|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
15-315 |
2.67e-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: 522.99 E-value: 2.67e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 15 GAGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARH 94
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 95 FRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVALEIRQ 171
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 172 AANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 251
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967234024 252 NNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 315
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
16-314 |
1.84e-77 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 256.22 E-value: 1.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 16 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC--HQGSFCMLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIA 92
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 93 RHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVALEIRQA 172
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 173 ANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 244
Cdd:pfam00443 156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967234024 245 IRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 314
Cdd:pfam00443 236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
9.23e-72 |
|
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: 241.12 E-value: 9.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCH--QGSFCMLCVMQNhIVQAFANSGNAiKPVSFIRDLK---KI 91
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 92 ARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVALEIRQ 171
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 172 AANIVRA---------------LELFVKADVLsGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KI 233
Cdd:cd02660 160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 234 TKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVV 304
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
|
330
....*....|
gi 967234024 305 LNQQAYVLFY 314
Cdd:cd02660 318 LKSQAYLLFY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
17-314 |
9.04e-66 |
|
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: 221.97 E-value: 9.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 96
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDP--YLDVALEIRQAA- 173
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 174 -NIVRALELFVKADVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 249
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967234024 250 SQNNGD------PVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 314
Cdd:cd02257 178 SEGEKDsdsdngSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
5.52e-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: 192.60 E-value: 5.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANyLLSKeharschqgsfcmlcvmqnhivqafansgnaiKPVSFIRDLKKIARHFR 96
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGNQEDAHEFLRYTIDAMQkaclngcakldrqtqatTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVAL----EIRQA 172
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 173 ANIVRALELFVKADVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 247
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 248 YMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSLVHSSN 300
Cdd:cd02667 186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 967234024 301 VKVVLNQQAYVLFY 314
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
4.29e-51 |
|
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: 179.79 E-value: 4.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 96
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGNQEDAHEFLRYTIDamqkaclngcaKLDRqtqattLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVALEIRQAANIV 176
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 177 RA------LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 246
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 247 PY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 314
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-317 |
1.02e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 176.29 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLS---KEHARSCHQGsfcmLCVMQnhiVQaFANSGNAIKPVSFIRDLKKIar 93
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQ---RL-FLFLQLSESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 94 hFRFG-------NQEDAHEFLRYTIDAMQKaclngcaKLdRQTQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVA 166
Cdd:cd02659 74 -RSFGwdslntfEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 167 LEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPE 241
Cdd:cd02659 145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 242 FLNIRPYMSQNNG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ- 308
Cdd:cd02659 224 ELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECf 302
|
330 340 350
....*....|....*....|....*....|
gi 967234024 309 ---------------------AYVLFYLRI 317
Cdd:cd02659 303 ggeetqktydsgprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
4.61e-41 |
|
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: 153.23 E-value: 4.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYtpplaNYLLSkeharsCHQGSFCmlCVMQNHivqafaNSGNAIKPVSFIRDLKKIARHFR 96
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------CLKDLFE--SISEQK------KRTGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQ-----TQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVAL 167
Cdd:cd02663 62 NYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 168 EIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEFL 243
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLEL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967234024 244 NIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVKVVLNQ-----QAYVLFY 314
Cdd:cd02663 222 RLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVEEFFGDspnqaTAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-296 |
2.67e-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: 142.94 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSkeharschqgsfcmlCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFR 96
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGN-------------------QEDAHEFLRYTIDAMQkaclngcAKLDRQT--QATTLVHQIFGGYLRSRVKCSMCKSV 155
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 156 SDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGG 231
Cdd:cd02668 139 SSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKK 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967234024 232 KITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLV 296
Cdd:cd02668 219 KLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
7.28e-34 |
|
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: 133.00 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSfcMLCVMQNHIVQAFANSGNAIKPVS-FIRDLKkiARHF 95
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS--VMKKLQLLQAHLMHTQRRAEAPPDyFLEASR--PPWF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 96 RFGNQEDAHEFLRYTIDamqkaclngcaKLDrqtqatTLVHQIFGGYLRSRVKCSMCKSVSDTYD--PYLDVALeirqaA 173
Cdd:cd02664 77 TPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-----P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 174 NIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI---- 245
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvrv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 246 ----------RPYMSQNNGD-----PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQWY 289
Cdd:cd02664 215 eskssespleKKEEESGDDGelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 967234024 290 QMNDSLVHSSNVKVVLN-------QQAYVLFY 314
Cdd:cd02664 295 LFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
17-317 |
6.12e-27 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 111.82 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLT-YTPPLANYL--LSKEharschqgsfcmLCVMQNHIVQAFA--NSGNAIKPVSFIRDLK-- 89
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddLSKE------------LKVLKNVIRKPEPdlNQEEALKLFTALWSSKeh 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 90 KIARHFRFGNQEDAHEFLRYTIDAMqkaclngcaKLDRQTQATTLVHQIFGGYLRSRVkcsmcKSVSDTYdpyldVALEI 169
Cdd:COG5533 69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTST-----GDWFDII-----IELPD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 170 RQAANIVRALELFVKAD---------VLSGENAYMCAKCKKKVPASKRftihRTSNVLTLSLKRFANFSGG-KITKDVGY 239
Cdd:COG5533 130 QTWVNNLKTLQEFIDNMeelvddetgVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 240 PEFLNIRPYMSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVLN---QQAYVLFYLR 316
Cdd:COG5533 206 KFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
.
gi 967234024 317 I 317
Cdd:COG5533 284 I 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
2.44e-25 |
|
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: 107.79 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC----------------HQGSFCMLCVMQNHIVQAFANSGNAIK 80
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpandlncqliklADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 81 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLvhqiFGGYLRSRVKCSMCKSVSDTYD 160
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 161 P--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSG 230
Cdd:cd02658 152 LseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 231 G---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSNVKVV 304
Cdd:cd02658 232 WvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDPPE 300
|
330
....*....|
gi 967234024 305 LNQQAYVLFY 314
Cdd:cd02658 301 MKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
16-314 |
3.18e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 104.97 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 16 AGLHNLGNTCFLNATIQCLTYTPPLAN---YLLSKEHARSCHQGSFcmlcvMQNHivQAFANSGNAIKPVSFIRDLKKIA 92
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 93 RHFRFGNQEDAHEFLRYTIDAMQKaclngcakldrqtqattLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVALEIRQA 172
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 173 -------------------ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS---- 229
Cdd:cd02671 161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 230 --GG--KITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVL 305
Cdd:cd02671 241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFL 313
|
330
....*....|....*...
gi 967234024 306 N---------QQAYVLFY 314
Cdd:cd02671 314 EalspntsstSTPYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
17-351 |
1.79e-23 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 107.65 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLAN--YLLSKEHARschqGSFCMLCVMQnhivQAFANSGNAIKPV-------SFIRD 87
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVdtteltrSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 88 lkkIARHFrfgNQEDAHEFLRYTIDAMQKAClngcakldRQTQATTLVHQIFGGYLRSRVKCSMCKSVSDTYDPYLDVAL 167
Cdd:COG5077 267 ---SDDSF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 168 EIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFL 243
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 244 NIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ---------- 307
Cdd:COG5077 412 DLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 967234024 308 ------------QAYVLFYLRipgsKKSPEGLISrtgssslPSRPSVVPDHSKKNV 351
Cdd:COG5077 490 kirdhsgikrfmSAYMLVYLR----KSMLDDLLN-------PVAAVDIPPHVEEVL 534
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-296 |
8.94e-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 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: 88.16 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHF- 95
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 96 ---RFGN--QEDAHEFLRYTIDAMQkaclngcAKLDRQTQATTLVHQIFGGYLRSRVKC---SMCKSVSDTYDPYLDVAL 167
Cdd:cd02657 81 ekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 168 EIRQaanIVRALELFVKADvLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRF-----ANfSGGKITKDVGYPEF 242
Cdd:cd02657 154 SITT---EVNYLQDGLKKG-LEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 967234024 243 LNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 296
Cdd:cd02657 229 LDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
16-296 |
1.66e-18 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 87.33 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 16 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSkeHARSCHQGSFCMLCVM------------QNhiVQAfANsgnaikpvs 83
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELgflfdmlekakgKN--CQA-SN--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 84 FIRDLKKIARHFRFGNQEDAHE-------------FLRYTIDAMQKaclNGCAKLDRQTQATTLVHQIFGGYLRSRVKCS 150
Cdd:pfam13423 67 FLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSS---EENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 151 MCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKKKVPASKRFTIHRTSNVLTLSLK 223
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 224 RFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMND 293
Cdd:pfam13423 224 LT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFND 302
|
...
gi 967234024 294 SLV 296
Cdd:pfam13423 303 FLV 305
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-314 |
1.41e-17 |
|
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: 83.18 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTytpplanyllskeharSChqgsfcmlcvmqnhivqafansgnaikpVSFIRDLKkiarhfR 96
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALA----------------SL----------------------------PSLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGNQEDAHEFLRYTIDAMQKACLNgcakldrqtqattlvhqIFGGYLRSRVKCSMCKSVS-DTYDPYLDVALEIRQA--- 172
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 173 --ANIVRALELFVKADVLSGenaYMCAKCKKKVPASKRftihrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNir 246
Cdd:cd02662 94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 247 pymsqnngdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKVV 304
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVL 229
|
330
....*....|
gi 967234024 305 LNQQAYVLFY 314
Cdd:cd02662 230 EQKSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
179-316 |
9.68e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.32 E-value: 9.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 179 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 255
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967234024 256 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 316
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
17-169 |
2.52e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 84.16 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHA----RSCHQGsfcmlcvMQNHIVQAFAN------SGN--AIKPVSF 84
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEesinEENPLG-------MHGSVASAYADlikqlyDGNlhAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 85 IRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCA-------------------KLDRQT------QATTLVHQIF 139
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRIIkkpytskpdlspgddvvvkKKAKECwwehlkRNDSIITDLF 418
|
170 180 190
....*....|....*....|....*....|
gi 967234024 140 GGYLRSRVKCSMCKSVSDTYDPYLDVALEI 169
Cdd:COG5560 419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-307 |
3.45e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 69.65 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKE----HARSCHQgsfcmlcvmqnhIVQAFA-------NSgNAIK----P 81
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnyenIKDRKSE------------LVKRLSelirkiwNP-RNFKghvsP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 82 VSFIRDLKKI-ARHFRFGNQEDAHEFLRYTIDAMqKACLNGCAKldrqtQATTLVHQIFGGYLR---------------- 144
Cdd:cd02669 188 HELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegsk 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 145 -SRVKCSMCKSVSDTYDPYLDVALEIR------QAANIVRALELFvkaDVLSGENAYMCAKCKKKVpasKRFTIHRTSNV 217
Cdd:cd02669 262 dKFFKDSRVKKTSVSPFLLLTLDLPPPplfkdgNEENIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 218 LTLSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQ 290
Cdd:cd02669 336 LIFHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFE 415
|
330
....*....|....*..
gi 967234024 291 MNDslvhsSNVKVVLNQ 307
Cdd:cd02669 416 IQD-----LNVKEVLPQ 427
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
18-314 |
2.28e-09 |
|
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: 59.08 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 18 LHNLGNTCFLNATIQCLTYTpplanyllskeharschqgsfcmlcvmqNHIVQAFANSgnaikpvsfirdlkkiarhfrf 97
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 98 gNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQTQATTLvhQIFGGYLRSRVKCSMCKSVSDTYDPYLDVALEIRQaa 173
Cdd:cd02673 32 -DQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 174 NIVRALELFVKADVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDvgypEFLNIRPYMSQn 252
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKK----NEEIMKKYCGT- 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967234024 253 ngdPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 314
Cdd:cd02673 181 ---DAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
17-315 |
1.88e-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: 47.17 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 17 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 96
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 97 FGNQEDAHEFLRYTIDAMQKA-------------CLNGCAKLDRQTQATTLVHqiFGGYLRsrvKCSMCKSVSDTYDPY- 162
Cdd:cd02665 19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 163 -LDVALEirqAANI-VRALELFVKADVLSG-ENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDV 237
Cdd:cd02665 94 nLHECLE---AAMFeGEVELLPSDHSVKSGqERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 238 GYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQ 308
Cdd:cd02665 154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPS 221
|
....*..
gi 967234024 309 AYVLFYL 315
Cdd:cd02665 222 AYCLMYI 228
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
400-835 |
3.30e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 400 PPKLPSGSPSPKLPQTpthIPTILDDP-------GKKVKKP-APPQHFSPRTAQG----LPGTSSSSSSRSGSQRQGSWD 467
Cdd:PHA03247 2552 PPPLPPAAPPAAPDRS---VPPPRPAPrpsepavTSRARRPdAPPQSARPRAPVDdrgdPRGPAPPSPLPPDTHAPDPPP 2628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 468 SRDAVLSTSPKLLATATANGHGLKRNDESTG---LDRRGSSSSSPEHSASSDSTKAPQTARSGAAHLCDSQETncSTAGH 544
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP--PPPPP 2706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 545 SKTPPSGADSKTVKLKSPVLSNATAEPASTMSP---PPAKKLALSAKKASTLWRATgndlrppppspssdLTHPMKTSHP 621
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPappAVPAGPATPGGPARPARPPT--------------TAGPPAPAPP 2772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 622 VVASTWPVRRARAVSPAPQSSSRLQPPFSPHPT-----LLSSTPKPPGMSEPQSCSSFSTALPQVNEDLVSLPHQLPEAS 696
Cdd:PHA03247 2773 AAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 697 E-------------PPRSPSEKKKKTFLGELQRLgSETCLPQHIREATAAPHGKRKRKKKKHPEDTAATALQEGQTQTQP 763
Cdd:PHA03247 2853 GgsvapggdvrrrpPSRSPAAKPAAPARPPVRRL-ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQP 2931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967234024 764 GSPTHKREgQAQLPAVrrqedgTQPRVNGQPVGCVTD---GHHASSR---KRRRKGAEGLGEEGGLHQDPPWHSSCSP 835
Cdd:PHA03247 2932 PPPPPPRP-QPPLAPT------TDPAGAGEPSGAVPQpwlGALVPGRvavPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
400-841 |
4.43e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 400 PPKLPSGSPSPKLPQTPTHIPTILDDPGKKVKKPAPPQHFSPRTAQGLpgtsssSSSRSGSQRQGSWDSRDAVLSTSPkl 479
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL------GRAAQASSPPQRPRRRAARPTVGS-- 2694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 480 lATATANGHGLKRNDEStgldrrgsssSSPEHSASSDSTKAPQTARSGAAhlcdsqetncSTAGHSKTPPSGADSKTvkl 559
Cdd:PHA03247 2695 -LTSLADPPPPPPTPEP----------APHALVSATPLPPGPAAARQASP----------ALPAAPAPPAVPAGPAT--- 2750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 560 ksPVLSNATAEPASTMSPP-PAKKLALSAKKASTLWRATGNDLrpppPSPSSDLTHPMKTSHPVVASTWPvrrARAVSPA 638
Cdd:PHA03247 2751 --PGGPARPARPPTTAGPPaPAPPAAPAAGPPRRLTRPAVASL----SESRESLPSPWDPADPPAAVLAP---AAALPPA 2821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 639 PQSSSRLQPPFSPHPTllsSTPKPPGMSEPQSCSSFSTAlpqVNEDLVSLPHQLPEASEPPRSPSEKKKKTFLGELQRLG 718
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPT---APPPPPGPPPPSLPLGGSVA---PGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967234024 719 SETCLPQHIREATAAPHGKRKRKKKKHPEDTAATALQEgQTQTQPGSPTHKREGQAQLPavrrqedGTQPRVNGQPVGCV 798
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP-PPPPRPQPPLAPTTDPAGAG-------EPSGAVPQPWLGAL 2967
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 967234024 799 TDGHHASSRKR------RRKGAEGLGEEGGLHQDP---PWHSSCSPMGDGDP 841
Cdd:PHA03247 2968 VPGRVAVPRFRvpqpapSREAPASSTPPLTGHSLSrvsSWASSLALHEETDP 3019
|
|
| |
