|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
121-421 |
7.00e-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: 525.30 E-value: 7.00e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 121 GAGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARH 200
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 201 FRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQ 277
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 278 AANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661 161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867163788 358 NNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 421
Cdd:cd02661 241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
122-420 |
9.84e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 258.14 E-value: 9.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 122 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC--HQGSFCMLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIA 198
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 199 RHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA 278
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 279 ANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 350
Cdd:pfam00443 156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867163788 351 IRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 420
Cdd:pfam00443 236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
2.55e-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: 243.82 E-value: 2.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCH--QGSFCMLCVMQNhIVQAFANSGNAiKPVSFIRDLK---KI 197
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 198 ARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQ 277
Cdd:cd02660 80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 278 AANIVRA---------------LELFVKADVLsGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KI 339
Cdd:cd02660 160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 340 TKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVV 410
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
|
330
....*....|
gi 1867163788 411 LNQQAYVLFY 420
Cdd:cd02660 318 LKSQAYLLFY 327
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
123-420 |
5.71e-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: 223.13 E-value: 5.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAA- 279
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 280 -NIVRALELFVKADVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 355
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867163788 356 SQNNGD------PVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 420
Cdd:cd02257 178 SEGEKDsdsdngSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
7.03e-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: 7.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANyLLSKeharschqgsfcmlcvmqnhivqafansgnaiKPVSFIRDLKKIARHFR 202
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGNQEDAHEFLRYTIDAMQkaclngcakldrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL----EIRQA 278
Cdd:cd02667 48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 279 ANIVRALELFVKADVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 353
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 354 YMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSLVHSSN 406
Cdd:cd02667 186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
|
330
....*....|....
gi 1867163788 407 VKVVLNQQAYVLFY 420
Cdd:cd02667 265 LEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
6.27e-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: 179.41 E-value: 6.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGNQEDAHEFLRYTIDamqkaclngcaKLDRqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIV 282
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 283 RA------LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 352
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 353 PY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 420
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-423 |
1.38e-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: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLS---KEHARSCHQGsfcmLCVMQnhiVQaFANSGNAIKPVSFIRDLKKIar 199
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQ---RL-FLFLQLSESPVKTTELTDKT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 200 hFRFG-------NQEDAHEFLRYTIDAMQKaclngcaKLdRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVA 272
Cdd:cd02659 74 -RSFGwdslntfEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 273 LEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPE 347
Cdd:cd02659 145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 348 FLNIRPYMSQNNG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ- 414
Cdd:cd02659 224 ELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECf 302
|
330 340 350
....*....|....*....|....*....|
gi 1867163788 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 |
4.95e-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: 4.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYtpplaNYLLSkeharsCHQGSFCmlCVMQNHivqafaNSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF-----ENLLT------CLKDLFE--SISEQK------KRTGVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQ-----TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL 273
Cdd:cd02663 62 NYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 274 EIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEFL 349
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLEL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867163788 350 NIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVKVVLNQ-----QAYVLFY 420
Cdd:cd02663 222 RLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVEEFFGDspnqaTAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
3.89e-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: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSkeharschqgsfcmlCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGN-------------------QEDAHEFLRYTIDAMQkaclngcAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCKSV 261
Cdd:cd02668 66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 262 SDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGG 337
Cdd:cd02668 139 SSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKK 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867163788 338 KITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLV 402
Cdd:cd02668 219 KLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.68e-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: 135.31 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSfcMLCVMQNHIVQAFANSGNAIKPVS-FIRDLKkiARHF 201
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS--VMKKLQLLQAHLMHTQRRAEAPPDyFLEASR--PPWF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 202 RFGNQEDAHEFLRYTIDamqkaclngcaKLDrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDVALeirqaA 279
Cdd:cd02664 77 TPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-----P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 280 NIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI---- 351
Cdd:cd02664 135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvrv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 352 ----------RPYMSQNNGD-----PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQWY 395
Cdd:cd02664 215 eskssespleKKEEESGDDGelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
|
330 340 350
....*....|....*....|....*....|..
gi 1867163788 396 QMNDSLVHSSNVKVVLN-------QQAYVLFY 420
Cdd:cd02664 295 LFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-423 |
6.91e-27 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 111.82 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLT-YTPPLANYL--LSKEharschqgsfcmLCVMQNHIVQAFA--NSGNAIKPVSFIRDLK-- 195
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddLSKE------------LKVLKNVIRKPEPdlNQEEALKLFTALWSSKeh 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 196 KIARHFRFGNQEDAHEFLRYTIDAMqkaclngcaKLDRQTQATTLVHQIFGGYLRSRVkcsvcKSVSDTYdpyldVALEI 275
Cdd:COG5533 69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTST-----GDWFDII-----IELPD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 276 RQAANIVRALELFVKAD---------VLSGENAYMCAKCKKKVPASKRftihRTSNVLTLSLKRFANFSGG-KITKDVGY 345
Cdd:COG5533 130 QTWVNNLKTLQEFIDNMeelvddetgVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 346 PEFLNIRPYMSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVLN---QQAYVLFYLR 422
Cdd:COG5533 206 KFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
|
.
gi 1867163788 423 I 423
Cdd:COG5533 284 I 284
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.48e-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: 108.56 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC----------------HQGSFCMLCVMQNHIVQAFANSGNAIK 186
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpandlncqliklADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 187 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLvhqiFGGYLRSRVKCSVCKSVSDTYD 266
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 267 P--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSG 336
Cdd:cd02658 152 LseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 337 G---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSNVKVV 410
Cdd:cd02658 232 WvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDPPE 300
|
330
....*....|
gi 1867163788 411 LNQQAYVLFY 420
Cdd:cd02658 301 MKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-420 |
2.62e-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: 105.36 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 122 AGLHNLGNTCFLNATIQCLTYTPPLAN---YLLSKEHARSCHQGSFcmlcvMQNHivQAFANSGNAIKPVSFIRDLKKIA 198
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 199 RHFRFGNQEDAHEFLRYTIDAMQKaclngcakldrqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA 278
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 279 -------------------ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS---- 335
Cdd:cd02671 161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 336 --GG--KITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVL 411
Cdd:cd02671 241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFL 313
|
330
....*....|....*...
gi 1867163788 412 N---------QQAYVLFY 420
Cdd:cd02671 314 EalspntsstSTPYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
123-454 |
2.94e-23 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 107.26 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLAN--YLLSKEHARschqGSFCMLCVMQnhivQAFANSGNAIKPV-------SFIRD 193
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVdtteltrSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 194 lkkIARHFrfgNQEDAHEFLRYTIDAMQKAClngcakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL 273
Cdd:COG5077 267 ---SDDSF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 274 EIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFL 349
Cdd:COG5077 333 NVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 350 NIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ---------- 413
Cdd:COG5077 412 DLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1867163788 414 ------------QAYVLFYLRipgsKKSPEGLISrtgssslPGRPSVIPDHSK 454
Cdd:COG5077 490 kirdhsgikrfmSAYMLVYLR----KSMLDDLLN-------PVAAVDIPPHVE 531
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
122-402 |
5.04e-19 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 89.25 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 122 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSkeHARSCHQGSFCMLCVM------------QNhiVQAfANsgnaikpvs 189
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELgflfdmlekakgKN--CQA-SN--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 190 FIRDLKKIARHFRFGNQEDAHE-------------FLRYTIDAMQKaclNGCAKLDRQTQATTLVHQIFGGYLRSRVKCS 256
Cdd:pfam13423 67 FLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSS---EENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 257 VCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKKKVPASKRFTIHRTSNVLTLSLK 329
Cdd:pfam13423 144 NCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 330 RFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMND 399
Cdd:pfam13423 224 LT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFND 302
|
...
gi 1867163788 400 SLV 402
Cdd:pfam13423 303 FLV 305
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-402 |
6.11e-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: 88.93 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHF- 201
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 202 ---RFGN--QEDAHEFLRYTIDAMQkaclngcAKLDRQTQATTLVHQIFGGYLRSRVKC---SVCKSVSDTYDPYLDVAL 273
Cdd:cd02657 81 ekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 274 EIRQaanIVRALELFVKADvLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRF-----ANfSGGKITKDVGYPEF 348
Cdd:cd02657 154 SITT---EVNYLQDGLKKG-LEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1867163788 349 LNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 402
Cdd:cd02657 229 LDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-420 |
1.97e-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: 82.80 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTytpplanyllskeharSChqgsfcmlcvmqnhivqafansgnaikpVSFIRDLKkiarhfR 202
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALA----------------SL----------------------------PSLIEYLE------E 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGNQEDAHEFLRYTIDAMQKACLNgcakldrqtqattlvhqIFGGYLRSRVKCSVCKSVS-DTYDPYLDVALEIRQA--- 278
Cdd:cd02662 31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 279 --ANIVRALELFVKADVLSGenaYMCAKCKKKVPASKRftihrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNir 352
Cdd:cd02662 94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 353 pymsqnngdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKVV 410
Cdd:cd02662 160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVL 229
|
330
....*....|
gi 1867163788 411 LNQQAYVLFY 420
Cdd:cd02662 230 EQKSAYMLFY 239
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
123-275 |
1.11e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.32 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHA----RSCHQGsfcmlcvMQNHIVQAFAN------SGN--AIKPVSF 190
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEesinEENPLG-------MHGSVASAYADlikqlyDGNlhAFTPSGF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 191 IRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCA-------------------KLDRQT------QATTLVHQIF 245
Cdd:COG5560 340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRIIkkpytskpdlspgddvvvkKKAKECwwehlkRNDSIITDLF 418
|
170 180 190
....*....|....*....|....*....|
gi 1867163788 246 GGYLRSRVKCSVCKSVSDTYDPYLDVALEI 275
Cdd:COG5560 419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
285-422 |
1.12e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.32 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 285 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 361
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867163788 362 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 422
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-413 |
1.22e-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: 71.20 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKE----HARSCHQgsfcmlcvmqnhIVQAFA-------NSgNAIK----P 187
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnyenIKDRKSE------------LVKRLSelirkiwNP-RNFKghvsP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 188 VSFIRDLKKI-ARHFRFGNQEDAHEFLRYTIDAMqKACLNGCAKldrqtQATTLVHQIFGGYLR---------------- 250
Cdd:cd02669 188 HELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegsk 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 251 -SRVKCSVCKSVSDTYDPYLDVALEIR------QAANIVRALELFvkaDVLSGENAYMCAKCKKKVpasKRFTIHRTSNV 323
Cdd:cd02669 262 dKFFKDSRVKKTSVSPFLLLTLDLPPPplfkdgNEENIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 324 LTLSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQ 396
Cdd:cd02669 336 LIFHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFE 415
|
330
....*....|....*..
gi 1867163788 397 MNDslvhsSNVKVVLNQ 413
Cdd:cd02669 416 IQD-----LNVKEVLPQ 427
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
124-420 |
2.76e-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: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 124 LHNLGNTCFLNATIQCLTYTpplanyllskeharschqgsfcmlcvmqNHIVQAFANSgnaikpvsfirdlkkiarhfrf 203
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 204 gNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQTQATTLvhQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQaa 279
Cdd:cd02673 32 -DQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 280 NIVRALELFVKADVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDvgypEFLNIRPYMSQn 358
Cdd:cd02673 107 NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKK----NEEIMKKYCGT- 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867163788 359 ngdPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 420
Cdd:cd02673 181 ---DAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
506-840 |
9.34e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 506 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 553
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 554 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 628
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 629 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 700
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 701 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 780
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163788 781 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 840
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
123-421 |
2.62e-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: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 123 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-------------------------------------------------------------- 18
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 203 FGNQEDAHEFLRYTIDAMQKA-------------CLNGCAKLDRQTQATTLVHqiFGGYLRsrvKCSVCKSVSDTYDPY- 268
Cdd:cd02665 19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 269 -LDVALEirqAANI-VRALELFVKADVLSG-ENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDV 343
Cdd:cd02665 94 nLHECLE---AAMFeGEVELLPSDHSVKSGqERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163788 344 GYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQ 414
Cdd:cd02665 154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPS 221
|
....*..
gi 1867163788 415 AYVLFYL 421
Cdd:cd02665 222 AYCLMYI 228
|
|
| |
