDTPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
33-357 |
1.25e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 113.83 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 33 LTGLKNLGNTCYMNSILQCLSNTPQLTEycisdKYKNYISR-SNKTNGQVIEEvaaLIKELWNGQYKCVASRDLRYVVGQ 111
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKH-----GLKHLVSLiSSVEQLQSSFL---LNPEKYNDELANQAPRRLLNALRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 112 YQKIFRGVDQQDSHEFLTILMDWLhsdlqtlhvprqREMISAsekawleftkakesmilhLFYGQMKSTVKCVACHKESA 191
Cdd:cd02671 96 VNPMYEGYLQHDAQEVLQCILGNI------------QELVEK------------------DFQGQLVLRTRCLECETFTE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 192 TYESFSNLSLELP----------------PNSNVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVL 252
Cdd:cd02671 146 RREDFQDISVPVQeselskseesseispdPKTEMKTLKWAISQFASVERIVGEDkyfCENCHHYTEAERSLLFDKLPEVI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 253 VVHLKRFYADPSNSGSY--MKKQNY-----LRFPLENLDMNPyiaraesravTPKTYQLYAVSNHYG-TMEGGHYTAfck 324
Cdd:cd02671 226 TIHLKCFAANGSEFDCYggLSKVNTplltpLKLSLEEWSTKP----------KNDVYRLFAVVMHSGaTISSGHYTA--- 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 386766198 325 sanYGKWFKFDDQVV---------SALDSSNVVSSAAYILFY 357
Cdd:cd02671 293 ---YVRWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
35-357 |
1.40e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 112.81 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLteyciSDKYKNY---ISRSNKTNGQVIEEVAALIKELWNGQ--------------- 96
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPEL-----RDALKNYnpaRRGANQSSDNLTNALRDLFDTMDKKQepvppieflqllrma 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 97 YKCVASRDLRyvvGQYQkifrgvdQQDSHEFLTilmdwlhsdlQTLHVPRQRemisasekawLEFTKAKESMILHLFYGQ 176
Cdd:cd02657 76 FPQFAEKQNQ---GGYA-------QQDAEECWS----------QLLSVLSQK----------LPGAGSKGSFIDQLFGIE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 177 MKSTVKCVAC-HKESATYESFSNLSlelppnsnvCQLNQCMDMYFSGERI-HGWN----CPSCKTKRDAI--KKLDISKL 248
Cdd:cd02657 126 LETKMKCTESpDEEEVSTESEYKLQ---------CHISITTEVNYLQDGLkKGLEeeieKHSPTLGRDAIytKTSRISRL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 249 PPVLVVHLKRFYADPSNSgsymKKQNYLR---FPLEnLDMNPYiaraesraVTPK-TYQLYAVSNHYG-TMEGGHYTAFC 323
Cdd:cd02657 197 PKYLTVQFVRFFWKRDIQ----KKAKILRkvkFPFE-LDLYEL--------CTPSgYYELVAVITHQGrSADSGHYVAWV 263
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 386766198 324 KSANYGKWFKFDDQVVSALDSSNVVSSA-------AYILFY 357
Cdd:cd02657 264 RRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
35-357 |
2.43e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLS-NTPQLTEYcISDKYKNYISRSNKTNG----QVIEEVAALIKELWNGQYKCVAsrdlryvv 109
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDEL-LDDLSKELKVLKNVIRKpepdLNQEEALKLFTALWSSKEHKVG-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 110 gqyqKIFRGVDQQDSHEFLTILMDWLHSDL----QTLHVPRQREMISASEKAWLEFTKAKesmilhlfygQMKSTVkcva 185
Cdd:COG5533 72 ----WIPPMGSQEDAHELLGKLLDELKLDLvnsfTIRIFKTTKDKKKTSTGDWFDIIIEL----------PDQTWV---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 186 chKESATYESFSNLSLELPPNSnvCQLNQCMDmyfSGERIhgwncpSCKTKRDAIKKldisKLPPVLVVHLKRFyadpSN 265
Cdd:COG5533 134 --NNLKTLQEFIDNMEELVDDE--TGVKAKEN---EELEV------QAKQEYEVSFV----KLPKILTIQLKRF----AN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 266 SGSYMKKQNYLRfplENLDMNpyIARAESRAVTPKT-YQLYAVSNHYGTMEGGHYTAFCKSAnyGKWFKFDDQVVSALDS 344
Cdd:COG5533 193 LGGNQKIDTEVD---EKFELP--VKHDQILNIVKETyYDLVGFVLHQGSLEGGHYIAYVKKG--GKWEKANDSDVTPVSE 265
|
330
....*....|....*.
gi 386766198 345 SNVVSSA---AYILFY 357
Cdd:COG5533 266 EEAINEKaknAYLYFY 281
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
32-357 |
4.22e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 102.78 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 32 GLTGLKNLGNTCYMNSILQCLSNTPQLTEYCIS-DKYKNYISRSnktnGQVIEEVAALIKELWNGQ-YKCVASRD--LRY 107
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyENYENIKDRK----SELVKRLSELIRKIWNPRnFKGHVSPHelLQA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 108 VVGQYQKIFRGVDQQDSHEFLTILMDWLHSDLQ--------TLHVPRQREMISASEKAWLEFTKAKESMILHLFYGQMKS 179
Cdd:cd02669 194 VSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGgskkpnssIIHDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 180 TVKCvachkesatyesFSNLSLELPPN---------SNVCQLN--QCMDMYFSgerihgwncPSCKTKRDAIKKLDISKL 248
Cdd:cd02669 274 SVSP------------FLLLTLDLPPPplfkdgneeNIIPQVPlkQLLKKYDG---------KTETELKDSLKRYLISRL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 249 PPVLVVHLKRFyadPSNSGSYMKKQNYLRFPLENLDMNPYIARAESRAVTPKTYQLYAVSNHYGT-MEGGHYTAFCKSAN 327
Cdd:cd02669 333 PKYLIFHIKRF---SKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKS 409
|
330 340 350
....*....|....*....|....*....|
gi 386766198 328 YGKWFKFDDQVVSALDSSNVVSSAAYILFY 357
Cdd:cd02669 410 TNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-357 |
4.64e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 68.32 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 36 LKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvVGQYQKI 115
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSS------------------------------------------------------IGKINTE 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 116 FRGVDQQDSHEFLTIL---MDWLHSDLQTLHVPRQREMISASEKAWLEFTKakESMILhlfygqmkstvkCVACHKESAT 192
Cdd:cd02673 28 FDNDDQQDAHEFLLTLleaIDDIMQVNRTNVPPSNIEIKRLNPLEAFKYTI--ESSYV------------CIGCSFEENV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 193 YESFSNLSLELPPN-SNVCQLNQCMDMYFSG-ERIhgwnCPSCKTKrDAIKKLDISKLPPVLVVHLKRFYADPSNSgSYM 270
Cdd:cd02673 94 SDVGNFLDVSMIDNkLDIDELLISNFKTWSPiEKD----CSSCKCE-SAISSERIMTFPECLSINLKRYKLRIATS-DYL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 271 KKQNYLRFPLENldmnpyiaraesravTPKTYQLYAVSNHYG-TMEGGHYTAFCKS-ANYGKWFKFDDQVVSALDSSNV- 347
Cdd:cd02673 168 KKNEEIMKKYCG---------------TDAKYSLVAVICHLGeSPYDGHYIAYTKElYNGSSWLYCSDDEIRPVSKNDVs 232
|
330
....*....|..
gi 386766198 348 --VSSAAYILFY 357
Cdd:cd02673 233 tnARSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
121-357 |
5.69e-12 |
|
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: 64.89 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 121 QQDSHEFLTILMDWLHSDLQ-TLHVPRQREmisasekawleftKAKESMIlHLFYGqmKSTVKCVACHKESATYESFSNL 199
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQaAAEAISPGE-------------KSKNPMV-QLFYG--TFLTEGVLEGKPFCNCETFGQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 200 SLELPPNSNvcqLNQCMDMYFSGERIHgwNCPSCKTKRDAIKKLdISKLPPVLVVHLKRFYadpSNSGSYMKKQNYLRFP 279
Cdd:cd02665 86 PLQVNGYGN---LHECLEAAMFEGEVE--LLPSDHSVKSGQERW-FTELPPVLTFELSRFE---FNQGRPEKIHDKLEFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 280 lenldmnpyiaraesRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVVSSA-------- 351
Cdd:cd02665 157 ---------------QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggrnps 221
|
....*.
gi 386766198 352 AYILFY 357
Cdd:cd02665 222 AYCLMY 227
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
34-348 |
2.36e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 34 TGLKNLGNTCYMNSILQCL--------------SNTPQLTEYCISDKY--KNYISRSNKTNG-QVIEEVAALIKELWNGQ 96
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFftikplrdlvlnfdESKAELASDYPTERRigGREVSRSELQRSnQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 97 YKCVA-SRDLRYVVgqyqkifrgVDQQDSHEFLTILMDWLHSDLqtlhvprqrEMISASE-KAWLEFTKAKESMILHLFY 174
Cdd:cd02666 82 TRSVTpSKELAYLA---------LRQQDVTECIDNVLFQLEVAL---------EPISNAFaGPDTEDDKEQSDLIKRLFS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 175 GQMK-STVKCVACHKESAT--YESFSNLSL-------ELPPNSNVCQLNQCMDMYFSGERihgwncpscktkrdaikkld 244
Cdd:cd02666 144 GKTKqQLVPESMGNQPSVRtkTERFLSLLVdvgkkgrEIVVLLEPKDLYDALDRYFDYDS-------------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 245 ISKLPPVLVVHLK----RFYADPSNSGSYMKK-----QNYLRFPLENLDMNPYIARAESRAVTPK-----------TYQL 304
Cdd:cd02666 204 LTKLPQRSQVQAQlaqpLQRELISMDRYELPSsiddiDELIREAIQSESSLVRQAQNELAELKHEiekqfddlksyGYRL 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 386766198 305 YAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVV 348
Cdd:cd02666 284 HAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVF 327
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
35-336 |
6.50e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 53.43 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 35 GLKNLGNTCYMNSILQCLSNTPQLteYCISdkyKNYISRSNKTNGQVIEEVAALIK--ELWNGQYkCVASrdlryvvgQY 112
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPL--RNLA---LSHLATECLKEHCLLCELGFLFDmlEKAKGKN-CQAS--------NF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 113 QKIFRGVDQQDSHEfltiLMDWLHSD---------LQTLHvprqR---EMISASEKAWLEFTKAKESMILHLFYGQMKST 180
Cdd:pfam13423 68 LRALSSIPEASALG----LLDEDRETnsaislsslIQSFN----RfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 181 VKCVACHKESATYESFSNLSLELP-------PNSNVCQLNQCMDMYFSGERIH-GWnCPSCKTKRDAIKKLDISKLPPVL 252
Cdd:pfam13423 140 IRCSNCGHESVRESSTHVLDLIYPrkpssnnKKPPNQTFSSILKSSLERETTTkAW-CEKCKRYQPLESRRTVRNLPPVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 253 VVHLKRFYADPSNSGsymKKQNYLrfPLE-NLDMNPYIARAESRAVtpktYQLYA-VSNHYGTMEGGHYTAFCKSANY-- 328
Cdd:pfam13423 219 SLNAALTNEEWRQLW---KTPGWL--PPEiGLTLSDDLQGDNEIVK----YELRGvVVHIGDSGTSGHLVSFVKVADSel 289
|
330
....*....|...
gi 386766198 329 -----GKWFKFDD 336
Cdd:pfam13423 290 edpteSQWYLFND 302
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
194-357 |
5.52e-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: 50.22 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 194 ESFSNLSLELPPNSNVCQLNQCMDMYFSGErihgwncpscktkrdaikklDISKLPPVLVVHLKRFyadpSNSGSYMKKQ 273
Cdd:cd02670 64 ERLLQIPVPDDDDGGGITLEQCLEQYFNNS--------------------VFAKAPSCLIICLKRY----GKTEGKAQKM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766198 274 NYLRFPLENLDMNPYIARAE--------SRAVTPKTYQ-----------LYAVSNHYGT-MEGGHYTAFCKSANYG---- 329
Cdd:cd02670 120 FKKILIPDEIDIPDFVADDPracskcqlECRVCYDDKDfsptcgkfklsLCSAVCHRGTsLETGHYVAFVRYGSYSltet 199
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 386766198 330 -------KWFKFDD-------QVVSALDSSNVVSSaAYILFY 357
Cdd:cd02670 200 dneaynaQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
|
|
| |
