|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
55-367 |
5.41e-51 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 172.63 E-value: 5.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 55 VGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPF--QMLLLLEKMQD-SRQKAVRPLELAYCLQKCN 131
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 132 VPL--FVQHDAAQLYLKLWNLIKDQITDVHLVER---LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDS-KP 205
Cdd:pfam00443 81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENeslITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 206 LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSqil 285
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLS--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 286 PMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTygnpnyhwqETAYLL 365
Cdd:pfam00443 238 RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308
|
..
gi 32313610 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 |
3.21e-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: 171.29 E-value: 3.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTR-ILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCN 131
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNaVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 132 VPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPlslfdVDSKPLKTLED 211
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ-----VAVKGKKNLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 212 ALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS--IRNSQTRKICHSLYFPQSLDFSQIL---P 286
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLELDMEPYTekgL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 287 MKRESCDAEEQSGG-QYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDI-----QCTYGNPNYHWQE 360
Cdd:cd02659 236 AKKEGDSEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfGGEETQKTYDSGP 315
|
330
....*....|....*....
gi 32313610 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 |
1.32e-49 |
|
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: 167.27 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNvdftrilkritvprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvplf 135
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 136 vQHDAAQLYLKLWNLIKDQITDVHLVER--------LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLfDVDSKPLK 207
Cdd:cd02257 22 -QQDAHEFLLFLLDKLHEELKKSSKRTSdssslkslIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL-PVKGLPQV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQvLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSLYFPQSLDFSQILP 286
Cdd:cd02257 100 SLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKR-LKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 287 MKRESCDAEEQSGgQYELFAVIAHVG-MADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNpnyhwQETAYLL 365
Cdd:cd02257 179 EGEKDSDSDNGSY-KYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSL-----SSSAYIL 252
|
...
gi 32313610 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 |
3.31e-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: 152.57 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPR--GADEQRRSVPF-------QMLLLLEKMQDSRQKAVRPLELAYC 126
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEdaELKNMPPDKPHepqtiidQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 127 LQKCNVplfVQHDAAQLYLKLWNLIKD---QITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvds 203
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAklsKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 204 KPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSlyfpqSLDFS 282
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNA-----SISFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 283 QILPMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWFCFNDSNIclVSWEDIQCTYGN-------- 353
Cdd:cd02668 228 EILDMGEYLAESDEGS-YVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDV--EEMPGKPLKLGNsedpakpr 304
|
330
....*....|....*....
gi 32313610 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 |
2.09e-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: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 137 QHDAAQLYLKLWNLIKDQITDVhlverLQALYtirvKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLK-TLEDALHC 215
Cdd:cd02674 22 QQDAQEFLLFLLDGLHSIIVDL-----FQGQL----KSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvTLEDCLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 216 FFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDfsqilpMKRESCDA 294
Cdd:cd02674 93 FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPlNDLD------LTPYVDTR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32313610 295 EEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNIclvswediqcTYGNPNYHWQETAYLLVY 367
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRV----------TKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
9.44e-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: 110.88 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKC----- 130
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAfpqfa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 131 ---NVPLFVQHDAAQLYLKLWNLIKdQITDVHLVER--LQALYTIRVKDSLICVDC-AMESSRNSSMLTLPLSLFDvdSK 204
Cdd:cd02657 81 ekqNQGGYAQQDAEECWSQLLSVLS-QKLPGAGSKGsfIDQLFGIELETKMKCTESpDEEEVSTESEYKLQCHISI--TT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 205 PLKTLEDALHcffqpRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTR-KICHSLYFPQSLDFS 282
Cdd:cd02657 158 EVNYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWkRDIQKKaKILRKVKFPFELDLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 283 QILPMKrescdaeeqsgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHwqeT 361
Cdd:cd02657 233 ELCTPS-----------GYYELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGGDWH---I 298
|
....*.
gi 32313610 362 AYLLVY 367
Cdd:cd02657 299 AYILLY 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
2.40e-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: 110.27 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQrrSVPFQMLLLLEKMQDSRQKAVRPLElaYCLQKCNVPLF 135
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ--SVMKKLQLLQAHLMHTQRRAEAPPD--YFLEASRPPWF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 136 V---QHDAAQlYLKlwnlikdqitdvHLVERLQAL----YTIRVKDSLICVDCAMESSRNSSMLTLPLSlfdvdskpLKT 208
Cdd:cd02664 77 TpgsQQDCSE-YLR------------YLLDRLHTLiekmFGGKLSTTIRCLNCNSTSARTERFRDLDLS--------FPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 209 LEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIrNSQT---RKICHSLYFPQSLDfsqiL 285
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY-DQKThvrEKIMDNVSINEVLS----L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 286 PMKRES----------------CDAEEQSGGQYELFAVIAHVGMA-DSGHYCVYIRNAVD-------------------- 328
Cdd:cd02664 211 PVRVESkssesplekkeeesgdDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpepkdaeendes 290
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 32313610 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 |
2.71e-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: 109.29 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVmnvdFTRILKRITVPRGADEQRRSVPFQMLLLLEKM----QDSRQKAVRPLELAYCLqKCN 131
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLT----HTPPLANYLLSREHSKDCCNEGFCMMCALEAHveraLASSGPGSAPRIFSSNL-KQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 132 VPLFV---QHDAAQL--YL-------KLWNLIKDQITDVHLVER--LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLS 197
Cdd:cd02661 78 SKHFRigrQEDAHEFlrYLldamqkaCLDRFKKLKAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 198 LFDVDSkplktLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSirNSQTRKICHSLYFPQ 277
Cdd:cd02661 158 IKGADS-----LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 278 SLDFSQILPMKRESCDaeeqsggQYELFAVIAHVGM-ADSGHYCVYIRNAvDGKWFCFNDSNICLVSWEDIqctygnpny 356
Cdd:cd02661 231 TLDLSPYMSQPNDGPL-------KYKLYAVLVHSGFsPHSGHYYCYVKSS-NGKWYNMDDSKVSPVSIETV--------- 293
|
330
....*....|..
gi 32313610 357 hWQETAYLLVYM 368
Cdd:cd02661 294 -LSQKAYILFYI 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
53-371 |
9.67e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 106.11 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRItvPRGADEQRRSVPFQMLLLLEKMQDSRQkAVRPLELAYCLQKCNV 132
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 133 PLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvdsKPLKTLEDA 212
Cdd:COG5077 269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV-----KGMKNLQES 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 213 LHCFFQPRELSSKSKCFCENCGKKTRGKQVLkLTHLPQTLTIHLMRFSI--RNSQTRKICHSLYFPQSLDfsqILPMKRE 290
Cdd:COG5077 344 FRRYIQVETLDGDNRYNAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYdfERDMMVKINDRYEFPLEID---LLPFLDR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 291 SCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVS-WEDIQCTYG----------NPN-YHW 358
Cdd:COG5077 420 DADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATeKEVLEENFGgdhpykdkirDHSgIKR 499
|
330
....*....|...
gi 32313610 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 |
1.07e-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: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 54 LVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVpfqmLLLLEKMQDSRQKAVRPLELAYCLQKCNvP 133
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSS----FLLNPEKYNDELANQAPRRLLNALREVN-P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 134 LF---VQHDAAQLYLKLWNLIKDqitdvhLVERL-QALYTIRVKdsliCVDCAMESSRNSSML---------TLPLSLFD 200
Cdd:cd02671 99 MYegyLQHDAQEVLQCILGNIQE------LVEKDfQGQLVLRTR----CLECETFTERREDFQdisvpvqesELSKSEES 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 201 VDSKP-----LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQT------RKI 269
Cdd:cd02671 169 SEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 270 chSLYFPQSLDFSqilpmkrescdAEEQSGGQ----YELFAVIAHVGMA-DSGHYCVYIRnavdgkWFCFNDSNICLVSW 344
Cdd:cd02671 249 --NTPLLTPLKLS-----------LEEWSTKPkndvYRLFAVVMHSGATiSSGHYTAYVR------WLLFDDSEVKVTEE 309
|
330 340
....*....|....*....|...
gi 32313610 345 EDIQcTYGNPNYHWQETAYLLVY 367
Cdd:cd02671 310 KDFL-EALSPNTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
208-367 |
1.46e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 99.57 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDFSQILP 286
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 287 MKrescdaeEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQctygnpnyhwQETAYLLV 366
Cdd:COG5560 756 MV-------DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSV----------TSSAYVLF 818
|
.
gi 32313610 367 Y 367
Cdd:COG5560 819 Y 819
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.18e-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: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVDFTRIL--KRITVPRGADEQRRSVPFQMLLLLEKMQ---DSRQKAvrPLELAYCLQKC 130
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNSCLSCAMDEIFQEFYysgDRSPYG--PINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 131 NVPL--FVQHDAAQLYLKLWNLIKDQITDVH-----------LVERLqalYTIRVKDSLICVDCAMESSRNSSMLTLPLS 197
Cdd:cd02660 80 SRNLagYSQQDAHEFFQFLLDQLHTHYGGDKneandeshcncIIHQT---FSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 198 LfDVDSKP-----------LKTLEDALHCFFQPRELSSKSKCfCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQ 265
Cdd:cd02660 157 I-PNKSTPswalgesgvsgTPTLSDCLDRFTRPEKLGDFAYK-CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 266 TRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQ--YELFAVIAHVGMADSGHYCVYIRNAvDGKWFCFNDSNICLVS 343
Cdd:cd02660 235 SRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDytYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVS 313
|
330 340
....*....|....*....|....
gi 32313610 344 WEDIQctygnpnyhwQETAYLLVY 367
Cdd:cd02660 314 EEEVL----------KSQAYLLFY 327
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
1.36e-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: 90.83 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVDFTrILKritvprgadeqrrsvpfqmlLLLEKMQDSRQK--AVRPLELAYCLQKCNvP 133
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-CLK--------------------DLFESISEQKKRtgVISPKKFITRLKREN-E 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 134 LF---VQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLI-----------------CVDCAMESSRNSSMLT 193
Cdd:cd02663 59 LFdnyMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQptwvheifqgiltnetrCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 194 LPlslfdVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTR--KICH 271
Cdd:cd02663 139 LS-----IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyiKLFY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 272 SLYFPQSLDfsqilpMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRnaVDGKWFCFNDSNICLVSWEDIQCT 350
Cdd:cd02663 214 RVVFPLELR------LFNTTDDAENPD-RLYELVAVVVHIGGgPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEF 284
|
330
....*....|....*..
gi 32313610 351 YGNPNYhwQETAYLLVY 367
Cdd:cd02663 285 FGDSPN--QATAYVLFY 299
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
4.59e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 88.98 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVmnvdftrilkritvprgADEQRRSvpfqmlLLLEkmqdsrqkavRPLELAYCLQKCNVPL- 134
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-----------------QTPALRE------LLSE----------TPKELFSQVCRKAPQFk 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 135 -FVQHDAAQLylkLWNLIKDQITDVHLVERLQALYTIrvkdslICVDCAMESSRNSSMLTLPLSLFDvDSKPLKTLEDAL 213
Cdd:cd02667 48 gYQQQDSHEL---LRYLLDGLRTFIDSIFGGELTSTI------MCESCGTVSLVYEPFLDLSLPRSD-EIKSECSIESCL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 214 HCFFQPRELSSKSKCFCENCgkkTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQTRKICHSLYFPQSLDFSQILPMKRESC 292
Cdd:cd02667 118 KQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQqPRSANLRKVSRHVSFPEILDLAPFCDPKCNSS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 293 DAEEQSggQYELFAVIAHVGMADSGHYCVYI--RNAVD-------------------GKWFCFNDSNICLVSWEDIQcty 351
Cdd:cd02667 195 EDKSSV--LYRLYGVVEHSGTMRSGHYVAYVkvRPPQQrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVL--- 269
|
330
....*....|....*.
gi 32313610 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 |
8.39e-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: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQV-----------FVMNVDFTRILKRIT---------VPRGADEQRRSVPfqmlLLLEKMQDSRQ 115
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVlfsipsfqwryDDLENKFPSDVVDPAndlncqlikLADGLLSGRYSKP----ASLKSENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 116 KAVRPLELAYCLQKcNVPLFV---QHDAAQLYLKLWNLI--------KDQITDV---HLVERLQALYTIRVKdslicvdc 181
Cdd:cd02658 77 VGIKPSMFKALIGK-GHPEFStmrQQDALEFLLHLIDKLdresfknlGLNPNDLfkfMIEDRLECLSCKKVK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 182 amESSRNSSMLTLPLSLFDVDSKPLK-------TLEDALHCFFQPRELSSkskcFCENCGKKTRGKQVLKLTHLPQTLTI 254
Cdd:cd02658 148 --YTSELSEILSLPVPKDEATEKEEGelvyepvPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 255 HLMRFSIRNSQTrkichslyfPQSLDFSQILPmkrescdaEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVD--GKW 331
Cdd:cd02658 222 NMKRFQLLENWV---------PKKLDVPIDVP--------EELGPGKYELIAFISHKGTsVHSGHYVAHIKKEIDgeGKW 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 32313610 332 FCFNDSNICLVSwediqctygNPNYHwQETAYLLVY 367
Cdd:cd02658 285 VLFNDEKVVASQ---------DPPEM-KKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
56-367 |
1.00e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.46 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVD-----FTRILKRITV-------PRGADEQRrsvpfQMLLLLEKMQDSRQKAVRPLEl 123
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldelLDDLSKELKVlknvirkPEPDLNQE-----EALKLFTALWSSKEHKVGWIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 124 ayclqkcnvPLFVQHDAAQLYLKLWNLIKDQitDVHLVERLQALYTIRVKDSLIcvdcameSSRNSSMLTLPLSLFDVDs 203
Cdd:COG5533 75 ---------PMGSQEDAHELLGKLLDELKLD--LVNSFTIRIFKTTKDKKKTST-------GDWFDIIIELPDQTWVNN- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 204 kpLKTLEDALHCF--FQPRELSSKSKcfcENCGKKTRGKQVLKLT--HLPQTLTIHLMRFSIRNSQtRKICHSL--YFPQ 277
Cdd:COG5533 136 --LKTLQEFIDNMeeLVDDETGVKAK---ENEELEVQAKQEYEVSfvKLPKILTIQLKRFANLGGN-QKIDTEVdeKFEL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 278 SLDFSQILPMKREscdaeeqsgGQYELFAVIAHVGMADSGHYCVYIRnaVDGKWFCFNDSNICLVSWEDIQctygNPNyh 357
Cdd:COG5533 210 PVKHDQILNIVKE---------TYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAI----NEK-- 272
|
330
....*....|
gi 32313610 358 wQETAYLLVY 367
Cdd:COG5533 273 -AKNAYLYFY 281
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
55-367 |
4.47e-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: 75.61 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 55 VGLHNIGQTCCLNSLIQVF---------VMNVD---FTRILKRITVPR------GADEQRRSVPF--QMLLLLEKMQDSR 114
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFftikplrdlVLNFDeskAELASDYPTERRiggrevSRSELQRSNQFvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 115 QKAVRPL-ELAY----------CLQKCnvpLFvQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLicVDCAM 183
Cdd:cd02666 82 TRSVTPSkELAYlalrqqdvteCIDNV---LF-QLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQL--VPESM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 184 E--SSRNSSM---LTLPLSLFDV--DSKPL---KTLEDALHCFFQPRELSS---KSKCFCENCGKKTRGKQVLKLTHLPQ 250
Cdd:cd02666 156 GnqPSVRTKTerfLSLLVDVGKKgrEIVVLlepKDLYDALDRYFDYDSLTKlpqRSQVQAQLAQPLQRELISMDRYELPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 251 TL-TIHLMRFSIRNSQTRKICHSLYFPQSLDFsqilpmKRESCDAEEQSGGqYELFAVIAHVGMADSGHYCVYIRNAVDG 329
Cdd:cd02666 236 SIdDIDELIREAIQSESSLVRQAQNELAELKH------EIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEEN 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 32313610 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 |
6.53e-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: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvplf 135
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 136 vQHDAAQLYLklwnlikdqitdvHLVERLQALYT----IRVKDSLICVDCAMESS-RNSSMLTLPLSLFDVDSKPLKTLE 210
Cdd:cd02662 34 -QQDAHELFQ-------------VLLETLEQLLKfpfdGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTTLE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 211 DALHCFFQPRELSSKSkcfCENCGkktrgkqvLKLTHLPQTLTIHLMR--FSIRNSQTRKICHsLYFPQSLdfsqilpmk 288
Cdd:cd02662 100 HCLDDFLSTEIIDDYK---CDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTSTKNSCK-VSFPERL--------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 289 rescdaeeqSGGQYELFAVIAHVGMADSGHYCVY--------------------IRNAVDGKWFCFNDSNICLVSWEDIq 348
Cdd:cd02662 159 ---------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV- 228
|
330
....*....|....*....
gi 32313610 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 |
1.11e-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: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 246 THLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLdfsQILPmkrescdaeeqsggqYELFAVIAHVGMADSGHYCVYIRN 325
Cdd:cd02665 126 TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII---QQVP---------------YELHAVLVHEGQANAGHYWAYIYK 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 32313610 326 AVDGKWFCFNDSNICLVSWEDIQ----CTYGNPnyhwqeTAYLLVYM 368
Cdd:cd02665 188 QSRQEWEKYNDISVTESSWEEVErdsfGGGRNP------SAYCLMYI 228
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
164-336 |
3.42e-11 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 63.44 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 164 LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSL----FDVDSKPLKT-----LEDALHcffqpRELSSKSkcFCENCG 234
Cdd:pfam13423 128 LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYprkpSSNNKKPPNQtfssiLKSSLE-----RETTTKA--WCEKCK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 235 KKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHslYFPQSLDfsqilpMKRESCDAEEQSGGQYELFAVIAHVGMA 314
Cdd:pfam13423 201 RYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTPG--WLPPEIG------LTLSDDLQGDNEIVKYELRGVVVHIGDS 272
|
170 180 190
....*....|....*....|....*....|
gi 32313610 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 |
2.34e-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: 51.38 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 137 QHDAAQLYLKLWNLIKD--------QITDVHLVERLQALYTIR--VKDSLICVDCAMESSRNSSMLTLPLSLFDVDskpL 206
Cdd:cd02673 33 QQDAHEFLLTLLEAIDDimqvnrtnVPPSNIEIKRLNPLEAFKytIESSYVCIGCSFEENVSDVGNFLDVSMIDNK---L 109
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 207 KTLEDALHCFFQPRELSSK-SKCFCENCGKKTRgkqvlkLTHLPQTLTIHLMRFSIRNSQtrkichSLYFPQSldfsqil 285
Cdd:cd02673 110 DIDELLISNFKTWSPIEKDcSSCKCESAISSER------IMTFPECLSINLKRYKLRIAT------SDYLKKN------- 170
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32313610 286 pmkRESCDAEEQSGGQYELFAVIAHVG-MADSGHYCVYIRNAVDG-KWFCFNDSNICLVSWEDI 347
Cdd:cd02673 171 ---EEIMKKYCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKNDV 231
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|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-339 |
1.10e-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: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 191 MLTL---PLSLF-DVDSK---PLKTLEDALHCFFQPRELSSKskcfcencGKKTRgkqvLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02669 280 LLTLdlpPPPLFkDGNEEniiPQVPLKQLLKKYDGKTETELK--------DSLKR----YLISRLPKYLIFHIKRFSKNN 347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32313610 264 SQTRKICHSLYFPQS-LDFSQILPmkreSCDAEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWFCFNDSNI 339
Cdd:cd02669 348 FFKEKNPTIVNFPIKnLDLSDYVH----FDKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNV 421
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|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
184-336 |
1.84e-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: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 184 ESSRNSSMLTLPLSLfDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02672 92 GTSRNSVSLLYTLSL-PLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVINLSVT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32313610 264 SQTRKICHSLYfPQSLDFSQILPMKRESCDAEEQSGGQ-----YELFAVIAHVGMADSG-HYCV---YIRNAVD-GKWFC 333
Cdd:cd02672 171 NGEFDDINVVL-PSGKVMQNKVSPKAIDHDKLVKNRGQesiykYELVGYVCEINDSSRGqHNVVfviKVNEESThGRWYL 249
|
...
gi 32313610 334 FND 336
Cdd:cd02672 250 FND 252
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