|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
4.06e-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: 313.07 E-value: 4.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 611
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 612 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSV 691
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTST 62
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 692 TFDPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR-- 765
Cdd:cd02674 63 TFEPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgs 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 766 WSKLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVS 845
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVS 221
|
....*....
gi 24643789 846 SSAYILFYE 854
Cdd:cd02674 222 SSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
531-853 |
5.89e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 313.22 E-value: 5.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 531 CGLRNIGNTCFMNSVIQCLSHTQELTRFL--RSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHT-VTPMELKRAFSTKH 607
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLlrISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 608 RMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCG 687
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE------------------------NESLITDLFRGQLKSRLKCLSCG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 688 NTSVTFDPFWDLSVPLPSSSRCKLEA----CLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSE 763
Cdd:pfam00443 137 EVSETFEPFSDLSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 764 TR--WSKLSNIVEFPTsdsELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSD 836
Cdd:pfam00443 217 NRstWEKLNTEVEFPL---ELDLSRYlaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTE 293
|
330
....*....|....*..
gi 24643789 837 ALSENHLVSSSAYILFY 853
Cdd:pfam00443 294 VDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
532-854 |
5.86e-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: 239.69 E-value: 5.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 611
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 612 dyNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltweWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 691
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRT-------------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 692 TFDPFWDLSVPLP--SSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtRRKCTKSFTIQRFPKYLVIHLKRFSETRW--- 766
Cdd:cd02257 80 STEPELFLSLPLPvkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDgtk 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 767 SKLSNIVEFPtsdSELNMGSY-------GANSNSNVHYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSDAL 838
Cdd:cd02257 159 EKLNTKVSFP---LELDLSPYlsegekdSDSDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVS 235
|
330 340
....*....|....*....|
gi 24643789 839 SE----NHLVSSSAYILFYE 854
Cdd:cd02257 236 EEevleFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
531-853 |
3.21e-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: 3.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 531 CGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMY 610
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 611 SDYNQQDAQEFLRFFLDSLHSA-LNSGVKGETLNIDDNlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNT 689
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAcLDRFKKLKAVDPSSQ-----------------ETTLVQQIFGGYLRSQVKCLNCKHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 690 SVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKL 769
Cdd:cd02661 145 SNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 770 SNIVEFPtsdSELNMGSYGANSNSN-VHYSLYAISNHMG-STAGGHYVALCKHPvSRKWHEFNDNIVSdALSENHLVSSS 847
Cdd:cd02661 223 NKQISFP---ETLDLSPYMSQPNDGpLKYKLYAVLVHSGfSPHSGHYYCYVKSS-NGKWYNMDDSKVS-PVSIETVLSQK 297
|
....*.
gi 24643789 848 AYILFY 853
Cdd:cd02661 298 AYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-853 |
6.35e-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: 190.28 E-value: 6.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSH-HgsrSLSTKDQQILH----EFAKLIQEMW-TANVHTVTPMELKRAFST 605
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDrH---SCTCLSCSPNSclscAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 606 KHRMYSDYNQQDAQEFLRFFLDSLHSAlNSGVKGETlniddnlSDNKkadltwewytrHENSLVRDLFVGQLKSTLKCTT 685
Cdd:cd02660 79 HSRNLAGYSQQDAHEFFQFLLDQLHTH-YGGDKNEA-------NDES-----------HCNCIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 686 CGNTSVTFDPFWDLSVPLPSSSRC-------------KLEACLDLFIREEVLdGDEMPTCAKCKTRRKCTKSFTIQRFPK 752
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 753 YLVIHLKRF---SETRWSKLSNIVEFPTsdsELNMGSYGANS----------NSNVHYSLYAISNHMGSTAGGHYVALCK 819
Cdd:cd02660 219 VLCFQLKRFehsLNKTSRKIDTYVQFPL---ELNMTPYTSSSigdtqdsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCR 295
|
330 340 350
....*....|....*....|....*....|....
gi 24643789 820 HPVSrKWHEFNDNIVSdALSENHLVSSSAYILFY 853
Cdd:cd02660 296 QGDG-QWFKFDDAMIT-RVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
1.06e-52 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 185.28 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRflrshhgsrslstkdqqilhefakLIQEmwtanvhtvTPMELKRAFSTKHRMYS 611
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE------------------------LLSE---------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 612 DYNQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsdnkkadltwewytrheNSLVRDLFVGQLKSTLKCTTCGNTSV 691
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL------------------------------------RTFIDSIFGGELTSTIMCESCGTVSL 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 692 TFDPFWDLSVPL--PSSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtrrKCTKSFTIQRFPKYLVIHLKRFSETRWS-- 767
Cdd:cd02667 92 VYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnl 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 768 -KLSNIVEFPtsdSELNMGSY------GANSNSNVHYSLYAISNHMGSTAGGHYVA----------LCKH---------- 820
Cdd:cd02667 169 rKVSRHVSFP---EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAyvkvrppqqrLSDLtkskpaadea 245
|
330 340 350
....*....|....*....|....*....|....*
gi 24643789 821 -PVSRKWHEFNDNIVSdALSENHLVSSSAYILFYE 854
Cdd:cd02667 246 gPGSGQWYYISDSDVR-EVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
526-706 |
5.24e-47 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 180.46 E-value: 5.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 526 KSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELK 600
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 601 RAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVG 675
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQG 420
|
170 180 190
....*....|....*....|....*....|.
gi 24643789 676 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS 706
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
1.23e-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: 165.95 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTrflrshhgsrslSTKD--QQILHEFAKliqemwtanVHTVTPMELKRAFSTKHRM 609
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT------------CLKDlfESISEQKKR---------TGVISPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 610 YSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKADLTWewytrhenslVRDLFVGQLKSTLKCTTCGNT 689
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNETRCLTCETV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 690 SVTFDPFWDLSVPLPSSsrCKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF--SET--R 765
Cdd:cd02663 130 SSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQlnR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 766 WSKLSNIVEFPTsdsELNM-GSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHpvSRKWHEFNDNIVsDALSENHL 843
Cdd:cd02663 208 YIKLFYRVVFPL---ELRLfNTTDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETV-EKIDENAV 281
|
330
....*....|....*....
gi 24643789 844 V--------SSSAYILFYE 854
Cdd:cd02663 282 EeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
1.69e-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: 166.44 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFL--------RSHHGSRSLSTKDQQ-ILHEFAKLIQEMWTANVHTVTPMELKRA 602
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnstedAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 603 FStkhrmYSDYNQQDAQEFLRFFLDSLHSALNSgvkgetlniddnlSDNKKAdltwewytrheNSLVRDLFVGQLKSTLK 682
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEAKLSK-------------SKNPDL-----------KNIVQDLFRGEYSYVTQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 683 CTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS 762
Cdd:cd02668 132 CSKCGRESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 763 ETRWS----KLSNIVEFPtsdSELNMGSYGANSNSNVH-YSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSD 836
Cdd:cd02668 210 FDRKTgakkKLNASISFP---EILDMGEYLAESDEGSYvYELSGVLIHQGVSAySGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
330 340 350
....*....|....*....|....*....|....*...
gi 24643789 837 --------------------ALSENHLVSSSAYILFYE 854
Cdd:cd02668 287 mpgkplklgnsedpakprksEIKKGTHSSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
529-855 |
4.14e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 165.51 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 529 GLCGLRNIGNTCFMNSVIQCLSHTQELtRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHR 608
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEF-RNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 609 MYSDYNQQDAQEFLRFFLDSLHSALnsgvKGetlniddnlsdnkkadltwewyTRHENsLVRDLFVGQLKSTLKCTTCGN 688
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKL----KG----------------------TGQEG-LIKNLFGGKLVNYIICKECPH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 689 TSVTFDPFWDLSVPLpssSRCK-LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF-----S 762
Cdd:cd02659 133 ESEREEYFLDLQVAV---KGKKnLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 763 ETRwSKLSNIVEFPtsdSELNMGSY-------------GANSNSNVhYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEF 829
Cdd:cd02659 210 MMR-IKINDRFEFP---LELDMEPYtekglakkegdseKKDSESYI-YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKF 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24643789 830 NDNIVS-----DALSEN----------------HLVSSSAYILFYER 855
Cdd:cd02659 285 NDDVVTpfdpnDAEEECfggeetqktydsgpraFKRTTNAYMLFYER 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
1.17e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 138.01 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRslsTKDQQILheFAKLIQEMWTANVHTVTPMELKRAF--STKHRM 609
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPR---LGDSQSV--MKKLQLLQAHLMHTQRRAEAPPDYFleASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 610 YSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNT 689
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLHT------------------------------------LIEKMFGGKLSTTIRCLNCNST 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 690 SVTFD--PFWDLSVPLpsssrckLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS----- 762
Cdd:cd02664 120 SARTErfRDLDLSFPS-------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkt 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 763 ETRWSKLSNI-----VEFPTSDS-----------ELNMGSYGANSNSNVHYSLYAISNHMG-STAGGHYVALCKHPVSRK 825
Cdd:cd02664 193 HVREKIMDNVsinevLSLPVRVEskssesplekkEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQTDAD 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24643789 826 --------------------WHEFNDNIVSDALSE---NHLV---SSSAYILFYE 854
Cdd:cd02664 273 stgqecpepkdaeendesknWYLFNDSRVTFSSFEsvqNVTSrfpKDTPYILFYE 327
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
6.05e-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: 126.68 E-value: 6.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQEL-TRFLRSHHGSRSLSTKDQQILHEFAKLIQEMwTANVHTVTPMELKRAFSTKHRMY 610
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELrDALKNYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 611 SD------YNQQDAQEFLRFFLDSLHSALNSGVKgetlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCT 684
Cdd:cd02657 80 AEkqnqggYAQQDAEECWSQLLSVLSQKLPGAGS--------------------------KGSFIDQLFGIELETKMKCT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 685 TCGN-TSVTFDPFWDLSVPLPSSSRCK-LEACLDLFIREEV------LDGDEMPTcakcKTRRkctksftIQRFPKYLVI 756
Cdd:cd02657 134 ESPDeEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEIekhsptLGRDAIYT----KTSR-------ISRLPKYLTV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 757 HLKRF----SETRWSKLSNIVEFPtsdseLNMGSYGANSNSNVhYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFND 831
Cdd:cd02657 203 QFVRFfwkrDIQKKAKILRKVKFP-----FELDLYELCTPSGY-YELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDD 276
|
330 340 350
....*....|....*....|....*....|...
gi 24643789 832 NIVS-------DALS---ENHlvssSAYILFYE 854
Cdd:cd02657 277 DKVSevteediLKLSgggDWH----IAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
8.09e-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: 8.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--QQILHEFAKLIQEM-----------WTANVHT---VT 595
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKLADGLlsgryskpaslKSENDPYqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 596 PMELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTwewytrhenslvrDLFVG 675
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDK---------------LDRESFKNLGLNPN-------------DLFKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 676 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS------------SRCKLEACLDLFIREEVLDGdempTCAKCKTRRKCTK 743
Cdd:cd02658 133 MIEDRLECLSCKKVKYTSELSEILSLPVPKDeatekeegelvyEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 744 SFTIQRFPKYLVIHLKRFS-ETRW--SKLSNIVEFPtsdSELNMGSygansnsnvhYSLYAISNHMG-STAGGHYVALCK 819
Cdd:cd02658 209 TTGFKTFPDYLVINMKRFQlLENWvpKKLDVPIDVP---EELGPGK----------YELIAFISHKGtSVHSGHYVAHIK 275
|
330 340 350
....*....|....*....|....*....|....*...
gi 24643789 820 HPVSR--KWHEFNDNIVsdALSEN-HLVSSSAYILFYE 854
Cdd:cd02658 276 KEIDGegKWVLFNDEKV--VASQDpPEMKKLGYIYFYQ 311
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
711-855 |
8.99e-30 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 126.92 E-value: 8.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 711 LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS--KLSNIVEFPTSDSELNMGSYg 788
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDDLDLSGVEY- 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24643789 789 ANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENhLVSSSAYILFYER 855
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPED-SVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
529-854 |
3.68e-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: 121.66 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 529 GLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANV--HTVTPMELKRAFSTK 606
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 607 -HRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKadLTWEWYTRHENSLvrdlfvGQLKSTLKCTT 685
Cdd:cd02669 198 sKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSIIHDCFQGKVQ--IETQKIKPHAEEE------GSKDKFFKDSR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 686 CGNTSVTfdPFWDLSVPLPSSSrckleacldLFIRE------------EVLDGDEMPTCAKCKTRRkctKSFTIQRFPKY 753
Cdd:cd02669 270 VKKTSVS--PFLLLTLDLPPPP---------LFKDGneeniipqvplkQLLKKYDGKTETELKDSL---KRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 754 LVIHLKRFSETRWSKLSN--IVEFPTSDSELN--MGSYGANSNSNVHYSLyaISN--HMGSTAG-GHYVALCKHPVSRKW 826
Cdd:cd02669 336 LIFHIKRFSKNNFFKEKNptIVNFPIKNLDLSdyVHFDKPSLNLSTKYNL--VANivHEGTPQEdGTWRVQLRHKSTNKW 413
|
330 340
....*....|....*....|....*...
gi 24643789 827 HEFNDNIVSDALSENHLVSSSaYILFYE 854
Cdd:cd02669 414 FEIQDLNVKEVLPQLIFLSES-YIQIWE 440
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-854 |
3.16e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 114.00 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFLrshhgsrslstkdQQILhefakliqemwtanvhtvtpmelkrafstkhrmys 611
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-------------EEFL----------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 612 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCG-NTS 690
Cdd:cd02662 33 --EQQDAHELFQVLLETLEQ------------------------------------LLKFPFDGLLASRIVCLQCGeSSK 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 691 VTFDPFWDLSVPLPSSSR---CKLEACLDLFIREEVLDGdemPTCAKCKTrrkctksfTIQRFPKYLVIHLKRFSETRW- 766
Cdd:cd02662 75 VRYESFTMLSLPVPNQSSgsgTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRSVFDGRg 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 767 --SKLSNIVEFPtsdSELnmgsygansnSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRK------------------- 825
Cdd:cd02662 144 tsTKNSCKVSFP---ERL----------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstsh 210
|
330 340 350
....*....|....*....|....*....|
gi 24643789 826 -WHEFNDNIVSDALSENHLVSSSAYILFYE 854
Cdd:cd02662 211 pWWRISDTTVKEVSESEVLEQKSAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
519-853 |
6.45e-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: 112.68 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 519 ASSSRDEKSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLrsHHGSRSLSTKDQ-QILHEfakLIQEMWTANVHTVTPM 597
Cdd:cd02671 13 TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGL--KHLVSLISSVEQlQSSFL---LNPEKYNDELANQAPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 598 ELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQL 677
Cdd:cd02671 88 RLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE------------------------------------LVEKDFQGQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 678 KSTLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDL-----------------FIREEVLDGDEMPTCAKCKTRRK 740
Cdd:cd02671 132 VLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEIspdpktemktlkwaisqFASVERIVGEDKYFCENCHHYTE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 741 CTKSFTIQRFPKYLVIHLKRFSETRW--------SKLSNIVEFPTSDSELNMGSyganSNSNVHYSLYAISNHMGST-AG 811
Cdd:cd02671 212 AERSLLFDKLPEVITIHLKCFAANGSefdcygglSKVNTPLLTPLKLSLEEWST----KPKNDVYRLFAVVMHSGATiSS 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24643789 812 GHYVAlckhpvSRKWHEFNDNIVS--------DALSENHLVSSSAYILFY 853
Cdd:cd02671 288 GHYTA------YVRWLLFDDSEVKvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
532-856 |
3.37e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCL--------SHTQELTRFLRS----HHGSRSLSTKDQQIlhefaKLIQEMWTANVHTVTPmel 599
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldELLDDLSKELKVlknvIRKPEPDLNQEEAL-----KLFTALWSSKEHKVGW--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 600 krafstKHRMYSdynQQDAQEFLRFFLDSLhsalnsgvkgetlNIDDnlsdnkkadltwewytrhenslvrdlfVGQLKS 679
Cdd:COG5533 73 ------IPPMGS---QEDAHELLGKLLDEL-------------KLDL---------------------------VNSFTI 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 680 TLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDEmPTCAKCKT------RRKCTKSFTIQRFPKY 753
Cdd:COG5533 104 RIFKTTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMEELVDD-ETGVKAKEneelevQAKQEYEVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 754 LVIHLKRFS-ETRWSKLSNIVefptsDSELNMG---SYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKhpVSRKWHEF 829
Cdd:COG5533 183 LTIQLKRFAnLGGNQKIDTEV-----DEKFELPvkhDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKA 255
|
330 340
....*....|....*....|....*....
gi 24643789 830 NDNIVSDALSEN--HLVSSSAYILFYERT 856
Cdd:COG5533 256 NDSDVTPVSEEEaiNEKAKNAYLYFYERI 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
524-837 |
3.65e-21 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 99.56 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 524 DEKSE-GLCGLRNIGNTCFMNSVIQCLSHTQeltRFLRSHHG--SRSLSTKDQqILHEFAKLIQEMWTANvHTVTPMELK 600
Cdd:COG5077 186 NSKKEtGYVGLRNQGATCYMNSLLQSLFFIA---KFRKDVYGipTDHPRGRDS-VALALQRLFYNLQTGE-EPVDTTELT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 601 RAF---STKHRMysdynQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsDNKKADltwewyTRHENSLvRDLFVGQL 677
Cdd:COG5077 261 RSFgwdSDDSFM-----QHDIQEFNRVLQDNL--------------------EKSMRG------TVVENAL-NGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 678 KSTLKCTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDempTCAKCKTR--RKCTKSFTIQRFPKYLV 755
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLH 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 756 IHLKRFS---ET-RWSKLSNIVEFPtsdSELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKW 826
Cdd:COG5077 384 LQLKRFEydfERdMMVKINDRYEFP---LEIDLLPFldrdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRW 460
|
330
....*....|.
gi 24643789 827 HEFNDNIVSDA 837
Cdd:COG5077 461 YKFDDTRVTRA 471
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-853 |
1.79e-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: 72.52 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--------------------QQILHEFAKLIQEMWTANV 591
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterriggrevsrselqrsNQFVYELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 592 HTVTPmelkrafsTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDnkkadltwewytrhENSLVRD 671
Cdd:cd02666 83 RSVTP--------SKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKE--------------QSDLIKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 672 LFVGQLKSTL-KCTTCGNTSVTFDPFWDLSVPL----------PSSSRCKLEACLDLFIREEVL-----DGDEMPTCAKC 735
Cdd:cd02666 141 LFSGKTKQQLvPESMGNQPSVRTKTERFLSLLVdvgkkgreivVLLEPKDLYDALDRYFDYDSLtklpqRSQVQAQLAQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 736 KTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTSDSELNMGSYGANSNSNVhYSLYAISNHMGSTAGGHYV 815
Cdd:cd02666 221 LQRELISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYW 299
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24643789 816 ALCKHPVSRKWHEFNDNIVSDALSE---NHLVSSSA--YILFY 853
Cdd:cd02666 300 VYIKDFEENVWRKYNDETVTVVPASevfLFTLGNTAtpYFLVY 342
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
532-831 |
2.33e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 71.92 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLstKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTK----- 606
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECL--KEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 607 -HRMYSDYNQQDA-------QEFLRFFLDSLHSalnsgvkgETLNIDDNLSDNKkadltwewytrhenSLVRDLFVGQLK 678
Cdd:pfam13423 80 lGLLDEDRETNSAislssliQSFNRFLLDQLSS--------EENSTPPNPSPAE--------------SPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 679 STLKCTTCGNTSVTFDPF--WDLSVPLPSSSRCKLEACLDL-------FIREEVLDGdempTCAKCK------TRRkctk 743
Cdd:pfam13423 138 TTIRCSNCGHESVRESSThvLDLIYPRKPSSNNKKPPNQTFssilkssLERETTTKA----WCEKCKryqpleSRR---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 744 sfTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTsdsELNMGSYGANSNSN--VHYSLYAISNHMGSTAG-GHYVALCKH 820
Cdd:pfam13423 210 --TVRNLPPVLSLNAALTNEEWRQLWKTPGWLPP---EIGLTLSDDLQGDNeiVKYELRGVVVHIGDSGTsGHLVSFVKV 284
|
330
....*....|....*...
gi 24643789 821 PVSR-------KWHEFND 831
Cdd:pfam13423 285 ADSEledptesQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
533-854 |
3.68e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 58.31 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 533 LRNIGNTCFMNSVIQCLShtqeltrflrshhgsrSLStkdqQILHEFAkliqemwtanvhtvtpmelkrafstkhrmysD 612
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS----------------SIG----KINTEFD-------------------------------N 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 613 YNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTWEWYTRHENSLvrDLFVGQLKSTLKCTTCGNTSVT 692
Cdd:cd02673 31 DDQQDAHEFLLTLLEA---------------IDDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 693 FDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDemptCAKCKtrrkCTKSFTIQR---FPKYLVIHLKRFsetrwsKL 769
Cdd:cd02673 94 SDVGNFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSCK----CESAISSERimtFPECLSINLKRY------KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 770 SNIVEFPTSDSELNMGSYGANSNSnvhYSLYAISNHMG-STAGGHYVALCKHPVS-RKWHEFNDNIV----SDALSENhl 843
Cdd:cd02673 160 RIATSDYLKKNEEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIrpvsKNDVSTN-- 234
|
330
....*....|.
gi 24643789 844 VSSSAYILFYE 854
Cdd:cd02673 235 ARSSGYLIFYD 245
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
532-853 |
2.62e-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: 52.56 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 532 GLRNIGNTCFMNSVIQCLshtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkraFSTkhrmys 611
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-----------------------------------------------------FSQ------ 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 612 dynQQDAQEFLRFFLDSLHSALNSGVKGETlniDDNLSDNKKADLTWEwytrhenslvRDLFVGQLKST--LKCTTCGNT 689
Cdd:cd02665 22 ---QQDVSEFTHLLLDWLEDAFQAAAEAIS---PGEKSKNPMVQLFYG----------TFLTEGVLEGKpfCNCETFGQY 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 690 SVTFDPFWDLsvplpsssrcklEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKsftiqrFPKYLVIHLKRFS--ETRWS 767
Cdd:cd02665 86 PLQVNGYGNL------------HECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEfnQGRPE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643789 768 KLSNIVEFPtsdSELNmgsygansnsNVHYSLYAISNHMGSTAGGHYVA-LCKHPVSRkWHEFND---------NIVSDA 837
Cdd:cd02665 148 KIHDKLEFP---QIIQ----------QVPYELHAVLVHEGQANAGHYWAyIYKQSRQE-WEKYNDisvtessweEVERDS 213
|
330
....*....|....*.
gi 24643789 838 LSEnhLVSSSAYILFY 853
Cdd:cd02665 214 FGG--GRNPSAYCLMY 227
|
|
| |
