|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1-256 |
9.49e-147 |
|
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: 437.48 E-value: 9.49e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 1 MLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVH 77
Cdd:cd02661 46 MMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 78 QIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSN 157
Cdd:cd02661 126 QIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 158 VLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLV 237
Cdd:cd02661 206 VLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKV 285
|
250
....*....|....*....
gi 767995422 238 HSSNVKVVLNQQAYVLFYL 256
Cdd:cd02661 286 SPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
38-255 |
5.37e-61 |
|
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: 208.11 E-value: 5.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 38 FGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAA- 114
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 115 -NIVRALELFVKADVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 190
Cdd:cd02257 99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995422 191 SQNNGD------PVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 255
Cdd:cd02257 178 SEGEKDsdsdngSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1-255 |
1.72e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 206.14 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 1 MLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQI 79
Cdd:pfam00443 47 LLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 80 FGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIH 153
Cdd:pfam00443 122 FRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKIS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 154 RTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SN 226
Cdd:pfam00443 202 RLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyEN 280
|
250 260 270
....*....|....*....|....*....|
gi 767995422 227 GQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 255
Cdd:pfam00443 281 NRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-255 |
1.28e-54 |
|
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: 192.97 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 3 CVMQNhIVQAFANSGNAiKPVSFIRDLK---KIARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQI 79
Cdd:cd02660 49 CAMDE-IFQEFYYSGDR-SPYGPINLLYlswKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 80 FGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRA---------------LELFVKADVLsGENAYMCAKCKKKV 144
Cdd:cd02660 127 FSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 145 PASKRFTIHRTSNVLTLSLKRFANFSGG---KITKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVHSGyS 212
Cdd:cd02660 206 EATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-T 284
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767995422 213 CHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 255
Cdd:cd02660 285 LDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
22-255 |
2.38e-46 |
|
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: 167.56 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 22 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQkaclngcakldrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD 101
Cdd:cd02667 32 PKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 102 PYLDVAL----EIRQAANIVRALELFVKADVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSgg 172
Cdd:cd02667 95 PFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 173 KITKDVGYPEFLNIRPYMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYYCYVKASN--------------------- 226
Cdd:cd02667 170 KVSRHVSFPEILDLAPFCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpg 248
|
250 260 270
....*....|....*....|....*....|
gi 767995422 227 -GQWYQMNDSLVHSSNVKVVLNQQAYVLFY 255
Cdd:cd02667 249 sGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
38-255 |
1.13e-45 |
|
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: 164.00 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 38 FGNQEDAHEFLRYTIDamqkaclngcaKLDRqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIV 117
Cdd:cd02674 19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 118 RA------LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 187
Cdd:cd02674 82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 188 PY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 255
Cdd:cd02674 161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-258 |
5.26e-42 |
|
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: 157.03 E-value: 5.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 39 GNQEDAHEFLRYTIDAMQKaclngcaKLdRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR 118
Cdd:cd02659 84 FEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 119 ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPEFLNIRPYMSQN 193
Cdd:cd02659 156 SLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPLELDMEPYTEKG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 194 NG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ------------ 249
Cdd:cd02659 235 LAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktyds 313
|
250
....*....|....*....
gi 767995422 250 ----------AYVLFYLRI 258
Cdd:cd02659 314 gprafkrttnAYMLFYERK 332
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
20-255 |
7.96e-36 |
|
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: 137.83 E-value: 7.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 20 IKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQ-----TQATTLVHQIFGGYLRSRVKC 90
Cdd:cd02663 44 ISPKKFITRLKRENELFDNYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNnnnnaEPQPTWVHEIFQGILTNETRC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 91 SVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NF 169
Cdd:cd02663 124 LTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 170 SGGKITK---DVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVK 243
Cdd:cd02663 204 QLNRYIKlfyRVVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVE 282
|
250
....*....|....*..
gi 767995422 244 VVLNQ-----QAYVLFY 255
Cdd:cd02663 283 EFFGDspnqaTAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
2-237 |
4.24e-31 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 124.84 E-value: 4.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 2 LCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFRFGN-------------------QEDAHEFLRYTIDAMQkaclng 62
Cdd:cd02668 30 ECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 63 cAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKC 140
Cdd:cd02668 104 -AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 141 KKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGGKITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHA 215
Cdd:cd02668 183 NSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKKLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYS 261
|
250 260
....*....|....*....|...
gi 767995422 216 GHYYCYVK-ASNGQWYQMNDSLV 237
Cdd:cd02668 262 GHYIAHIKdEQTGEWYKFNDEDV 284
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-255 |
1.26e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 117.59 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 36 FRFGNQEDAHEFLRYTIDamqkaclngcaKLDrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDVALeirqa 113
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 114 ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI--- 186
Cdd:cd02664 134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 187 -----------RPYMSQNNGD-----PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQW 229
Cdd:cd02664 214 veskssespleKKEEESGDDGelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNW 293
|
250 260 270
....*....|....*....|....*....|...
gi 767995422 230 YQMNDSLVHSSNVKVVLN-------QQAYVLFY 255
Cdd:cd02664 294 YLFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; ... |
19-258 |
2.25e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227820 [Multi-domain] Cd Length: 415 Bit Score: 110.11 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 19 AIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCAKLDRQTQAT------------------------- 73
Cdd:COG5533 140 SISPRNFIDILSGRNKLFSGDMQQDSQEFLIFFLDLLHED-LNGNKSRSPILELKdefeevreelplshfshhewnlhlr 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 74 ---TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAA--NIVRALELFVKADVLSGENAYMCAKCKKKVPASK 148
Cdd:COG5533 219 snkSLVAKTFFGQDKSRLQCEACNYTSTTIAMFSTLLVPPYEVVqlGLQECIDRFYEEEKLEGKDAWRCPKCGRKESSRK 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 149 RFTIHRTSNVLTLSLKRFANFsggkitkdVGYPEFLNIRPYMS-------------QNNGD--PVMYGLYAVLVHSGySC 213
Cdd:COG5533 299 RMEILVLPDVLIIHISRFHIS--------VMGRKKIDTPQGWKntasvevnvtllfNNGIGyiPRKYSLLGVVCHNG-TL 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767995422 214 HAGHYYCYVKASNGqWYQMNDSLVHS-SNVKVVLNQQAYVLFYLRI 258
Cdd:COG5533 370 NGGHYFSEVKRSGT-WNVYDDSQVRKgSRTTSGSHPSSYILFYTRS 414
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
41-289 |
3.87e-20 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 96.48 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 41 QEDAHEFLRYTIDAMQKAClngcakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRAL 120
Cdd:COG5077 273 QHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 121 ELFVKADVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNIRPYMSQN--- 193
Cdd:COG5077 345 RRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDRDadk 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 194 --NGDPVmYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ---------------------- 248
Cdd:COG5077 424 seNSDAV-YVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfm 501
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767995422 249 QAYVLFYLRipgsKKSPEGLISrtgssslPGRPSVIPDHSK 289
Cdd:COG5077 502 SAYMLVYLR----KSMLDDLLN-------PVAAVDIPPHVE 531
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
20-255 |
7.42e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 88.53 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 20 IKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLvhqiFGGYLRSRVKCSVCKSVSDT 99
Cdd:cd02658 79 IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 100 YDP--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANF 169
Cdd:cd02658 150 SELseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 170 SGG---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSNVK 243
Cdd:cd02658 230 ENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDP 298
|
250
....*....|..
gi 767995422 244 VVLNQQAYVLFY 255
Cdd:cd02658 299 PEMKKLGYIYFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
120-257 |
8.45e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 85.32 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 120 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 196
Cdd:COG5560 681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995422 197 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 257
Cdd:COG5560 761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
41-255 |
2.80e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 78.01 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 41 QEDAHEFLRYTIDAMQKaclngcakldrqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA------- 113
Cdd:cd02671 105 QHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESelsksee 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 114 ------------ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS------GG--K 173
Cdd:cd02671 168 sseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefdcyGGlsK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 174 ITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVLN------ 247
Cdd:cd02671 248 VNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEalspnt 320
|
250
....*....|.
gi 767995422 248 ---QQAYVLFY 255
Cdd:cd02671 321 sstSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-255 |
2.33e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 73.55 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 3 CVMqNHIVQAFANSGnaikpvSFIRDLKkiarhfRFGNQEDAHEFLRYTIDAMQKACLNgcakldrqtqattlvhqIFGG 82
Cdd:cd02662 9 CFM-NSVLQALASLP------SLIEYLE------EFLEQQDAHELFQVLLETLEQLLKF-----------------PFDG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 83 YLRSRVKCSVCKSVS-DTYDPYLDVALEIRQA-----ANIVRALELFVKADVLSGenaYMCAKCKKKVPASKRftihrts 156
Cdd:cd02662 59 LLASRIVCLQCGESSkVRYESFTMLSLPVPNQssgsgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 157 nVLTLSLKRFAnFSG-GKITKD---VGYPEFLNirpymsqnngdPVMYGLYAVLVHSGySCHAGHYYCYVKAS------- 225
Cdd:cd02662 129 -ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-----------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdke 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767995422 226 --------------NGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 255
Cdd:cd02662 195 pgsfvrmregpsstSHPWWRISDTTVkEVSESEVLEQKSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
70-237 |
1.81e-12 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 433195 [Multi-domain] Cd Length: 305 Bit Score: 69.22 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 70 TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKK 142
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 143 KVPASKRFTIHRTSNVLTLSLKRFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYC 220
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLNAALT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVS 280
|
170 180
....*....|....*....|....*
gi 767995422 221 YVKASN--------GQWYQMNDSLV 237
Cdd:pfam13423 281 FVKVADseledpteSQWYLFNDFLV 305
|
|
| UBP14 |
COG5207 |
Uncharacterized Zn-finger protein, UBP-type [General function prediction only]; |
18-192 |
2.71e-10 |
|
Uncharacterized Zn-finger protein, UBP-type [General function prediction only];
Pssm-ID: 227532 [Multi-domain] Cd Length: 749 Bit Score: 64.32 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 18 NAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAclngcakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVS 97
Cdd:COG5207 371 NGISPLDFKMLIGQDHPEFGKFAQQDAHEFLLFLLEKIRKG---------ERSYLIPPITSLFEFEVERRLSCSGCMDVS 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 98 DTYDPYLDVALEIRQ---AANIVRALELFVKADVLSgenaYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGG 172
Cdd:COG5207 442 YSYESMLMICIFLEGndePQDIRKSVEAFFLPDTIE----WSCENCKGKKKASRKPFIKSLPKYLILQVGRYSlqNYKVE 517
|
170 180
....*....|....*....|..
gi 767995422 173 KITK--DVGYPEFLNIRPYMSQ 192
Cdd:COG5207 518 KLSDpiEMRSDDMIKLGSFMSK 539
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
15-237 |
5.12e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 52.33 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 15 NSGNAIKPVSFIRDLKKIARHF----RFGN--QEDAHEFLRYTIDAMQkaclngcAKLDRQTQATTLVHQIFGGYLRSRV 88
Cdd:cd02657 58 KKQEPVPPIEFLQLLRMAFPQFaekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 89 KC---SVCKSVSDTYDPYLDVALEIRQaanIVRALELFVKADvLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKR 165
Cdd:cd02657 131 KCtesPDEEEVSTESEYKLQCHISITT---EVNYLQDGLKKG-LEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVR 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767995422 166 F-----ANfSGGKITKDVGYPEFLNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 237
Cdd:cd02657 207 FfwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-255 |
5.90e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 51.76 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 29 LKKIARHFRFGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQTQATTLvhQIFGGYLRSRVKCSVCKSVSDTYDPYL 104
Cdd:cd02673 21 IGKINTEFDNDDQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 105 DVALEIRQaaNIVRALELFVKADVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDvgypEF 183
Cdd:cd02673 99 FLDVSMID--NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKK----NE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995422 184 LNIRPYMSQnngdPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 255
Cdd:cd02673 172 EIMKKYCGT----DAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
36-248 |
7.22e-06 |
|
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: 49.62 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 36 FRFGNQEDAHEFLRYTIDAMqKACLNGCAKldrqtQATTLVHQIFGGYLR-----------------SRVKCSVCKSVSD 98
Cdd:cd02669 202 FSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegskdKFFKDSRVKKTSV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 99 TYDPYLDVALEIR------QAANIVRALELFvkaDVLSGENAYMCAKCKKKVpasKRFTIHRTSNVLTLSLKRF--ANFS 170
Cdd:cd02669 276 SPFLLLTLDLPPPplfkdgNEENIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFskNNFF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 171 GGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQMNDslvhsSNVKVV 245
Cdd:cd02669 350 KEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD-----LNVKEV 424
|
...
gi 767995422 246 LNQ 248
Cdd:cd02669 425 LPQ 427
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
341-675 |
1.14e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 341 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 388
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 389 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 463
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 464 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 535
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 536 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 615
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995422 616 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 675
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
38-256 |
2.52e-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: 46.40 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 38 FGNQEDAHEFLRYTIDAMQKA-------------CLNGCAKLDRQTQATTLVHqiFGGYLRsrvKCSVCKSVSDTYDPY- 103
Cdd:cd02665 19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 104 -LDVALEirqAANI-VRALELFVKADVLSG-ENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDV 178
Cdd:cd02665 94 nLHECLE---AAMFeGEVELLPSDHSVKSGqERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 179 GYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQ 249
Cdd:cd02665 154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPS 221
|
....*..
gi 767995422 250 AYVLFYL 256
Cdd:cd02665 222 AYCLMYI 228
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
9-110 |
4.72e-05 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 47.19 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995422 9 IVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCA-------------------KLDRQ 69
Cdd:COG5560 323 IKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRIIkkpytskpdlspgddvvvkKKAKE 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767995422 70 T------QATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI 110
Cdd:COG5560 402 CwwehlkRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
|