|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
7.22e-101 |
|
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: 314.23 E-value: 7.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 693
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 694 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSV 773
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTST 62
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 774 TFDPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR-- 847
Cdd:cd02674 63 TFEPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgs 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 848 WSKLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVS 927
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVS 221
|
....*....
gi 24643793 928 SSAYILFYE 936
Cdd:cd02674 222 SSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
613-935 |
8.78e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 314.77 E-value: 8.78e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 613 CGLRNIGNTCFMNSVIQCLSHTQELTRFL--RSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHT-VTPMELKRAFSTKH 689
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLlrISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 690 RMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCG 769
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE------------------------NESLITDLFRGQLKSRLKCLSCG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 770 NTSVTFDPFWDLSVPLPSSSRCKLEA----CLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSE 845
Cdd:pfam00443 137 EVSETFEPFSDLSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 846 TR--WSKLSNIVEFPTsdsELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSD 918
Cdd:pfam00443 217 NRstWEKLNTEVEFPL---ELDLSRYlaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTE 293
|
330
....*....|....*..
gi 24643793 919 ALSENHLVSSSAYILFY 935
Cdd:pfam00443 294 VDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
614-936 |
3.66e-73 |
|
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: 241.62 E-value: 3.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 693
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 694 dyNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltweWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 773
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRT-------------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 774 TFDPFWDLSVPLP--SSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtRRKCTKSFTIQRFPKYLVIHLKRFSETRW--- 848
Cdd:cd02257 80 STEPELFLSLPLPvkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDgtk 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 849 SKLSNIVEFPtsdSELNMGSY-------GANSNSNVHYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSDAL 920
Cdd:cd02257 159 EKLNTKVSFP---LELDLSPYlsegekdSDSDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVS 235
|
330 340
....*....|....*....|
gi 24643793 921 SE----NHLVSSSAYILFYE 936
Cdd:cd02257 236 EEevleFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
613-935 |
7.09e-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: 234.09 E-value: 7.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 613 CGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMY 692
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 693 SDYNQQDAQEFLRFFLDSLHSA-LNSGVKGETLNIDDNlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNT 771
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAcLDRFKKLKAVDPSSQ-----------------ETTLVQQIFGGYLRSQVKCLNCKHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 772 SVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKL 851
Cdd:cd02661 145 SNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 852 SNIVEFPtsdSELNMGSYGANSNSN-VHYSLYAISNHMG-STAGGHYVALCKHPvSRKWHEFNDNIVSdALSENHLVSSS 929
Cdd:cd02661 223 NKQISFP---ETLDLSPYMSQPNDGpLKYKLYAVLVHSGfSPHSGHYYCYVKSS-NGKWYNMDDSKVS-PVSIETVLSQK 297
|
....*.
gi 24643793 930 AYILFY 935
Cdd:cd02661 298 AYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-935 |
8.25e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 190.66 E-value: 8.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSH-HgsrSLSTKDQQILH----EFAKLIQEMW-TANVHTVTPMELKRAFST 687
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDrH---SCTCLSCSPNSclscAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 688 KHRMYSDYNQQDAQEFLRFFLDSLHSAlNSGVKGETlniddnlSDNKkadltwewytrHENSLVRDLFVGQLKSTLKCTT 767
Cdd:cd02660 79 HSRNLAGYSQQDAHEFFQFLLDQLHTH-YGGDKNEA-------NDES-----------HCNCIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 768 CGNTSVTFDPFWDLSVPLPSSSRC-------------KLEACLDLFIREEVLdGDEMPTCAKCKTRRKCTKSFTIQRFPK 834
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 835 YLVIHLKRF---SETRWSKLSNIVEFPTsdsELNMGSYGANS----------NSNVHYSLYAISNHMGSTAGGHYVALCK 901
Cdd:cd02660 219 VLCFQLKRFehsLNKTSRKIDTYVQFPL---ELNMTPYTSSSigdtqdsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCR 295
|
330 340 350
....*....|....*....|....*....|....
gi 24643793 902 HPVSrKWHEFNDNIVSdALSENHLVSSSAYILFY 935
Cdd:cd02660 296 QGDG-QWFKFDDAMIT-RVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
4.77e-53 |
|
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: 186.82 E-value: 4.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRflrshhgsrslstkdqqilhefakLIQEmwtanvhtvTPMELKRAFSTKHRMYS 693
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE------------------------LLSE---------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 694 DYNQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsdnkkadltwewytrheNSLVRDLFVGQLKSTLKCTTCGNTSV 773
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL------------------------------------RTFIDSIFGGELTSTIMCESCGTVSL 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 774 TFDPFWDLSVPL--PSSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtrrKCTKSFTIQRFPKYLVIHLKRFSETRWS-- 849
Cdd:cd02667 92 VYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnl 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 850 -KLSNIVEFPtsdSELNMGSY------GANSNSNVHYSLYAISNHMGSTAGGHYVA----------LCKH---------- 902
Cdd:cd02667 169 rKVSRHVSFP---EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAyvkvrppqqrLSDLtkskpaadea 245
|
330 340 350
....*....|....*....|....*....|....*
gi 24643793 903 -PVSRKWHEFNDNIVSdALSENHLVSSSAYILFYE 936
Cdd:cd02667 246 gPGSGQWYYISDSDVR-EVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
608-788 |
1.30e-47 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 183.16 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 608 KSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELK 682
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 683 RAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVG 757
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQG 420
|
170 180 190
....*....|....*....|....*....|.
gi 24643793 758 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS 788
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
1.14e-45 |
|
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: 166.33 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTrflrshhgsrslSTKD--QQILHEFAKliqemwtanVHTVTPMELKRAFSTKHRM 691
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT------------CLKDlfESISEQKKR---------TGVISPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 692 YSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKADLTWewytrhenslVRDLFVGQLKSTLKCTTCGNT 771
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNETRCLTCETV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 772 SVTFDPFWDLSVPLPSSsrCKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF--SET--R 847
Cdd:cd02663 130 SSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQlnR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 848 WSKLSNIVEFPTsdsELNM-GSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHpvSRKWHEFNDNIVsDALSENHL 925
Cdd:cd02663 208 YIKLFYRVVFPL---ELRLfNTTDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETV-EKIDENAV 281
|
330
....*....|....*....
gi 24643793 926 V--------SSSAYILFYE 936
Cdd:cd02663 282 EeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
1.36e-45 |
|
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: 166.83 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFL--------RSHHGSRSLSTKDQQ-ILHEFAKLIQEMWTANVHTVTPMELKRA 684
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnstedAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 685 FStkhrmYSDYNQQDAQEFLRFFLDSLHSALNSgvkgetlniddnlSDNKKAdltwewytrheNSLVRDLFVGQLKSTLK 764
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEAKLSK-------------SKNPDL-----------KNIVQDLFRGEYSYVTQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 765 CTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS 844
Cdd:cd02668 132 CSKCGRESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 845 ETRWS----KLSNIVEFPtsdSELNMGSYGANSNSNVH-YSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSD 918
Cdd:cd02668 210 FDRKTgakkKLNASISFP---EILDMGEYLAESDEGSYvYELSGVLIHQGVSAySGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
330 340 350
....*....|....*....|....*....|....*...
gi 24643793 919 --------------------ALSENHLVSSSAYILFYE 936
Cdd:cd02668 287 mpgkplklgnsedpakprksEIKKGTHSSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
611-937 |
5.40e-45 |
|
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: 165.51 E-value: 5.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 611 GLCGLRNIGNTCFMNSVIQCLSHTQELtRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHR 690
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEF-RNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 691 MYSDYNQQDAQEFLRFFLDSLHSALnsgvKGetlniddnlsdnkkadltwewyTRHENsLVRDLFVGQLKSTLKCTTCGN 770
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKL----KG----------------------TGQEG-LIKNLFGGKLVNYIICKECPH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 771 TSVTFDPFWDLSVPLpssSRCK-LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF-----S 844
Cdd:cd02659 133 ESEREEYFLDLQVAV---KGKKnLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 845 ETRwSKLSNIVEFPtsdSELNMGSY-------------GANSNSNVhYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEF 911
Cdd:cd02659 210 MMR-IKINDRFEFP---LELDMEPYtekglakkegdseKKDSESYI-YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKF 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24643793 912 NDNIVS-----DALSEN----------------HLVSSSAYILFYER 937
Cdd:cd02659 285 NDDVVTpfdpnDAEEECfggeetqktydsgpraFKRTTNAYMLFYER 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
2.86e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 139.93 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRslsTKDQQILheFAKLIQEMWTANVHTVTPMELKRAF--STKHRM 691
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPR---LGDSQSV--MKKLQLLQAHLMHTQRRAEAPPDYFleASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 692 YSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNT 771
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLHT------------------------------------LIEKMFGGKLSTTIRCLNCNST 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 772 SVTFD--PFWDLSVPLpsssrckLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS----- 844
Cdd:cd02664 120 SARTErfRDLDLSFPS-------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkt 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 845 ETRWSKLSNI-----VEFPTSDS-----------ELNMGSYGANSNSNVHYSLYAISNHMG-STAGGHYVALCKHPVSRK 907
Cdd:cd02664 193 HVREKIMDNVsinevLSLPVRVEskssesplekkEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQTDAD 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24643793 908 --------------------WHEFNDNIVSDALSE---NHLV---SSSAYILFYE 936
Cdd:cd02664 273 stgqecpepkdaeendesknWYLFNDSRVTFSSFEsvqNVTSrfpKDTPYILFYE 327
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
2.03e-32 |
|
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: 128.22 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQEL-TRFLRSHHGSRSLSTKDQQILHEFAKLIQEMwTANVHTVTPMELKRAFSTKHRMY 692
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELrDALKNYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 693 SD------YNQQDAQEFLRFFLDSLHSALNSGVKgetlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCT 766
Cdd:cd02657 80 AEkqnqggYAQQDAEECWSQLLSVLSQKLPGAGS--------------------------KGSFIDQLFGIELETKMKCT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 767 TCGN-TSVTFDPFWDLSVPLPSSSRCK-LEACLDLFIREEV------LDGDEMPTcakcKTRRkctksftIQRFPKYLVI 838
Cdd:cd02657 134 ESPDeEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEIekhsptLGRDAIYT----KTSR-------ISRLPKYLTV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 839 HLKRF----SETRWSKLSNIVEFPtsdseLNMGSYGANSNSNVhYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFND 913
Cdd:cd02657 203 QFVRFfwkrDIQKKAKILRKVKFP-----FELDLYELCTPSGY-YELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDD 276
|
330 340 350
....*....|....*....|....*....|...
gi 24643793 914 NIVS-------DALS---ENHlvssSAYILFYE 936
Cdd:cd02657 277 DKVSevteediLKLSgggDWH----IAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
9.19e-32 |
|
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: 126.28 E-value: 9.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--QQILHEFAKLIQEM-----------WTANVHT---VT 677
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKLADGLlsgryskpaslKSENDPYqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 678 PMELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTwewytrhenslvrDLFVG 757
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDK---------------LDRESFKNLGLNPN-------------DLFKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 758 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS------------SRCKLEACLDLFIREEVLDGdempTCAKCKTRRKCTK 825
Cdd:cd02658 133 MIEDRLECLSCKKVKYTSELSEILSLPVPKDeatekeegelvyEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 826 SFTIQRFPKYLVIHLKRFS-ETRW--SKLSNIVEFPtsdSELNMGSygansnsnvhYSLYAISNHMG-STAGGHYVALCK 901
Cdd:cd02658 209 TTGFKTFPDYLVINMKRFQlLENWvpKKLDVPIDVP---EELGPGK----------YELIAFISHKGtSVHSGHYVAHIK 275
|
330 340 350
....*....|....*....|....*....|....*...
gi 24643793 902 HPVSR--KWHEFNDNIVsdALSEN-HLVSSSAYILFYE 936
Cdd:cd02658 276 KEIDGegKWVLFNDEKV--VASQDpPEMKKLGYIYFYQ 311
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
793-937 |
3.16e-30 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 128.46 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 793 LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS--KLSNIVEFPTSDSELNMGSYg 870
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDDLDLSGVEY- 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24643793 871 ANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENhLVSSSAYILFYER 937
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPED-SVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
611-936 |
5.90e-29 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 121.27 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 611 GLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANV--HTVTPMELKRAFSTK 688
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 689 -HRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKadLTWEWYTRHENSLvrdlfvGQLKSTLKCTT 767
Cdd:cd02669 198 sKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSIIHDCFQGKVQ--IETQKIKPHAEEE------GSKDKFFKDSR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 768 CGNTSVTfdPFWDLSVPLPSSSrckleacldLFIRE------------EVLDGDEMPTCAKCKTRRkctKSFTIQRFPKY 835
Cdd:cd02669 270 VKKTSVS--PFLLLTLDLPPPP---------LFKDGneeniipqvplkQLLKKYDGKTETELKDSL---KRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 836 LVIHLKRFSETRWSKLSN--IVEFPTSDSELN--MGSYGANSNSNVHYSLyaISN--HMGSTAG-GHYVALCKHPVSRKW 908
Cdd:cd02669 336 LIFHIKRFSKNNFFKEKNptIVNFPIKNLDLSdyVHFDKPSLNLSTKYNL--VANivHEGTPQEdGTWRVQLRHKSTNKW 413
|
330 340
....*....|....*....|....*...
gi 24643793 909 HEFNDNIVSDALSENHLVSSSaYILFYE 936
Cdd:cd02669 414 FEIQDLNVKEVLPQLIFLSES-YIQIWE 440
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-936 |
6.75e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 115.93 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFLrshhgsrslstkdQQILhefakliqemwtanvhtvtpmelkrafstkhrmys 693
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-------------EEFL----------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 694 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCG-NTS 772
Cdd:cd02662 33 --EQQDAHELFQVLLETLEQ------------------------------------LLKFPFDGLLASRIVCLQCGeSSK 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 773 VTFDPFWDLSVPLPSSSR---CKLEACLDLFIREEVLDGdemPTCAKCKTrrkctksfTIQRFPKYLVIHLKRFSETRW- 848
Cdd:cd02662 75 VRYESFTMLSLPVPNQSSgsgTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRSVFDGRg 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 849 --SKLSNIVEFPtsdSELnmgsygansnSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRK------------------- 907
Cdd:cd02662 144 tsTKNSCKVSFP---ERL----------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstsh 210
|
330 340 350
....*....|....*....|....*....|
gi 24643793 908 -WHEFNDNIVSDALSENHLVSSSAYILFYE 936
Cdd:cd02662 211 pWWRISDTTVKEVSESEVLEQKSAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
601-935 |
5.22e-27 |
|
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: 113.06 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 601 ASSSRDEKSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLrsHHGSRSLSTKDQ-QILHEfakLIQEMWTANVHTVTPM 679
Cdd:cd02671 13 TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGL--KHLVSLISSVEQlQSSFL---LNPEKYNDELANQAPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 680 ELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQL 759
Cdd:cd02671 88 RLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE------------------------------------LVEKDFQGQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 760 KSTLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDL-----------------FIREEVLDGDEMPTCAKCKTRRK 822
Cdd:cd02671 132 VLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEIspdpktemktlkwaisqFASVERIVGEDKYFCENCHHYTE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 823 CTKSFTIQRFPKYLVIHLKRFSETRW--------SKLSNIVEFPTSDSELNMGSyganSNSNVHYSLYAISNHMGST-AG 893
Cdd:cd02671 212 AERSLLFDKLPEVITIHLKCFAANGSefdcygglSKVNTPLLTPLKLSLEEWST----KPKNDVYRLFAVVMHSGATiSS 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24643793 894 GHYVAlckhpvSRKWHEFNDNIVS--------DALSENHLVSSSAYILFY 935
Cdd:cd02671 288 GHYTA------YVRWLLFDDSEVKvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
614-938 |
3.80e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCL--------SHTQELTRFLRS----HHGSRSLSTKDQQIlhefaKLIQEMWTANVHTVTPmel 681
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldELLDDLSKELKVlknvIRKPEPDLNQEEAL-----KLFTALWSSKEHKVGW--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 682 krafstKHRMYSdynQQDAQEFLRFFLDSLhsalnsgvkgetlNIDDnlsdnkkadltwewytrhenslvrdlfVGQLKS 761
Cdd:COG5533 73 ------IPPMGS---QEDAHELLGKLLDEL-------------KLDL---------------------------VNSFTI 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 762 TLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDEmPTCAKCKT------RRKCTKSFTIQRFPKY 835
Cdd:COG5533 104 RIFKTTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMEELVDD-ETGVKAKEneelevQAKQEYEVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 836 LVIHLKRFS-ETRWSKLSNIVefptsDSELNMG---SYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKhpVSRKWHEF 911
Cdd:COG5533 183 LTIQLKRFAnLGGNQKIDTEV-----DEKFELPvkhDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKA 255
|
330 340
....*....|....*....|....*....
gi 24643793 912 NDNIVSDALSEN--HLVSSSAYILFYERT 938
Cdd:COG5533 256 NDSDVTPVSEEEaiNEKAKNAYLYFYERI 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
606-919 |
1.48e-21 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 101.10 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 606 DEKSE-GLCGLRNIGNTCFMNSVIQCLSHTQeltRFLRSHHG--SRSLSTKDQqILHEFAKLIQEMWTANvHTVTPMELK 682
Cdd:COG5077 186 NSKKEtGYVGLRNQGATCYMNSLLQSLFFIA---KFRKDVYGipTDHPRGRDS-VALALQRLFYNLQTGE-EPVDTTELT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 683 RAF---STKHRMysdynQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsDNKKADltwewyTRHENSLvRDLFVGQL 759
Cdd:COG5077 261 RSFgwdSDDSFM-----QHDIQEFNRVLQDNL--------------------EKSMRG------TVVENAL-NGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 760 KSTLKCTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDempTCAKCKTR--RKCTKSFTIQRFPKYLV 837
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLH 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 838 IHLKRFS---ET-RWSKLSNIVEFPtsdSELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKW 908
Cdd:COG5077 384 LQLKRFEydfERdMMVKINDRYEFP---LEIDLLPFldrdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRW 460
|
330
....*....|.
gi 24643793 909 HEFNDNIVSDA 919
Cdd:COG5077 461 YKFDDTRVTRA 471
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-935 |
1.25e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 73.29 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--------------------QQILHEFAKLIQEMWTANV 673
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterriggrevsrselqrsNQFVYELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 674 HTVTPmelkrafsTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDnkkadltwewytrhENSLVRD 753
Cdd:cd02666 83 RSVTP--------SKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKE--------------QSDLIKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 754 LFVGQLKSTL-KCTTCGNTSVTFDPFWDLSVPL----------PSSSRCKLEACLDLFIREEVL-----DGDEMPTCAKC 817
Cdd:cd02666 141 LFSGKTKQQLvPESMGNQPSVRTKTERFLSLLVdvgkkgreivVLLEPKDLYDALDRYFDYDSLtklpqRSQVQAQLAQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 818 KTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTSDSELNMGSYGANSNSNVhYSLYAISNHMGSTAGGHYV 897
Cdd:cd02666 221 LQRELISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYW 299
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24643793 898 ALCKHPVSRKWHEFNDNIVSDALSE---NHLVSSSA--YILFY 935
Cdd:cd02666 300 VYIKDFEENVWRKYNDETVTVVPASevfLFTLGNTAtpYFLVY 342
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
614-913 |
4.59e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 71.15 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLstKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTK----- 688
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECL--KEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 689 -HRMYSDYNQQDA-------QEFLRFFLDSLHSalnsgvkgETLNIDDNLSDNKkadltwewytrhenSLVRDLFVGQLK 760
Cdd:pfam13423 80 lGLLDEDRETNSAislssliQSFNRFLLDQLSS--------EENSTPPNPSPAE--------------SPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 761 STLKCTTCGNTSVTFDPF--WDLSVPLPSSSRCKLEACLDL-------FIREEVLDGdempTCAKCK------TRRkctk 825
Cdd:pfam13423 138 TTIRCSNCGHESVRESSThvLDLIYPRKPSSNNKKPPNQTFssilkssLERETTTKA----WCEKCKryqpleSRR---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 826 sfTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTsdsELNMGSYGANSNSN--VHYSLYAISNHMGSTAG-GHYVALCKH 902
Cdd:pfam13423 210 --TVRNLPPVLSLNAALTNEEWRQLWKTPGWLPP---EIGLTLSDDLQGDNeiVKYELRGVVVHIGDSGTsGHLVSFVKV 284
|
330
....*....|....*...
gi 24643793 903 PVSR-------KWHEFND 913
Cdd:pfam13423 285 ADSEledptesQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
615-936 |
6.62e-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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 60.62 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 615 LRNIGNTCFMNSVIQCLShtqeltrflrshhgsrSLStkdqQILHEFAkliqemwtanvhtvtpmelkrafstkhrmysD 694
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS----------------SIG----KINTEFD-------------------------------N 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 695 YNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTWEWYTRHENSLvrDLFVGQLKSTLKCTTCGNTSVT 774
Cdd:cd02673 31 DDQQDAHEFLLTLLEA---------------IDDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 775 FDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDemptCAKCKtrrkCTKSFTIQR---FPKYLVIHLKRFsetrwsKL 851
Cdd:cd02673 94 SDVGNFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSCK----CESAISSERimtFPECLSINLKRY------KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 852 SNIVEFPTSDSELNMGSYGANSNSnvhYSLYAISNHMG-STAGGHYVALCKHPVS-RKWHEFNDNIV----SDALSENhl 925
Cdd:cd02673 160 RIATSDYLKKNEEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIrpvsKNDVSTN-- 234
|
330
....*....|.
gi 24643793 926 VSSSAYILFYE 936
Cdd:cd02673 235 ARSSGYLIFYD 245
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
614-935 |
3.71e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 52.18 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 614 GLRNIGNTCFMNSVIQCLshtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkraFSTkhrmys 693
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-----------------------------------------------------FSQ------ 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 694 dynQQDAQEFLRFFLDSLHSALNSGVKGETlniDDNLSDNKKADLTWEwytrhenslvRDLFVGQLKST--LKCTTCGNT 771
Cdd:cd02665 22 ---QQDVSEFTHLLLDWLEDAFQAAAEAIS---PGEKSKNPMVQLFYG----------TFLTEGVLEGKpfCNCETFGQY 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 772 SVTFDPFWDLsvplpsssrcklEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKsftiqrFPKYLVIHLKRFS--ETRWS 849
Cdd:cd02665 86 PLQVNGYGNL------------HECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEfnQGRPE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643793 850 KLSNIVEFPtsdSELNmgsygansnsNVHYSLYAISNHMGSTAGGHYVA-LCKHPVSRkWHEFND---------NIVSDA 919
Cdd:cd02665 148 KIHDKLEFP---QIIQ----------QVPYELHAVLVHEGQANAGHYWAyIYKQSRQE-WEKYNDisvtessweEVERDS 213
|
330
....*....|....*.
gi 24643793 920 LSEnhLVSSSAYILFY 935
Cdd:cd02665 214 FGG--GRNPSAYCLMY 227
|
|
| |
