|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
440-745 |
7.07e-166 |
|
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: 487.17 E-value: 7.07e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 440 PRGLFNCGNSCYANAVLQCLMCTKPLMIYLLLRLHSKDCCSKNWCLMCELEQYASTLRESGGPVSPSRIL-SNLRNIGCR 518
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 519 LGGGSQEDAHEFLRHLVMSMQGACLDGLGGEKQVEASLQETTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEIHG 598
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 599 WvESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRFQTGKYGKINKCVTFPDMLDMVPFVT 678
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245746 679 GAGDNPPLYFLYAVVVHVDTENasFSGHYISYVKDMQGTWLRIDDSEVQAVSLNQVMSEGAYMLFYM 745
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
441-744 |
6.12e-68 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 229.64 E-value: 6.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 441 RGLFNCGNSCYANAVLQCLMCTKPLMIYLLLRLHSKDCCSKNWC--LMCELEQ--YASTLRESGGPVSPSRILSNLRNIG 516
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 517 CRLGGGSQEDAHEFLRHLvmsmqgacLDGLGGEKQVEASLQETTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEI 596
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFL--------LDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 597 HG-----WVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRFQ--TGKYGKINKCVTFPD 669
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 670 MLDMVPFVTGAGD----NPPLYFLYAVVVHVDTENasfSGHYISYVKDMQ-GTWLRIDDSEVQAVSL-NQVMSEGAYMLF 743
Cdd:pfam00443 233 ELDLSRYLAEELKpktnNLQDYRLVAVVVHSGSLS---SGHYIAYIKAYEnNRWYKFDDEKVTEVDEeTAVLSSSAYILF 309
|
.
gi 1002245746 744 Y 744
Cdd:pfam00443 310 Y 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
442-745 |
4.01e-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: 219.66 E-value: 4.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCtkplmiylllrlhskdccsknwclmceleqyastlresggpvspsrilsnlrnigcrlgg 521
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 522 gSQEDAHEFLRHLVMSMQGACLDGLGGEkqvEASLQETTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEIHGW-- 599
Cdd:cd02257 21 -EQQDAHEFLLFLLDKLHEELKKSSKRT---SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKgl 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 600 -VESLQDALTQFTAPEDLDGENMYKCGRCSaYVKARKQLSVHEVPNILTVVLKRFQ---TGKYGKINKCVTFPDMLDMVP 675
Cdd:cd02257 97 pQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 676 FVT------GAGDNPPLYFLYAVVVHVDTenASFSGHYISYVKDM-QGTWLRIDDSEVQAVSLNQVMSEG-----AYMLF 743
Cdd:cd02257 176 YLSegekdsDSDNGSYKYELVAVVVHSGT--SADSGHYVAYVKDPsDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253
|
..
gi 1002245746 744 YM 745
Cdd:cd02257 254 YE 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
441-744 |
4.91e-63 |
|
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: 216.47 E-value: 4.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 441 RGLFNCGNSCYANAVLQCLMCTKPLMIYLLLRLHSKDC--CSKNWCLMCELEQYASTLRESG--GPVSPSRILSNLRNIG 516
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAMDEIFQEFYYSGdrSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 517 CRLGGGSQEDAHEFLRHLVMSMQGACLDGLGgEKQVEASLQetTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEI 596
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN-EANDESHCN--CIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 597 -----HGWVES---------LQDALTQFTAPEDLdGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRFQ---TGKYG 659
Cdd:cd02660 158 pnkstPSWALGesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 660 KINKCVTFPDMLDMVPFVT-GAGDNPP--------LYFLYAVVVHVDTENasfSGHYISYVKDMQGTWLRIDDSEVQAVS 730
Cdd:cd02660 237 KIDTYVQFPLELNMTPYTSsSIGDTQDsnsldpdyTYDLFAVVVHKGTLD---TGHYTAYCRQGDGQWFKFDDAMITRVS 313
|
330
....*....|....
gi 1002245746 731 LNQVMSEGAYMLFY 744
Cdd:cd02660 314 EEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
5.11e-52 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 183.74 E-value: 5.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKplmiyLLLRLHSKdccsknwclmceleqyastlresggpvSPSRILSNLRNIGCRLGG 521
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTP-----ALRELLSE---------------------------TPKELFSQVCRKAPQFKG 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 522 GSQEDAHEFLRHLvmsmqgacLDGLggekqveaslqeTTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEIHGWVE 601
Cdd:cd02667 49 YQQQDSHELLRYL--------LDGL------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 602 ---SLQDALTQFTAPEDLDGENMYKCGRCSayvKARKQLSVHEVPNILTVVLKRFQTGKYG---KINKCVTFPDMLDMVP 675
Cdd:cd02667 109 secSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 676 FVTGAGDNP-----PLYFLYAVVVHVDTenaSFSGHYISYVKD----------------------MQGTWLRIDDSEVQA 728
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSGT---MRSGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262
|
330
....*....|....*.
gi 1002245746 729 VSLNQVMSEGAYMLFY 744
Cdd:cd02667 263 VSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-747 |
8.99e-52 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 185.15 E-value: 8.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPL--MIYLLLRLHSKDCCSKnwcLMCELEQYASTLRESGGPVSPSRILSNLRNIGCR- 518
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDDDNKS---VPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 519 LGGGSQEDAHEFLRHLVMSMQGaCLDGLGGEKqveaslqettLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEIHG 598
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEE-KLKGTGQEG----------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 599 wVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRF----QTGKYGKINKCVTFPDMLDMV 674
Cdd:cd02659 150 -KKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKINDRFEFPLELDME 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 675 PFvTGAGDNPP------------LYFLYAVVVHvdTENASfSGHYISYVKD-MQGTWLRIDDSEVQAVSLNQVMSE---- 737
Cdd:cd02659 229 PY-TEKGLAKKegdsekkdsesyIYELHGVLVH--SGDAH-GGHYYSYIKDrDDGKWYKFNDDVVTPFDPNDAEEEcfgg 304
|
330 340
....*....|....*....|....*...
gi 1002245746 738 ------------------GAYMLFYMRS 747
Cdd:cd02659 305 eetqktydsgprafkrttNAYMLFYERK 332
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
5.52e-50 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 176.32 E-value: 5.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMctkplmiylllrlhskdccsknwclmceleqyastlresggpvspsrilsnlrnigcrlgg 521
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 522 GSQEDAHEFLRHLvmsmqgacLDGLggekqveaslqeTTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEI----- 596
Cdd:cd02674 20 ADQQDAQEFLLFL--------LDGL------------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsg 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 597 HGWVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRFQT--GKYGKINKCVTFP-DMLDM 673
Cdd:cd02674 80 DAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFsrGSTRKLTTPVTFPlNDLDL 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002245746 674 VPFVTGAGDNPP-LYFLYAVVVHVDTENasfSGHYISYVKD-MQGTWLRIDDSEVQAVSLNQVMSEGAYMLFY 744
Cdd:cd02674 160 TPYVDTRSFTGPfKYDLYAVVNHYGSLN---GGHYTAYCKNnETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
1.23e-40 |
|
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: 152.08 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLM------CTKPLMiylllrlHSKDCCSKNWclmceleqyastlresgGPVSPSRILSNLRNI 515
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYfenlltCLKDLF-------ESISEQKKRT-----------------GVISPKKFITRLKRE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 516 GCRLGGGSQEDAHEFLRHLVMSmqgaCLDGLGGEKQVEASLQ----------ETTLIQQMFGGRLKSKVKCLRCYHESER 585
Cdd:cd02663 57 NELFDNYMHQDAHEFLNFLLNE----IAEILDAERKAEKANRklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 586 YENIMDLTLEIHGWVeSLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRF----QTGKYGKI 661
Cdd:cd02663 133 DETFLDLSIDVEQNT-SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIKL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 662 NKCVTFPdmLDMVPFVTGAGDNPP--LYFLYAVVVHVDteNASFSGHYISYVKdMQGTWLRIDDSEVQAVSLNQVM---- 735
Cdd:cd02663 212 FYRVVFP--LELRLFNTTDDAENPdrLYELVAVVVHIG--GGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeffg 286
|
330
....*....|...
gi 1002245746 736 ----SEGAYMLFY 744
Cdd:cd02663 287 dspnQATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
8.09e-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: 144.49 E-value: 8.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPL--MIYLLlrlhskdccsKNWCLMCELEQYASTLRESGGPVSP-SRILSNLRN---- 514
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFrkAVYEC----------NSTEDAELKNMPPDKPHEPQTIIDQlQLIFAQLQFgnrs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 515 --------IGCRLGGGSQEDAHEFLRhLVMSMQGACLdglggEKQVEASLQetTLIQQMFGGRLKSKVKCLRCYHESERY 586
Cdd:cd02668 71 vvdpsgfvKALGLDTGQQQDAQEFSK-LFLSLLEAKL-----SKSKNPDLK--NIVQDLFRGEYSYVTQCSKCGRESSLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 587 ENIMDLTLEIHGwVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRF----QTGKYGKIN 662
Cdd:cd02668 143 SKFYELELQLKG-HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGAKKKLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 663 KCVTFPDMLDMVPFVTGAGDNPPLYFLYAVVVHVDteNASFSGHYISYVKDMQ-GTWLRIDDSEVQAVSLNQVM------ 735
Cdd:cd02668 222 ASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDEQtGEWYKFNDEDVEEMPGKPLKlgnsed 299
|
330 340
....*....|....*....|....
gi 1002245746 736 ---------------SEGAYMLFY 744
Cdd:cd02668 300 pakprkseikkgthsSRTAYMLVY 323
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
3.52e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 139.93 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPL-MIYLLLRLHSKDCCSknwCLMCELEQYASTL----RESGGPvsPSRILSNLRNIG 516
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFrRQVLSLNLPRLGDSQ---SVMKKLQLLQAHLmhtqRRAEAP--PDYFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 517 crLGGGSQEDAHEFLRHLvmsmqgacLDGLggekqveaslqeTTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEi 596
Cdd:cd02664 76 --FTPGSQQDCSEYLRYL--------LDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLS- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 597 hgwVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRFQ----TGKYGKINKCVTFPDMLD 672
Cdd:cd02664 133 ---FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkTHVREKIMDNVSINEVLS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 673 MVPFVTGAGDNPPL-------------------YFLYAVVVHVDTenASFSGHYISYV---------------------K 712
Cdd:cd02664 210 LPVRVESKSSESPLekkeeesgddgelvtrqvhYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqecpepkdaeeN 287
|
330 340 350
....*....|....*....|....*....|....*....
gi 1002245746 713 DMQGTWLRIDDSEVQAVSLNQVM-------SEGAYMLFY 744
Cdd:cd02664 288 DESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
1.56e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 126.55 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLmCTKPLMIYLLLRLHSKDCCSKNWCLMCEL--EQYASTLRESggpvSPSRILSNLRNIGCRL 519
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVL-YFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDELANQ----APRRLLNALREVNPMY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 520 GGGSQEDAHEFLRHLVMSMQgacldglggekqveaslqetTLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTL----- 594
Cdd:cd02671 101 EGYLQHDAQEVLQCILGNIQ--------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVpvqes 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 595 EIHGWVES-------------LQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLKRF-----QTG 656
Cdd:cd02671 161 ELSKSEESseispdpktemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFaangsEFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 657 KYGKINKCVTF-PDMLDMVPFVTGAGDNPPLYFLYAVVVHVDTENAsfSGHYISYVKdmqgtWLRIDDSEVQ-------- 727
Cdd:cd02671 241 CYGGLSKVNTPlLTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATIS--SGHYTAYVR-----WLLFDDSEVKvteekdfl 313
|
330
....*....|....*...
gi 1002245746 728 -AVSLNQVMSEGAYMLFY 744
Cdd:cd02671 314 eALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
1.96e-29 |
|
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: 119.36 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCL-MCTKPLMIYLLLRLHSKDCCSKNWCLMCELEQYASTLRESGGPVSPSRILSNLRNigC--- 517
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLrSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRM--Afpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 518 -----RLGGGSQEDAHEFLRHLVMSMQgACLDGLGGEKQVeaslqettlIQQMFGGRLKSKVKCLRCYHESE---RYENI 589
Cdd:cd02657 79 faekqNQGGYAQQDAEECWSQLLSVLS-QKLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEEEvstESEYK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 590 MDLTLEIHGWVESLQDALTQftAPEDLDGENMYKCGRCSAYVKARKqlsVHEVPNILTVVLKRF----QTGKYGKINKCV 665
Cdd:cd02657 149 LQCHISITTEVNYLQDGLKK--GLEEEIEKHSPTLGRDAIYTKTSR---ISRLPKYLTVQFVRFfwkrDIQKKAKILRKV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 666 TFPDMLDMVPFVTGAGdnppLYFLYAVVVHvDTENASfSGHYISYVK-DMQGTWLRIDDSEVQAVSLNQV--MSEG---- 738
Cdd:cd02657 224 KFPFELDLYELCTPSG----YYELVAVITH-QGRSAD-SGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDIlkLSGGgdwh 297
|
....*..
gi 1002245746 739 -AYMLFY 744
Cdd:cd02657 298 iAYILLY 304
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
442-746 |
1.86e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.81 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPL--MIYLLlrlhSKDCCSKNWCLMCELEQYASTLRESGGPVSPSRILSNlrNIGCRL 519
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGI----PTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRS--FGWDSD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 520 GGGSQEDAHEFLRHLvmsmqgacLDGLggEKQVEASLQETTLiQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEIHGw 599
Cdd:COG5077 269 DSFMQHDIQEFNRVL--------QDNL--EKSMRGTVVENAL-NGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 600 VESLQDALTQFTAPEDLDGENMYKCGRcSAYVKARKQLSVHEVPNILTVVLKRFQ----TGKYGKINKCVTFPDMLDMVP 675
Cdd:COG5077 337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLLP 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 676 FVTGAGD----NPPLYFLYAVVVHV-DTENasfsGHYISYVK-DMQGTWLRIDDSEVQAVSLNQVMSE------------ 737
Cdd:COG5077 416 FLDRDADksenSDAVYVLYGVLVHSgDLHE----GHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491
|
330
....*....|....*....
gi 1002245746 738 ----------GAYMLFYMR 746
Cdd:COG5077 492 rdhsgikrfmSAYMLVYLR 510
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
6.53e-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: 104.37 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPLMIYLllrlhskdccskNWCLmceleqyastlresggpvspsrilsnlrnigcrlgg 521
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL------------EEFL------------------------------------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 522 gSQEDAHEFLRHLVmsmqgacldglggekqveaslqeTTLIQQM---FGGRLKSKVKCLRCYHESE-RYENIMDLTLEI- 596
Cdd:cd02662 33 -EQQDAHELFQVLL-----------------------ETLEQLLkfpFDGLLASRIVCLQCGESSKvRYESFTMLSLPVp 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 597 -HGWVE--SLQDALTQFTAPEDLDGenmYKCGRCsayvkarkQLSVHEVPNILTVVLKRFQTGKYGKI--NKC-VTFPDM 670
Cdd:cd02662 89 nQSSGSgtTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFDGRGTStkNSCkVSFPER 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 671 LdmvpfvtgagdNPPLYFLYAVVVHVDTENasfSGHYISY------VKDMQG---------------TWLRIDDSEVQAV 729
Cdd:cd02662 158 L-----------PKVLYRLRAVVVHYGSHS---SGHYVCYrrkplfSKDKEPgsfvrmregpsstshPWWRISDTTVKEV 223
|
330
....*....|....*.
gi 1002245746 730 SLNQVMSEG-AYMLFY 744
Cdd:cd02662 224 SESEVLEQKsAYMLFY 239
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-744 |
9.14e-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: 105.87 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPLMIYLLLRLHSKDCCSKN--WCLMCELEQYASTLREsgGPVSPSRILS---NLRNIG 516
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKLADGLLS--GRYSKPASLKsenDPYQVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 517 CR-------LGGGSQE-------DAHEFLRHLvmsmqgacLDGLGGEKQVEASLQETTLIQQMFGGRLkskvKCLRCYH- 581
Cdd:cd02658 79 IKpsmfkalIGKGHPEfstmrqqDALEFLLHL--------IDKLDRESFKNLGLNPNDLFKFMIEDRL----ECLSCKKv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 582 -ESERYENIMDLTLEIHGWVES-----------LQDALTQFTAPEDLDgenmYKCGRCSAYVKARKQLSVHEVPNILTVV 649
Cdd:cd02658 147 kYTSELSEILSLPVPKDEATEKeegelvyepvpLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVIN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 650 LKRFQTGKYG---KINKCVTFPDMLDmvpfvtgagdnPPLYFLYAVVVHVDTenASFSGHYISYVK---DMQGTWLRIDD 723
Cdd:cd02658 223 MKRFQLLENWvpkKLDVPIDVPEELG-----------PGKYELIAFISHKGT--SVHSGHYVAHIKkeiDGEGKWVLFND 289
|
330 340
....*....|....*....|.
gi 1002245746 724 SEVQAVSLNQVMSEGAYMLFY 744
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
442-733 |
8.13e-21 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 94.26 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPlmIYLLLRLHSKDCCSKNWCLMCEL------EQYAstlreSGGPVSPS---RILSNL 512
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPP--LRNLALSHLATECLKEHCLLCELgflfdmLEKA-----KGKNCQASnflRALSSI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 513 R---NIGcRLGGGSQEDAHEFLRHLVMSMQGACLDGLG--GEKQVEASLQETTLIQQMFGGRLKSKVKCLRCYHESERYE 587
Cdd:pfam13423 75 PeasALG-LLDEDRETNSAISLSSLIQSFNRFLLDQLSseENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 588 NIMDLTLEIHGWVESLQDALTQFTAPEDL----DGENMYK--CGRCSAYVKARKQLSVHEVPNILTVVLKrFQTGKYGKI 661
Cdd:pfam13423 154 STHVLDLIYPRKPSSNNKKPPNQTFSSILksslERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAA-LTNEEWRQL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002245746 662 NKCVTF-PDMLDMVPFVTGAGDNPP-LYFLYAVVVHVDteNASFSGHYISYVKdmqgtwlrIDDSEVQAVSLNQ 733
Cdd:pfam13423 233 WKTPGWlPPEIGLTLSDDLQGDNEIvKYELRGVVVHIG--DSGTSGHLVSFVK--------VADSELEDPTESQ 296
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
579-746 |
1.09e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 91.48 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 579 CYHESERYENIMDL-------TLEIHGWVESLQDALTQFTAPEDLDGENMYKCGRCSAYVKARKQLSVHEVPNILTVVLK 651
Cdd:COG5560 646 CEWEEKRYLSLFSYdplwtirEIGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLK 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 652 RFQTGKYG--KINKCVTFP-DMLDMVPFVTGAGDNPPLYFLYAvvvhVDTENASFS-GHYISYVKDMQ-GTWLRIDDSEV 726
Cdd:COG5560 726 RFSSVRSFrdKIDDLVEYPiDDLDLSGVEYMVDDPRLIYDLYA----VDNHYGGLSgGHYTAYARNFAnNGWYLFDDSRI 801
|
170 180
....*....|....*....|
gi 1002245746 727 QAVSLNQVMSEGAYMLFYMR 746
Cdd:COG5560 802 TEVDPEDSVTSSAYVLFYRR 821
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
442-746 |
7.74e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.08 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 442 GLFNCGNSCYANAVLQCLMCTKPLMIYLLLRL----------HSKDCCSKNWCLMCEL-EQYASTLRESGGPVSPSrils 510
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLskelkvlknvIRKPEPDLNQEEALKLfTALWSSKEHKVGWIPPM---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 511 nlrnigcrlggGSQEDAHEFLrhlvmsmqGACLDGLGGEK--QVEASLQETTliqqmfggrlKSKVKCLrcyheserYEN 588
Cdd:COG5533 77 -----------GSQEDAHELL--------GKLLDELKLDLvnSFTIRIFKTT----------KDKKKTS--------TGD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 589 IMDLTLE--IHGWVE---SLQDALTQFTapEDLDGENMYKCGRC-SAYVKARKQ--LSVHEVPNILTVVLKRFQT-GKYG 659
Cdd:COG5533 120 WFDIIIElpDQTWVNnlkTLQEFIDNME--ELVDDETGVKAKENeELEVQAKQEyeVSFVKLPKILTIQLKRFANlGGNQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 660 KINKCVTFPdmLDMvPFVTGA--GDNPPLYF-LYAVVVHVDTENasfSGHYISYVKdMQGTWLRIDDSEVQAVSLNQ--- 733
Cdd:COG5533 198 KIDTEVDEK--FEL-PVKHDQilNIVKETYYdLVGFVLHQGSLE---GGHYIAYVK-KGGKWEKANDSDVTPVSEEEain 270
|
330
....*....|...
gi 1002245746 734 VMSEGAYMLFYMR 746
Cdd:COG5533 271 EKAKNAYLYFYER 283
|
|
| zf-MYND |
pfam01753 |
MYND finger; |
88-125 |
1.30e-10 |
|
MYND finger;
Pssm-ID: 460312 Cd Length: 39 Bit Score: 57.04 E-value: 1.30e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1002245746 88 CATCHGPAKT--RCSRCKSVRYCSGKCQIIHWRQgHKQTC 125
Cdd:pfam01753 1 CAVCGKEALKllRCSRCKSVYYCSKECQKADWPY-HKKEC 39
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
432-596 |
9.32e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 59.51 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 432 QYEVRGISPRGLFNCGNSCYANAVLQCLMCTKPLMIYLLLRLHSKDCCSKN-WCLMCELEQ-YASTLRESGGP----VSP 505
Cdd:COG5560 257 RSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENpLGMHGSVASaYADLIKQLYDGnlhaFTP 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 506 SRILSNLRNIGCRLGGGSQEDAHEFLRHLvmsmqgacLDGL--------------------GGEKQVEASLQET------ 559
Cdd:COG5560 337 SGFKKTIGSFNEEFSGYDQQDSQEFIAFL--------LDGLhedlnriikkpytskpdlspGDDVVVKKKAKECwwehlk 408
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002245746 560 ---TLIQQMFGGRLKSKVKCLRCYHESERYENIMDLTLEI 596
Cdd:COG5560 409 rndSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-744 |
1.80e-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: 53.30 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 443 LFNCGNSCYANAVLQCLmctkplmiylllrlhskdccsknwclmceleqyastlresggpVSPSRILSNLRNigcrlggG 522
Cdd:cd02673 2 LVNTGNSCYFNSTMQAL-------------------------------------------SSIGKINTEFDN-------D 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 523 SQEDAHEFLRHLVmsmqgACLDGLggeKQVEASLQETTLIQ-------QMFGGRLKSKVKCLRCYHESERYE-------N 588
Cdd:cd02673 32 DQQDAHEFLLTLL-----EAIDDI---MQVNRTNVPPSNIEikrlnplEAFKYTIESSYVCIGCSFEENVSDvgnfldvS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 589 IMDLTLEIhgwVESLQDALTQFTAPEdldgENMYKCGRCSAYVKARkqlsVHEVPNILTVVLKRFQ----TGKYGKINKc 664
Cdd:cd02673 104 MIDNKLDI---DELLISNFKTWSPIE----KDCSSCKCESAISSER----IMTFPECLSINLKRYKlriaTSDYLKKNE- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 665 vtfpdmLDMVPFVTgagdNPPLYFLYAVVVHV-DTENAsfsGHYISYVKDMQG--TWLRIDDSEVQAVSLNQVMSE---G 738
Cdd:cd02673 172 ------EIMKKYCG----TDAKYSLVAVICHLgESPYD---GHYIAYTKELYNgsSWLYCSDDEIRPVSKNDVSTNarsS 238
|
....*.
gi 1002245746 739 AYMLFY 744
Cdd:cd02673 239 GYLIFY 244
|
|
| zf-HIT_ZNHIT1_like |
cd21437 |
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ... |
79-116 |
6.03e-06 |
|
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar proteins; The family includes ZNHIT1 and its yeast counterpart, the vacuolar protein sorting-associated protein 71 (Vps71p). ZNHIT1, also known as cyclin-G1-binding protein 1 (CGBP1), zinc finger protein subfamily 4A member 1 (ZNFN4A1), or p18 Hamlet, may have a role in inducing apoptosis through p53 signaling. It binds to Rev-erb beta and releases its inhibitory effect on the transcription of apolipoprotein C3 (APOC3) without affecting its DNA-binding activity. The yeast counterpart Vps71p, also referred to as SWR complex protein 6 (Swc6p), plays a role in the exchange of histone H2A for the H2A variant HZT1, a euchromatin-specific factor, leading to chromatin remodeling and transcriptional changes of targeted genes. It is indirectly involved in vacuolar protein sorting. Members of this family contain a zf-HIT domain characterized by a "treble-clef" fold through interleaved CCCC and CCHC zinc finger motifs, both of which bind a zinc ion.
Pssm-ID: 467791 Cd Length: 43 Bit Score: 44.15 E-value: 6.03e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1002245746 79 PSARPEYHECATCHGPAKTRCSRCkSVRYCSGKCQIIH 116
Cdd:cd21437 1 PSRLPPRKFCSVCGYWGKYTCVRC-GARYCSLKCLETH 37
|
|
| zf-HIT_ZNHIT2-3 |
cd23024 |
zinc finger HIT (zf-HIT) found in zinc finger HIT domain-containing protein 2 (ZNHIT2), 3 ... |
88-125 |
4.73e-03 |
|
zinc finger HIT (zf-HIT) found in zinc finger HIT domain-containing protein 2 (ZNHIT2), 3 (ZNHIT3) and similar proteins; ZNHIT2 and ZNHIT3 are members of the zf-HIT domain-containing protein family that play crucial roles in various biological processes. ZNHIT2 acts as a bridging factor between the R2TP/PFDL complex and U5 snRNP, while ZNHIT3 interacts specifically with the ligand binding domain of the thyroid receptor and is involved in small nucleolar ribonucleoprotein particle assembly, transcriptional regulation, and snoRNP assembly. ZNHIT3 is also associated with HNF-4alpha and may play a role in MODY, while its dysfunction is linked to PEHO syndrome. Both proteins contain the zf-HIT domain and interact with other proteins through their HIT-type zinc finger in the presence of ATP, ADP, or other factors.
Pssm-ID: 467796 [Multi-domain] Cd Length: 37 Bit Score: 35.70 E-value: 4.73e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1002245746 88 CATCH-GPAKTRCSRCkSVRYCSGKCqiihWRQgHKQTC 125
Cdd:cd23024 3 CGVCNkNESKYKCPRC-NIPYCSLAC----YKS-HKESC 35
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
641-744 |
5.03e-03 |
|
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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 39.82 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245746 641 EVPNILTVVLKRF--QTGKYGKINKCVTFPDMLDMVPFVTGAG-----------------DNPPLYF-----LYAVVVHv 696
Cdd:cd02670 97 KAPSCLIICLKRYgkTEGKAQKMFKKILIPDEIDIPDFVADDPracskcqlecrvcyddkDFSPTCGkfklsLCSAVCH- 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002245746 697 dTENASFSGHYISYVK------------DMQGTWLRIDDSEVQAVSLNQV------MSEGAYMLFY 744
Cdd:cd02670 176 -RGTSLETGHYVAFVRygsysltetdneAYNAQWVFFDDMADRDGVSNGFnipaarLLEDPYMLFY 240
|
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