|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
55-367 |
3.58e-50 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 170.32 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 55 VGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPF--QMLLLLEKMQD-SRQKAVRPLELAYCLQKCN 131
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 132 VPL--FVQHDAAQLYLKLWNLIKDQITDVHLVER---LQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDS-KP 205
Cdd:pfam00443 81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENeslITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 206 LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSqil 285
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLS--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 286 PMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTygnpnyhwqETAYLL 365
Cdd:pfam00443 238 RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308
|
..
gi 48146549 366 VY 367
Cdd:pfam00443 309 FY 310
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
53-372 |
4.14e-50 |
|
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: 170.90 E-value: 4.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTR-ILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCN 131
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNaVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 132 VPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLICVDCAMESSRNSSMLTLPlslfdVDSKPLKTLED 211
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ-----VAVKGKKNLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 212 ALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS--IRNSQTRKICHSLYFPQSLDFSQIL---P 286
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLELDMEPYTekgL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 287 MKRESCDAEEQSGG-QYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDI-----QCTYGNPNYHWQE 360
Cdd:cd02659 236 AKKEGDSEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfGGEETQKTYDSGP 315
|
330
....*....|....*....
gi 48146549 361 T-------AYLLVYMKMEC 372
Cdd:cd02659 316 RafkrttnAYMLFYERKSP 334
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
56-368 |
1.81e-48 |
|
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: 164.19 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMnvdftrilkritvprgadEQRRSVPFqMLLLLEKMQDSRQKAVRPLElayclqkcnvplf 135
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------EQQDAHEF-LLFLLDKLHEELKKSSKRTS------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 136 vqhdaaqlYLKLWNLIKDQITDVHLVERLQalymirvkdsliCVDCAMESSRNSSMLTLPLSLfDVDSKPLKTLEDALHC 215
Cdd:cd02257 49 --------DSSSLKSLIHDLFGGKLESTIV------------CLECGHESVSTEPELFLSLPL-PVKGLPQVSLEDCLEK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 216 FFQPRELSSKSKCFCENCGKKTRGKQvLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSLYFPQSLDFSQILPMKRESCDA 294
Cdd:cd02257 108 FFKEEILEGDNCYKCEKKKKQEATKR-LKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDS 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48146549 295 EEQSGgQYELFAVIAHVG-MADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNpnyhwQETAYLLVYM 368
Cdd:cd02257 187 DNGSY-KYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSL-----SSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
4.12e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 152.19 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPR--GADEQRRSVPF-------QMLLLLEKMQDSRQKAVRPLELAYC 126
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEdaELKNMPPDKPHepqtiidQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 127 LQKCNVplfVQHDAAQLYLKLWNLIKD---QITDVHLVERLQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvds 203
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAklsKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 204 KPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSlyfpqSLDFS 282
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNA-----SISFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 283 QILPMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWFCFNDSNIclVSWEDIQCTYGN-------- 353
Cdd:cd02668 228 EILDMGEYLAESDEGS-YVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDV--EEMPGKPLKLGNsedpakpr 304
|
330
....*....|....*....
gi 48146549 354 -----PNYHWQETAYLLVY 367
Cdd:cd02668 305 kseikKGTHSSRTAYMLVY 323
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
137-367 |
2.05e-31 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 118.54 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 137 QHDAAQLYLKLWNLIKDQITDVhlverLQALYmirvKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLK-TLEDALHC 215
Cdd:cd02674 22 QQDAQEFLLFLLDGLHSIIVDL-----FQGQL----KSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvTLEDCLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 216 FFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDfsqilpMKRESCDA 294
Cdd:cd02674 93 FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPlNDLD------LTPYVDTR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48146549 295 EEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNIclvswediqcTYGNPNYHWQETAYLLVY 367
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRV----------TKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
3.28e-27 |
|
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: 109.89 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQrrSVPFQMLLLLEKMQDSRQKAVRPLElaYCLQKCNVPLF 135
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ--SVMKKLQLLQAHLMHTQRRAEAPPD--YFLEASRPPWF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 136 V---QHDAAQlYLKlwnlikdqitdvHLVERLQAL----YMIRVKDSLICVDCAMESSRNSSMLTLPLSlfdvdskpLKT 208
Cdd:cd02664 77 TpgsQQDCSE-YLR------------YLLDRLHTLiekmFGGKLSTTIRCLNCNSTSARTERFRDLDLS--------FPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 209 LEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIrNSQT---RKICHSLYFPQSLDfsqiL 285
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY-DQKThvrEKIMDNVSINEVLS----L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 286 PMKRES----------------CDAEEQSGGQYELFAVIAHVGMA-DSGHYCVYIRNAVD-------------------- 328
Cdd:cd02664 211 PVRVESkssesplekkeeesgdDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpepkdaeendes 290
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 48146549 329 GKWFCFNDSNICLVSWEDIQ--CTYGNPNyhwqeTAYLLVY 367
Cdd:cd02664 291 KNWYLFNDSRVTFSSFESVQnvTSRFPKD-----TPYILFY 326
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-368 |
3.78e-27 |
|
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: 108.90 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVmnvdFTRILKRITVPRGADEQRRSVPFQMLLLLEKM----QDSRQKAVRPLELAYCLqKCN 131
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLT----HTPPLANYLLSREHSKDCCNEGFCMMCALEAHveraLASSGPGSAPRIFSSNL-KQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 132 VPLFV---QHDAAQL--YL-------KLWNLIKDQITDVHLVER--LQALYMIRVKDSLICVDCAMESSRNSSMLTLPLS 197
Cdd:cd02661 78 SKHFRigrQEDAHEFlrYLldamqkaCLDRFKKLKAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 198 LFDVDSkplktLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSirNSQTRKICHSLYFPQ 277
Cdd:cd02661 158 IKGADS-----LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 278 SLDFSQILPMKRESCDaeeqsggQYELFAVIAHVGM-ADSGHYCVYIRNAvDGKWFCFNDSNICLVSWEDIqctygnpny 356
Cdd:cd02661 231 TLDLSPYMSQPNDGPL-------KYKLYAVLVHSGFsPHSGHYYCYVKSS-NGKWYNMDDSKVSPVSIETV--------- 293
|
330
....*....|..
gi 48146549 357 hWQETAYLLVYM 368
Cdd:cd02661 294 -LSQKAYILFYI 304
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
5.34e-27 |
|
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: 108.57 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKC----- 130
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAfpqfa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 131 ---NVPLFVQHDAAQLYLKLWNLIKdQITDVHLVER--LQALYMIRVKDSLICVDC-AMESSRNSSMLTLPLSLFDvdSK 204
Cdd:cd02657 81 ekqNQGGYAQQDAEECWSQLLSVLS-QKLPGAGSKGsfIDQLFGIELETKMKCTESpDEEEVSTESEYKLQCHISI--TT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 205 PLKTLEDALHcffqpRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTR-KICHSLYFPQSLDFS 282
Cdd:cd02657 158 EVNYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWkRDIQKKaKILRKVKFPFELDLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 283 QILPMKrescdaeeqsgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHwqeT 361
Cdd:cd02657 233 ELCTPS-----------GYYELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGGDWH---I 298
|
....*.
gi 48146549 362 AYLLVY 367
Cdd:cd02657 299 AYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
53-371 |
7.32e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 106.49 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRItvPRGADEQRRSVPFQMLLLLEKMQDSRQkAVRPLELAYCLQKCNV 132
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 133 PLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvdsKPLKTLEDA 212
Cdd:COG5077 269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV-----KGMKNLQES 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 213 LHCFFQPRELSSKSKCFCENCGKKTRGKQVLkLTHLPQTLTIHLMRFSI--RNSQTRKICHSLYFPQSLDfsqILPMKRE 290
Cdd:COG5077 344 FRRYIQVETLDGDNRYNAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYdfERDMMVKINDRYEFPLEID---LLPFLDR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 291 SCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVS-WEDIQCTYG----------NPN-YHW 358
Cdd:COG5077 420 DADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATeKEVLEENFGgdhpykdkirDHSgIKR 499
|
330
....*....|...
gi 48146549 359 QETAYLLVYMKME 371
Cdd:COG5077 500 FMSAYMLVYLRKS 512
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-367 |
7.31e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 100.74 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 54 LVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVpfqmLLLLEKMQDSRQKAVRPLELAYCLQKCNvP 133
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSS----FLLNPEKYNDELANQAPRRLLNALREVN-P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 134 LF---VQHDAAQLYLKLWNLIKDqitdvhLVERL-QALYMIRVKdsliCVDCAMESSRNSSML---------TLPLSLFD 200
Cdd:cd02671 99 MYegyLQHDAQEVLQCILGNIQE------LVEKDfQGQLVLRTR----CLECETFTERREDFQdisvpvqesELSKSEES 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 201 VDSKP-----LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQT------RKI 269
Cdd:cd02671 169 SEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 270 chSLYFPQSLDFSqilpmkrescdAEEQSGGQ----YELFAVIAHVGMA-DSGHYCVYIRnavdgkWFCFNDSNICLVSW 344
Cdd:cd02671 249 --NTPLLTPLKLS-----------LEEWSTKPkndvYRLFAVVMHSGATiSSGHYTAYVR------WLLFDDSEVKVTEE 309
|
330 340
....*....|....*....|...
gi 48146549 345 EDIQcTYGNPNYHWQETAYLLVY 367
Cdd:cd02671 310 KDFL-EALSPNTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
208-367 |
1.47e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 99.57 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDFSQILP 286
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 287 MKrescdaeEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQctygnpnyhwQETAYLLV 366
Cdd:COG5560 756 MV-------DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSV----------TSSAYVLF 818
|
.
gi 48146549 367 Y 367
Cdd:COG5560 819 Y 819
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
6.78e-21 |
|
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: 91.60 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVDFTrILKritvprgadeqrrsvpfqmlLLLEKMQDSRQK--AVRPLELAYCLQKCNvP 133
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-CLK--------------------DLFESISEQKKRtgVISPKKFITRLKREN-E 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 134 LF---VQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLI-----------------CVDCAMESSRNSSMLT 193
Cdd:cd02663 59 LFdnyMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQptwvheifqgiltnetrCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 194 LPlslfdVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTR--KICH 271
Cdd:cd02663 139 LS-----IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyiKLFY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 272 SLYFPQSLDfsqilpMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRnaVDGKWFCFNDSNICLVSWEDIQCT 350
Cdd:cd02663 214 RVVFPLELR------LFNTTDDAENPD-RLYELVAVVVHIGGgPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEF 284
|
330
....*....|....*..
gi 48146549 351 YGNPNYhwQETAYLLVY 367
Cdd:cd02663 285 FGDSPN--QATAYVLFY 299
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.47e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 91.28 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVDFTRIL--KRITVPRGADEQRRSVPFQMLLLLEKMQ---DSRQKAvrPLELAYCLQKC 130
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNSCLSCAMDEIFQEFYysgDRSPYG--PINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 131 NVPL--FVQHDAAQLYLKLWNLIKDQITDVH-----------LVERLQALYMirvKDSLICVDCAMESSRNSSMLTLPLS 197
Cdd:cd02660 80 SRNLagYSQQDAHEFFQFLLDQLHTHYGGDKneandeshcncIIHQTFSGSL---QSSVTCQRCGGVSTTVDPFLDLSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 198 LfDVDSKP-----------LKTLEDALHCFFQPRELSSKSKCfCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQ 265
Cdd:cd02660 157 I-PNKSTPswalgesgvsgTPTLSDCLDRFTRPEKLGDFAYK-CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 266 TRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQ--YELFAVIAHVGMADSGHYCVYIRNAvDGKWFCFNDSNICLVS 343
Cdd:cd02660 235 SRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDytYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVS 313
|
330 340
....*....|....*....|....
gi 48146549 344 WEDIQctygnpnyhwQETAYLLVY 367
Cdd:cd02660 314 EEEVL----------KSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.42e-19 |
|
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: 87.44 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVmnvdftrilkritvprgADEQRRSvpfqmlLLLEkmqdsrqkavRPLELAYCLQKCNVPL- 134
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-----------------QTPALRE------LLSE----------TPKELFSQVCRKAPQFk 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 135 -FVQHDAAQLylkLWNLIKDQITDVHLVERLQALYMIrvkdslICVDCAMESSRNSSMLTLPLSLFDvDSKPLKTLEDAL 213
Cdd:cd02667 48 gYQQQDSHEL---LRYLLDGLRTFIDSIFGGELTSTI------MCESCGTVSLVYEPFLDLSLPRSD-EIKSECSIESCL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 214 HCFFQPRELSSKSKCFCENCgkkTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQTRKICHSLYFPQSLDFSQILPMKRESC 292
Cdd:cd02667 118 KQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQqPRSANLRKVSRHVSFPEILDLAPFCDPKCNSS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 293 DAEEQSggQYELFAVIAHVGMADSGHYCVYI--RNAVD-------------------GKWFCFNDSNICLVSWEDIQcty 351
Cdd:cd02667 195 EDKSSV--LYRLYGVVEHSGTMRSGHYVAYVkvRPPQQrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVL--- 269
|
330
....*....|....*.
gi 48146549 352 gnpnyhwQETAYLLVY 367
Cdd:cd02667 270 -------KSEAYLLFY 278
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
8.31e-19 |
|
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: 85.84 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQV-----------FVMNVDFTRILKRIT---------VPRGADEQRRSVPfqmlLLLEKMQDSRQ 115
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVlfsipsfqwryDDLENKFPSDVVDPAndlncqlikLADGLLSGRYSKP----ASLKSENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 116 KAVRPLELAYCLQKcNVPLFV---QHDAAQLYLKLWNLI--------KDQITDV---HLVERLQALYMIRVKdslicvdc 181
Cdd:cd02658 77 VGIKPSMFKALIGK-GHPEFStmrQQDALEFLLHLIDKLdresfknlGLNPNDLfkfMIEDRLECLSCKKVK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 182 amESSRNSSMLTLPLSLFDVDSKPLK-------TLEDALHCFFQPRELSSkskcFCENCGKKTRGKQVLKLTHLPQTLTI 254
Cdd:cd02658 148 --YTSELSEILSLPVPKDEATEKEEGelvyepvPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 255 HLMRFSIRNSQTrkichslyfPQSLDFSQILPmkrescdaEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVD--GKW 331
Cdd:cd02658 222 NMKRFQLLENWV---------PKKLDVPIDVP--------EELGPGKYELIAFISHKGTsVHSGHYVAHIKKEIDgeGKW 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 48146549 332 FCFNDSNICLVSwediqctygNPNYHwQETAYLLVY 367
Cdd:cd02658 285 VLFNDEKVVASQ---------DPPEM-KKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
56-367 |
4.43e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 77.54 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVD-----FTRILKRITV-------PRGADEQRrsvpfQMLLLLEKMQDSRQKAVRPLEl 123
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldelLDDLSKELKVlknvirkPEPDLNQE-----EALKLFTALWSSKEHKVGWIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 124 ayclqkcnvPLFVQHDAAQLYLKLWNLIKDQitDVHLVERLqalYMIRVKDSlicvdcamESSRNSSMLTLPLSLFDVDS 203
Cdd:COG5533 75 ---------PMGSQEDAHELLGKLLDELKLD--LVNSFTIR---IFKTTKDK--------KKTSTGDWFDIIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 204 -KPLKTLEDALHCF--FQPRELSSKSKcfcENCGKKTRGKQVLKLT--HLPQTLTIHLMRFSIRNSQtRKICHSL--YFP 276
Cdd:COG5533 133 vNNLKTLQEFIDNMeeLVDDETGVKAK---ENEELEVQAKQEYEVSfvKLPKILTIQLKRFANLGGN-QKIDTEVdeKFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 277 QSLDFSQILPMKREscdaeeqsgGQYELFAVIAHVGMADSGHYCVYIRnaVDGKWFCFNDSNICLVSWEDIQctygNPNy 356
Cdd:COG5533 209 LPVKHDQILNIVKE---------TYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAI----NEK- 272
|
330
....*....|.
gi 48146549 357 hwQETAYLLVY 367
Cdd:COG5533 273 --AKNAYLYFY 281
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
55-367 |
4.95e-15 |
|
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: 75.22 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 55 VGLHNIGQTCCLNSLIQVF---------VMNVD---FTRILKRITVPR------GADEQRRSVPF--QMLLLLEKMQDSR 114
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFftikplrdlVLNFDeskAELASDYPTERRiggrevSRSELQRSNQFvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 115 QKAVRPL-ELAY----------CLQKCnvpLFvQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLicVDCAM 183
Cdd:cd02666 82 TRSVTPSkELAYlalrqqdvteCIDNV---LF-QLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQL--VPESM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 184 E--SSRNSSM---LTLPLSLFDV--DSKPL---KTLEDALHCFFQPRELSS---KSKCFCENCGKKTRGKQVLKLTHLPQ 250
Cdd:cd02666 156 GnqPSVRTKTerfLSLLVDVGKKgrEIVVLlepKDLYDALDRYFDYDSLTKlpqRSQVQAQLAQPLQRELISMDRYELPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 251 TL-TIHLMRFSIRNSQTRKICHSLYFPQSLDFsqilpmKRESCDAEEQSGGqYELFAVIAHVGMADSGHYCVYIRNAVDG 329
Cdd:cd02666 236 SIdDIDELIREAIQSESSLVRQAQNELAELKH------EIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEEN 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 48146549 330 KWFCFNDSNICLVSWEDI-QCTYGNpnyhwQETAYLLVY 367
Cdd:cd02666 309 VWRKYNDETVTVVPASEVfLFTLGN-----TATPYFLVY 342
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
6.99e-15 |
|
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: 73.55 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvplf 135
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 136 vQHDAAQLYLklwnlikdqitdvHLVERLQALYM----IRVKDSLICVDCAMESS-RNSSMLTLPLSLFDVDSKPLKTLE 210
Cdd:cd02662 34 -QQDAHELFQ-------------VLLETLEQLLKfpfdGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTTLE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 211 DALHCFFQPRELSSKSkcfCENCGkktrgkqvLKLTHLPQTLTIHLMR--FSIRNSQTRKICHsLYFPQSLdfsqilpmk 288
Cdd:cd02662 100 HCLDDFLSTEIIDDYK---CDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTSTKNSCK-VSFPERL--------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 289 rescdaeeqSGGQYELFAVIAHVGMADSGHYCVY--------------------IRNAVDGKWFCFNDSNICLVSWEDIq 348
Cdd:cd02662 159 ---------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV- 228
|
330
....*....|....*....
gi 48146549 349 ctygnpnyHWQETAYLLVY 367
Cdd:cd02662 229 --------LEQKSAYMLFY 239
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
246-368 |
1.12e-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: 66.81 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 246 THLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLdfsQILPmkrescdaeeqsggqYELFAVIAHVGMADSGHYCVYIRN 325
Cdd:cd02665 126 TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII---QQVP---------------YELHAVLVHEGQANAGHYWAYIYK 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 48146549 326 AVDGKWFCFNDSNICLVSWEDIQ----CTYGNPnyhwqeTAYLLVYM 368
Cdd:cd02665 188 QSRQEWEKYNDISVTESSWEEVErdsfGGGRNP------SAYCLMYI 228
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
164-336 |
1.17e-10 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 61.90 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 164 LQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSL----FDVDSKPLKT-----LEDALHcffqpRELSSKSkcFCENCG 234
Cdd:pfam13423 128 LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYprkpSSNNKKPPNQtfssiLKSSLE-----RETTTKA--WCEKCK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 235 KKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHslYFPQSLDfsqilpMKRESCDAEEQSGGQYELFAVIAHVGMA 314
Cdd:pfam13423 201 RYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPG--WLPPEIG------LTLSDDLQGDNEIVKYELRGVVVHIGDS 272
|
170 180 190
....*....|....*....|....*....|
gi 48146549 315 D-SGHYCVYIRNAV-------DGKWFCFND 336
Cdd:pfam13423 273 GtSGHLVSFVKVADseledptESQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
137-347 |
2.86e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 50.99 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 137 QHDAAQLYLKLWNLIKD--------QITDVHLVERLQALYMIR--VKDSLICVDCAMESSRNSSMLTLPLSLFDVDskpL 206
Cdd:cd02673 33 QQDAHEFLLTLLEAIDDimqvnrtnVPPSNIEIKRLNPLEAFKytIESSYVCIGCSFEENVSDVGNFLDVSMIDNK---L 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 207 KTLEDALHCFFQPRELSSK-SKCFCENCGKKTRgkqvlkLTHLPQTLTIHLMRFSIRNSQtrkichSLYFPQSldfsqil 285
Cdd:cd02673 110 DIDELLISNFKTWSPIEKDcSSCKCESAISSER------IMTFPECLSINLKRYKLRIAT------SDYLKKN------- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48146549 286 pmkRESCDAEEQSGGQYELFAVIAHVG-MADSGHYCVYIRNAVDG-KWFCFNDSNICLVSWEDI 347
Cdd:cd02673 171 ---EEIMKKYCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDV 231
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-339 |
1.13e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 46.93 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 191 MLTL---PLSLF-DVDSK---PLKTLEDALHCFFQPRELSSKskcfcencGKKTRgkqvLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02669 280 LLTLdlpPPPLFkDGNEEniiPQVPLKQLLKKYDGKTETELK--------DSLKR----YLISRLPKYLIFHIKRFSKNN 347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48146549 264 SQTRKICHSLYFPQS-LDFSQILPmkreSCDAEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWFCFNDSNI 339
Cdd:cd02669 348 FFKEKNPTIVNFPIKnLDLSDYVH----FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNV 421
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-336 |
1.66e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 42.88 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 184 ESSRNSSMLTLPLSLfDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02672 92 GTSRNSVSLLYTLSL-PLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVINLSVT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48146549 264 SQTRKICHSLYfPQSLDFSQILPMKRESCDAEEQSGGQ-----YELFAVIAHVGMADSG-HYCV---YIRNAVD-GKWFC 333
Cdd:cd02672 171 NGEFDDINVVL-PSGKVMQNKVSPKAIDHDKLVKNRGQesiykYELVGYVCEINDSSRGqHNVVfviKVNEESThGRWYL 249
|
...
gi 48146549 334 FND 336
Cdd:cd02672 250 FND 252
|
|
| |
