|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-308 |
6.14e-167 |
|
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: 473.69 E-value: 6.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 3 PCGLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNDWCFLCEFENHLDRANYSRFPFSPMNIISR-LPNIGGN 81
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSnLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 82 LGYGRQEDAHELMRFAIDMMQSVCLDEFGGEKVVPPRAQETTLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTVEIHG 161
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 162 DAvSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQGGRFGKLNKRISFPETFDLGPYMS 241
Cdd:cd02661 161 AD-SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334184421 242 GGGEGSDVYKLYAVIVHLDMLNasFFGHYICYVKDFRGNWYRIDDSEVEKVELEDVLSQRAYMLLYS 308
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
1.75e-69 |
|
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: 225.33 E-value: 1.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNDW--CFLCEFENHLDRANYS--RFPFSPMNIISRLPNIGG 80
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsCLSCAMDEIFQEFYYSgdRSPYGPINLLYLSWKHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 81 NL-GYGrQEDAHELMRFAIDMMQSVCLDefggekVVPPRAQE---TTLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLT 156
Cdd:cd02660 82 NLaGYS-QQDAHEFFQFLLDQLHTHYGG------DKNEANDEshcNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 157 VEIHGDAV--------------SLEECLDQFTAKEWLqGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQ---GG 219
Cdd:cd02660 155 LDIPNKSTpswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 220 RFGKLNKRISFPETFDLGPYMSGGGEGSD---------VYKLYAVIVHLDMLNAsffGHYICYVKDFRGNWYRIDDSEVE 290
Cdd:cd02660 234 TSRKIDTYVQFPLELNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKGTLDT---GHYTAYCRQGDGQWFKFDDAMIT 310
|
330
....*....|....*..
gi 334184421 291 KVELEDVLSQRAYMLLY 307
Cdd:cd02660 311 RVSEEEVLKSQAYLLFY 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
4-307 |
2.64e-67 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 218.85 E-value: 2.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 4 CGLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNDWC--FLCEFE---NHLDRANYSRfPFSPMNIISRLPNI 78
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRdlfKALQKNSKSS-SVSPKMFKKSLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 79 GGNLGYGRQEDAHELMRFAIDMMQSVCLDEFGGEkvvppraqETTLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTVE 158
Cdd:pfam00443 80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE--------NESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 159 IHGDA-----VSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQGGRFG--KLNKRISFP 231
Cdd:pfam00443 152 IPGDSaelktASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 232 ETFDLGPYMSGGGEG----SDVYKLYAVIVHLDMLNasfFGHYICYVKDFRGN-WYRIDDSEVEKVELE-DVLSQRAYML 305
Cdd:pfam00443 232 LELDLSRYLAEELKPktnnLQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEEtAVLSSSAYIL 308
|
..
gi 334184421 306 LY 307
Cdd:pfam00443 309 FY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
5-307 |
1.47e-65 |
|
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: 212.34 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLswtrplvayllerghkrecrrndwcflcefenhldranysrfpfspmniisrlpniggnlgY 84
Cdd:cd02257 1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------F 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 85 GRQEDAHELMRFAIDMMQSVCLDEFGGEKvvpPRAQETTLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTVEIHGD-- 162
Cdd:cd02257 20 SEQQDAHEFLLFLLDKLHEELKKSSKRTS---DSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKgl 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 163 -AVSLEECLDQFTAKEWLQGDNLYKCDRCDdYVKACKRLSIRCAPNILTIALKRFQ---GGRFGKLNKRISFPETFDLGP 238
Cdd:cd02257 97 pQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 239 YM------SGGGEGSDVYKLYAVIVHldMLNASFFGHYICYVKDF-RGNWYRIDDSEVEKVELEDVLSQR-----AYMLL 306
Cdd:cd02257 176 YLsegekdSDSDNGSYKYELVAVVVH--SGTSADSGHYVAYVKDPsDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253
|
.
gi 334184421 307 Y 307
Cdd:cd02257 254 Y 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-308 |
2.03e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 182.49 E-value: 2.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSwtrplvayllerghkrecrrndwcflcefenhldranysrfpfspmniisrlpniggnlgy 84
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 85 GRQEDAHELMRFAIDMMQSvcldefggekvvppraqettLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTVEI----- 159
Cdd:cd02674 20 ADQQDAQEFLLFLLDGLHS--------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsg 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 160 HGDAVSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRF--QGGRFGKLNKRISFP-ETFDL 236
Cdd:cd02674 80 DAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFsfSRGSTRKLTTPVTFPlNDLDL 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334184421 237 GPY-MSGGGEGSDVYKLYAVIVHLDMLNAsffGHYICYVKDFRGN-WYRIDDSEVEKVELEDVLSQRAYMLLYS 308
Cdd:cd02674 160 TPYvDTRSFTGPFKYDLYAVVNHYGSLNG---GHYTAYCKNNETNdWYKFDDSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
2.11e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 176.04 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLERghkrecRRNdwcFLCEFenhldRANYSRFPfspmniisrlpniggnlGY 84
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET------PKE---LFSQV-----CRKAPQFK-----------------GY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 85 gRQEDAHELMRFAIDMMQSVcldefggekvvppraqettlIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTV---EIHG 161
Cdd:cd02667 50 -QQQDSHELLRYLLDGLRTF--------------------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsDEIK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 162 DAVSLEECLDQFTAKEWLQGDNLYKCDRCDdyvKACKRLSIRCAPNILTIALKRFQGGRFG---KLNKRISFPETFDLGP 238
Cdd:cd02667 109 SECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 239 YMSGGGEGSD-----VYKLYAVIVHldmLNASFFGHYICYVKD----------------------FRGNWYRIDDSEVEK 291
Cdd:cd02667 186 FCDPKCNSSEdkssvLYRLYGVVEH---SGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262
|
330
....*....|....*.
gi 334184421 292 VELEDVLSQRAYMLLY 307
Cdd:cd02667 263 VSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
4-312 |
5.91e-44 |
|
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: 157.80 E-value: 5.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 4 CGLTNCGNSCFANVVLQCLSWT---RPLVAYLLERGHKRECRrNDWCFL-----------CEFENHLDRANYSRFPFSPM 69
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTpefRNAVYSIPPTEDDDDNK-SVPLALqrlflflqlseSPVKTTELTDKTRSFGWDSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 70 NIisrlpniggnlgyGRQEDAHELMRFAIDMMqsvcldefggEKVVPPRAQETtLIQYIFGGLLQSQVQCTACSNVSDQY 149
Cdd:cd02659 82 NT-------------FEQHDVQEFFRVLFDKL----------EEKLKGTGQEG-LIKNLFGGKLVNYIICKECPHESERE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 150 ENMMDLTVEIHGDAvSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRF----QGGRFGKLN 225
Cdd:cd02659 138 EYFLDLQVAVKGKK-NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKIN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 226 KRISFPETFDLGPYMSGGG-----------EGSDVYKLYAVIVHLDMLNAsffGHYICYVKDFR-GNWYRIDDSEVEKVE 293
Cdd:cd02659 217 DRFEFPLELDMEPYTEKGLakkegdsekkdSESYIYELHGVLVHSGDAHG---GHYYSYIKDRDdGKWYKFNDDVVTPFD 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 334184421 294 LEDVLSQ----------------------RAYMLLYSRVQP 312
Cdd:cd02659 294 PNDAEEEcfggeetqktydsgprafkrttNAYMLFYERKSP 334
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-308 |
5.49e-38 |
|
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: 141.40 E-value: 5.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSwtrplvayllergHKRECRRNDWCFLCEFENHLDRANYSRfPFSPMNIISRLPNIGGNLGY 84
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWF-------------MNLEFRKAVYECNSTEDAELKNMPPDK-PHEPQTIIDQLQLIFAQLQF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 85 GR-------------------QEDAHELMRFAIDMMQSvCLDEFGGEKVVppraqetTLIQYIFGGLLQSQVQCTACSNV 145
Cdd:cd02668 67 GNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLEA-KLSKSKNPDLK-------NIVQDLFRGEYSYVTQCSKCGRE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 146 SDQYENMMDLTVEIHGDAvSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRF----QGGRF 221
Cdd:cd02668 139 SSLPSKFYELELQLKGHK-TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 222 GKLNKRISFPETFDLGPYMSGGGEGSDVYKLYAVIVHLDmlNASFFGHYICYVKDF-RGNWYRIDDSEVEKVE------- 293
Cdd:cd02668 218 KKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDEqTGEWYKFNDEDVEEMPgkplklg 295
|
330 340
....*....|....*....|....*....
gi 334184421 294 -LEDVLSQR-------------AYMLLYS 308
Cdd:cd02668 296 nSEDPAKPRkseikkgthssrtAYMLVYK 324
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-308 |
3.99e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 138.60 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCL------SWTRPLVAYLLErgHKRecrRNDWCFLCEFENHLDRANYSRFpfSPMniisrlpni 78
Cdd:cd02663 1 GLENFGNTCYCNSVLQALyfenllTCLKDLFESISE--QKK---RTGVISPKKFITRLKRENELFD--NYM--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 79 ggnlgygrQEDAHELMRFAIDMMQSVCLDEFGGEKVVPPRAQE------TTLIQYIFGGLLQSQVQCTACSNVSDQYENM 152
Cdd:cd02663 65 --------HQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNnnaepqPTWVHEIFQGILTNETRCLTCETVSSRDETF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 153 MDLTVEIHGdAVSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRF----QGGRFGKLNKRI 228
Cdd:cd02663 137 LDLSIDVEQ-NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIKLFYRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 229 SFPETFDLgPYMSGGGEGSD-VYKLYAVIVHLDmlNASFFGHYICYVKDFRGnWYRIDDSEVEKVELEDVL--------S 299
Cdd:cd02663 216 VFPLELRL-FNTTDDAENPDrLYELVAVVVHIG--GGPNHGHYVSIVKSHGG-WLLFDDETVEKIDENAVEeffgdspnQ 291
|
....*....
gi 334184421 300 QRAYMLLYS 308
Cdd:cd02663 292 ATAYVLFYQ 300
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
1.18e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 115.76 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWT---RPLVAYLLERGHKRECRRNDWCFLCEFENHLDRANYSRfpfSPMNIISRL-PNIGG 80
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCpgfKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAPR---RLLNALREVnPMYEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 81 NLgygrQEDAHELMRFAIDMMQSvcldefggekvvppraqettLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTVEIH 160
Cdd:cd02671 103 YL----QHDAQEVLQCILGNIQE--------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 161 GDAVS------------------LEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQ----- 217
Cdd:cd02671 159 ESELSkseesseispdpktemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAangse 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 218 ---GGRFGKLNKRIsfPETFDLGPYMSGGGEGSDVYKLYAVIVHLDMLNASffGHYICYVKdfrgnWYRIDDSEV---EK 291
Cdd:cd02671 239 fdcYGGLSKVNTPL--LTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISS--GHYTAYVR-----WLLFDDSEVkvtEE 309
|
330 340
....*....|....*....|..
gi 334184421 292 VELEDVLSQRA------YMLLY 307
Cdd:cd02671 310 KDFLEALSPNTsststpYLLFY 331
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
8.10e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 107.41 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRND--WCFLCEFE---NHLDRANYSRfPFSPMNIISRLPN-- 77
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIklaDGLLSGRYSK-PASLKSENDPYQVgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 78 --------IGGN---LGYGRQEDAHELMRFAIDMMQsvclDEFGGEKVVPPraqettliQYIFGGLLQSQVQCTACSNV- 145
Cdd:cd02658 80 kpsmfkalIGKGhpeFSTMRQQDALEFLLHLIDKLD----RESFKNLGLNP--------NDLFKFMIEDRLECLSCKKVk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 146 -SDQYENMMDLTVEIH-----------GDAVSLEECLDQFTAKEWLQgdnlYKCDRCDDYVKACKRLSIRCAPNILTIAL 213
Cdd:cd02658 148 yTSELSEILSLPVPKDeatekeegelvYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 214 KRFQ---GGRFGKLNKRISFPETFDLGPymsgggegsdvYKLYAVIVHldMLNASFFGHYICYVK---DFRGNWYRIDDS 287
Cdd:cd02658 224 KRFQlleNWVPKKLDVPIDVPEELGPGK-----------YELIAFISH--KGTSVHSGHYVAHIKkeiDGEGKWVLFNDE 290
|
330 340
....*....|....*....|
gi 334184421 288 EVEKVELEDVLSQRAYMLLY 307
Cdd:cd02658 291 KVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
9.60e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 102.44 E-value: 9.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLErghkrecrrndwcflcefenhldranysrfpfspmnIISrlpniggnlgy 84
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE------------------------------------FLE----------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 85 grQEDAHELMRFAIDMMQSVCldefggekvvppraqettliQYIFGGLLQSQVQCTACSNVS-DQYENMMDLTV----EI 159
Cdd:cd02662 34 --QQDAHELFQVLLETLEQLL--------------------KFPFDGLLASRIVCLQCGESSkVRYESFTMLSLpvpnQS 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 160 HGDAVSLEECLDQFTAKEWLQGdnlYKCDRCddyvkackRLSIRCAPNILTIALKRFQGGRFGKLNKR---ISFPETfdL 236
Cdd:cd02662 92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTSTKNsckVSFPER--L 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 237 GPYMsgggegsdvYKLYAVIVHLDMLNAsffGHYICY---------------------VKDFRGNWYRIDDSEVEKVELE 295
Cdd:cd02662 159 PKVL---------YRLRAVVVHYGSHSS---GHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSES 226
|
330
....*....|...
gi 334184421 296 DVLSQR-AYMLLY 307
Cdd:cd02662 227 EVLEQKsAYMLFY 239
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
4.96e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 99.87 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNDWCF----LCEFENHLDRANY---SRF-------PFSPmn 70
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKklqlLQAHLMHTQRRAEappDYFleasrppWFTP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 71 iisrlpniggnlgyGRQEDAHELMRFAIDMMQsvcldefggekvvppraqetTLIQYIFGGLLQSQVQCTACSNVSDQYE 150
Cdd:cd02664 79 --------------GSQQDCSEYLRYLLDRLH--------------------TLIEKMFGGKLSTTIRCLNCNSTSARTE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 151 NMMDLTVEIhgdaVSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQ----GGRFGKLNK 226
Cdd:cd02664 125 RFRDLDLSF----PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkTHVREKIMD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 227 RISFPETFDLGPYMSGGGEGSD-------------------VYKLYAVIVHLDMlnASFFGHYICYV------------- 274
Cdd:cd02664 201 NVSINEVLSLPVRVESKSSESPlekkeeesgddgelvtrqvHYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqec 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 334184421 275 --------KDFRGNWYRIDDSEVEKV---ELEDVLS----QRAYMLLY 307
Cdd:cd02664 279 pepkdaeeNDESKNWYLFNDSRVTFSsfeSVQNVTSrfpkDTPYILFY 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
157-309 |
1.83e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 91.87 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 157 VEIHGDAVSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQGGRFG--KLNKRISFPET- 233
Cdd:COG5560 668 IGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDd 747
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334184421 234 FDLGPYMSGGGEGSDVYKLYAVIVHLDMLNAsffGHYICYVKDFRGN-WYRIDDSEVEKVELEDVLSQRAYMLLYSR 309
Cdd:COG5560 748 LDLSGVEYMVDDPRLIYDLYAVDNHYGGLSG---GHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
5-309 |
2.17e-19 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 91.86 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWT---RPLVaYLLERGHKREcrRNDWCFLcefenhLDRANY----SRFPFSPMNIISRlpN 77
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIakfRKDV-YGIPTDHPRG--RDSVALA------LQRLFYnlqtGEEPVDTTELTRS--F 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 78 IGGNLGYGRQEDAHELMRFAIDMMQSvcldEFGGEKVvppraqeTTLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTV 157
Cdd:COG5077 264 GWDSDDSFMQHDIQEFNRVLQDNLEK----SMRGTVV-------ENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 158 EIHGDAvSLEECLDQFTAKEWLQGDNLYKCDrcdDY--VKACKRLSIRCAPNILTIALKRFQ----GGRFGKLNKRISFP 231
Cdd:COG5077 333 NVKGMK-NLQESFRRYIQVETLDGDNRYNAE---KHglQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFP 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 232 ETFDLGPYMSGGGEGSD----VYKLYAVIVHLDMLNAsffGHYICYVK-DFRGNWYRIDDSEVEKVELEDVLSQ------ 300
Cdd:COG5077 409 LEIDLLPFLDRDADKSEnsdaVYVLYGVLVHSGDLHE---GHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdh 485
|
330 340
....*....|....*....|....*
gi 334184421 301 ----------------RAYMLLYSR 309
Cdd:COG5077 486 pykdkirdhsgikrfmSAYMLVYLR 510
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
7.76e-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 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: 81.22 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLE--RGHKRECRRNDWcFLCEFENHLDRANYSRFPFSPMNIISRL----PNI 78
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNynPARRGANQSSDN-LTNALRDLFDTMDKKQEPVPPIEFLQLLrmafPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 79 G--GNLGYGRQEDAHELMRFAIDMMQSvcldefggekVVPPRAQETTLIQYIFGGLLQSQVQCTACSN---VSDQYENMM 153
Cdd:cd02657 80 AekQNQGGYAQQDAEECWSQLLSVLSQ----------KLPGAGSKGSFIDQLFGIELETKMKCTESPDeeeVSTESEYKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 154 DLTVEIHGDAVSLEECLDQ------FTAKEWLQGDNLYKcdrcddyvkacKRLSIRCAPNILTIALKRF----QGGRFGK 223
Cdd:cd02657 150 QCHISITTEVNYLQDGLKKgleeeiEKHSPTLGRDAIYT-----------KTSRISRLPKYLTVQFVRFfwkrDIQKKAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 224 LNKRISFPETFDLGPYMSGGGegsdVYKLYAVIVHLDMLNASffGHYICYVK-DFRGNWYRIDDSEVEKVELEDVLSQR- 301
Cdd:cd02657 219 ILRKVKFPFELDLYELCTPSG----YYELVAVITHQGRSADS--GHYVAWVRrKNDGKWIKFDDDKVSEVTEEDILKLSg 292
|
330
....*....|..
gi 334184421 302 ------AYMLLY 307
Cdd:cd02657 293 ggdwhiAYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
5-309 |
1.52e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.85 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKrecrrndwcflcefeNHLDRANYSRFPFSPMNI-----------IS 73
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSK---------------ELKVLKNVIRKPEPDLNQeealklftalwSS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 74 RLPNIGGNLGYGRQEDAHELMrfaidmmqSVCLDEFGGEKVvpprAQETTLIQYIFGgllqsqvqctacSNVSDQYENMM 153
Cdd:COG5533 66 KEHKVGWIPPMGSQEDAHELL--------GKLLDELKLDLV----NSFTIRIFKTTK------------DKKKTSTGDWF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 154 DLTVE-----IHGDAVSLEECLDQF-------TAKEWLQGDNLYKCDRCDDYVKACKrlsircAPNILTIALKRF-QGGR 220
Cdd:COG5533 122 DIIIElpdqtWVNNLKTLQEFIDNMeelvddeTGVKAKENEELEVQAKQEYEVSFVK------LPKILTIQLKRFaNLGG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 221 FGKLNKRISfpETFDL--GPYMSGGGEGSDVYKLYAVIVHLDMLNAsffGHYICYVKDfRGNWYRIDDSEVEKV---ELE 295
Cdd:COG5533 196 NQKIDTEVD--EKFELpvKHDQILNIVKETYYDLVGFVLHQGSLEG---GHYIAYVKK-GGKWEKANDSDVTPVseeEAI 269
|
330
....*....|....
gi 334184421 296 DVLSQRAYMLLYSR 309
Cdd:COG5533 270 NEKAKNAYLYFYER 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
4-164 |
5.67e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 58.74 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 4 CGLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNdwcflcefeNHLD------RANYSRF---------PFSP 68
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEE---------NPLGmhgsvaSAYADLIkqlydgnlhAFTP 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 69 MNIISRLPNIGGN-LGYgRQEDAHELMRFAIDMM-----------QSVCLDEFGGEKVVPPRAQETT----------LIQ 126
Cdd:COG5560 337 SGFKKTIGSFNEEfSGY-DQQDSQEFIAFLLDGLhedlnriikkpYTSKPDLSPGDDVVVKKKAKECwwehlkrndsIIT 415
|
170 180 190
....*....|....*....|....*....|....*...
gi 334184421 127 YIFGGLLQSQVQCTACSNVSDQYENMMDLTVEIHGDAV 164
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMV 453
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
5-307 |
6.65e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 51.55 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 5 GLTNCGNSCFANVVLQCLSWTRPLVAYLLE----RGHKR----------ECRRNDW-CFLceFENHldranysrfpFSP- 68
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLyenyENIKDrkselvkrlsELIRKIWnPRN--FKGH----------VSPh 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 69 --MNIISRLPNigGNLGYGRQEDAHELMRFAIDMMQSvCLDEFGGEKvvppraqeTTLIQYIFGGLLQsqVQCTACSNVS 146
Cdd:cd02669 189 elLQAVSKVSK--KKFSITEQSDPVEFLSWLLNTLHK-DLGGSKKPN--------SSIIHDCFQGKVQ--IETQKIKPHA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 147 DQYENMMD-----------------LTVEIHGDA-------------VSLEECLDQFTAKEwlqgdnlykcdrCDDYVKA 196
Cdd:cd02669 256 EEEGSKDKffkdsrvkktsvspfllLTLDLPPPPlfkdgneeniipqVPLKQLLKKYDGKT------------ETELKDS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 197 CKRLSIRCAPNILTIALKRFQGGRF-GKLNKRI-SFPET-FDLGPYMSGGGEGSDV---YKLYAVIVHLDMLNASffGHY 270
Cdd:cd02669 324 LKRYLISRLPKYLIFHIKRFSKNNFfKEKNPTIvNFPIKnLDLSDYVHFDKPSLNLstkYNLVANIVHEGTPQED--GTW 401
|
330 340 350
....*....|....*....|....*....|....*...
gi 334184421 271 ICYV-KDFRGNWYRIDDSEVEKVELEDVLSQRAYMLLY 307
Cdd:cd02669 402 RVQLrHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
122-307 |
1.15e-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: 239137 [Multi-domain] Cd Length: 268 Bit Score: 50.20 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 122 TTLIQyIFGGLLQSQVQCTACSNVSDQYENMMDLTV----EIHGDAVSLE------ECLDQFTAKEwlQGDNLYkCDRCD 191
Cdd:cd02672 66 STLIQ-NFTRFLLETISQDQLGTPFSCGTSRNSVSLlytlSLPLGSTKTSkestflQLLKRSLDLE--KVTKAW-CDTCC 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 192 DYVKACKRLSIRCAPNI----LTIALKRFQGGR---------FGKLNKRISFPETFDLGPYMSGGGEGSDVYKLYAVIVH 258
Cdd:cd02672 142 KYQPLEQTTSIRHLPDIlllvLVINLSVTNGEFddinvvlpsGKVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGYVCE 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 334184421 259 LD-----MLNASFFGHYICYVKDFRgnWYRIDDSEVEKVeledvlSQRAYMLLY 307
Cdd:cd02672 222 INdssrgQHNVVFVIKVNEESTHGR--WYLFNDFLVTPV------SELAYILLY 267
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
155-307 |
3.68e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 47.94 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 155 LTVEIHGDavsLEECLDQFTAKEWLQGDnlykcdRCDDYVKACKRLSIRCAPNILTIALKRFQ--GGRFGKLNKRISFPE 232
Cdd:cd02665 87 LQVNGYGN---LHECLEAAMFEGEVELL------PSDHSVKSGQERWFTELPPVLTFELSRFEfnQGRPEKIHDKLEFPQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 233 TFDLGPYmsgggegsdvyKLYAVIVHLDMLNAsffGHYICYV-KDFRGNWYRIDDSEVEKVELEDVLSQ--------RAY 303
Cdd:cd02665 158 IIQQVPY-----------ELHAVLVHEGQANA---GHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDsfgggrnpSAY 223
|
....
gi 334184421 304 MLLY 307
Cdd:cd02665 224 CLMY 227
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
3-307 |
3.43e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 45.95 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 3 PCGLTNCGNSCFANVVLQCLSWTRPLVAYLLE----------------RGHKRECRRNDWCFLCEFENHLdranysRFPF 66
Cdd:cd02666 1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeskaelasdypterRIGGREVSRSELQRSNQFVYEL------RSLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 67 SPMnIISRLPNI--GGNLGYG--RQEDAHELM---RFAIDMMQSVCLDEFGGEKVVPPRAQETTLIQYIFGGLLQSQVQC 139
Cdd:cd02666 75 NDL-IHSNTRSVtpSKELAYLalRQQDVTECIdnvLFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 140 TA--CSNVSDQYENMMDLTVEI---------HGDAVSLEECLDQF---------TAKEWLQGDN----LYKCDRCDDY-- 193
Cdd:cd02666 154 SMgnQPSVRTKTERFLSLLVDVgkkgreivvLLEPKDLYDALDRYfdydsltklPQRSQVQAQLaqplQRELISMDRYel 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184421 194 VKACKRLSIRCAPNILTI-ALKRFQGGRFGKLNKRISfpETFDlgpymsggGEGSDVYKLYAVIVHLDmlNASFfGHYIC 272
Cdd:cd02666 234 PSSIDDIDELIREAIQSEsSLVRQAQNELAELKHEIE--KQFD--------DLKSYGYRLHAVFIHRG--EASS-GHYWV 300
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 334184421 273 YVKDFRGN-WYRIDDSEVEKVELEDVLSQR------AYMLLY 307
Cdd:cd02666 301 YIKDFEENvWRKYNDETVTVVPASEVFLFTlgntatPYFLVY 342
|
|
| |
