|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
189-539 |
7.50e-54 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 184.40 E-value: 7.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 189 PRGLINSGNLCFLNSTLQALLSCPPFV-DLLRNLKNREIPKVGYSTLTAFVEFIS-ALEVPSSTVPNRDvaafdvgkpfs 266
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLAnYLLSREHSKDCCNEGFCMMCALEAHVErALASSGPGSAPRI----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 267 plmFDGVLKNFSPDLPSGilgrpRQEDAQEFLSFVMDRMHaellkldgKSSSTNGGKSfvvasaeddewetvgrKNKTAV 346
Cdd:cd02661 70 ---FSSNLKQISKHFRIG-----RQEDAHEFLRYLLDAMQ--------KACLDRFKKL----------------KAVDPS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 347 MRTQSFVpselSEIFWGELASMVKA-KGNKPSGTQQPFFSLHLDIYpdAVRTIEDALRLFSAPETLEG---YRPSAAGKA 422
Cdd:cd02661 118 SQETTLV----QQIFGGYLRSQVKClNCKHVSNTYDPFLDLSLDIK--GADSLEDALEQFTKPEQLDGenkYKCERCKKK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 423 GVVaaSKSMKIQKQSKIMILHLKRFGYGSHGstKLNKPVHFPLELVLnRDLLVSSSTEGRKYELVATITHHGRESSKGHY 502
Cdd:cd02661 192 VKA--SKQLTIHRAPNVLTIHLKRFSNFRGG--KINKQISFPETLDL-SPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHY 266
|
330 340 350
....*....|....*....|....*....|....*..
gi 659090146 503 TADVRYHNNQWLRFDDASVTAIGKNNVLHDRAYVLFY 539
Cdd:cd02661 267 YCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
190-539 |
8.61e-52 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 179.18 E-value: 8.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 190 RGLINSGNLCFLNSTLQALLSCPPFVDLLRNLKNrEIPKVGYST----LTAFVEFISALEVPSStvpnrdvaafdvGKPF 265
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISP-LSEDSRYNKdinlLCALRDLFKALQKNSK------------SSSV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 266 SPLMFDGVLKNFSPDLPSGilgrpRQEDAQEFLSFVMDRMHAELlkldgKSSSTNGGKSFVVasaeddewetvgrknkta 345
Cdd:pfam00443 68 SPKMFKKSLGKLNPDFSGY-----KQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLIT------------------ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 346 vmrtqsfvpselsEIFWGELASMVKAKG-NKPSGTQQPFFSLHLDIYPDAVRTIE----DALRLFSAPETLEGY-RPSAA 419
Cdd:pfam00443 120 -------------DLFRGQLKSRLKCLScGEVSETFEPFSDLSLPIPGDSAELKTaslqICFLQFSKLEELDDEeKYYCD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 420 GKAGVVAASKSMKIQKQSKIMILHLKRFGYGSHGSTKLNKPVHFPLELVLNRDL---LVSSSTEGRKYELVATITHHGRE 496
Cdd:pfam00443 187 KCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLELDLSRYLaeeLKPKTNNLQDYRLVAVVVHSGSL 266
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 659090146 497 SSkGHYTADVR-YHNNQWLRFDDASVTAIG-KNNVLHDRAYVLFY 539
Cdd:pfam00443 267 SS-GHYIAYIKaYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
191-540 |
1.20e-48 |
|
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: 168.82 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLScppfvdllrnlknreipkvgystltafvefisalevpsstvpnrdvaafdvgkpfsplmf 270
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 271 dgvlknfspdlpsgilgrpRQEDAQEFLSFVMDRMHAELLKLDGKSSSTNGGKSFVVasaeddewetvgrknktavmrtq 350
Cdd:cd02257 21 -------------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIH----------------------- 58
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 351 sfvpselsEIFWGELASMVKAKGNKPSGTQQ---PFFSLHLDIYPDAVRTIEDALRLFSAPETLEGYRPSAAGKAGVVAA 427
Cdd:cd02257 59 --------DLFGGKLESTIVCLECGHESVSTepeLFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKKKQEA 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 428 SKSMKIQKQSKIMILHLKRFGYGSHGST-KLNKPVHFPLELVLNRDLLVS-----SSTEGRKYELVATITHHGRESSKGH 501
Cdd:cd02257 131 TKRLKIKKLPPVLIIHLKRFSFNEDGTKeKLNTKVSFPLELDLSPYLSEGekdsdSDNGSYKYELVAVVVHSGTSADSGH 210
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 659090146 502 YTADVRYH-NNQWLRFDDASVTAIGKNNVLHDR-----AYVLFYK 540
Cdd:cd02257 211 YVAYVKDPsDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
290-540 |
2.72e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 142.81 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 290 RQEDAQEFLSFVMDRMHaellkldgkssstnggkSFVVasaeddewetvgrknktavmrtqsfvpselsEIFWGELASMV 369
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH-----------------SIIV-------------------------------DLFQGQLKSRL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 370 KAKG-NKPSGTQQPFFSLHLDI----YPDAVRTIEDALRLFSAPETLEG-YRPSAAGKAGVVAASKSMKIQKQSKIMILH 443
Cdd:cd02674 53 TCLTcGKTSTTFEPFTYLSLPIpsgsGDAPKVTLEDCLRLFTKEETLDGdNAWKCPKCKKKRKATKKLTISRLPKVLIIH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 444 LKRFGYGSHGSTKLNKPVHFPLE-LVLNRDLLVSSSTEGRKYELVATITHHGrESSKGHYTADVR-YHNNQWLRFDDASV 521
Cdd:cd02674 133 LKRFSFSRGSTRKLTTPVTFPLNdLDLTPYVDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRV 211
|
250
....*....|....*....
gi 659090146 522 TAIGKNNVLHDRAYVLFYK 540
Cdd:cd02674 212 TKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
190-540 |
1.81e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 138.27 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 190 RGLINSGNLCFLNSTLQALLSCPPFVDLL------RNLKNREIPK-VGYSTLTAFVEFISalevPSSTVPnrdvaafdvg 262
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFlsdrhsCTCLSCSPNScLSCAMDEIFQEFYY----SGDRSP---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 263 kpFSPLMFDGVLKNFSPDLpsgilGRPRQEDAQEFLSFVMDRMHAELLKLDGKSSSTNGGKSFVvasaeddewetvgrkn 342
Cdd:cd02660 67 --YGPINLLYLSWKHSRNL-----AGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCII---------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 343 ktavmrtqsfvpselSEIFWGELASMVKAKG-NKPSGTQQPFFSLHLDIYPDAVR-------------TIEDALRLFSAP 408
Cdd:cd02660 124 ---------------HQTFSGSLQSSVTCQRcGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 409 ETLEGYRPSAAGKAGVVAASKSMKIQKQSKIMILHLKRFGYGSHG-STKLNKPVHFPLEL--------VLNRDLLVSSST 479
Cdd:cd02660 189 EKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtSRKIDTYVQFPLELnmtpytssSIGDTQDSNSLD 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659090146 480 EGRKYELVATITHHGrESSKGHYTADVRYHNNQWLRFDDASVTAIGKNNVLHDRAYVLFYK 540
Cdd:cd02660 269 PDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-540 |
3.56e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 108.57 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVDLLRNLK-NREIPKVGYSTLTAfvEFISALEVPSSTVpnrdvaafdvgKPFSPLM 269
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNpARRGANQSSDNLTN--ALRDLFDTMDKKQ-----------EPVPPIE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 270 FdgvLKNFSPDLPS----GILGRPRQEDAQEFLSFVMDRMHAELLKLDGKSSStnggksfvvasaeddewetvgrknkta 345
Cdd:cd02657 68 F---LQLLRMAFPQfaekQNQGGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF--------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 346 vmrtqsfvpseLSEIFWGELASMVKAKGN--KPSGTQQPFFSLHLDIYPDA-VRTIEDALRLfSAPETLEGYRPSAAGKA 422
Cdd:cd02657 118 -----------IDQLFGIELETKMKCTESpdEEEVSTESEYKLQCHISITTeVNYLQDGLKK-GLEEEIEKHSPTLGRDA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 423 GVvaaSKSMKIQKQSKIMILHLKRFGYGSHGST--KLNKPVHFPLELVLNrDLLVSSStegrKYELVATITHHGRESSKG 500
Cdd:cd02657 186 IY---TKTSRISRLPKYLTVQFVRFFWKRDIQKkaKILRKVKFPFELDLY-ELCTPSG----YYELVAVITHQGRSADSG 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 659090146 501 HYTADVRYHN-NQWLRFDDASVTAIGKNNVLH-------DRAYVLFYK 540
Cdd:cd02657 258 HYVAWVRRKNdGKWIKFDDDKVSEVTEEDILKlsgggdwHIAYILLYK 305
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-540 |
1.73e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 106.63 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLscppFVDLLRNLKnreipkvgystlTAFVEFISALEVPSSTVPNRDVAAFDVGKPfsplMF 270
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLTCLK------------DLFESISEQKKRTGVISPKKFITRLKRENE----LF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 271 DGVLknfspdlpsgilgrprQEDAQEFLSFVMDRMhAELLkldgkssstnggksfvvasaeDDEWETVGRKNKTAVMRTQ 350
Cdd:cd02663 61 DNYM----------------HQDAHEFLNFLLNEI-AEIL---------------------DAERKAEKANRKLNNNNNA 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 351 SFVPSELSEIFWGELASMVKA-KGNKPSGTQQPFFSLHLDIYPDAvrTIEDALRLFSAPETLEG-YRPSAAGKAGVVAAS 428
Cdd:cd02663 103 EPQPTWVHEIFQGILTNETRClTCETVSSRDETFLDLSIDVEQNT--SITSCLRQFSATETLCGrNKFYCDECCSLQEAE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 429 KSMKIQKQSKIMILHLKRFGYGS--HGSTKLNKPVHFPLELVLNRDLLVSSSTEgRKYELVATITHHGRESSKGHYTADV 506
Cdd:cd02663 181 KRMKIKKLPKILALHLKRFKYDEqlNRYIKLFYRVVFPLELRLFNTTDDAENPD-RLYELVAVVVHIGGGPNHGHYVSIV 259
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 659090146 507 RyHNNQWLRFDDASVTAIGKNNVLH--------DRAYVLFYK 540
Cdd:cd02663 260 K-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-540 |
8.61e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 98.93 E-value: 8.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFV---DLLRNLKNREIPKVGYSTLTAFVEFISALEVPSSTVPNRDVaafDVGKPF-- 265
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQwryDDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLK---SENDPYqv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 266 --SPLMFDGVLKNFSPDLPSGilgrpRQEDAQEFLSFVMDRMHAELLKldgkSSSTNGGKSFVVASAEDDEWETVGRKNK 343
Cdd:cd02658 78 giKPSMFKALIGKGHPEFSTM-----RQQDALEFLLHLIDKLDRESFK----NLGLNPNDLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 344 TavMRTQSF--VPSELSEIfwgelasmvkakGNKPSGTQqpffslhldIYPDAvrTIEDALRLFSAPETLEGYRPSAAGK 421
Cdd:cd02658 149 T--SELSEIlsLPVPKDEA------------TEKEEGEL---------VYEPV--PLEDCLKAYFAPETIEDFCSTCKEK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 422 AGVvaaSKSMKIQKQSKIMILHLKRFGYGSHG-STKLNKPVHFPLELVlnrdllvsssteGRKYELVATITHHGRESSKG 500
Cdd:cd02658 204 TTA---TKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPIDVPEELG------------PGKYELIAFISHKGTSVHSG 268
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 659090146 501 HYTADVR---YHNNQWLRFDDASVTAIGKNNVLHDRAYVLFYK 540
Cdd:cd02658 269 HYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-539 |
2.04e-21 |
|
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: 94.38 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVDLLrnlknreipkvgystltafvefisaLEVPSstvpnrdvaafdvgkpfspLMF 270
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL-------------------------SETPK-------------------ELF 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 271 DGVLKnFSPDLPSGilgrpRQEDAQEFLSFVMDRMhaellkldgkssstnggksfvvasaeddewetvgrknktavmrtQ 350
Cdd:cd02667 37 SQVCR-KAPQFKGY-----QQQDSHELLRYLLDGL--------------------------------------------R 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 351 SFVPSelseIFWGELASMVKA-KGNKPSGTQQPFFSLHLDIYPDAV--RTIEDALRLFSAPETLEGyrPSAAGKAGVVAA 427
Cdd:cd02667 67 TFIDS----IFGGELTSTIMCeSCGTVSLVYEPFLDLSLPRSDEIKseCSIESCLKQFTEVEILEG--NNKFACENCTKA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 428 SKSMKIQKQSKIMILHLKRF-GYGSHGSTKLNKPVHFPLELVLNR----DLLVSSSTEGRKYELVATITHHGrESSKGHY 502
Cdd:cd02667 141 KKQYLISKLPPVLVIHLKRFqQPRSANLRKVSRHVSFPEILDLAPfcdpKCNSSEDKSSVLYRLYGVVEHSG-TMRSGHY 219
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 659090146 503 TADVRYHN----------------------NQWLRFDDASVTAIGKNNVLHDRAYVLFY 539
Cdd:cd02667 220 VAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-539 |
4.81e-19 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 86.65 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVDLLRNLKNreipkvgystltafvefisalevpsstvpnrdvaafdvgkpfsplmf 270
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFLE----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 271 dgvlknfspdlpsgilgrprQEDAQEFLSFVMDRMHAellkldgkssstnggksfvvasaeddewetvgrknktavmrtQ 350
Cdd:cd02662 34 --------------------QQDAHELFQVLLETLEQ------------------------------------------L 51
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 351 SFVPSElseifwGELASMVK--AKGNKPSGTQQPFFSLHLDIyPDAVR----TIEDALRLFSAPETLEGYRpsaagkagv 424
Cdd:cd02662 52 LKFPFD------GLLASRIVclQCGESSKVRYESFTMLSLPV-PNQSSgsgtTLEHCLDDFLSTEIIDDYK--------- 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 425 vAASKSMKIQKQSKIMILHLKRFGYGSHG-STKLNKPVHFPLELvlnrdllvssstEGRKYELVATITHHGRESSkGHYT 503
Cdd:cd02662 116 -CDRCQTVIVRLPQILCIHLSRSVFDGRGtSTKNSCKVSFPERL------------PKVLYRLRAVVVHYGSHSS-GHYV 181
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 659090146 504 ADVRYH---------------------NNQWLRFDDASVTAIGKNNVLHDR-AYVLFY 539
Cdd:cd02662 182 CYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVLEQKsAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
191-541 |
1.19e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 83.31 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVD--LLRNLKNreipkvgystLTAFVEFISAlevpSSTVPNRDVAAfdvgKPFSPL 268
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDelLDDLSKE----------LKVLKNVIRK----PEPDLNQEEAL----KLFTAL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 269 MFDGVLKnFSPDLPSGilgrpRQEDAQEFLSFVMDrmHAELLKldgkssstnggksfvVASAEDDEWETVGRKNKTAVmr 348
Cdd:COG5533 63 WSSKEHK-VGWIPPMG-----SQEDAHELLGKLLD--ELKLDL---------------VNSFTIRIFKTTKDKKKTST-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 349 tqsfvpSELSEIFwgelASMVKAKGNKPSGTQQPFFSLHLDIYPDAVRTIEdalrlfSAPETLEgyrpsaagkaGVVAAS 428
Cdd:COG5533 118 ------GDWFDII----IELPDQTWVNNLKTLQEFIDNMEELVDDETGVKA------KENEELE----------VQAKQE 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 429 KSMKIQKQSKIMILHLKRFGYgSHGSTKLNKPVHFPLELVLNRDLLVSSSTEGRkYELVATITHHGRESSkGHYTADVRy 508
Cdd:COG5533 172 YEVSFVKLPKILTIQLKRFAN-LGGNQKIDTEVDEKFELPVKHDQILNIVKETY-YDLVGFVLHQGSLEG-GHYIAYVK- 247
|
330 340 350
....*....|....*....|....*....|....*.
gi 659090146 509 HNNQWLRFDDASVTAI---GKNNVLHDRAYVLFYKQ 541
Cdd:COG5533 248 KGGKWEKANDSDVTPVseeEAINEKAKNAYLYFYER 283
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-542 |
8.95e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 81.53 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFvdllRNLKNReIPKVGYSTLTAFVefISALEVPSS---TVPNRDVAAFDVGKPFSp 267
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEF----RNAVYS-IPPTEDDDDNKSV--PLALQRLFLflqLSESPVKTTELTDKTRS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 268 lmFDG-VLKNFspdlpsgilgrpRQEDAQEFLSFVMDrmhaellKLDGKSSSTnggksfvvasaeddewetvGRKNKtav 346
Cdd:cd02659 76 --FGWdSLNTF------------EQHDVQEFFRVLFD-------KLEEKLKGT-------------------GQEGL--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 347 mrtqsfvpseLSEIFWGELASMVKAKG-NKPSGTQQPFFSLHLDIYPdaVRTIEDALRLFSAPETLEG---YRPSAAGKA 422
Cdd:cd02659 113 ----------IKNLFGGKLVNYIICKEcPHESEREEYFLDLQVAVKG--KKNLEESLDAYVQGETLEGdnkYFCEKCGKK 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 423 GVVaaSKSMKIQKQSKIMILHLKRFGYG--SHGSTKLNKPVHFPLELVLN----RDLLVSSSTEGRK------YELVATI 490
Cdd:cd02659 181 VDA--EKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLELDMEpyteKGLAKKEGDSEKKdsesyiYELHGVL 258
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659090146 491 THHGRESSkGHYTA---DVRyhNNQWLRFDDASVTAIGKNNVLHD----------------------RAYVLFYKQV 542
Cdd:cd02659 259 VHSGDAHG-GHYYSyikDRD--DGKWYKFNDDVVTPFDPNDAEEEcfggeetqktydsgprafkrttNAYMLFYERK 332
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
397-540 |
1.20e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 83.39 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 397 TIEDALRLFSAPETL-----------EGYRPSaagkagvvaaSKSMKIQKQSKIMILHLKRFGYGSHGSTKLNKPVHFPL 465
Cdd:COG5560 676 TLQDCLNEFSKPEQLglsdswycpgcKEFRQA----------SKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPI 745
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659090146 466 -ELVLNRdLLVSSSTEGRKYELVATITHHGRESSkGHYTADVR-YHNNQWLRFDDASVTAIGKNNVLHDRAYVLFYK 540
Cdd:COG5560 746 dDLDLSG-VEYMVDDPRLIYDLYAVDNHYGGLSG-GHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-540 |
7.35e-13 |
|
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: 69.92 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 176 ASNVSVTSSTTLLP-RGLINSGNLCFLNSTLQALLSCPPFVDLLRNLKNREIPKvgySTLTAFVEFISAL--EVPSSTVP 252
Cdd:cd02671 10 SSATSCEKRENLLPfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSV---EQLQSSFLLNPEKynDELANQAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 253 NRDVAAFDVGKPfsplMFDGVLknfspdlpsgilgrprQEDAQEFLSFVMDRMHaELLKLDGKSSstnggksfVVASAED 332
Cdd:cd02671 87 RRLLNALREVNP----MYEGYL----------------QHDAQEVLQCILGNIQ-ELVEKDFQGQ--------LVLRTRC 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 333 DEWETVGRknktavmRTQSF----VPSELSEIFWGELASmvkakgnkpsgtqqpffslhlDIYPDA---VRTIEDALRLF 405
Cdd:cd02671 138 LECETFTE-------RREDFqdisVPVQESELSKSEESS---------------------EISPDPkteMKTLKWAISQF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 406 SAPETLEGY-RPSAAGKAGVVAASKSMKIQKQSKIMILHLKRFGYGSH------GSTKLNKPVHFPLELVLNRdllVSSS 478
Cdd:cd02671 190 ASVERIVGEdKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSefdcygGLSKVNTPLLTPLKLSLEE---WSTK 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659090146 479 TEGRKYELVATITHHGRESSKGHYTADVRyhnnqWLRFDDASV---------TAIGKNNVLHDRAYVLFYK 540
Cdd:cd02671 267 PKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFYK 332
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-527 |
3.53e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 67.45 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLscppfvdllRNLKNREIpkvgystltafvefisALEVPSSTVPNRDVAAFDvgKPFSP--- 267
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWF---------MNLEFRKA----------------VYECNSTEDAELKNMPPD--KPHEPqti 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 268 -----LMFdGVLKNFSPDL--PSGI-----LGRPRQEDAQEFLSFVMDRMHAELLKLDGKSSSTnggksfvvasaeddew 335
Cdd:cd02668 54 idqlqLIF-AQLQFGNRSVvdPSGFvkalgLDTGQQQDAQEFSKLFLSLLEAKLSKSKNPDLKN---------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 336 etvgrknktavmrtqsFVPselsEIFWGELA-SMVKAKGNKPSGTQQPFFSLHLDIypDAVRTIEDALRLFSAPETLEG- 413
Cdd:cd02668 117 ----------------IVQ----DLFRGEYSyVTQCSKCGRESSLPSKFYELELQL--KGHKTLEECIDEFLKEEQLTGd 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 414 YRPSAAGKAGVVAASKSMKIQKQSKIMILHLKRFGYGSHGST--KLNKPVHFPLELVLNRdLLVSSSTEGRKYELVATIT 491
Cdd:cd02668 175 NQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAkkKLNASISFPEILDMGE-YLAESDEGSYVYELSGVLI 253
|
330 340 350
....*....|....*....|....*....|....*..
gi 659090146 492 HHGRESSKGHYTADVR-YHNNQWLRFDDASVTAIGKN 527
Cdd:cd02668 254 HQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-540 |
5.63e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 67.13 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFV-DLLRNLKNREIPKVgySTLTAFVEFISALEVPSstvpnrdvaafdvGKPFSPlm 269
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRrQVLSLNLPRLGDSQ--SVMKKLQLLQAHLMHTQ-------------RRAEAP-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 270 fdgVLKNFSPDLPSGILGRpRQEDAQEFLSFVMDRMHAELLKldgkssstnggksfvvasaeddeweTVGRKNKTAVMRT 349
Cdd:cd02664 64 ---PDYFLEASRPPWFTPG-SQQDCSEYLRYLLDRLHTLIEK-------------------------MFGGKLSTTIRCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 350 QSFVPSELSEIFwgelasmvkakgnkpsgtqqPFFSLhldiypdAVRTIEDALRLFSAPETLEG----YRPSAAGKAGVV 425
Cdd:cd02664 115 NCNSTSARTERF--------------------RDLDL-------SFPSVQDLLNYFLSPEKLTGdnqyYCEKCASLQDAE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 426 aasKSMKIQKQSKIMILHLKRFGY--GSHGSTKL------NKPVHFPL-------ELVLNRDLLVSSSTEGR-----KYE 485
Cdd:cd02664 168 ---KEMKVTGAPEYLILTLLRFSYdqKTHVREKImdnvsiNEVLSLPVrveskssESPLEKKEEESGDDGELvtrqvHYR 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 486 LVATITHHGRESSKGHY--------TADVRYHNNQ-------------WLRFDDASVTAIGKN---NVL----HDRAYVL 537
Cdd:cd02664 245 LYAVVVHSGYSSESGHYftyardqtDADSTGQECPepkdaeendesknWYLFNDSRVTFSSFEsvqNVTsrfpKDTPYIL 324
|
...
gi 659090146 538 FYK 540
Cdd:cd02664 325 FYE 327
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
191-540 |
1.27e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 60.41 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVDLLRNLKNREIPKvgySTLTAFVEFISALevpsstvpnrdvaafdVGKPFSPLMF 270
Cdd:cd02669 121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIK---DRKSELVKRLSEL----------------IRKIWNPRNF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 271 DGvlkNFSPD-----------LPSGILgrpRQEDAQEFLSFVMDRMHAELLKLDGKSSStnggksfVVASAEDdewetvG 339
Cdd:cd02669 182 KG---HVSPHellqavskvskKKFSIT---EQSDPVEFLSWLLNTLHKDLGGSKKPNSS-------IIHDCFQ------G 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 340 RKNKTavmrTQSFVPSELSEIfwgelASMVKAKGNKPSGTQ-QPFFSLHLD-----IYPDAvrTIEDALRLFSAPETLEG 413
Cdd:cd02669 243 KVQIE----TQKIKPHAEEEG-----SKDKFFKDSRVKKTSvSPFLLLTLDlppppLFKDG--NEENIIPQVPLKQLLKK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 414 YrpSAAGKAGVVAASKSMKIQKQSKIMILHLKRFGYGSHGSTKLNKPVHFPLELVLNRDLL---VSSSTEGRKYELVATI 490
Cdd:cd02669 312 Y--DGKTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVhfdKPSLNLSTKYNLVANI 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 659090146 491 THHGRESSKGHYTADVRYH-NNQWLRFDDASVTAIGKNNVLHDRAYVLFYK 540
Cdd:cd02669 390 VHEGTPQEDGTWRVQLRHKsTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
191-395 |
1.74e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 60.67 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVDLL-----RNLKNREIPK-VGYSTLTAFVEFISALEVPsstvpnrDVAAfdvgkp 264
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFlsdeyEESINEENPLgMHGSVASAYADLIKQLYDG-------NLHA------ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 265 FSPLMFDGVLKNFSpdlpSGILGRpRQEDAQEFLSFVMDRMHAELLKLDGKSSSTN----GGKSFVVASAEDDEWETVGR 340
Cdd:COG5560 334 FTPSGFKKTIGSFN----EEFSGY-DQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKpdlsPGDDVVVKKKAKECWWEHLK 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 659090146 341 KNKtavmrtqsfvpSELSEIFWGELASMVKAKG-NKPSGTQQPFFSLHLDIYPDAV 395
Cdd:COG5560 409 RND-----------SIITDLFQGMYKSTLTCPGcGSVSITFDPFMDLTLPLPVSMV 453
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
191-532 |
4.92e-09 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 59.11 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 191 GLINSGNLCFLNSTLQALLSCPPFVDLLRNLKN---REIPKVGYSTLTAFVEfISALEVPSSTVpnrdvaafDVGKPFSP 267
Cdd:COG5077 195 GLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTdhpRGRDSVALALQRLFYN-LQTGEEPVDTT--------ELTRSFGW 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 268 LMFDGVLknfspdlpsgilgrprQEDAQEFLSFVMDRMhaellkldgkssstnggksfvvasaeddewETVGRKNKtavm 347
Cdd:COG5077 266 DSDDSFM----------------QHDIQEFNRVLQDNL------------------------------EKSMRGTV---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 348 rtqsfVPSELSEIFWGELASMVKA-KGNKPSGTQQPFFSLHLDIypDAVRTIEDALRLFSAPETLEGYRPSAAGKAGVVA 426
Cdd:COG5077 296 -----VENALNGIFVGKMKSYIKCvNVNYESARVEDFWDIQLNV--KGMKNLQESFRRYIQVETLDGDNRYNAEKHGLQD 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 427 ASKSMKIQKQSKIMILHLKRFGYG--SHGSTKLNKPVHFPLEL----VLNRDLLVSSSTEGrKYELVATITHHGrESSKG 500
Cdd:COG5077 369 AKKGVIFESLPPVLHLQLKRFEYDfeRDMMVKINDRYEFPLEIdllpFLDRDADKSENSDA-VYVLYGVLVHSG-DLHEG 446
|
330 340 350
....*....|....*....|....*....|...
gi 659090146 501 HYTADVRYH-NNQWLRFDDASVTAIGKNNVLHD 532
Cdd:COG5077 447 HYYALLKPEkDGRWYKFDDTRVTRATEKEVLEE 479
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
470-539 |
1.00e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 56.00 E-value: 1.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659090146 470 NRDLLVSSSTEGRKYELVATITHHGRESSKGHYTADVR--YHNNQWLRFDDASVTAIGKNNVLHD---RAYVLFY 539
Cdd:cd02673 170 NEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKelYNGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
433-540 |
3.59e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 48.29 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 433 IQKQSKIMILHLKRFGYGSHGSTKLNKPVHFPLELVL-------NRDLLVSSSTEGRKYE--------------LVATIT 491
Cdd:cd02670 95 FAKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIpdfvaddPRACSKCQLECRVCYDdkdfsptcgkfklsLCSAVC 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659090146 492 HHGRESSKGHYTADVRY------------HNNQWLRFDDASVTAIGKNNVLHDR------AYVLFYK 540
Cdd:cd02670 175 HRGTSLETGHYVAFVRYgsysltetdneaYNAQWVFFDDMADRDGVSNGFNIPAarlledPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
477-540 |
2.00e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 40.19 E-value: 2.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 659090146 477 SSTEGRKYELVATITHHGRESSKGHYTADVRYHNN-----QWLRFDDASVTAIGKNnvlhdrAYVLFYK 540
Cdd:cd02672 206 GQESIYKYELVGYVCEINDSSRGQHNVVFVIKVNEesthgRWYLFNDFLVTPVSEL------AYILLYQ 268
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
359-539 |
6.11e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 38.31 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 359 EIFWGElASMVKAKGNKPSGTQQPFFSLHLDIypDAVRTIEDALRlfsaPETLEGYRPSAAGKAGVVAASKSMkIQKQSK 438
Cdd:cd02665 59 QLFYGT-FLTEGVLEGKPFCNCETFGQYPLQV--NGYGNLHECLE----AAMFEGEVELLPSDHSVKSGQERW-FTELPP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659090146 439 IMILHLKRFGYGSHGSTKLNKPVHFPLELvlnrdllvssstEGRKYELVATITHHGrESSKGHYTADV-RYHNNQWLRFD 517
Cdd:cd02665 131 VLTFELSRFEFNQGRPEKIHDKLEFPQII------------QQVPYELHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYN 197
|
170 180 190
....*....|....*....|....*....|
gi 659090146 518 DASVTAIGKNNVLHD--------RAYVLFY 539
Cdd:cd02665 198 DISVTESSWEEVERDsfgggrnpSAYCLMY 227
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
463-521 |
8.56e-03 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 38.41 E-value: 8.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659090146 463 FPLELVLNRDLLVSSSTEGRKYELVATITHHGRESSKGHYTADVR----YH----NNQWLRFDDASV 521
Cdd:pfam13423 239 LPPEIGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadsELedptESQWYLFNDFLV 305
|
|
| |
