|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
121-421 |
6.31e-179 |
|
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: 521.84 E-value: 6.31e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 121 GAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHMVQAFANSGNAIKPVSFIRDLKKIARH 200
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 201 FRFGNQEDAHEFLRYTIDAMQKACLNGYAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIALEIRQ 277
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 278 AANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157820619 358 SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLSQQAYVLFYL 421
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
122-420 |
7.57e-79 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 259.68 E-value: 7.57e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 122 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSC--HQGSFCMLCVMQNHMVQAFANS-GNAIKPVSFIRDLKKIA 198
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 199 RHFRFGNQEDAHEFLRYTIDAMQKAClngyaKLDRQTQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIALEIRQA 278
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 279 ANIVR------ALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 350
Cdd:pfam00443 156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157820619 351 IRPYMSQSS----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLSQQAYVLFY 420
Cdd:pfam00443 236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
8.86e-74 |
|
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: 246.52 E-value: 8.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCH--QGSFCMLCVMQNhMVQAFANSGNAiKPVSFIRDLK---KI 197
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 198 ARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIALEIRQ 277
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 278 AANIVRA---------------LELFVKSDVLsGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFANFSGG---KI 339
Cdd:cd02660 160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 340 TKDVGYPEFLNIRPYMSQSSGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVV 410
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
|
330
....*....|
gi 157820619 411 LSQQAYVLFY 420
Cdd:cd02660 318 LKSQAYLLFY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
123-420 |
1.49e-67 |
|
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: 226.98 E-value: 1.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLtytpplanyllskeharschqgsfcmlcvmqnhmvqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDP--YLDIALEIRQAA- 279
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 280 -NIVRALELFVKSDVLSGENAYMCaKCKKKVPASKRFSIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 355
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157820619 356 SQ------SSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----SQQAYVLFY 420
Cdd:cd02257 178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.67e-55 |
|
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: 193.76 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANyLLSKeharschqgsfcmlcvmqnhmvqafansgnaiKPVSFIRDLKKIARHFR 202
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGNQEDAHEFLRYTIDAMQkaclngyakldrqtqatTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIAL----EIRQA 278
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 279 ANIVRALELFVKSDVLSGENAYMCAKCKKkvpASKRFSIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 353
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 354 YMSQS-----SGDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSLVHSSN 406
Cdd:cd02667 186 FCDPKcnsseDKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 157820619 407 VKVVLSQQAYVLFY 420
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
2.40e-52 |
|
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: 183.26 E-value: 2.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLtytpplanyllskeharschqgsfcmlcvmqnhmvqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGNQEDAHEFLRYTIDamqkaclngyaKLDRqtqattLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIALEIRQAANIV 282
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 283 RA------LELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 352
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 353 PY-MSQSSGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLSQQAYVLFY 420
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-423 |
1.19e-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: 182.07 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLS---KEHARSCHQGsfcmLCVMQnhmVQaFANSGNAIKPVSFIRDLKKIar 199
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQ---RL-FLFLQLSESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 200 hFRFG-------NQEDAHEFLRYTIDAMQKaclngyaKLdRQTQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIA 272
Cdd:cd02659 74 -RSFGwdslntfEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 273 LEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPE 347
Cdd:cd02659 145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 348 FLNIRPYMSQSSG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLSQQ- 414
Cdd:cd02659 224 ELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECf 302
|
330 340 350
....*....|....*....|....*....|
gi 157820619 415 ---------------------AYVLFYLRI 423
Cdd:cd02659 303 ggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
5.46e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 158.63 E-value: 5.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYtpplaNYLLSkeharsCHQGSFCmlCVMQNHmvqafaNSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------CLKDLFE--SISEQK------KRTGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGNQEDAHEFLRYTIDAMQKaCLNGYAKLDRQ----------TQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIA 272
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIAE-ILDAERKAEKAnrklnnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 273 LEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEF 348
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 349 LNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVKVVL-----SQQAYVLFY 420
Cdd:cd02663 221 LRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVEEFFgdspnQATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
2.17e-37 |
|
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: 143.33 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSkeharschqgsfcmlCVMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGN-------------------QEDAHEFLRYTIDAMQkaclngyAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCRSV 261
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 262 SDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFA----NFSGG 337
Cdd:cd02668 139 SSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKK 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157820619 338 KITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLV 402
Cdd:cd02668 219 KLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
8.23e-37 |
|
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: 141.86 E-value: 8.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGSfcMLCVMQnhMVQAFA--NSGNAIKPVS-FIRDLKkiAR 199
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS--VMKKLQ--LLQAHLmhTQRRAEAPPDyFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 200 HFRFGNQEDAHEFLRYTIDamqkaclngyaKLDrqtqatTLVHQIFGGYLRSRVKCSVCRSVSDTYD--PYLDIALeirq 277
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 278 aANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLN--I 351
Cdd:cd02664 134 -PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 352 RPYMSQS----------SGD-------PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQ 393
Cdd:cd02664 213 RVESKSSesplekkeeeSGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKN 292
|
330 340 350
....*....|....*....|....*....|....
gi 157820619 394 WYQMNDSLVHSS------NVKVVLSQQ-AYVLFY 420
Cdd:cd02664 293 WYLFNDSRVTFSsfesvqNVTSRFPKDtPYILFY 326
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.94e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 113.96 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSC----------------HQGSFCMLCVMQNHMVQAFANSGNAIK 186
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpandlncqliklADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 187 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngyaKLDRQTQATTLvhqiFGGYLRSRVKCSVCRSVSDTYD 266
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 267 ---------PYLDIA-----LEIRQAANIVRALELFVKSDVLsgenAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFA 332
Cdd:cd02658 152 lseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 333 NFSGG---KITKDVGYPEFLnirpymsqssgDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSlvhssn 406
Cdd:cd02658 228 LLENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDE------ 290
|
330 340
....*....|....*....|.
gi 157820619 407 vKVVLSQQ-------AYVLFY 420
Cdd:cd02658 291 -KVVASQDppemkklGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-420 |
6.98e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 109.98 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 122 AGLHNLGNTCFLNSTIQCLTYTPPLAN---YLLSKEHARSCHQGSFcmlcvMQNHmvQAFANSGNAIKPVSFIRDLKKIA 198
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 199 RHFRFGNQEDAHEFLRYTIDAMQKaclngyakldrqtqattLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIALEIRQA 278
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 279 -------------------ANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFANFS---- 335
Cdd:cd02671 161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 336 --GG--KITKDVGYPEFLNIRPYMSQSSGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVH-------- 403
Cdd:cd02671 241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKvteekdfl 313
|
330 340
....*....|....*....|
gi 157820619 404 ---SSNVKVVLSqqAYVLFY 420
Cdd:cd02671 314 ealSPNTSSTST--PYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-423 |
1.00e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 108.35 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLT-YTPPLANYLLSKEHA----RSCHQGSFCMLcvMQNHMVQAFANsgnaikpvSFIRDLKKI 197
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKElkvlKNVIRKPEPDL--NQEEALKLFTA--------LWSSKEHKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 198 ARHFRFGNQEDAHEFLRYTIDAMqkaclngyaKLDRQTQATTLVHQIFGGYLRSRVKcsvcrSVSDTYdpyldIALEIRQ 277
Cdd:COG5533 71 GWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTSTG-----DWFDII-----IELPDQT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 278 AANIVRALELFV---------KSDVLSGENAYMCAKCKKKVPASKRfsihRTSNVLTLSLKRFANFSGG-KITKDVGYPE 347
Cdd:COG5533 132 WVNNLKTLQEFIdnmeelvddETGVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 348 FLNIRPymSQSSGD--PVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVL---SQQAYVLFYLR 422
Cdd:COG5533 208 ELPVKH--DQILNIvkETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAInekAKNAYLYFYER 283
|
.
gi 157820619 423 I 423
Cdd:COG5533 284 I 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
123-451 |
1.29e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 111.12 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLAN--YLLSKEHARschqGSFCMLCVMQnhmvQAFANSGNAIKPV-------SFIRD 193
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVdtteltrSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 194 lkkIARHFrfgNQEDAHEFLRYTIDAMQKAClngyakldRQTQATTLVHQIFGGYLRSRVKCSVCRSVSDTYDPYLDIAL 273
Cdd:COG5077 267 ---SDDSF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 274 EIRQAANIVRALELFVKSDVLSGENAYMCAKcKKKVPASKRFSIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFL 349
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 350 NIRPYMS----QSSGDPVMYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLSQ----------- 413
Cdd:COG5077 412 DLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdk 490
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157820619 414 -----------QAYVLFYLRipgskKSPEGPVSRvgatlPSRPKVIPEH 451
Cdd:COG5077 491 irdhsgikrfmSAYMLVYLR-----KSMLDDLLN-----PVAAVDIPPH 529
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.49e-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 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: 93.55 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHMVQAFANSGNAIKPVSFIRDLKKIARHF- 201
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 202 ---RFGN--QEDAHEFLRYTIDAMQkaclngyAKLDRQTQATTLVHQIFGGYLRSRVKC---SVCRSVSDTYDPYLDIAL 273
Cdd:cd02657 81 ekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 274 EIRQAANIVRA-LELFVK------SDVLSGENAYmcakckkkvpaSKRFSIHRTSNVLTLSLKRF-----ANfSGGKITK 341
Cdd:cd02657 154 SITTEVNYLQDgLKKGLEeeiekhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 342 DVGYPEFLNIRPYMSQSSgdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLVHSSNVKVVL-------SQ 413
Cdd:cd02657 222 KVKFPFELDLYELCTPSG----YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVSEVTEEDILklsgggdWH 297
|
....*..
gi 157820619 414 QAYVLFY 420
Cdd:cd02657 298 IAYILLY 304
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
3.99e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 87.81 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTytpplanyllskeharSChqgsfcmlcvmqnhmvqafansgnaikpVSFIRDLKkiarhfR 202
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALA----------------SL----------------------------PSLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGNQEDAHEFLRYTIDAMQKACLNgyakldrqtqattlvhqIFGGYLRSRVKCSVCRSVS-DTYDPYLDIALEIRQA--- 278
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 279 --ANIVRALELFVKSDVLSGenaYMCAKCKKK-VPASKRFSIHrtsnvltlsLKRFAnFSG-GKITKD---VGYPEFLNi 351
Cdd:cd02662 94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTViVRLPQILCIH---------LSRSV-FDGrGTSTKNsckVSFPERLP- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 352 rpymsqssgdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKV 409
Cdd:cd02662 160 ----------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEV 228
|
330
....*....|.
gi 157820619 410 VLSQQAYVLFY 420
Cdd:cd02662 229 LEQKSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
122-402 |
3.61e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 86.56 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 122 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSkeHARSCHQGSFCMLC----VMqnHM--------VQAfANsgnaikpvs 189
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCelgfLF--DMlekakgknCQA-SN--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 190 FIRDLKKIARHFRFGNQEDAHE-------------FLRYTIDAMQKaclNGYAKLDRQTQATTLVHQIFGGYLRSRVKCS 256
Cdd:pfam13423 67 FLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSS---EENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 257 VCRSVSDTYDPYLDIALEI-RQAANIVRALELFVKSDVL----SGENAY--MCAKCKKKVPASKRFSIHRTSNVLTLSLK 329
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 330 RFaNFSGGKITKDVGY-PEFLNIRPYM-SQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMND 399
Cdd:pfam13423 224 LT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFND 302
|
...
gi 157820619 400 SLV 402
Cdd:pfam13423 303 FLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
285-422 |
4.07e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 86.48 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 285 LELFVKSDVLSGENAYMCAKCKKKVPASKRFSIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQSSGD 361
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820619 362 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLSQQAYVLFYLR 422
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-275 |
4.35e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 86.48 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHA----RSCHQGsfcmlcvMQNHMVQAFAN------SGN--AIKPVSF 190
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEesinEENPLG-------MHGSVASAYADlikqlyDGNlhAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 191 IRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNG------------YAKLDRQTQAT-------------TLVHQIF 245
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRiikkpytskpdlSPGDDVVVKKKakecwwehlkrndSIITDLF 418
|
170 180 190
....*....|....*....|....*....|
gi 157820619 246 GGYLRSRVKCSVCRSVSDTYDPYLDIALEI 275
Cdd:COG5560 419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-413 |
9.63e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 71.58 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 123 GLHNLGNTCFLNSTIQCLTYTPPLANYLLSKE----HARSCHQ--GSFCMLcvmqnhmVQAFANSgNAIK----PVSFIR 192
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnyenIKDRKSElvKRLSEL-------IRKIWNP-RNFKghvsPHELLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 193 DLKKI-ARHFRFGNQEDAHEFLRYTIDAMqKACLNGYAKldrqtQATTLVHQIFGGYLR-----------------SRVK 254
Cdd:cd02669 193 AVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegskdKFFK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 255 CSVCRSVSDTydPYLDIALEIRQAA--------NIVRALELFvksDVLSGENAYMCAKCKKKVpasKRFSIHRTSNVLTL 326
Cdd:cd02669 267 DSRVKKTSVS--PFLLLTLDLPPPPlfkdgneeNIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKYLIF 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 327 SLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQ---SSGDPVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQMND 399
Cdd:cd02669 339 HIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
|
330
....*....|....
gi 157820619 400 slvhsSNVKVVLSQ 413
Cdd:cd02669 419 -----LNVKEVLPQ 427
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
124-420 |
4.86e-10 |
|
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: 61.01 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 124 LHNLGNTCFLNSTIQCLTytpplanyllskeharschqgsfcmlcvmqnhmvqafansgnaikpvsfirDLKKIARHFRF 203
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS---------------------------------------------------SIGKINTEFDN 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 204 GNQEDAHEFLRYTI----DAMQKACLNGYAKLDRQTQATTLvhQIFGGYLRSRVKCSVCRSVSDTYDPYLDIALEIRQaa 279
Cdd:cd02673 31 DDQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 280 NIVRALELFVKSDVLSGENAYMCAKCKKKVpASKRFSIHRTSNVLTLSLKRF-ANFSGGKITKDVgypeflniRPYMSQS 358
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKKN--------EEIMKKY 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157820619 359 SGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLSQQAYVLFY 420
Cdd:cd02673 178 CGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
203-421 |
2.05e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 46.78 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 203 FGNQEDAHEFLRYTIDAMQKA-------------CLNGYAKLDRQTQATTLVHqiFGGYLRsrvKCSVCRSVSDTYDPY- 268
Cdd:cd02665 19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 269 -LDIALEirqAANIVRALELF--VKSDVLSGENAYMcakckkKVPAskrfsihrtsnVLTLSLKRFA--NFSGGKITKDV 343
Cdd:cd02665 94 nLHECLE---AAMFEGEVELLpsDHSVKSGQERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 344 GYPEFLNIRPYMsqssgdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMNDSLVHSSNVKVVLSQ--------Q 414
Cdd:cd02665 154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpS 221
|
....*..
gi 157820619 415 AYVLFYL 421
Cdd:cd02665 222 AYCLMYI 228
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-402 |
5.58e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 122 AGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSchqgsfcmlcVMQNHMVQAFANSGNAIKPVS------FIRDLK 195
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSElqrsnqFVYELR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 196 KIARHFRFGN----------------QEDAHEFLRYTIDAMQKA-----CLNGYAKLDRQTQATTLVHQIF-GGYLRSRV 253
Cdd:cd02666 72 SLFNDLIHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVAlepisNAFAGPDTEDDKEQSDLIKRLFsGKTKQQLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 254 KCS--VCRSVSDTYDPYLDIALEIRQAANIVR----------ALELFVKSDVL------SGENAYMCAKCKKKVPASKRF 315
Cdd:cd02666 152 PESmgNQPSVRTKTERFLSLLVDVGKKGREIVvllepkdlydALDRYFDYDSLtklpqrSQVQAQLAQPLQRELISMDRY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 316 SIHRTSNVlTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQSSG-DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQ 393
Cdd:cd02666 232 ELPSSIDD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDlKSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENV 309
|
....*....
gi 157820619 394 WYQMNDSLV 402
Cdd:cd02666 310 WRKYNDETV 318
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
493-807 |
1.31e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.60 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 493 SISGLklqnGCAPaKSPAGSPSPRLAPTPTHmptildepgeKVKKSAPPQSRTTSPTA-SQGF--PGTGESRSQRPGSWA 569
Cdd:pfam05109 392 TVSGL----GTAP-KTLIITRTATNATTTTH----------KVIFSKAPESTTTSPTLnTTGFaaPNTTTGLPSSTHVPT 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 570 SRDSIFSTSPKLAKAITNGHRLKGEGNGvdlekGDSSSSSPEHSASSDAAKAPQTSEGRAAHVCDSQGTNCPATGHSKVL 649
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGTTSG-----ASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPT 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820619 650 SNGVDAKMGKlKSPALSSTTTEPTSlMSPPPAkklalsakKASTLRRATGNDIGSPSPSAFCDLTSPmKATHPVVASPGP 729
Cdd:pfam05109 532 PNATSPTLGK-TSPTSAVTTPTPNA-TSPTPA--------VTTPTPNATIPTLGKTSPTSAVTTPTP-NATSPTVGETSP 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157820619 730 VSKTRAAAAPAPQPSphphsaslssssakPLGTSEPQSCCSSAWTPLPQVNGHFTSHLHQLPEANEALHSPSRKRKKT 807
Cdd:pfam05109 601 QANTTNHTLGGTSST--------------PVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNST 664
|
|
| |
