|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
55-367 |
1.24e-49 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 169.16 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 55 VGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPF--QMLLLLEKMQD-SRQKAVRPLELAYCLQKCN 131
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLlcALRDLFKALQKnSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 132 VPL--FVQHDAAQLYLKLWNLIKDQITDVHLVER---LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDS-KP 205
Cdd:pfam00443 81 PDFsgYKQQDAQEFLLFLLDGLHEDLNGNHSTENeslITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAeLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 206 LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSqil 285
Cdd:pfam00443 161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLS--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 286 PMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQCTygnpnyhwqETAYLL 365
Cdd:pfam00443 238 RYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS---------SSAYIL 308
|
..
gi 7159737 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 |
6.64e-49 |
|
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: 167.82 E-value: 6.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTR-ILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCN 131
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNaVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 132 VPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPlslfdVDSKPLKTLED 211
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ-----VAVKGKKNLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 212 ALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS--IRNSQTRKICHSLYFPQSLDFSQIL---P 286
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLELDMEPYTekgL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 287 MKRESCDAEEQSGG-QYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDI-----QCTYGNPNYHWQE 360
Cdd:cd02659 236 AKKEGDSEKKDSESyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfGGEETQKTYDSGP 315
|
330
....*....|....*....
gi 7159737 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 |
1.58e-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: 164.58 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNvdftrilkritvprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvplf 135
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 136 vQHDAAQLYLKLWNLIKDQITDVHLVER--------LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLfDVDSKPLK 207
Cdd:cd02257 22 -QQDAHEFLLFLLDKLHEELKKSSKRTSdssslkslIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPL-PVKGLPQV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQvLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSLYFPQSLDFSQILP 286
Cdd:cd02257 100 SLEDCLEKFFKEEILEGDNCYKCEKKKKQEATKR-LKIKKLPPVLIIHLKRFSFnEDGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 287 MKRESCDAEEQSGgQYELFAVIAHVG-MADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQCTYGNpnyhwQETAYLL 365
Cdd:cd02257 179 EGEKDSDSDNGSY-KYELVAVVVHSGtSADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGSL-----SSSAYIL 252
|
...
gi 7159737 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 |
7.74e-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: 151.80 E-value: 7.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPR--GADEQRRSVPF-------QMLLLLEKMQDSRQKAVRPLELAYC 126
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEdaELKNMPPDKPHepqtiidQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 127 LQKCNVplfVQHDAAQLYLKLWNLIKD---QITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvds 203
Cdd:cd02668 81 LGLDTG---QQQDAQEFSKLFLSLLEAklsKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 204 KPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTRKICHSlyfpqSLDFS 282
Cdd:cd02668 153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFdRKTGAKKKLNA-----SISFP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 283 QILPMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWSCFNDSNIclVSWEDIQCTYGN-------- 353
Cdd:cd02668 228 EILDMGEYLAESDEGS-YVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDV--EEMPGKPLKLGNsedpakpr 304
|
330
....*....|....*....
gi 7159737 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 |
3.51e-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: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 137 QHDAAQLYLKLWNLIKDQITDVhlverLQALYtirvKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLK-TLEDALHC 215
Cdd:cd02674 22 QQDAQEFLLFLLDGLHSIIVDL-----FQGQL----KSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvTLEDCLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 216 FFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDfsqilpMKRESCDA 294
Cdd:cd02674 93 FTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPlNDLD------LTPYVDTR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7159737 295 EEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNIclvswediqcTYGNPNYHWQETAYLLVY 367
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRV----------TKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
7.16e-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: 108.19 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKC----- 130
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAfpqfa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 131 ---NVPLFVQHDAAQLYLKLWNLIKdQITDVHLVER--LQALYTIRVKDSLICVDC-AMESSRNSSMLTLPLSLFDvdSK 204
Cdd:cd02657 81 ekqNQGGYAQQDAEECWSQLLSVLS-QKLPGAGSKGsfIDQLFGIELETKMKCTESpDEEEVSTESEYKLQCHISI--TT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 205 PLKTLEDALHcffqpRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSI-RNSQTR-KICHSLYFPQSLDFS 282
Cdd:cd02657 158 EVNYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWkRDIQKKaKILRKVKFPFELDLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 283 QILPMKrescdaeeqsgGQYELFAVIAHVGM-ADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQCTYGNPNYHwqeT 361
Cdd:cd02657 233 ELCTPS-----------GYYELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGGDWH---I 298
|
....*.
gi 7159737 362 AYLLVY 367
Cdd:cd02657 299 AYILLY 304
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-368 |
2.15e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 106.98 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVmnvdFTRILKRITVPRGADEQRRSVPFQMLLLLEKM----QDSRQKAVRPLELAYCLqKCN 131
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLT----HTPPLANYLLSREHSKDCCNEGFCMMCALEAHveraLASSGPGSAPRIFSSNL-KQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 132 VPLFV---QHDAAQL--YL-------KLWNLIKDQITDVHLVER--LQALYTIRVKDSLICVDCAMESSRNSSMLTLPLS 197
Cdd:cd02661 78 SKHFRigrQEDAHEFlrYLldamqkaCLDRFKKLKAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 198 LFDVDSkplktLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSirNSQTRKICHSLYFPQ 277
Cdd:cd02661 158 IKGADS-----LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINKQISFPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 278 SLDFSQILPMKRESCDaeeqsggQYELFAVIAHVGM-ADSGHYCVYIRNAvDGKWSCFNDSNICLVSWEDIqctygnpny 356
Cdd:cd02661 231 TLDLSPYMSQPNDGPL-------KYKLYAVLVHSGFsPHSGHYYCYVKSS-NGKWYNMDDSKVSPVSIETV--------- 293
|
330
....*....|..
gi 7159737 357 hWQETAYLLVYM 368
Cdd:cd02661 294 -LSQKAYILFYI 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
56-367 |
2.74e-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: 107.19 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQrrSVPFQMLLLLEKMQDSRQKAVRPLElaYCLQKCNVPLF 135
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQ--SVMKKLQLLQAHLMHTQRRAEAPPD--YFLEASRPPWF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 136 V---QHDAAQlYLKlwnlikdqitdvHLVERLQAL----YTIRVKDSLICVDCAMESSRNSSMLTLPLSlfdvdskpLKT 208
Cdd:cd02664 77 TpgsQQDCSE-YLR------------YLLDRLHTLiekmFGGKLSTTIRCLNCNSTSARTERFRDLDLS--------FPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 209 LEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIrNSQT---RKICHSLYFPQSLDfsqiL 285
Cdd:cd02664 136 VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY-DQKThvrEKIMDNVSINEVLS----L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 286 PMKRES----------------CDAEEQSGGQYELFAVIAHVGMA-DSGHYCVYIRNAVD-------------------- 328
Cdd:cd02664 211 PVRVESkssesplekkeeesgdDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpepkdaeendes 290
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 7159737 329 GKWSCFNDSNICLVSWEDIQ--CTYGNPNyhwqeTAYLLVY 367
Cdd:cd02664 291 KNWYLFNDSRVTFSSFESVQnvTSRFPKD-----TPYILFY 326
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
53-371 |
7.10e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 103.41 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 53 GLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRItvPRGADEQRRSVPFQMLLLLEKMQDSRQkAVRPLELAYCLQKCNV 132
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI--PTDHPRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 133 PLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLfdvdsKPLKTLEDA 212
Cdd:COG5077 269 DSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV-----KGMKNLQES 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 213 LHCFFQPRELSSKSKCFCENCGKKTRGKQVLkLTHLPQTLTIHLMRFSI--RNSQTRKICHSLYFPQSLDfsqILPMKRE 290
Cdd:COG5077 344 FRRYIQVETLDGDNRYNAEKHGLQDAKKGVI-FESLPPVLHLQLKRFEYdfERDMMVKINDRYEFPLEID---LLPFLDR 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 291 SCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVS-WEDIQCTYG----------NPN-YHW 358
Cdd:COG5077 420 DADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATeKEVLEENFGgdhpykdkirDHSgIKR 499
|
330
....*....|...
gi 7159737 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 |
3.97e-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: 98.43 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 54 LVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVpfqmLLLLEKMQDSRQKAVRPLELAYCLQKCNvP 133
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSS----FLLNPEKYNDELANQAPRRLLNALREVN-P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 134 LF---VQHDAAQLYLKLWNLIKDqitdvhLVERL-QALYTIRVKdsliCVDCAMESSRNSSML---------TLPLSLFD 200
Cdd:cd02671 99 MYegyLQHDAQEVLQCILGNIQE------LVEKDfQGQLVLRTR----CLECETFTERREDFQdisvpvqesELSKSEES 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 201 VDSKP-----LKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQT------RKI 269
Cdd:cd02671 169 SEISPdpkteMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 270 chSLYFPQSLDFSqilpmkrescdAEEQSGGQ----YELFAVIAHVGMA-DSGHYCVYIRnavdgkWSCFNDSNICLVSW 344
Cdd:cd02671 249 --NTPLLTPLKLS-----------LEEWSTKPkndvYRLFAVVMHSGATiSSGHYTAYVR------WLLFDDSEVKVTEE 309
|
330 340
....*....|....*....|...
gi 7159737 345 EDIQcTYGNPNYHWQETAYLLVY 367
Cdd:cd02671 310 KDFL-EALSPNTSSTSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
208-367 |
1.35e-21 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.49 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 208 TLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFP-QSLDFSQILP 286
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPiDDLDLSGVEY 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 287 MKrescdaeEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWSCFNDSNICLVSWEDIQctygnpnyhwQETAYLLV 366
Cdd:COG5560 756 MV-------DDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSV----------TSSAYVLF 818
|
.
gi 7159737 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 |
5.37e-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: 89.74 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVDFTRIL--KRITVPRGADEQRRSVPFQMLLLLEKMQ---DSRQKAvrPLELAYCLQKC 130
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNSCLSCAMDEIFQEFYysgDRSPYG--PINLLYLSWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 131 NVPL--FVQHDAAQLYLKLWNLIKDQITDVH-----------LVERLqalYTIRVKDSLICVDCAMESSRNSSMLTLPLS 197
Cdd:cd02660 80 SRNLagYSQQDAHEFFQFLLDQLHTHYGGDKneandeshcncIIHQT---FSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 198 LfDVDSKP-----------LKTLEDALHCFFQPRELSSKSKCfCENCGKKTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQ 265
Cdd:cd02660 157 I-PNKSTPswalgesgvsgTPTLSDCLDRFTRPEKLGDFAYK-CSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLNKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 266 TRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQ--YELFAVIAHVGMADSGHYCVYIRNAvDGKWSCFNDSNICLVS 343
Cdd:cd02660 235 SRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDytYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVS 313
|
330 340
....*....|....*....|....
gi 7159737 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 |
1.10e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 88.14 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVDFTrILKritvprgadeqrrsvpfqmlLLLEKMQDSRQK--AVRPLELAYCLQKCNvP 133
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT-CLK--------------------DLFESISEQKKRtgVISPKKFITRLKREN-E 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 134 LF---VQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLI-----------------CVDCAMESSRNSSMLT 193
Cdd:cd02663 59 LFdnyMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQptwvheifqgiltnetrCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 194 LPlslfdVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTR--KICH 271
Cdd:cd02663 139 LS-----IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyiKLFY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 272 SLYFPQSLDfsqilpMKRESCDAEEQSgGQYELFAVIAHVGM-ADSGHYCVYIRnaVDGKWSCFNDSNICLVSWEDIQCT 350
Cdd:cd02663 214 RVVFPLELR------LFNTTDDAENPD-RLYELVAVVVHIGGgPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEF 284
|
330
....*....|....*..
gi 7159737 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 |
5.07e-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: 85.90 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVmnvdftrilkritvprgADEQRRSvpfqmlLLLEkmqdsrqkavRPLELAYCLQKCNVPL- 134
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-----------------QTPALRE------LLSE----------TPKELFSQVCRKAPQFk 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 135 -FVQHDAAQLylkLWNLIKDQITDVHLVERLQALYTIrvkdslICVDCAMESSRNSSMLTLPLSLFDvDSKPLKTLEDAL 213
Cdd:cd02667 48 gYQQQDSHEL---LRYLLDGLRTFIDSIFGGELTSTI------MCESCGTVSLVYEPFLDLSLPRSD-EIKSECSIESCL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 214 HCFFQPRELSSKSKCFCENCgkkTRGKQVLKLTHLPQTLTIHLMRFS-IRNSQTRKICHSLYFPQSLDFSQILPMKRESC 292
Cdd:cd02667 118 KQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQqPRSANLRKVSRHVSFPEILDLAPFCDPKCNSS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 293 DAEEQSggQYELFAVIAHVGMADSGHYCVYI--RNAVD-------------------GKWSCFNDSNICLVSWEDIQcty 351
Cdd:cd02667 195 EDKSSV--LYRLYGVVEHSGTMRSGHYVAYVkvRPPQQrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVL--- 269
|
330
....*....|....*.
gi 7159737 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 |
9.98e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 85.84 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQV-----------FVMNVDFTRILKRIT---------VPRGADEQRRSVPfqmlLLLEKMQDSRQ 115
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVlfsipsfqwryDDLENKFPSDVVDPAndlncqlikLADGLLSGRYSKP----ASLKSENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 116 KAVRPLELAYCLQKcNVPLFV---QHDAAQLYLKLWNLI--------KDQITDV---HLVERLQALYTIRVKdslicvdc 181
Cdd:cd02658 77 VGIKPSMFKALIGK-GHPEFStmrQQDALEFLLHLIDKLdresfknlGLNPNDLfkfMIEDRLECLSCKKVK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 182 amESSRNSSMLTLPLSLFDVDSKPLK-------TLEDALHCFFQPRELSSkskcFCENCGKKTRGKQVLKLTHLPQTLTI 254
Cdd:cd02658 148 --YTSELSEILSLPVPKDEATEKEEGelvyepvPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 255 HLMRFSIRNSQTrkichslyfPQSLDFSQILPmkrescdaEEQSGGQYELFAVIAHVGM-ADSGHYCVYIRNAVD--GKW 331
Cdd:cd02658 222 NMKRFQLLENWV---------PKKLDVPIDVP--------EELGPGKYELIAFISHKGTsVHSGHYVAHIKKEIDgeGKW 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 7159737 332 SCFNDSNICLVSwediqctygNPNYHwQETAYLLVY 367
Cdd:cd02658 285 VLFNDEKVVASQ---------DPPEM-KKLGYIYFY 310
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
56-367 |
2.00e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 78.69 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVD-----FTRILKRITV-------PRGADEQRrsvpfQMLLLLEKMQDSRQKAVRPLEl 123
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldelLDDLSKELKVlknvirkPEPDLNQE-----EALKLFTALWSSKEHKVGWIP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 124 ayclqkcnvPLFVQHDAAQLYLKLWNLIKDQitDVHLVERLQALYTIRVKDSLIcvdcameSSRNSSMLTLPLSLFDVDs 203
Cdd:COG5533 75 ---------PMGSQEDAHELLGKLLDELKLD--LVNSFTIRIFKTTKDKKKTST-------GDWFDIIIELPDQTWVNN- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 204 kpLKTLEDALHCF--FQPRELSSKSKcfcENCGKKTRGKQVLKLT--HLPQTLTIHLMRFSIRNSQtRKICHSL--YFPQ 277
Cdd:COG5533 136 --LKTLQEFIDNMeeLVDDETGVKAK---ENEELEVQAKQEYEVSfvKLPKILTIQLKRFANLGGN-QKIDTEVdeKFEL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 278 SLDFSQILPMKREscdaeeqsgGQYELFAVIAHVGMADSGHYCVYIRnaVDGKWSCFNDSNICLVSWEDIQctygNPNyh 357
Cdd:COG5533 210 PVKHDQILNIVKE---------TYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAI----NEK-- 272
|
330
....*....|
gi 7159737 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 |
6.74e-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: 74.84 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 55 VGLHNIGQTCCLNSLIQVF---------VMNVD---FTRILKRITVPR------GADEQRRSVPF--QMLLLLEKMQDSR 114
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFftikplrdlVLNFDeskAELASDYPTERRiggrevSRSELQRSNQFvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 115 QKAVRPL-ELAY----------CLQKCnvpLFvQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLicVDCAM 183
Cdd:cd02666 82 TRSVTPSkELAYlalrqqdvteCIDNV---LF-QLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQL--VPESM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 184 E--SSRNSSM---LTLPLSLFDV--DSKPL---KTLEDALHCFFQPRELSS---KSKCFCENCGKKTRGKQVLKLTHLPQ 250
Cdd:cd02666 156 GnqPSVRTKTerfLSLLVDVGKKgrEIVVLlepKDLYDALDRYFDYDSLTKlpqRSQVQAQLAQPLQRELISMDRYELPS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 251 TL-TIHLMRFSIRNSQTRKICHSLYFPQSLDFsqilpmKRESCDAEEQSGGqYELFAVIAHVGMADSGHYCVYIRNAVDG 329
Cdd:cd02666 236 SIdDIDELIREAIQSESSLVRQAQNELAELKH------EIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYWVYIKDFEEN 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 7159737 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 |
5.62e-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: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 56 GLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVprgadeqrrsvpfqmllllekmqdsrqkavrplelayclqkcnvplf 135
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 136 vQHDAAQLYLklwnlikdqitdvHLVERLQALYT----IRVKDSLICVDCAMESS-RNSSMLTLPLSLFDVDSKPLKTLE 210
Cdd:cd02662 34 -QQDAHELFQ-------------VLLETLEQLLKfpfdGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTTLE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 211 DALHCFFQPRELSSKSkcfCENCGkktrgkqvLKLTHLPQTLTIHLMR--FSIRNSQTRKICHsLYFPQSLdfsqilpmk 288
Cdd:cd02662 100 HCLDDFLSTEIIDDYK---CDRCQ--------TVIVRLPQILCIHLSRsvFDGRGTSTKNSCK-VSFPERL--------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 289 rescdaeeqSGGQYELFAVIAHVGMADSGHYCVY--------------------IRNAVDGKWSCFNDSNICLVSWEDIq 348
Cdd:cd02662 159 ---------PKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEV- 228
|
330
....*....|....*....
gi 7159737 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 |
1.23e-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: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 246 THLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLdfsQILPmkrescdaeeqsggqYELFAVIAHVGMADSGHYCVYIRN 325
Cdd:cd02665 126 TELPPVLTFELSRFEFNQGRPEKIHDKLEFPQII---QQVP---------------YELHAVLVHEGQANAGHYWAYIYK 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 7159737 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 |
5.21e-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: 50.22 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 137 QHDAAQLYLKLWNLIKD--------QITDVHLVERLQALYTIR--VKDSLICVDCAMESSRNSSMLTLPLSLFDVDskpL 206
Cdd:cd02673 33 QQDAHEFLLTLLEAIDDimqvnrtnVPPSNIEIKRLNPLEAFKytIESSYVCIGCSFEENVSDVGNFLDVSMIDNK---L 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 207 KTLEDALHCFFQPRELSSK-SKCFCENCGKKTRgkqvlkLTHLPQTLTIHLMRFSIRNSQtrkichSLYFPQSldfsqil 285
Cdd:cd02673 110 DIDELLISNFKTWSPIEKDcSSCKCESAISSER------IMTFPECLSINLKRYKLRIAT------SDYLKKN------- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7159737 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 |
1.83e-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: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 191 MLTL---PLSLF-DVDSK---PLKTLEDALHCFFQPRELSSKskcfcencGKKTRgkqvLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02669 280 LLTLdlpPPPLFkDGNEEniiPQVPLKQLLKKYDGKTETELK--------DSLKR----YLISRLPKYLIFHIKRFSKNN 347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7159737 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 |
5.82e-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: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 184 ESSRNSSMLTLPLSLfDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRN 263
Cdd:cd02672 92 GTSRNSVSLLYTLSL-PLGSTKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHLPDILLLVLVINLSVT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7159737 264 SQTRKICHSLYfPQSLDFSQILPMKRESCDAEEQSGGQ-----YELFAVIAHVGMADSG-HYCV---YIRNAVD-GKWSC 333
Cdd:cd02672 171 NGEFDDINVVL-PSGKVMQNKVSPKAIDHDKLVKNRGQesiykYELVGYVCEINDSSRGqHNVVfviKVNEESThGRWYL 249
|
...
gi 7159737 334 FND 336
Cdd:cd02672 250 FND 252
|
|
| |
