|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
360-689 |
5.52e-153 |
|
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: 446.05 E-value: 5.52e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 360 RGLINLGNTCFMNCIVQALTRIPLLKEFFLSDKHK--CMMTSPSLCLVCEMSSLFQAM-YSGNQSPHIPYKLLHLIWIHA 436
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSctCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 437 EHLAGYRQQDAHEFLIAILDVLHRHSRDDgIEQEGNLNHCNCIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLPV 516
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGD-KNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 517 SYTPGRAGSTGQKPRVISLTDCLKWFTRPEDLGSSAkIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEH-LGKQRRKI 595
Cdd:cd02660 160 KSTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHsLNKTSRKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 596 NTFISFPLELDMTPFLASTKESIMKGQPLTEcvpiENKYSLFAVINHHGTLESGHYTSFVRQEKDQWFSCDDAVVTKATM 675
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIGDTQDSNSLDP----DYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSE 314
|
330
....*....|....
gi 157818203 676 EELLYSEGYLLFYH 689
Cdd:cd02660 315 EEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
360-688 |
4.30e-82 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 262.76 E-value: 4.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 360 RGLINLGNTCFMNCIVQALTRIPLLKEFFLSDKHKCMMTSPSLC--LVCEMSSLFQAMYSGNQSPHI-PYKLLHLIWIHA 436
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 437 EHLAGYRQQDAHEFLIAILDVLHRhsrddgieqEGNLNHCN---CIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLD 513
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE---------DLNGNHSTeneSLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 514 LPVSYTPgragstgqkPRVISLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGKQRR 593
Cdd:pfam00443 152 IPGDSAE---------LKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 594 KINTFISFPLELDMTPFLAstkesimkgQPLTECVPIENKYSLFAVINHHGTLESGHYTSFVRQEKD-QWFSCDDAVVTK 672
Cdd:pfam00443 223 KLNTEVEFPLELDLSRYLA---------EELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRWYKFDDEKVTE 293
|
330
....*....|....*..
gi 157818203 673 ATME-ELLYSEGYLLFY 688
Cdd:pfam00443 294 VDEEtAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
360-688 |
1.50e-70 |
|
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: 232.17 E-value: 1.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 360 RGLINLGNTCFMNCIVQALTRIPLLKEFFLSDKHKCMMTSPSLCLVCEMSSLFQAMYSGNQSPHIPYKLLHLIWIHAEHL 439
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 440 AGYRQQDAHEFLIAILDVLHR--HSRDDGIEQEGNLNHCNCIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLpvs 517
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKacLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 518 ytpgragstgqkPRVISLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEhlGKQRRKINT 597
Cdd:cd02661 159 ------------KGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFS--NFRGGKINK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 598 FISFPLELDMTPFLASTKESimkgqPLtecvpienKYSLFAVINHHGT-LESGHYTSFVRQEKDQWFSCDDAVVTKATME 676
Cdd:cd02661 225 QISFPETLDLSPYMSQPNDG-----PL--------KYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIE 291
|
330
....*....|..
gi 157818203 677 ELLYSEGYLLFY 688
Cdd:cd02661 292 TVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
361-688 |
5.03e-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: 223.51 E-value: 5.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTripllkefflsdkhkcmmtspslclvcemsslfqamysgnqsphipykllhliwihaehla 440
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 441 gYRQQDAHEFLIAILDVLHRHSrDDGIEQEGNLNHCNCIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLPVSYTP 520
Cdd:cd02257 20 -SEQQDAHEFLLFLLDKLHEEL-KKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGLP 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 521 gragstgqkprVISLTDCLKWFTRPEDLGSSAKIKCSRCqSYQQSTKQLTMKKLPIVACFHLKRFEHLGK-QRRKINTFI 599
Cdd:cd02257 98 -----------QVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNEDgTKEKLNTKV 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 600 SFPLELDMTPFLASTKESIMKGQPLTecvpienKYSLFAVINHHGTL-ESGHYTSFVR-QEKDQWFSCDDAVVTKATMEE 677
Cdd:cd02257 166 SFPLELDLSPYLSEGEKDSDSDNGSY-------KYELVAVVVHSGTSaDSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEE 238
|
330
....*....|....*.
gi 157818203 678 LLY-----SEGYLLFY 688
Cdd:cd02257 239 VLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
5.17e-68 |
|
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: 222.55 E-value: 5.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRipllkefflsdkhkcmmtspslclvcemsslfqamysgnqsphipykllhliwihaehla 440
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 441 gyRQQDAHEFLIAILDVLHRhsrddgieqegnlnhcncIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLPvsytp 520
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP----- 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 521 gragSTGQKPRVISLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGKQRRKINTFIS 600
Cdd:cd02674 76 ----SGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVT 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 601 FPLE-LDMTPFLASTkesimkgqplteCVPIENKYSLFAVINHHGTLESGHYTSFVR-QEKDQWFSCDDAVVTKATMEEL 678
Cdd:cd02674 152 FPLNdLDLTPYVDTR------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSV 219
|
330
....*....|
gi 157818203 679 LYSEGYLLFY 688
Cdd:cd02674 220 VSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
8.80e-49 |
|
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: 172.57 E-value: 8.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKEFFLSdkhkcmmtSPSLCL--VCEMSSLFQamysgnqsphipykllhliwihaeh 438
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE--------TPKELFsqVCRKAPQFK------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 439 laGYRQQDAHEFLIAILDVLhrhsrddgieqegnlnhcNCIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLPVSY 518
Cdd:cd02667 48 --GYQQQDSHELLRYLLDGL------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEI 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 519 TPGRagstgqkprviSLTDCLKWFTRPEDLGSSAKIKCSRCqsyQQSTKQLTMKKLPIVACFHLKRFEHLGKQR-RKINT 597
Cdd:cd02667 108 KSEC-----------SIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANlRKVSR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 598 FISFPLELDMTPFLASTKESIMKGQPLtecvpienKYSLFAVINHHGTLESGHYTSFVR--------------------- 656
Cdd:cd02667 174 HVSFPEILDLAPFCDPKCNSSEDKSSV--------LYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadea 245
|
330 340 350
....*....|....*....|....*....|...
gi 157818203 657 -QEKDQWFSCDDAVVTKATMEELLYSEGYLLFY 688
Cdd:cd02667 246 gPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
358-693 |
3.41e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 172.83 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 358 GLRGLINLGNTCFMNCIVQALTRIPLLKEFFLSDKHKcMMTSPSLCLVCEMSSLFQAMYSGnQSPHIPYKLLHLI----W 433
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLS-ESPVKTTELTDKTrsfgW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 434 ihaEHLAGYRQQDAHEFLIAILDVLHRHSRddGIEQEGnlnhcncIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLD 513
Cdd:cd02659 79 ---DSLNTFEQHDVQEFFRVLFDKLEEKLK--GTGQEG-------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 514 LpvsytpgragsTGQKprviSLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGK--Q 591
Cdd:cd02659 147 V-----------KGKK----NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFEtmM 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 592 RRKINTFISFPLELDMTPFlasTKESIMKGQPLTEC-VPIENKYSLFAVINHHGTLESGHYTSFVRQ-EKDQWFSCDDAV 669
Cdd:cd02659 212 RIKINDRFEFPLELDMEPY---TEKGLAKKEGDSEKkDSESYIYELHGVLVHSGDAHGGHYYSYIKDrDDGKWYKFNDDV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 157818203 670 VTKATMEELL----------------------YSEGYLLFYHRQDI 693
Cdd:cd02659 289 VTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERKSP 334
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
1.59e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 139.38 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKEFFLSDKHK--CMMTSPSLCLVCEMSSLFQAMYSGNQS-------PHIPYK---- 427
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfpSDVVDPANDLNCQLIKLADGLLSGRYSkpaslksENDPYQvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 428 ---LLHLIWI-HAEHLAGyRQQDAHEFLIAILDVLHRHSRDDGIEqegNLNHcnciidyIFTGGLQSDVTCQVCHGVSTT 503
Cdd:cd02658 81 psmFKALIGKgHPEFSTM-RQQDALEFLLHLIDKLDRESFKNLGL---NPND-------LFKFMIEDRLECLSCKKVKYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 504 IDpcWDISLDLPVSYTPGRAGSTGQKPRV-ISLTDCLKWFTRPEDLgssaKIKCSRCQSYQQSTKQLTMKKLPIVACFHL 582
Cdd:cd02658 150 SE--LSEILSLPVPKDEATEKEEGELVYEpVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 583 KRFE-HLGKQRRKINTFISFPLELDmtpflastkesimkgqpltecvpiENKYSLFAVINHHGT-LESGHYTSFVRQE-- 658
Cdd:cd02658 224 KRFQlLENWVPKKLDVPIDVPEELG------------------------PGKYELIAFISHKGTsVHSGHYVAHIKKEid 279
|
330 340 350
....*....|....*....|....*....|.
gi 157818203 659 -KDQWFSCDDAVVTKATMEELLYSEGYLLFY 688
Cdd:cd02658 280 gEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
1.09e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 136.67 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALtripllkeFFLsdkhkcmmtspslCLVCEMSSLFQAMYSGNQSPHI--PYKLLHLIWIHAEH 438
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL--------YFE-------------NLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 439 LAGYRQQDAHEFL-------IAILDVLHRHSRDDGIEQEGNL--NHCNCIIDyIFTGGLQSDVTCQVCHGVSTTIDPCWD 509
Cdd:cd02663 60 FDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNaePQPTWVHE-IFQGILTNETRCLTCETVSSRDETFLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 510 ISLDLPVSYtpgragstgqkprviSLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLG 589
Cdd:cd02663 139 LSIDVEQNT---------------SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 590 KQRRKINTF--ISFPLELDM--TPFLASTKESImkgqpltecvpienkYSLFAVINHHG-TLESGHYTSFVRQeKDQWFS 664
Cdd:cd02663 204 QLNRYIKLFyrVVFPLELRLfnTTDDAENPDRL---------------YELVAVVVHIGgGPNHGHYVSIVKS-HGGWLL 267
|
330 340 350
....*....|....*....|....*....|..
gi 157818203 665 CDDAVVTK---ATMEELLY-----SEGYLLFY 688
Cdd:cd02663 268 FDDETVEKideNAVEEFFGdspnqATAYVLFY 299
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
526-690 |
5.72e-31 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 129.62 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 526 TGQKPRVISLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGKQRRKINTFISFPL-E 604
Cdd:COG5560 668 IGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIdD 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 605 LDMTPFLASTKESIMkgqpltecvpienKYSLFAVINHHGTLESGHYTSFVRQEKDQ-WFSCDDAVVTKATMEELLYSEG 683
Cdd:COG5560 748 LDLSGVEYMVDDPRL-------------IYDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSSA 814
|
....*..
gi 157818203 684 YLLFYHR 690
Cdd:COG5560 815 YVLFYRR 821
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
5.55e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 118.46 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKEFFlsdKHKCMMTSP--SLCLVCEmssLFQAMYSGNQSPHIPYKLLHLIWIHAEH 438
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGL---KHLVSLISSveQLQSSFL---LNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 439 LAGYRQQDAHEFLIAILDVLHRhsrddgieqegnlnhcncIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLPVSY 518
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQE------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 519 TPGRAGSTGQKPRVISLTDCLKW----FTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGKQR-- 592
Cdd:cd02671 162 LSKSEESSEISPDPKTEMKTLKWaisqFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdc 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 593 ----RKINTFISFPLELDMtpFLASTKESimkgqpltecvpiENKYSLFAVINHHG-TLESGHYTSFVRqekdqWFSCDD 667
Cdd:cd02671 242 ygglSKVNTPLLTPLKLSL--EEWSTKPK-------------NDVYRLFAVVMHSGaTISSGHYTAYVR-----WLLFDD 301
|
330 340 350
....*....|....*....|....*....|
gi 157818203 668 AVVTKATMEELL---------YSEGYLLFY 688
Cdd:cd02671 302 SEVKVTEEKDFLealspntssTSTPYLLFY 331
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-672 |
1.21e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 117.14 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTR-IPLLKEFFL--SDKHKCMMTSPSLCL-----VCE-MSSLFQAMYSGNQSPHIPYKLlhl 431
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMnLEFRKAVYEcnSTEDAELKNMPPDKPhepqtIIDqLQLIFAQLQFGNRSVVDPSGF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 432 iwIHAEHLAGYRQQDAHEFLIAILDVLhrhsrDDGIEQEGNLNHCNcIIDYIFTGGLQSDVTCQVCHGVSTTIDPCWDIS 511
Cdd:cd02668 78 --VKALGLDTGQQQDAQEFSKLFLSLL-----EAKLSKSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYELE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 512 LDLpvsytpgrAGSTgqkprviSLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGK- 590
Cdd:cd02668 150 LQL--------KGHK-------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKt 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 591 -QRRKINTFISFPLELDMTPFLAstkesimkGQPLTECVpienkYSLFAVINHHGT-LESGHYTSFVRQEK-DQWFSCDD 667
Cdd:cd02668 215 gAKKKLNASISFPEILDMGEYLA--------ESDEGSYV-----YELSGVLIHQGVsAYSGHYIAHIKDEQtGEWYKFND 281
|
....*
gi 157818203 668 AVVTK 672
Cdd:cd02668 282 EDVEE 286
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
1.29e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 116.66 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKE---FFLSDKHKCMmtSPSLCLVCEMSSLFQAMySGNQSPHIPYKLLHLIWIHAE 437
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGAN--QSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 438 HLA------GYRQQDAHEFLIAILDVLHRHSRDDGIEQEgnlnhcncIIDYIFTGGLQSDVTCQVCHGV-STTIDPcwDI 510
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGS--------FIDQLFGIELETKMKCTESPDEeEVSTES--EY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 511 SLDLPVSytpgragstgQKPRVISLTDCLKwftrpEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKRFEHLGK 590
Cdd:cd02657 148 KLQCHIS----------ITTEVNYLQDGLK-----KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 591 --QRRKINTFISFPLELDMTPFLASTkesimkgqpltecvpieNKYSLFAVINHHG-TLESGHYTSFVRQEKDQ-WFSCD 666
Cdd:cd02657 213 iqKKAKILRKVKFPFELDLYELCTPS-----------------GYYELVAVITHQGrSADSGHYVAWVRRKNDGkWIKFD 275
|
330 340
....*....|....*....|....*....
gi 157818203 667 DAVVTKATMEELLYSEG-------YLLFY 688
Cdd:cd02657 276 DDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
361-690 |
2.01e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 109.51 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTripllkefFLSDKHKCMMTSPSLCLvcemsSLFQAMYSGNQSP---HIPYKLLHLIWIHAE 437
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA--------LYLPKLDELLDDLSKEL-----KVLKNVIRKPEPDlnqEEALKLFTALWSSKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 438 HLAG-----YRQQDAHEFLIAILDVLhrhsrddgieqegNLNHCNCI-IDYIFTGGlqsdvtcqvcHGVSTTIDPCWDIS 511
Cdd:COG5533 68 HKVGwippmGSQEDAHELLGKLLDEL-------------KLDLVNSFtIRIFKTTK----------DKKKTSTGDWFDII 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 512 LDLPvsytpgragsTGQKPRVISLTDCLkwFTRPEDLGSSAK-IKCSRCQSYQQSTKQL---TMKKLPIVACFHLKRFEH 587
Cdd:COG5533 125 IELP----------DQTWVNNLKTLQEF--IDNMEELVDDETgVKAKENEELEVQAKQEyevSFVKLPKILTIQLKRFAN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 588 LGkQRRKINTFISFPLELdmtPFLASTKESIMKgqpltecvpiENKYSLFAVINHHGTLESGHYTSFVRQeKDQWFSCDD 667
Cdd:COG5533 193 LG-GNQKIDTEVDEKFEL---PVKHDQILNIVK----------ETYYDLVGFVLHQGSLEGGHYIAYVKK-GGKWEKAND 257
|
330 340
....*....|....*....|....*..
gi 157818203 668 AVVTKATMEElLYSE----GYLLFYHR 690
Cdd:COG5533 258 SDVTPVSEEE-AINEkaknAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
355-688 |
2.25e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 109.72 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 355 YTVGLRGLINLGNTCFMNCIVQALTRIPLLKEFFLS-DKHKCMMTSPSLcLVCEMSSLFQAMYS-----GNQSPHipyKL 428
Cdd:cd02669 115 YLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyENYENIKDRKSE-LVKRLSELIRKIWNprnfkGHVSPH---EL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 429 LHLIWIHAEHLAGYRQQ-DAHEFLIAILDVLHRHSRDDGIEQEGnlnhcncIIDYIFTGGLQ--------------SDVT 493
Cdd:cd02669 191 LQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSKKPNSS-------IIHDCFQGKVQietqkikphaeeegSKDK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 494 CQVCHGVSTTID-PCWDISLDLPvsyTPGRAGSTGQKPRV--ISLTDCLKWFTrpedlGSSakikcsrCQSYQQSTKQLT 570
Cdd:cd02669 264 FFKDSRVKKTSVsPFLLLTLDLP---PPPLFKDGNEENIIpqVPLKQLLKKYD-----GKT-------ETELKDSLKRYL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 571 MKKLPIVACFHLKRFEHLGKQRRKINTFISFPLE-LDMTPFLASTKESimkgqpltecVPIENKYSLFAVINHHGT-LES 648
Cdd:cd02669 329 ISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDYVHFDKPS----------LNLSTKYNLVANIVHEGTpQED 398
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 157818203 649 GHYTSFVRQEK-DQWFSCDDAVVTKATMEELLYSEGYLLFY 688
Cdd:cd02669 399 GTWRVQLRHKStNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
1.11e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 105.65 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALtripllkefflsdkhkcMMTSPSlclvcEMSSLFQAMYSGNQSpHIPYKLLHLIWIHAEHLA 440
Cdd:cd02664 1 GLINLGNTCYMNSVLQAL-----------------FMAKDF-----RRQVLSLNLPRLGDS-QSVMKKLQLLQAHLMHTQ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 441 GY--------------------RQQDAHEFLIAILDVLHrhsrddgieqegnlnhcnCIIDYIFTGGLQSDVTCQVCHGV 500
Cdd:cd02664 58 RRaeappdyfleasrppwftpgSQQDCSEYLRYLLDRLH------------------TLIEKMFGGKLSTTIRCLNCNST 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 501 STTIDPCWDISLDLPvsytpgragstgqkprviSLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQSTKQLTMKKLPIVACF 580
Cdd:cd02664 120 SARTERFRDLDLSFP------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLIL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 581 HLKRFEHLGKQ--RRKINTFISFPLELDMtPFLASTKES-------IMKGQPLTECVPIENKYSLFAVINHHGT-LESGH 650
Cdd:cd02664 182 TLLRFSYDQKThvREKIMDNVSINEVLSL-PVRVESKSSesplekkEEESGDDGELVTRQVHYRLYAVVVHSGYsSESGH 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818203 651 YTSFVR---------------------QEKDQWFSCDDAVVTKATMEEL--LYSEG-----YLLFY 688
Cdd:cd02664 261 YFTYARdqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVqnVTSRFpkdtpYILFY 326
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
357-696 |
3.47e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 108.80 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 357 VGLRgliNLGNTCFMNCIVQALTRIpllkEFFLSDKHKCMMTSPS--LCLVCEMSSLFQAMYSGNqsphIPYKLLHL--- 431
Cdd:COG5077 194 VGLR---NQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHPRgrDSVALALQRLFYNLQTGE----EPVDTTELtrs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 432 -IWIHAEHlagYRQQDAHEFLIAILDVLHRHSRDDGIEqeGNLNHcnciidyIFTGGLQSDVTCQVCHGVSTTIDPCWDI 510
Cdd:COG5077 263 fGWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVE--NALNG-------IFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 511 SLDLPVSYTpgragstgqkprvisLTDCLKWFTRPEDLGSSakiKCSRCQSY--QQSTKQLTMKKLPIVACFHLKRFEH- 587
Cdd:COG5077 331 QLNVKGMKN---------------LQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYd 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 588 -LGKQRRKINTFISFPLELDMTPFL---ASTKESimkgqplTECVpienkYSLFAVINHHGTLESGHYTSFVRQEKD-QW 662
Cdd:COG5077 393 fERDMMVKINDRYEFPLEIDLLPFLdrdADKSEN-------SDAV-----YVLYGVLVHSGDLHEGHYYALLKPEKDgRW 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 157818203 663 FSCDDAVVTKATMEELL----------------------YSEGYLLFYHRQDIEKE 696
Cdd:COG5077 461 YKFDDTRVTRATEKEVLeenfggdhpykdkirdhsgikrFMSAYMLVYLRKSMLDD 516
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
338-517 |
5.36e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 107.66 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 338 ETSLVKPKKKRRKKTVYYTVGLRGLINLGNTCFMNCIVQALTRIPLLKEFFLSDK---------HKCMMTSpslcLVCEM 408
Cdd:COG5560 244 PDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeesineenPLGMHGS----VASAY 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 409 SSLFQAMYSGNQSPHIPYKLLHLIWIHAEHLAGYRQQDAHEFLIAILDVLHRH----------SRDDGIE---------- 468
Cdd:COG5560 320 ADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDlnriikkpytSKPDLSPgddvvvkkka 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157818203 469 ----QEGNLNHCNCIIDyIFTGGLQSDVTCQVCHGVSTTIDPCWDISLDLPVS 517
Cdd:COG5560 400 kecwWEHLKRNDSIITD-LFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
8.84e-22 |
|
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: 94.74 E-value: 8.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKEFflsdkhkcmmtspslclvcemsslfqamysgnqsphipykllhLIWIHAehla 440
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-------------------------------------------LEEFLE---- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 441 gyrQQDAHEFLIAILDVLHRHSRddgieqegnlnhcnciidYIFTGGLQSDVTCQVCHGVSTTIDPCWDiSLDLPVsytP 520
Cdd:cd02662 34 ---QQDAHELFQVLLETLEQLLK------------------FPFDGLLASRIVCLQCGESSKVRYESFT-MLSLPV---P 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 521 GRAGSTGQkprviSLTDCLKWFTRPEDLGSsakIKCSRCQsyqqstkqLTMKKLPIVACFHLKRFEHLGK---QRRKINt 597
Cdd:cd02662 89 NQSSGSGT-----TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDGRgtsTKNSCK- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 598 fISFPLELDmtpflastkesimkgqpltecvpiENKYSLFAVINHHGTLESGHYTSFVR--------------------- 656
Cdd:cd02662 152 -VSFPERLP------------------------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepgsfvrmregps 206
|
330 340 350
....*....|....*....|....*....|...
gi 157818203 657 QEKDQWFSCDDAVVTKATMEE-LLYSEGYLLFY 688
Cdd:cd02662 207 STSHPWWRISDTTVKEVSESEvLEQKSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
361-663 |
1.53e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 75.00 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKEFFLSdkHKCMMTSPSLCLVCEMSSLFQAMYSGNQSP-----------HIPY-KL 428
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNcqasnflralsSIPEaSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 429 LHLIWIHAEHLAG--YRQ--QDAHEFLiaiLDVLHRhsrdDGIEQEGNLNHCNCIIDYIFTGGLQSDVTCQVCHGVSTTI 504
Cdd:pfam13423 80 LGLLDEDRETNSAisLSSliQSFNRFL---LDQLSS----EENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 505 DpcwdISLDLPVSYtPGRAGSTGQKPRVISLTDCLKWFTRPEdlgSSAKIKCSRCQSYQQSTKQLTMKKLPIVACFHLKR 584
Cdd:pfam13423 153 S----STHVLDLIY-PRKPSSNNKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 585 FEHLGKQRRKINTFisFPLELDMTPFLASTKESIMKgqpltecvpienKYSLFAVINH-HGTLESGHYTSFVR------- 656
Cdd:pfam13423 225 TNEEWRQLWKTPGW--LPPEIGLTLSDDLQGDNEIV------------KYELRGVVVHiGDSGTSGHLVSFVKvadsele 290
|
....*...
gi 157818203 657 -QEKDQWF 663
Cdd:pfam13423 291 dPTESQWY 298
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
362-688 |
2.64e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 67.17 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 362 LINLGNTCFMNCIVQALTRIPLLKEFFLSDKhkcmmtspslclvcemsslfqamysgnqsphipykllhliwihaehlag 441
Cdd:cd02673 2 LVNTGNSCYFNSTMQALSSIGKINTEFDNDD------------------------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 442 yrQQDAHEFL---IAILDVLHRHSRDDGIEQEGNLNHCNCIIDYIFTggLQSDVTCQVCHGVSTTIDPCWdislDLPVSY 518
Cdd:cd02673 33 --QQDAHEFLltlLEAIDDIMQVNRTNVPPSNIEIKRLNPLEAFKYT--IESSYVCIGCSFEENVSDVGN----FLDVSM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 519 TPGRAGStgqkprVISLTDCLKWFTRPEDLGSSAKikcsrCQSYQQSTKQLTMKKLPIVacfHLKRFehlgKQRRkintf 598
Cdd:cd02673 105 IDNKLDI------DELLISNFKTWSPIEKDCSSCK-----CESAISSERIMTFPECLSI---NLKRY----KLRI----- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 599 isfpleldmtpflaSTKESIMKGQPLTECVPIE-NKYSLFAVINHHG-TLESGHYTSFVRQ--EKDQWFSCDDAVVTKAT 674
Cdd:cd02673 162 --------------ATSDYLKKNEEIMKKYCGTdAKYSLVAVICHLGeSPYDGHYIAYTKElyNGSSWLYCSDDEIRPVS 227
|
330
....*....|....*..
gi 157818203 675 MEELLY---SEGYLLFY 688
Cdd:cd02673 228 KNDVSTnarSSGYLIFY 244
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
232-292 |
2.80e-12 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 62.28 E-value: 2.80e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157818203 232 CRVCSThKNRLHSCLSCVFFGCFT--EKHIHIHAETKQHNLAVDLYHGVIYCFMCKDYVYDKD 292
Cdd:pfam02148 1 CSLCGN-TSNLWLCLTCGHVGCGRyqNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-688 |
3.62e-10 |
|
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: 62.12 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 361 GLINLGNTCFMNCIVQALTRIPLLKEFFLS-DKHKCMMTSP-------------------SLCLVCEMSSLFQAMYSGNQ 420
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfDESKAELASDypterriggrevsrselqrSNQFVYELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 421 SPHIPYKLLhliwihaeHLAGYRQQDAHEFLIAILD----VLHRHSRDDGIEQEGNLNHCNCIIDYIFTGGL-QSDVTCQ 495
Cdd:cd02666 83 RSVTPSKEL--------AYLALRQQDVTECIDNVLFqlevALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTkQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 496 VCHGVSTTIDPCWDISLDLPVSYTPGRAGSTGQKPrviSLTDCLKWFTRPEDLGSSAKIKCSRCQSYQQST-KQLTMKK- 573
Cdd:cd02666 155 MGNQPSVRTKTERFLSLLVDVGKKGREIVVLLEPK---DLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQrELISMDRy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 574 -LPIVacfhLKRFEHLgkQRRKINTFISfpLELDMTPFLASTKESI------MKgqpltecvpiENKYSLFAVINHHGTL 646
Cdd:cd02666 232 eLPSS----IDDIDEL--IREAIQSESS--LVRQAQNELAELKHEIekqfddLK----------SYGYRLHAVFIHRGEA 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157818203 647 ESGHYTSFVR--QEKDQWFSCDDAVVTKATMEELLYSEG-----YLLFY 688
Cdd:cd02666 294 SSGHYWVYIKdfEENVWRKYNDETVTVVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
572-688 |
3.90e-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: 54.84 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 572 KKLPIVACFHLKRFEHLGKQRRKINTFISFPLELDMTPFLASTKESIMKGQpLTECV----------PIENKYSLFAVIN 641
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQ-LECRVcyddkdfsptCGKFKLSLCSAVC 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157818203 642 HHGT-LESGHYTSFVRQEKD------------QWFSCDDAVVTKATMEE------LLYSEGYLLFY 688
Cdd:cd02670 175 HRGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDMADRDGVSNGfnipaaRLLEDPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
514-678 |
1.57e-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: 43.70 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 514 LPVSYTPGRagstgqkprviSLTDCLKWFTRPEDLGSSAKIkcsrcQSYQQSTKQLTMKkLPIVACFHLKRFEHLGKQRR 593
Cdd:cd02665 85 YPLQVNGYG-----------NLHECLEAAMFEGEVELLPSD-----HSVKSGQERWFTE-LPPVLTFELSRFEFNQGRPE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818203 594 KINTFISFPLELDMTPflastkesimkgqpltecvpienkYSLFAVINHHGTLESGHYTSFV-RQEKDQWFSCDDAVVTK 672
Cdd:cd02665 148 KIHDKLEFPQIIQQVP------------------------YELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTE 203
|
....*.
gi 157818203 673 ATMEEL 678
Cdd:cd02665 204 SSWEEV 209
|
|
| |
