|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
55-367 |
1.67e-49 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 168.78 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 55 VGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPF--QMLLLLEKMQD-SRQKAVRPLELAYCLQKCN 131
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 132 VPF--FVQHDAAQLYLKLWNLIKDQITDVHLVER---LQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDS-KP 205
Cdd:pfam00443 81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENeslITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 206 LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSqil 285
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLS--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 286 PMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQCTygnpnyhwqETAYLL 365
Cdd:pfam00443 238 RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308
|
..
gi 23391971 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 |
4.45e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 165.51 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTR-ILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCN 131
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNaVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 132 VPFFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLICVDCAMESSRNSSMLTLPlslfdVDSKPLKTLED 211
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ-----VAVKGKKNLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 212 ALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS--IRNSQTRKICHSLYFPQSLDFSQIL---P 286
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLELDMEPYTekgL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 287 MKRESCDAEEQSGG-QYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDI-----QCTYGNPNYHWQE 360
Cdd:cd02659 236 AKKEGDSEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfGGEETQKTYDSGP 315
|
330
....*....|....*....
gi 23391971 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 |
2.26e-47 |
|
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: 161.50 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFvmnvdftrilkritvprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvpFF 135
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL------------------------------------------------------------FS 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 136 VQHDAAQLYLKLWNLIKDQITDVHLVER--------LQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLfDVDSKPLK 207
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEELKKSSKRTSdssslkslIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL-PVKGLPQV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQvLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSLYFPQSLDFSQILP 286
Cdd:cd02257 100 SLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKR-LKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 287 MKRESCDAEEQSGgQYELFAVIAHVG-MADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQCTYGNpnyhwQETAYLL 365
Cdd:cd02257 179 EGEKDSDSDNGSY-KYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSL-----SSSAYIL 252
|
...
gi 23391971 366 VYM 368
Cdd:cd02257 253 FYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
9.45e-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: 151.42 E-value: 9.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPR--GADEQRRSVPF-------QMLLLLEKMQDSRQKAVRPLELAYC 126
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEdaELKNMPPDKPHepqtiidQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 127 LQKCNVpffVQHDAAQLYLKLWNLIKD---QITDVHLVERLQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvds 203
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAklsKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 204 KPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSlyfpqSLDFS 282
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNA-----SISFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 283 QILPMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWSCFNDSNIclVSWEDIQCTYGN-------- 353
Cdd:cd02668 228 EILDMGEYLAESDEGS-YVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDV--EEMPGKPLKLGNsedpakpr 304
|
330
....*....|....*....
gi 23391971 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 |
3.73e-30 |
|
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: 115.46 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 137 QHDAAQLYLKLWNLIKDQITDVhlverLQALYmirvKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLK-TLEDALHC 215
Cdd:cd02674 22 QQDAQEFLLFLLDGLHSIIVDL-----FQGQL----KSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvTLEDCLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 216 FFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDfsqilpMKRESCDA 294
Cdd:cd02674 93 FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPlNDLD------LTPYVDTR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23391971 295 EEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNIclvswediqcTYGNPNYHWQETAYLLVY 367
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRV----------TKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-368 |
8.85e-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: 108.13 E-value: 8.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVmnvdFTRILKRITVPRGADEQRRSVPFQMLLLLEKM----QDSRQKAVRPLELAYCLQKCN 131
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLT----HTPPLANYLLSREHSKDCCNEGFCMMCALEAHveraLASSGPGSAPRIFSSNLKQIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 132 VPFFV--QHDAAQL--YL-------KLWNLIKDQITDVHLVER--LQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSL 198
Cdd:cd02661 79 KHFRIgrQEDAHEFlrYLldamqkaCLDRFKKLKAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 199 FDVDSkplktLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSirNSQTRKICHSLYFPQS 278
Cdd:cd02661 159 KGADS-----LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINKQISFPET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 279 LDFSQILPMKRESCDaeeqsggQYELFAVIAHVGM-ADSGHYCVYIRNAvDGKWSCFNDSNICLVSWEDIqctygnpnyh 357
Cdd:cd02661 232 LDLSPYMSQPNDGPL-------KYKLYAVLVHSGFsPHSGHYYCYVKSS-NGKWYNMDDSKVSPVSIETV---------- 293
|
330
....*....|.
gi 23391971 358 WQETAYLLVYM 368
Cdd:cd02661 294 LSQKAYILFYI 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.79e-26 |
|
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: 107.58 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQrrSVPFQMLLLLEKMQDSRQKAVRPLElaYCLQKCNVPFF 135
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ--SVMKKLQLLQAHLMHTQRRAEAPPD--YFLEASRPPWF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 136 V---QHDAAQlYLKlwnlikdqitdvHLVERLQAL----YMIRVKDSLICVDCAMESSRNSSMLTLPLSlfdvdskpLKT 208
Cdd:cd02664 77 TpgsQQDCSE-YLR------------YLLDRLHTLiekmFGGKLSTTIRCLNCNSTSARTERFRDLDLS--------FPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 209 LEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIrNSQT---RKICHSLYFPQSLDfsqiL 285
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY-DQKThvrEKIMDNVSINEVLS----L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 286 PMKRES----------------CDAEEQSGGQYELFAVIAHVGMA-DSGHYCVYIRNAVD-------------------- 328
Cdd:cd02664 211 PVRVESkssesplekkeeesgdDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpepkdaeendes 290
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 23391971 329 GKWSCFNDSNICLVSWEDIQ--CTYGNPNyhwqeTAYLLVY 367
Cdd:cd02664 291 KNWYLFNDSRVTFSSFESVQnvTSRFPKD-----TPYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
2.55e-26 |
|
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: 106.65 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKC----- 130
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAfpqfa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 131 ---NVPFFVQHDAAQLYLKLWNLIKdQITDVHLVER--LQALYMIRVKDSLICVDC-AMESSRNSSMLTLPLSLFDvdSK 204
Cdd:cd02657 81 ekqNQGGYAQQDAEECWSQLLSVLS-QKLPGAGSKGsfIDQLFGIELETKMKCTESpDEEEVSTESEYKLQCHISI--TT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 205 PLKTLEDALHcffqpRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTR-KICHSLYFPQSLDFS 282
Cdd:cd02657 158 EVNYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWkRDIQKKaKILRKVKFPFELDLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 283 QILPMKrescdaeeqsgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQCTYGNPNYHwqeT 361
Cdd:cd02657 233 ELCTPS-----------GYYELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGGDWH---I 298
|
....*.
gi 23391971 362 AYLLVY 367
Cdd:cd02657 299 AYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
53-371 |
5.33e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 103.80 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRItvPRGADEQRRSVPFQMLLLLEKMQDSRQkAVRPLELAYCLQKCNV 132
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 133 PFFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvdsKPLKTLEDA 212
Cdd:COG5077 269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV-----KGMKNLQES 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 213 LHCFFQPRELSSKSKCFCENCGKKTRGKQVLkLTHLPQTLTIHLMRFSI--RNSQTRKICHSLYFPQSLDfsqILPMKRE 290
Cdd:COG5077 344 FRRYIQVETLDGDNRYNAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYdfERDMMVKINDRYEFPLEID---LLPFLDR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 291 SCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVS-WEDIQCTYG----------NPN-YHW 358
Cdd:COG5077 420 DADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATeKEVLEENFGgdhpykdkirDHSgIKR 499
|
330
....*....|...
gi 23391971 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 |
1.24e-23 |
|
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: 99.97 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 54 LVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVpfqmLLLLEKMQDSRQKAVRPLELAYCLQKCNVP 133
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSS----FLLNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 134 F--FVQHDAAQLYLKLWNLIKDqitdvhLVERL-QALYMIRVKdsliCVDCAMESSRNSSML---------TLPLSLFDV 201
Cdd:cd02671 100 YegYLQHDAQEVLQCILGNIQE------LVEKDfQGQLVLRTR----CLECETFTERREDFQdisvpvqesELSKSEESS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 202 DSKP-----LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQT------RKIc 270
Cdd:cd02671 170 EISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKV- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 271 hSLYFPQSLDFSqilpmkrescdAEEQSGGQ----YELFAVIAHVGMA-DSGHYCVYIRnavdgkWSCFNDSNICLVSWE 345
Cdd:cd02671 249 -NTPLLTPLKLS-----------LEEWSTKPkndvYRLFAVVMHSGATiSSGHYTAYVR------WLLFDDSEVKVTEEK 310
|
330 340
....*....|....*....|..
gi 23391971 346 DIQcTYGNPNYHWQETAYLLVY 367
Cdd:cd02671 311 DFL-EALSPNTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
208-367 |
1.30e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.49 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDFSQILP 286
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 287 MKrescdaeEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQctygnpnyhwQETAYLLV 366
Cdd:COG5560 756 MV-------DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSV----------TSSAYVLF 818
|
.
gi 23391971 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 |
3.89e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 89.29 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVMNVDFTrILKritvprgadeqrrsvpfqmlLLLEKMQDSRQK--AVRPLELAYCLQKCNVP 133
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-CLK--------------------DLFESISEQKKRtgVISPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 134 F--FVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLI-----------------CVDCAMESSRNSSMLTL 194
Cdd:cd02663 60 FdnYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQptwvheifqgiltnetrCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 195 PlslfdVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTR--KICHS 272
Cdd:cd02663 140 S-----IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyiKLFYR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 273 LYFPQSLDfsqilpMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRnaVDGKWSCFNDSNICLVSWEDIQCTY 351
Cdd:cd02663 215 VVFPLELR------LFNTTDDAENPD-RLYELVAVVVHIGGgPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFF 285
|
330
....*....|....*.
gi 23391971 352 GNPNYhwQETAYLLVY 367
Cdd:cd02663 286 GDSPN--QATAYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.98e-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: 87.06 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVmnvdftrilkritvprgADEQRRSvpfqmlLLLEkmqdsrqkavRPLELAYCLQKCNVPF- 134
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-----------------QTPALRE------LLSE----------TPKELFSQVCRKAPQFk 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 135 -FVQHDAAQLylkLWNLIKDQITDVHLVERLQALYMIrvkdslICVDCAMESSRNSSMLTLPLSLFDvDSKPLKTLEDAL 213
Cdd:cd02667 48 gYQQQDSHEL---LRYLLDGLRTFIDSIFGGELTSTI------MCESCGTVSLVYEPFLDLSLPRSD-EIKSECSIESCL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 214 HCFFQPRELSSKSKCFCENCgkkTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQTRKICHSLYFPQSLDFSQILPMKRESC 292
Cdd:cd02667 118 KQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQqPRSANLRKVSRHVSFPEILDLAPFCDPKCNSS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 293 DAEEQSggQYELFAVIAHVGMADSGHYCVYI--RNAVD-------------------GKWSCFNDSNICLVSWEDIQcty 351
Cdd:cd02667 195 EDKSSV--LYRLYGVVEHSGTMRSGHYVAYVkvRPPQQrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVL--- 269
|
330
....*....|....*.
gi 23391971 352 gnpnyhwQETAYLLVY 367
Cdd:cd02667 270 -------KSEAYLLFY 278
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
173-367 |
2.21e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 87.81 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 173 KDSLICVDCAMESSRNSSMLTLPLSLfDVDSKP-----------LKTLEDALHCFFQPRELSSKSKCfCENCGKKTRGKQ 241
Cdd:cd02660 132 QSSVTCQRCGGVSTTVDPFLDLSLDI-PNKSTPswalgesgvsgTPTLSDCLDRFTRPEKLGDFAYK-CSGCGSTQEATK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 242 VLKLTHLPQTLTIHLMRFS-IRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQ--YELFAVIAHVGMADSGH 318
Cdd:cd02660 210 QLSIKKLPPVLCFQLKRFEhSLNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDytYDLFAVVVHKGTLDTGH 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23391971 319 YCVYIRNAvDGKWSCFNDSNICLVSWEDIQctygnpnyhwQETAYLLVY 367
Cdd:cd02660 290 YTAYCRQG-DGQWFKFDDAMITRVSEEEVL----------KSQAYLLFY 327
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.07e-18 |
|
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: 85.45 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQV-----------FVMNVDFTRILKRIT---------VPRGADEQRRSVPfqmlLLLEKMQDSRQ 115
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVlfsipsfqwryDDLENKFPSDVVDPAndlncqlikLADGLLSGRYSKP----ASLKSENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 116 KAVRPLELAYCLQKCNVPFFV--QHDAAQLYLKLWNLI--------KDQITDV---HLVERLQALYMIRVKdslicvdca 182
Cdd:cd02658 77 VGIKPSMFKALIGKGHPEFSTmrQQDALEFLLHLIDKLdresfknlGLNPNDLfkfMIEDRLECLSCKKVK--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 183 mESSRNSSMLTLPLSLFDVDSKPLK-------TLEDALHCFFQPRELSSkskcFCENCGKKTRGKQVLKLTHLPQTLTIH 255
Cdd:cd02658 148 -YTSELSEILSLPVPKDEATEKEEGelvyepvPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 256 LMRFSIRNSQTrkichslyfPQSLDFSQILPmkrescdaEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVD--GKWS 332
Cdd:cd02658 223 MKRFQLLENWV---------PKKLDVPIDVP--------EELGPGKYELIAFISHKGTsVHSGHYVAHIKKEIDgeGKWV 285
|
330 340 350
....*....|....*....|....*....|....*
gi 23391971 333 CFNDSNICLVSwediqctygNPNYHwQETAYLLVY 367
Cdd:cd02658 286 LFNDEKVVASQ---------DPPEM-KKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
56-367 |
1.01e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 76.76 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVMNVD-----FTRILKRITV-------PRGADEQRrsvpfQMLLLLEKMQDSRQKAVRPLEl 123
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldelLDDLSKELKVlknvirkPEPDLNQE-----EALKLFTALWSSKEHKVGWIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 124 ayclqkcnvPFFVQHDAAQLYLKLWNLIKDQitDVHLVERLqalYMIRVKDSlicvdcamESSRNSSMLTLPLSLFDVDS 203
Cdd:COG5533 75 ---------PMGSQEDAHELLGKLLDELKLD--LVNSFTIR---IFKTTKDK--------KKTSTGDWFDIIIELPDQTW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 204 -KPLKTLEDALHCF--FQPRELSSKSKcfcENCGKKTRGKQVLKLT--HLPQTLTIHLMRFSIRNSQtRKICHSL--YFP 276
Cdd:COG5533 133 vNNLKTLQEFIDNMeeLVDDETGVKAK---ENEELEVQAKQEYEVSfvKLPKILTIQLKRFANLGGN-QKIDTEVdeKFE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 277 QSLDFSQILPMKREscdaeeqsgGQYELFAVIAHVGMADSGHYCVYIRnaVDGKWSCFNDSNICLVSWEDIQctygNPNy 356
Cdd:COG5533 209 LPVKHDQILNIVKE---------TYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAI----NEK- 272
|
330
....*....|.
gi 23391971 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 |
2.01e-14 |
|
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: 73.68 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 55 VGLHNIGQTCCLNSLIQVF---------VMNVD---FTRILKRITVPR------GADEQRRSVPF--QMLLLLEKMQDSR 114
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFftikplrdlVLNFDeskAELASDYPTERRiggrevSRSELQRSNQFvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 115 QKAVRPL-ELAY----------CLQkcNVPFfvQHDAAQLYLKLWNLIKDQITDVHLVERLQALYMIRVKDSLicVDCAM 183
Cdd:cd02666 82 TRSVTPSkELAYlalrqqdvteCID--NVLF--QLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQL--VPESM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 184 E--SSRNSSM---LTLPLSLFDV--DSKPL---KTLEDALHCFFQPRELSS---KSKCFCENCGKKTRGKQVLKLTHLPQ 250
Cdd:cd02666 156 GnqPSVRTKTerfLSLLVDVGKKgrEIVVLlepKDLYDALDRYFDYDSLTKlpqRSQVQAQLAQPLQRELISMDRYELPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 251 TL-TIHLMRFSIRNSQTRKICHSLYFPQSLDFsqilpmKRESCDAEEQSGGqYELFAVIAHVGMADSGHYCVYIRNAVDG 329
Cdd:cd02666 236 SIdDIDELIREAIQSESSLVRQAQNELAELKH------EIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEEN 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 23391971 330 KWSCFNDSNICLVSWEDI-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 |
5.73e-14 |
|
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: 70.86 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvpff 135
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 136 vQHDAAQLYLklwnlikdqitdvHLVERLQALYM----IRVKDSLICVDCAMESS-RNSSMLTLPLSLFDVDSKPLKTLE 210
Cdd:cd02662 34 -QQDAHELFQ-------------VLLETLEQLLKfpfdGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTTLE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 211 DALHCFFQPRELSSKSkcfCENCGkktrgkqvLKLTHLPQTLTIHLMR--FSIRNSQTRKICHsLYFPQSLdfsqilpmk 288
Cdd:cd02662 100 HCLDDFLSTEIIDDYK---CDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTSTKNSCK-VSFPERL--------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 289 rescdaeeqSGGQYELFAVIAHVGMADSGHYCVY--------------------IRNAVDGKWSCFNDSNICLVSWEDIq 348
Cdd:cd02662 159 ---------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV- 228
|
330
....*....|....*....
gi 23391971 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 |
1.34e-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: 66.43 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 246 THLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLdfsQILPmkrescdaeeqsggqYELFAVIAHVGMADSGHYCVYIRN 325
Cdd:cd02665 126 TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII---QQVP---------------YELHAVLVHEGQANAGHYWAYIYK 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 23391971 326 AVDGKWSCFNDSNICLVSWEDIQ----CTYGNPnyhwqeTAYLLVYM 368
Cdd:cd02665 188 QSRQEWEKYNDISVTESSWEEVErdsfGGGRNP------SAYCLMYI 228
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
137-347 |
6.80e-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: 49.83 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 137 QHDAAQLYLKLWNLIKD--------QITDVHLVERLQALYMIR--VKDSLICVDCAMESSRNSSMLTLPLSLFDVDskpL 206
Cdd:cd02673 33 QQDAHEFLLTLLEAIDDimqvnrtnVPPSNIEIKRLNPLEAFKytIESSYVCIGCSFEENVSDVGNFLDVSMIDNK---L 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 207 KTLEDALHCFFQPRELSSK-SKCFCENCGKKTRgkqvlkLTHLPQTLTIHLMRFSIRNSQtrkichSLYFPQSldfsqil 285
Cdd:cd02673 110 DIDELLISNFKTWSPIEKDcSSCKCESAISSER------IMTFPECLSINLKRYKLRIAT------SDYLKKN------- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23391971 286 pmkRESCDAEEQSGGQYELFAVIAHVG-MADSGHYCVYIRNAVDG-KWSCFNDSNICLVSWEDI 347
Cdd:cd02673 171 ---EEIMKKYCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDV 231
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-339 |
1.81e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 43.08 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 191 MLTL---PLSLF-DVDSK---PLKTLEDALHCFFQPRELSSKskcfcencGKKTRgkqvLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02669 280 LLTLdlpPPPLFkDGNEEniiPQVPLKQLLKKYDGKTETELK--------DSLKR----YLISRLPKYLIFHIKRFSKNN 347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23391971 264 SQTRKICHSLYFPQS-LDFSQILPmkreSCDAEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWSCFNDSNI 339
Cdd:cd02669 348 FFKEKNPTIVNFPIKnLDLSDYVH----FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNV 421
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-336 |
5.87e-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: 41.34 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 184 ESSRNSSMLTLPLSLfDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02672 92 GTSRNSVSLLYTLSL-PLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVINLSVT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23391971 264 SQTRKICHSLYfPQSLDFSQILPMKRESCDAEEQSGGQ-----YELFAVIAHVGMADSG-HYCV---YIRNAVD-GKWSC 333
Cdd:cd02672 171 NGEFDDINVVL-PSGKVMQNKVSPKAIDHDKLVKNRGQesiykYELVGYVCEINDSSRGqHNVVfviKVNEESThGRWYL 249
|
...
gi 23391971 334 FND 336
Cdd:cd02672 250 FND 252
|
|
| |
