|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
363-704 |
1.31e-155 |
|
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: 453.37 E-value: 1.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 363 RGLINLGNTCFMNCIVQALTHIPLLKDFFLSDKHK--CIMTSPSLCLVCEMSSLFHAM-YSGSRTPHIPYKLLHLIWIHA 439
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSctCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 440 EHLAGYRQQDAHEFLIAILDVLHRHSKDDSGgqEANNPNCCNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDLP 519
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKN--EANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 520 gscatfdsqnPERADSTVSRDDHIPGIPSLTDCLQWFTRPEHLGSSAkIKCNSCQSYQESTKQLTMKKLPIVACFHLKRF 599
Cdd:cd02660 159 ----------NKSTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 600 EH-VGKQRRKINTFISFPLELDMTPFLASTKESRMKEGQPPTDCvpnenKYSLFAVINHHGTLESGHYTSFIRQQKDQWF 678
Cdd:cd02660 228 EHsLNKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSNSLDPDY-----TYDLFAVVVHKGTLDTGHYTAYCRQGDGQWF 302
|
330 340
....*....|....*....|....*.
gi 1034673623 679 SCDDAIITKATIEDLLYSEGYLLFYH 704
Cdd:cd02660 303 KFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
363-703 |
1.51e-83 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 267.00 E-value: 1.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 363 RGLINLGNTCFMNCIVQALTHIPLLKDFFLSDKH--KCIMTSPSLCLVCEMSSLFHAMYSGSRTPHI-PYKLLHLIWIHA 439
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPlsEDSRYNKDINLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 440 EHLAGYRQQDAHEFLIAILDVLHRHSKddsggqeANNPNCCNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDLP 519
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN-------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 520 GscatfdsqnperadstvsrDDHIPGIPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHLKRF 599
Cdd:pfam00443 154 G-------------------DSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 600 EHVGKQRRKINTFISFPLELDMTPFLASTKESRMKEGQpptdcvpnenKYSLFAVINHHGTLESGHYTSFIRQQKD-QWF 678
Cdd:pfam00443 215 SYNRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQ----------DYRLVAVVVHSGSLSSGHYIAYIKAYENnRWY 284
|
330 340
....*....|....*....|....*.
gi 1034673623 679 SCDDAIITKATIE-DLLYSEGYLLFY 703
Cdd:pfam00443 285 KFDDEKVTEVDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
363-703 |
1.65e-71 |
|
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: 234.86 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 363 RGLINLGNTCFMNCIVQALTHIPLLKDFFLSDKHKCIMTSPSLCLVCEMSSLFHAMYSGSRTPHIPYKLLHLIWIHAEHL 442
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 443 AGYRQQDAHEFLIAILDVLHRHSKDDSGGQEANNPNC-CNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDlpgs 521
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSqETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 522 catfdsqnperadstvsrddhIPGIPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHLKRFEh 601
Cdd:cd02661 158 ---------------------IKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 602 vGKQRRKINTFISFPLELDMTPFLAStkesrmKEGQPPtdcvpnenKYSLFAVINHHGT-LESGHYTSFIRQQKDQWFSC 680
Cdd:cd02661 216 -NFRGGKINKQISFPETLDLSPYMSQ------PNDGPL--------KYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYNM 280
|
330 340
....*....|....*....|...
gi 1034673623 681 DDAIITKATIEDLLYSEGYLLFY 703
Cdd:cd02661 281 DDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
364-703 |
5.47e-68 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 223.90 E-value: 5.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHipllkdfflsdkhkcimtspslclvcemsslfhamysgsrtphipykllhliwihaehla 443
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 444 gyRQQDAHEFLIAILDVLHRHSKDDSGGQEANNPNccNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDLPGSca 523
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL--KSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVK-- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 524 tfdsqnperadstvsrddhIPGIPSLTDCLQWFTRPEHLGSSAKIKCnSCQSYQESTKQLTMKKLPIVACFHLKRFEHVG 603
Cdd:cd02257 95 -------------------GLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNE 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 604 K-QRRKINTFISFPLELDMTPFlastkesrMKEGQPPTDCVPNENKYSLFAVINHHGTL-ESGHYTSFIRQQ-KDQWFSC 680
Cdd:cd02257 155 DgTKEKLNTKVSFPLELDLSPY--------LSEGEKDSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYKF 226
|
330 340
....*....|....*....|....*...
gi 1034673623 681 DDAIITKATIEDLLY-----SEGYLLFY 703
Cdd:cd02257 227 NDDKVTEVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
4.00e-67 |
|
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: 220.62 E-value: 4.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHipllkdfflsdkhkcimtspslclvcemsslfhamysgsrtphipykllhliwihaehla 443
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 444 gyRQQDAHEFLIAILDVLHRhskddsggqeannpnccncIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDLPgsca 523
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP---- 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 524 tfdsqnperadstvSRDDHIPGIpSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHLKRFEHVG 603
Cdd:cd02674 76 --------------SGSGDAPKV-TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 604 KQRRKINTFISFPLE-LDMTPFLASTkesrmkegqpptdCVPNENKYSLFAVINHHGTLESGHYTSFIR-QQKDQWFSCD 681
Cdd:cd02674 141 GSTRKLTTPVTFPLNdLDLTPYVDTR-------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKnNETNDWYKFD 207
|
330 340
....*....|....*....|..
gi 1034673623 682 DAIITKATIEDLLYSEGYLLFY 703
Cdd:cd02674 208 DSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-706 |
6.55e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 180.53 E-value: 6.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 361 GLRGLINLGNTCFMNCIVQALTHIPLLKDFFLSDKHKcIMTSPSLCLVCEMSSLFHAMYSgSRTPHIPYKLLHLI----W 436
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQL-SESPVKTTELTDKTrsfgW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 437 ihaEHLAGYRQQDAHEFLIAILDVLHRHSKDDsgGQEAnnpnccncIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISL 516
Cdd:cd02659 79 ---DSLNTFEQHDVQEFFRVLFDKLEEKLKGT--GQEG--------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 517 DlpgscatfdsqnperadstvsrddhIPGIPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHL 596
Cdd:cd02659 146 A-------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 597 KRFEH--VGKQRRKINTFISFPLELDMTPFlasTKESRMKEGQPPTDCVPNENKYSLFAVINHHGTLESGHYTSFIRQQ- 673
Cdd:cd02659 201 KRFEFdfETMMRIKINDRFEFPLELDMEPY---TEKGLAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRd 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034673623 674 KDQWFSCDDAIITKATIEDLL----------------------YSEGYLLFYHKQ 706
Cdd:cd02659 278 DGKWYKFNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
1.45e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 172.19 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPLLKDFFLSdkhkcimtSPSLCL--VCEMSSLFHamysgsrtphipykllhliwihaeh 441
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------TPKELFsqVCRKAPQFK------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 442 laGYRQQDAHEFLIAILDVLhrhskddsggqeannpnccNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLdlpgs 521
Cdd:cd02667 48 --GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSL----- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 522 catfdsQNPERADSTVsrddhipgipSLTDCLQWFTRPEHLGSSAKIKCNSCqsyQESTKQLTMKKLPIVACFHLKRFEH 601
Cdd:cd02667 102 ------PRSDEIKSEC----------SIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQ 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 602 VGKQR-RKINTFISFPLELDMTPFLASTKESRMKEGQPptdcvpnenKYSLFAVINHHGTLESGHYTSFIR----QQ--- 673
Cdd:cd02667 163 PRSANlRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSV---------LYRLYGVVEHSGTMRSGHYVAYVKvrppQQrls 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034673623 674 ---------------KDQWFSCDDAIITKATIEDLLYSEGYLLFY 703
Cdd:cd02667 234 dltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
3.69e-39 |
|
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: 146.69 E-value: 3.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPL---LKDFFlsdkhKCIMTSPSLCLVCEmsslfhamysgsrtphiPYKLLHLIWIHAE 440
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLltcLKDLF-----ESISEQKKRTGVIS-----------------PKKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 441 HLAGYRQQDAHEFL-------IAILDVLHRHSKDDSGGQEANNPNCCNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWD 513
Cdd:cd02663 59 LFDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 514 ISLDLPGSCatfdsqnperadstvsrddhipgipSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVAC 593
Cdd:cd02663 139 LSIDVEQNT-------------------------SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 594 FHLKRFEHVGKQRRKINTF--ISFPLELdmtpflastkesRMKEgqPPTDCVPNENKYSLFAVINHHG-TLESGHYTSFI 670
Cdd:cd02663 194 LHLKRFKYDEQLNRYIKLFyrVVFPLEL------------RLFN--TTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIV 259
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034673623 671 RqQKDQWFSCDDAIITK---ATIEDLLY-----SEGYLLFY 703
Cdd:cd02663 260 K-SHGGWLLFDDETVEKideNAVEEFFGdspnqATAYVLFY 299
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
356-703 |
4.10e-36 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 145.80 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 356 SVYTVGLRGLINLGNTCFMNCIVQALTHIPLLKDFFLSDK---------HKCIMTSpslcLVCEMSSLFHAMYSGSRTPH 426
Cdd:COG5560 259 INKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeesineenPLGMHGS----VASAYADLIKQLYDGNLHAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 427 IPYKLLHLIWIHAEHLAGYRQQDAHEFLIAILDVLHR-----------HSKDDSGGQEA---NNPNCC-------NC-II 484
Cdd:COG5560 335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytSKPDLSPGDDVvvkKKAKECwwehlkrNDsII 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 485 DQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDLPGSCA---------TFDSQNP------------------------- 530
Cdd:COG5560 415 TDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtivvfpESGRRQPlkieldasstirglkklvdaeygkl 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 531 -------------------ERADSTVSRDDH----------------IP----------------GIPSLT--------- 550
Cdd:COG5560 495 gcfeikvmciyyggnynmlEPADKVLLQDIPqtdfvylyetndngieVPvvhlriekgykskrlfGDPFLQlnvlikasi 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 --------------------------------------------------------------------------------
Cdd:COG5560 575 ydklvkefeellvlvemkktdvdlvseqvrllreesspsswlkleteidtkreeqveeegqmnfndavvisceweekryl 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 551 ------------------------DCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHLKRFEHVGKQR 606
Cdd:COG5560 655 slfsydplwtireigaaertitlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFR 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 607 RKINTFISFPL-ELDMTPFLASTKESRMkegqpptdcvpnenKYSLFAVINHHGTLESGHYTSFIRQQKDQ-WFSCDDAI 684
Cdd:COG5560 735 DKIDDLVEYPIdDLDLSGVEYMVDDPRL--------------IYDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFDDSR 800
|
570
....*....|....*....
gi 1034673623 685 ITKATIEDLLYSEGYLLFY 703
Cdd:COG5560 801 ITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
1.16e-35 |
|
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: 137.07 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPLLKDFFLSDKHK--CIMTSPSLCLVCEMSSLFHAMYSG-------SRTPHIPYK---- 430
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpSDVVDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 431 ---LLHLIWI-HAEHLAGyRQQDAHEFLIAILDVLHRHSKDDSGgqeaNNPNccnciidQIFTGGLQSDVTCQACHSVST 506
Cdd:cd02658 81 psmFKALIGKgHPEFSTM-RQQDALEFLLHLIDKLDRESFKNLG----LNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 507 TIDPCWDISLDLPGSCATfDSQNPERADSTVsrddhipgipSLTDCLQWFTRPEHLgssaKIKCNSCQSYQESTKQLTMK 586
Cdd:cd02658 149 TSELSEILSLPVPKDEAT-EKEEGELVYEPV----------PLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 587 KLPIVACFHLKRFE-HVGKQRRKINTFISFPLELDmtpflastkesrmkegqPPtdcvpnenKYSLFAVINHHGT-LESG 664
Cdd:cd02658 214 TFPDYLVINMKRFQlLENWVPKKLDVPIDVPEELG-----------------PG--------KYELIAFISHKGTsVHSG 268
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034673623 665 HYTSFIRQ---QKDQWFSCDDAIITKATIEDLLYSEGYLLFY 703
Cdd:cd02658 269 HYVAHIKKeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
3.35e-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: 124.62 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPllkDFFLSDKHKC--IMTSPSLCLVCEmssLFHAMYSGSRTPHIPYKLLHLIWIHAEH 441
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVslISSVEQLQSSFL---LNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 442 LAGYRQQDAHEFLIAILdvlhrhskddsggqeannpNCCNCIIDQIFTGGLQSDVTCQACHSVSTTIDPCWDISLDLPgs 521
Cdd:cd02671 100 YEGYLQHDAQEVLQCIL-------------------GNIQELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQ-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 522 catfDSQNPERADSTVSRDDHIPGIPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHLKRFEH 601
Cdd:cd02671 159 ----ESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 602 VGKQR------RKINTFISFPLELDMtpFLASTKESRmkegqpptdcvpneNKYSLFAVINHHG-TLESGHYTSFIRqqk 674
Cdd:cd02671 235 NGSEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN--------------DVYRLFAVVMHSGaTISSGHYTAYVR--- 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034673623 675 dqWFSCDDAIITKATIEDLL---------YSEGYLLFY 703
Cdd:cd02671 296 --WLLFDDSEVKVTEEKDFLealspntssTSTPYLLFY 331
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
235-703 |
1.42e-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 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: 122.43 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 235 ICHVCSTHMNrLHSCLSC--VFFGCFTEKHIHKHAETKQHHLAVDLYHGVIYCFMCKDYVYDKDIEQIA-----KETKEK 307
Cdd:cd02669 18 VCSVSLSNLN-VYACLVCgkYFQGRGKGSHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIDSSLDDIKyvlnpTYTKEQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 308 ILRLltststdvSHQQFMTSGFEDKQstcetkeqepklvkpkkkrrkksvYTVGLRGLINLGNTCFMNCIVQALTHIPLL 387
Cdd:cd02669 97 ISDL--------DRDPKLSRDLDGKP------------------------YLPGFVGLNNIKNNDYANVIIQALSHVKPI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 388 KDFFLS-DKHKCIMTSPSLcLVCEMSSLFHAMYSgsrtPHI------PYKLLHLIWIHAEHLAGYRQQ-DAHEFLIAILD 459
Cdd:cd02669 145 RNFFLLyENYENIKDRKSE-LVKRLSELIRKIWN----PRNfkghvsPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 460 VLHRhskdDSGGQEANNPNccncIIDQIFTGGLQ-----------SDVTCQACHS----VSTTIDPCWDISLDLPgscat 524
Cdd:cd02669 220 TLHK----DLGGSKKPNSS----IIHDCFQGKVQietqkikphaeEEGSKDKFFKdsrvKKTSVSPFLLLTLDLP----- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 525 fdsQNPERADSTvsRDDHIPGIPsLTDCLQWFTrpehlGSsakikcnSCQSYQESTKQLTMKKLPIVACFHLKRFEHVGK 604
Cdd:cd02669 287 ---PPPLFKDGN--EENIIPQVP-LKQLLKKYD-----GK-------TETELKDSLKRYLISRLPKYLIFHIKRFSKNNF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 605 QRRKINTFISFPLE-LDMTPFLASTKESrmkeGQPPTdcvpnenKYSLFAVINHHGT-LESGHYTSFIRQQK-DQWFSCD 681
Cdd:cd02669 349 FKEKNPTIVNFPIKnLDLSDYVHFDKPS----LNLST-------KYNLVANIVHEGTpQEDGTWRVQLRHKStNKWFEIQ 417
|
490 500
....*....|....*....|..
gi 1034673623 682 DAIITKATIEDLLYSEGYLLFY 703
Cdd:cd02669 418 DLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-690 |
1.63e-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 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: 119.83 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTH-IPLLKDFFLsdkhkcimtspslclvCEMSSLFHAMYSGSRTPHIPYKLL-HLIWIHAEH 441
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMnLEFRKAVYE----------------CNSTEDAELKNMPPDKPHEPQTIIdQLQLIFAQL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 442 LAGYR------------------QQDAHEFLIAILDVLhrhskdDSGGQEANNPNCCNcIIDQIFTGGLQSDVTCQACHS 503
Cdd:cd02668 65 QFGNRsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLL------EAKLSKSKNPDLKN-IVQDLFRGEYSYVTQCSKCGR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 504 VSTTIDPCWDISLDLPGScatfdsqnperadstvsrddhipgiPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQL 583
Cdd:cd02668 138 ESSLPSKFYELELQLKGH-------------------------KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 584 TMKKLPIVACFHLKRFEHVGK--QRRKINTFISFPLELDMTPFLAstkesrmkeGQPPTDCVpnenkYSLFAVINHHGT- 660
Cdd:cd02668 193 RLTTLPPTLNFQLLRFVFDRKtgAKKKLNASISFPEILDMGEYLA---------ESDEGSYV-----YELSGVLIHQGVs 258
|
330 340 350
....*....|....*....|....*....|.
gi 1034673623 661 LESGHYTSFIR-QQKDQWFSCDDAIITKATI 690
Cdd:cd02668 259 AYSGHYIAHIKdEQTGEWYKFNDEDVEEMPG 289
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
1.44e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 107.80 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPLLKDFFLSDKHKCIMTS-PSLCLVCEMSSLFHAMySGSRTPHIPYKLLHLIWIHAEHL 442
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANqSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 443 A------GYRQQDAHEFLIAILDVLhRHSKDDSGGQEANnpnccnciIDQIFTGGLQSDVTCQAC-HSVSTTIDPcwDIS 515
Cdd:cd02657 80 AekqnqgGYAQQDAEECWSQLLSVL-SQKLPGAGSKGSF--------IDQLFGIELETKMKCTESpDEEEVSTES--EYK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 516 LdlpgSCATFDSQNperadstvsrddhipgIPSLTDCLQwftrpehLGSSAKIKCNSCQSYQES--TKQLTMKKLPIVAC 593
Cdd:cd02657 149 L----QCHISITTE----------------VNYLQDGLK-------KGLEEEIEKHSPTLGRDAiyTKTSRISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 594 FHLKRFEHVGK--QRRKINTFISFPLELDMTPFLASTkesrmkegqpptdcvpneNKYSLFAVINHHG-TLESGHYTSFI 670
Cdd:cd02657 202 VQFVRFFWKRDiqKKAKILRKVKFPFELDLYELCTPS------------------GYYELVAVITHQGrSADSGHYVAWV 263
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034673623 671 RQ-QKDQWFSCDDAIITKATIEDLLYSEG-------YLLFY 703
Cdd:cd02657 264 RRkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
2.32e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 107.58 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALThipLLKDF---FLSdKHKCIMTSPSLCLVCEMSSLFHAMYSGSRTPHIPYKLLHLIWihAE 440
Cdd:cd02664 1 GLINLGNTCYMNSVLQALF---MAKDFrrqVLS-LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR--PP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 441 HLAGYRQQDAHEFLIAILDVLHrhskddsggqeannpnccnCIIDQIFTGGLQSDVTCQACHSVSTTID--PCWDISLdl 518
Cdd:cd02664 75 WFTPGSQQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 519 pgscatfdsqnperadstvsrddhipgiPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKKLPIVACFHLKR 598
Cdd:cd02664 134 ----------------------------PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 599 FEHVGKQ--RRKINTFISFPLELDMtPFLASTKESR------MKEGQPPTDCVPNENKYSLFAVINHHGT-LESGHYTSF 669
Cdd:cd02664 186 FSYDQKThvREKIMDNVSINEVLSL-PVRVESKSSEsplekkEEESGDDGELVTRQVHYRLYAVVVHSGYsSESGHYFTY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034673623 670 IRQQKDQ---------------------WFSCDDAIITKATIEDL--LYSEG-----YLLFY 703
Cdd:cd02664 265 ARDQTDAdstgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnVTSRFpkdtpYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
2.90e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 99.36 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALthipllkdfflsdkhkcimtspslclvcemSSLfhamysgsrtphiPYKLLHLIWIHAehla 443
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------------------ASL-------------PSLIEYLEEFLE---- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 444 gyrQQDAHEFLIAILDVLHrhskddsggQEANNPnccnciidqiFTGGLQSDVTCQACHSVST-TIDPCWDISLDLPgsc 522
Cdd:cd02662 34 ---QQDAHELFQVLLETLE---------QLLKFP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 523 atfdsqnperadstvsrDDHIPGIPSLTDCLQWFTRPEHLGSsakIKCNSCQsyqestkqLTMKKLPIVACFHLKRF--- 599
Cdd:cd02662 89 -----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSvfd 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 600 EHVGKQRRKINtfISFPLELdmtpflastkesrmkegqpptdcvpNENKYSLFAVINHHGTLESGHYTSFIR-------- 671
Cdd:cd02662 141 GRGTSTKNSCK--VSFPERL-------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdk 193
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034673623 672 -------------QQKDQWFSCDDAIITKATIED-LLYSEGYLLFY 703
Cdd:cd02662 194 epgsfvrmregpsSTSHPWWRISDTTVKEVSESEvLEQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
364-705 |
3.14e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 97.57 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALThipllkdfFLSDKHKCIMTSPSLCLvcemsSLFHAMYSGSRTP---HIPYKLLHLIWIHAE 440
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA--------LYLPKLDELLDDLSKEL-----KVLKNVIRKPEPDlnqEEALKLFTALWSSKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 441 HLAG-----YRQQDAHEFLIAILDVLhrhskddsggqeanNPNCCNCIIDQIF-TGGlqsdvtcqacHSVSTTIDPCWDI 514
Cdd:COG5533 68 HKVGwippmGSQEDAHELLGKLLDEL--------------KLDLVNSFTIRIFkTTK----------DKKKTSTGDWFDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 515 SLDLPgscatfdsqnperadsTVSRDDhipGIPSLTDCLQWFtrpEHLGSSAK-IKCNSCQSYQESTKQL---TMKKLPI 590
Cdd:COG5533 124 IIELP----------------DQTWVN---NLKTLQEFIDNM---EELVDDETgVKAKENEELEVQAKQEyevSFVKLPK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 591 VACFHLKRFEHVGkQRRKINTFISFPLELdmtPFLAStkesrmkegqpPTDCVPNENKYSLFAVINHHGTLESGHYTSFI 670
Cdd:COG5533 182 ILTIQLKRFANLG-GNQKIDTEVDEKFEL---PVKHD-----------QILNIVKETYYDLVGFVLHQGSLEGGHYIAYV 246
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034673623 671 RqQKDQWFSCDDAIITKATIE---DLLYSEGYLLFYHK 705
Cdd:COG5533 247 K-KGGKWEKANDSDVTPVSEEeaiNEKAKNAYLYFYER 283
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
360-694 |
9.40e-22 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 101.10 E-value: 9.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 360 VGLRgliNLGNTCFMNCIVQALTHIpllkDFFLSDKHKCIMTSPS--LCLVCEMSSLFHAMysgsRTPHIPYKLLHL--- 434
Cdd:COG5077 194 VGLR---NQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHPRgrDSVALALQRLFYNL----QTGEEPVDTTELtrs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 435 -IWIHAEHlagYRQQDAHEFLIAILDVLHRHSKDDsggqEANNpnccncIIDQIFTGGLQSDVTCQACHSVSTTIDPCWD 513
Cdd:COG5077 263 fGWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGT----VVEN------ALNGIFVGKMKSYIKCVNVNYESARVEDFWD 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 514 ISLDLPGScatfdsqnperadstvsrddhipgiPSLTDCLQWFTRPEHLGSSakiKCNSCQSY--QESTKQLTMKKLPIV 591
Cdd:COG5077 330 IQLNVKGM-------------------------KNLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 592 ACFHLKRFEH--VGKQRRKINTFISFPLELDMTPFLasTKESRMKEGQpptDCVpnenkYSLFAVINHHGTLESGHYTSF 669
Cdd:COG5077 382 LHLQLKRFEYdfERDMMVKINDRYEFPLEIDLLPFL--DRDADKSENS---DAV-----YVLYGVLVHSGDLHEGHYYAL 451
|
330 340
....*....|....*....|....*.
gi 1034673623 670 IRQQKD-QWFSCDDAIITKATIEDLL 694
Cdd:COG5077 452 LKPEKDgRWYKFDDTRVTRATEKEVL 477
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
364-678 |
3.78e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 79.62 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPLLKDFFLSdkhkCIMTS--PSLCLVCEMSSLFHAMYSGSRTP-----------HIPY- 429
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS----HLATEclKEHCLLCELGFLFDMLEKAKGKNcqasnflralsSIPEa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 430 KLLHLIWIHAEHLAG--YRQ--QDAHEFLiaiLDVLHRHSKdDSGGQEANNPNccncIIDQIFTGGLQSDVTCQACHSVS 505
Cdd:pfam13423 78 SALGLLDEDRETNSAisLSSliQSFNRFL---LDQLSSEEN-STPPNPSPAES----PLEQLFGIDAETTIRCSNCGHES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 506 TTidpcwdisldlPGSCATFDSQNPERADSTVSRddhiPGIPSLTDCLQWFTRPEhlgSSAKIKCNSCQSYQESTKQLTM 585
Cdd:pfam13423 150 VR-----------ESSTHVLDLIYPRKPSSNNKK----PPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 586 KKLPIVACFHLKRFEHVGKQRRKINTFisFPLELDMTpflastkesrmkeGQPPTDCVPNENKYSLFAVINH-HGTLESG 664
Cdd:pfam13423 212 RNLPPVLSLNAALTNEEWRQLWKTPGW--LPPEIGLT-------------LSDDLQGDNEIVKYELRGVVVHiGDSGTSG 276
|
330 340
....*....|....*....|..
gi 1034673623 665 HYTSFIR--------QQKDQWF 678
Cdd:pfam13423 277 HLVSFVKvadseledPTESQWY 298
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
236-296 |
2.11e-13 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 65.36 E-value: 2.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034673623 236 CHVCSTHmNRLHSCLSCVFFGCFT--EKHIHKHAETKQHHLAVDLYHGVIYCFMCKDYVYDKD 296
Cdd:pfam02148 1 CSLCGNT-SNLWLCLTCGHVGCGRyqNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
365-703 |
3.97e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 57.92 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 365 LINLGNTCFMNCIVQALTHIPLLKDFFLSDKhkcimtspslclvcemsslfhamysgsrtphipykllhliwihaehlag 444
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKINTEFDNDD------------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 445 yrQQDAHEFLIAILdvlhrHSKDDSGGQEANNPNCCNCIIDQI-----FTGGLQSDVTCQACHSVSTTIDPCWDISLDLp 519
Cdd:cd02673 33 --QQDAHEFLLTLL-----EAIDDIMQVNRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSFEENVSDVGNFLDVSM- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 520 gscatfdsqnperadstvsrddhipgIPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQESTKQLTMKkLPIVACFHLKRF 599
Cdd:cd02673 105 --------------------------IDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSERIMT-FPECLSINLKRY 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 600 ehvgKQRRkintfisfpleldmtpflaSTKESRMKEGQPPTDCVPNENKYSLFAVINHHG-TLESGHYTSFIRQ--QKDQ 676
Cdd:cd02673 158 ----KLRI-------------------ATSDYLKKNEEIMKKYCGTDAKYSLVAVICHLGeSPYDGHYIAYTKElyNGSS 214
|
330 340 350
....*....|....*....|....*....|
gi 1034673623 677 WFSCDDAIITKATIEDLLY---SEGYLLFY 703
Cdd:cd02673 215 WLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
364-703 |
1.40e-08 |
|
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: 57.12 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 364 GLINLGNTCFMNCIVQALTHIPLLKDFFLS---DKHKCIMTSP-----------------SLCLVCEMSSLFHAM-YSGS 422
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeSKAELASDYPterriggrevsrselqrSNQFVYELRSLFNDLiHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 423 RTPHiPYKLLhliwihaeHLAGYRQQDAHEFLIAILDVLHRHSKDDS---GGQEANNPNCCNCIIDQIFTGGL-QSDVTC 498
Cdd:cd02666 83 RSVT-PSKEL--------AYLALRQQDVTECIDNVLFQLEVALEPISnafAGPDTEDDKEQSDLIKRLFSGKTkQQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 499 QACHSVSTTIDPCWDISLDLPgSCATFDSQNPERadstvsrddhipGIPSLTDCLQWFTRPEHLGSSAKIKCNSCQSYQ- 577
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLVD-VGKKGREIVVLL------------EPKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQp 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 578 ESTKQLTMKK--LPIVACFHLKRFEHVGKQRRKintfisfpLELDMTPFLASTKESRMKEGQPPTDcvpneNKYSLFAVI 655
Cdd:cd02666 221 LQRELISMDRyeLPSSIDDIDELIREAIQSESS--------LVRQAQNELAELKHEIEKQFDDLKS-----YGYRLHAVF 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034673623 656 NHHGTLESGHYTSFIR--QQKDQWFSCDDAIITKATIEDLLYSEG-----YLLFY 703
Cdd:cd02666 288 IHRGEASSGHYWVYIKdfEENVWRKYNDETVTVVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
586-703 |
1.83e-08 |
|
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: 55.61 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 586 KKLPIVACFHLKRFEHVGKQRRKINTFISFPLELDMTPFLASTKESRMKEGQPPTDCVPN--------ENKYSLFAVINH 657
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVCYDDkdfsptcgKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034673623 658 HGT-LESGHYTSFIRQQKD------------QWFSCDDAIITKATIED------LLYSEGYLLFY 703
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDMADRDGVSNGfnipaaRLLEDPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
545-693 |
5.77e-04 |
|
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: 42.16 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673623 545 GIPSLTDCLQWFT---RPEHLGSSAKIKCNSCQSYQEstkqltmkkLPIVACFHLKRFEHVGKQRRKINTFISFPLELdm 621
Cdd:cd02665 91 GYGNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQII-- 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034673623 622 tpflastkesrmkegqpptdcvpNENKYSLFAVINHHGTLESGHYTSFI-RQQKDQWFSCDDAIITKATIEDL 693
Cdd:cd02665 160 -----------------------QQVPYELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEV 209
|
|
| |
