|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
6.04e-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: 315.00 E-value: 6.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 705
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 706 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSV 785
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTST 62
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 786 TFDPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR-- 859
Cdd:cd02674 63 TFEPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgs 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 860 WSKLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVS 939
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVS 221
|
....*....
gi 665392823 940 SSAYILFYE 948
Cdd:cd02674 222 SSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
625-947 |
7.91e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 315.15 E-value: 7.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 625 CGLRNIGNTCFMNSVIQCLSHTQELTRFL--RSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHT-VTPMELKRAFSTKH 701
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLlrISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 702 RMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCG 781
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE------------------------NESLITDLFRGQLKSRLKCLSCG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 782 NTSVTFDPFWDLSVPLPSSSRCKLEA----CLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSE 857
Cdd:pfam00443 137 EVSETFEPFSDLSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 858 TR--WSKLSNIVEFPTsdsELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSD 930
Cdd:pfam00443 217 NRstWEKLNTEVEFPL---ELDLSRYlaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTE 293
|
330
....*....|....*..
gi 665392823 931 ALSENHLVSSSAYILFY 947
Cdd:pfam00443 294 VDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
626-948 |
3.05e-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: 3.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 705
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 706 dyNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltweWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 785
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRT-------------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 786 TFDPFWDLSVPLP--SSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtRRKCTKSFTIQRFPKYLVIHLKRFSETRW--- 860
Cdd:cd02257 80 STEPELFLSLPLPvkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDgtk 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 861 SKLSNIVEFPtsdSELNMGSY-------GANSNSNVHYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSDAL 932
Cdd:cd02257 159 EKLNTKVSFP---LELDLSPYlsegekdSDSDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVS 235
|
330 340
....*....|....*....|
gi 665392823 933 SE----NHLVSSSAYILFYE 948
Cdd:cd02257 236 EEevleFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
625-947 |
8.01e-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: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 625 CGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMY 704
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 705 SDYNQQDAQEFLRFFLDSLHSA-LNSGVKGETLNIDDNlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNT 783
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAcLDRFKKLKAVDPSSQ-----------------ETTLVQQIFGGYLRSQVKCLNCKHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 784 SVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKL 863
Cdd:cd02661 145 SNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 864 SNIVEFPtsdSELNMGSYGANSNSN-VHYSLYAISNHMG-STAGGHYVALCKHPvSRKWHEFNDNIVSdALSENHLVSSS 941
Cdd:cd02661 223 NKQISFP---ETLDLSPYMSQPNDGpLKYKLYAVLVHSGfSPHSGHYYCYVKSS-NGKWYNMDDSKVS-PVSIETVLSQK 297
|
....*.
gi 665392823 942 AYILFY 947
Cdd:cd02661 298 AYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-947 |
8.00e-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: 8.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSH-HgsrSLSTKDQQILH----EFAKLIQEMW-TANVHTVTPMELKRAFST 699
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDrH---SCTCLSCSPNSclscAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 700 KHRMYSDYNQQDAQEFLRFFLDSLHSAlNSGVKGETlniddnlSDNKkadltwewytrHENSLVRDLFVGQLKSTLKCTT 779
Cdd:cd02660 79 HSRNLAGYSQQDAHEFFQFLLDQLHTH-YGGDKNEA-------NDES-----------HCNCIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 780 CGNTSVTFDPFWDLSVPLPSSSRC-------------KLEACLDLFIREEVLdGDEMPTCAKCKTRRKCTKSFTIQRFPK 846
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 847 YLVIHLKRF---SETRWSKLSNIVEFPTsdsELNMGSYGANS----------NSNVHYSLYAISNHMGSTAGGHYVALCK 913
Cdd:cd02660 219 VLCFQLKRFehsLNKTSRKIDTYVQFPL---ELNMTPYTSSSigdtqdsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCR 295
|
330 340 350
....*....|....*....|....*....|....
gi 665392823 914 HPVSrKWHEFNDNIVSdALSENHLVSSSAYILFY 947
Cdd:cd02660 296 QGDG-QWFKFDDAMIT-RVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
6.35e-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: 186.44 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRflrshhgsrslstkdqqilhefakLIQEmwtanvhtvTPMELKRAFSTKHRMYS 705
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE------------------------LLSE---------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 706 DYNQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsdnkkadltwewytrheNSLVRDLFVGQLKSTLKCTTCGNTSV 785
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL------------------------------------RTFIDSIFGGELTSTIMCESCGTVSL 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 786 TFDPFWDLSVPL--PSSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtrrKCTKSFTIQRFPKYLVIHLKRFSETRWS-- 861
Cdd:cd02667 92 VYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnl 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 862 -KLSNIVEFPtsdSELNMGSY------GANSNSNVHYSLYAISNHMGSTAGGHYVA----------LCKH---------- 914
Cdd:cd02667 169 rKVSRHVSFP---EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAyvkvrppqqrLSDLtkskpaadea 245
|
330 340 350
....*....|....*....|....*....|....*
gi 665392823 915 -PVSRKWHEFNDNIVSdALSENHLVSSSAYILFYE 948
Cdd:cd02667 246 gPGSGQWYYISDSDVR-EVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
620-800 |
1.49e-47 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 183.16 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 620 KSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELK 694
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 695 RAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVG 769
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQG 420
|
170 180 190
....*....|....*....|....*....|.
gi 665392823 770 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS 800
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
1.02e-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: 166.72 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTrflrshhgsrslSTKD--QQILHEFAKliqemwtanVHTVTPMELKRAFSTKHRM 703
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT------------CLKDlfESISEQKKR---------TGVISPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 704 YSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKADLTWewytrhenslVRDLFVGQLKSTLKCTTCGNT 783
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNETRCLTCETV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 784 SVTFDPFWDLSVPLPSSsrCKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF--SET--R 859
Cdd:cd02663 130 SSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQlnR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 860 WSKLSNIVEFPTsdsELNM-GSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHpvSRKWHEFNDNIVsDALSENHL 937
Cdd:cd02663 208 YIKLFYRVVFPL---ELRLfNTTDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETV-EKIDENAV 281
|
330
....*....|....*....
gi 665392823 938 V--------SSSAYILFYE 948
Cdd:cd02663 282 EeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
1.27e-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: 167.21 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFL--------RSHHGSRSLSTKDQQ-ILHEFAKLIQEMWTANVHTVTPMELKRA 696
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnstedAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 697 FSTkhrmySDYNQQDAQEFLRFFLDSLHSALNSgvkgetlniddnlSDNKKAdltwewytrheNSLVRDLFVGQLKSTLK 776
Cdd:cd02668 81 LGL-----DTGQQQDAQEFSKLFLSLLEAKLSK-------------SKNPDL-----------KNIVQDLFRGEYSYVTQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 777 CTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS 856
Cdd:cd02668 132 CSKCGRESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 857 ETRWS----KLSNIVEFPtsdSELNMGSYGANSNSNVH-YSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSD 930
Cdd:cd02668 210 FDRKTgakkKLNASISFP---EILDMGEYLAESDEGSYvYELSGVLIHQGVSAySGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
330 340 350
....*....|....*....|....*....|....*...
gi 665392823 931 --------------------ALSENHLVSSSAYILFYE 948
Cdd:cd02668 287 mpgkplklgnsedpakprksEIKKGTHSSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
623-949 |
5.56e-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: 5.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 623 GLCGLRNIGNTCFMNSVIQCLSHTQELtRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHR 702
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEF-RNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 703 MYSDYNQQDAQEFLRFFLDSLHSALnsgvKGetlniddnlsdnkkadltwewyTRHENsLVRDLFVGQLKSTLKCTTCGN 782
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKL----KG----------------------TGQEG-LIKNLFGGKLVNYIICKECPH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 783 TSVTFDPFWDLSVPLpssSRCK-LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF-----S 856
Cdd:cd02659 133 ESEREEYFLDLQVAV---KGKKnLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 857 ETRwSKLSNIVEFPtsdSELNMGSY-------------GANSNSNVhYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEF 923
Cdd:cd02659 210 MMR-IKINDRFEFP---LELDMEPYtekglakkegdseKKDSESYI-YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKF 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 665392823 924 NDNIVS-----DALSEN----------------HLVSSSAYILFYER 949
Cdd:cd02659 285 NDDVVTpfdpnDAEEECfggeetqktydsgpraFKRTTNAYMLFYER 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
3.08e-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: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRslsTKDQQILheFAKLIQEMWTANVHTVTPMELKRAF--STKHRM 703
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPR---LGDSQSV--MKKLQLLQAHLMHTQRRAEAPPDYFleASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 704 YSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNT 783
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLHT------------------------------------LIEKMFGGKLSTTIRCLNCNST 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 784 SVTFD--PFWDLSVPLpsssrckLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS----- 856
Cdd:cd02664 120 SARTErfRDLDLSFPS-------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkt 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 857 ETRWSKLSNI-----VEFPTSDS-----------ELNMGSYGANSNSNVHYSLYAISNHMG-STAGGHYVALCKHPVSRK 919
Cdd:cd02664 193 HVREKIMDNVsinevLSLPVRVEskssesplekkEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQTDAD 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 665392823 920 --------------------WHEFNDNIVSDALSE---NHLV---SSSAYILFYE 948
Cdd:cd02664 273 stgqecpepkdaeendesknWYLFNDSRVTFSSFEsvqNVTSrfpKDTPYILFYE 327
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
1.99e-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: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQEL-TRFLRSHHGSRSLSTKDQQILHEFAKLIQEMwTANVHTVTPMELKRAFSTKHRMY 704
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELrDALKNYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 705 SD------YNQQDAQEFLRFFLDSLHSALNSGVKgetlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCT 778
Cdd:cd02657 80 AEkqnqggYAQQDAEECWSQLLSVLSQKLPGAGS--------------------------KGSFIDQLFGIELETKMKCT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 779 TCGN-TSVTFDPFWDLSVPLPSSSRCK-LEACLDLFIREEV------LDGDEMPTcakcKTRRkctksftIQRFPKYLVI 850
Cdd:cd02657 134 ESPDeEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEIekhsptLGRDAIYT----KTSR-------ISRLPKYLTV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 851 HLKRF----SETRWSKLSNIVEFPtsdseLNMGSYGANSNSNVhYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFND 925
Cdd:cd02657 203 QFVRFfwkrDIQKKAKILRKVKFP-----FELDLYELCTPSGY-YELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDD 276
|
330 340 350
....*....|....*....|....*....|...
gi 665392823 926 NIVS-------DALS---ENHlvssSAYILFYE 948
Cdd:cd02657 277 DKVSevteediLKLSgggDWH----IAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
9.34e-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: 9.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--QQILHEFAKLIQEM-----------WTANVHT---VT 689
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKLADGLlsgryskpaslKSENDPYqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 690 PMELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTwewytrhenslvrDLFVG 769
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDK---------------LDRESFKNLGLNPN-------------DLFKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 770 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS------------SRCKLEACLDLFIREEVLDGdempTCAKCKTRRKCTK 837
Cdd:cd02658 133 MIEDRLECLSCKKVKYTSELSEILSLPVPKDeatekeegelvyEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 838 SFTIQRFPKYLVIHLKRFS-ETRW--SKLSNIVEFPtsdSELNMGSygansnsnvhYSLYAISNHMG-STAGGHYVALCK 913
Cdd:cd02658 209 TTGFKTFPDYLVINMKRFQlLENWvpKKLDVPIDVP---EELGPGK----------YELIAFISHKGtSVHSGHYVAHIK 275
|
330 340 350
....*....|....*....|....*....|....*...
gi 665392823 914 HPVSR--KWHEFNDNIVsdALSEN-HLVSSSAYILFYE 948
Cdd:cd02658 276 KEIDGegKWVLFNDEKV--VASQDpPEMKKLGYIYFYQ 311
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
805-949 |
3.49e-30 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 128.46 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 805 LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS--KLSNIVEFPTSDSELNMGSYg 882
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDDLDLSGVEY- 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665392823 883 ANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENhLVSSSAYILFYER 949
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPED-SVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
623-948 |
5.80e-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: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 623 GLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANV--HTVTPMELKRAFSTK 700
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 701 -HRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKadLTWEWYTRHENSLvrdlfvGQLKSTLKCTT 779
Cdd:cd02669 198 sKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSIIHDCFQGKVQ--IETQKIKPHAEEE------GSKDKFFKDSR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 780 CGNTSVTfdPFWDLSVPLPSSSrckleacldLFIRE------------EVLDGDEMPTCAKCKTRRkctKSFTIQRFPKY 847
Cdd:cd02669 270 VKKTSVS--PFLLLTLDLPPPP---------LFKDGneeniipqvplkQLLKKYDGKTETELKDSL---KRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 848 LVIHLKRFSETRWSKLSN--IVEFPTSDSELN--MGSYGANSNSNVHYSLyaISN--HMGSTAG-GHYVALCKHPVSRKW 920
Cdd:cd02669 336 LIFHIKRFSKNNFFKEKNptIVNFPIKNLDLSdyVHFDKPSLNLSTKYNL--VANivHEGTPQEdGTWRVQLRHKSTNKW 413
|
330 340
....*....|....*....|....*...
gi 665392823 921 HEFNDNIVSDALSENHLVSSSaYILFYE 948
Cdd:cd02669 414 FEIQDLNVKEVLPQLIFLSES-YIQIWE 440
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-948 |
8.55e-29 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 115.54 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFLrshhgsrslstkdQQILhefakliqemwtanvhtvtpmelkrafstkhrmys 705
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-------------EEFL----------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 706 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCG-NTS 784
Cdd:cd02662 33 --EQQDAHELFQVLLETLEQ------------------------------------LLKFPFDGLLASRIVCLQCGeSSK 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 785 VTFDPFWDLSVPLPSSSR---CKLEACLDLFIREEVLDGdemPTCAKCKTrrkctksfTIQRFPKYLVIHLKRFSETRW- 860
Cdd:cd02662 75 VRYESFTMLSLPVPNQSSgsgTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRSVFDGRg 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 861 --SKLSNIVEFPtsdSELnmgsygansnSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRK------------------- 919
Cdd:cd02662 144 tsTKNSCKVSFP---ERL----------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstsh 210
|
330 340 350
....*....|....*....|....*....|
gi 665392823 920 -WHEFNDNIVSDALSENHLVSSSAYILFYE 948
Cdd:cd02662 211 pWWRISDTTVKEVSESEVLEQKSAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
613-947 |
5.36e-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: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 613 ASSSRDEKSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLrsHHGSRSLSTKDQ-QILHEfakLIQEMWTANVHTVTPM 691
Cdd:cd02671 13 TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGL--KHLVSLISSVEQlQSSFL---LNPEKYNDELANQAPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 692 ELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQL 771
Cdd:cd02671 88 RLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE------------------------------------LVEKDFQGQL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 772 KSTLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDL-----------------FIREEVLDGDEMPTCAKCKTRRK 834
Cdd:cd02671 132 VLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEIspdpktemktlkwaisqFASVERIVGEDKYFCENCHHYTE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 835 CTKSFTIQRFPKYLVIHLKRFSETRW--------SKLSNIVEFPTSDSELNMGSyganSNSNVHYSLYAISNHMGST-AG 905
Cdd:cd02671 212 AERSLLFDKLPEVITIHLKCFAANGSefdcygglSKVNTPLLTPLKLSLEEWST----KPKNDVYRLFAVVMHSGATiSS 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 665392823 906 GHYVAlckhpvSRKWHEFNDNIVS--------DALSENHLVSSSAYILFY 947
Cdd:cd02671 288 GHYTA------YVRWLLFDDSEVKvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
626-950 |
3.86e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCL--------SHTQELTRFLRS----HHGSRSLSTKDQQIlhefaKLIQEMWTANVHTVTPmel 693
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldELLDDLSKELKVlknvIRKPEPDLNQEEAL-----KLFTALWSSKEHKVGW--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 694 krafstKHRMYSdynQQDAQEFLRFFLDSLhsalnsgvkgetlNIDDnlsdnkkadltwewytrhenslvrdlfVGQLKS 773
Cdd:COG5533 73 ------IPPMGS---QEDAHELLGKLLDEL-------------KLDL---------------------------VNSFTI 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 774 TLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDEmPTCAKCKT------RRKCTKSFTIQRFPKY 847
Cdd:COG5533 104 RIFKTTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMEELVDD-ETGVKAKEneelevQAKQEYEVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 848 LVIHLKRFS-ETRWSKLSNIVefptsDSELNMG---SYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKhpVSRKWHEF 923
Cdd:COG5533 183 LTIQLKRFAnLGGNQKIDTEV-----DEKFELPvkhDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKA 255
|
330 340
....*....|....*....|....*....
gi 665392823 924 NDNIVSDALSEN--HLVSSSAYILFYERT 950
Cdd:COG5533 256 NDSDVTPVSEEEaiNEKAKNAYLYFYERI 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
618-931 |
1.52e-21 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 101.10 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 618 DEKSE-GLCGLRNIGNTCFMNSVIQCLSHTQeltRFLRSHHG--SRSLSTKDQqILHEFAKLIQEMWTANvHTVTPMELK 694
Cdd:COG5077 186 NSKKEtGYVGLRNQGATCYMNSLLQSLFFIA---KFRKDVYGipTDHPRGRDS-VALALQRLFYNLQTGE-EPVDTTELT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 695 RAF---STKHRMysdynQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsDNKKADltwewyTRHENSLvRDLFVGQL 771
Cdd:COG5077 261 RSFgwdSDDSFM-----QHDIQEFNRVLQDNL--------------------EKSMRG------TVVENAL-NGIFVGKM 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 772 KSTLKCTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDempTCAKCKTR--RKCTKSFTIQRFPKYLV 849
Cdd:COG5077 309 KSYIKCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLH 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 850 IHLKRFS---ET-RWSKLSNIVEFPtsdSELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKW 920
Cdd:COG5077 384 LQLKRFEydfERdMMVKINDRYEFP---LEIDLLPFldrdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRW 460
|
330
....*....|.
gi 665392823 921 HEFNDNIVSDA 931
Cdd:COG5077 461 YKFDDTRVTRA 471
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-947 |
1.27e-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: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--------------------QQILHEFAKLIQEMWTANV 685
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterriggrevsrselqrsNQFVYELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 686 HTVTPmelkrafsTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDnkkadltwewytrhENSLVRD 765
Cdd:cd02666 83 RSVTP--------SKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKE--------------QSDLIKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 766 LFVGQLKSTL-KCTTCGNTSVTFDPFWDLSVPL----------PSSSRCKLEACLDLFIREEVL-----DGDEMPTCAKC 829
Cdd:cd02666 141 LFSGKTKQQLvPESMGNQPSVRTKTERFLSLLVdvgkkgreivVLLEPKDLYDALDRYFDYDSLtklpqRSQVQAQLAQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 830 KTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTSDSELNMGSYGANSNSNVhYSLYAISNHMGSTAGGHYV 909
Cdd:cd02666 221 LQRELISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYW 299
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 665392823 910 ALCKHPVSRKWHEFNDNIVSDALSE---NHLVSSSA--YILFY 947
Cdd:cd02666 300 VYIKDFEENVWRKYNDETVTVVPASevfLFTLGNTAtpYFLVY 342
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
626-925 |
4.84e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 71.15 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLstKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTK----- 700
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECL--KEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 701 -HRMYSDYNQQDA-------QEFLRFFLDSLHSalnsgvkgETLNIDDNLSDNKkadltwewytrhenSLVRDLFVGQLK 772
Cdd:pfam13423 80 lGLLDEDRETNSAislssliQSFNRFLLDQLSS--------EENSTPPNPSPAE--------------SPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 773 STLKCTTCGNTSVTFDPF--WDLSVPLPSSSRCKLEACLDL-------FIREEVLDGdempTCAKCK------TRRkctk 837
Cdd:pfam13423 138 TTIRCSNCGHESVRESSThvLDLIYPRKPSSNNKKPPNQTFssilkssLERETTTKA----WCEKCKryqpleSRR---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 838 sfTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTsdsELNMGSYGANSNSN--VHYSLYAISNHMGSTAG-GHYVALCKH 914
Cdd:pfam13423 210 --TVRNLPPVLSLNAALTNEEWRQLWKTPGWLPP---EIGLTLSDDLQGDNeiVKYELRGVVVHIGDSGTsGHLVSFVKV 284
|
330
....*....|....*...
gi 665392823 915 PVSR-------KWHEFND 925
Cdd:pfam13423 285 ADSEledptesQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
627-948 |
7.65e-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: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 627 LRNIGNTCFMNSVIQCLShtqeltrflrshhgsrSLStkdqQILHEFAkliqemwtanvhtvtpmelkrafstkhrmysD 706
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS----------------SIG----KINTEFD-------------------------------N 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 707 YNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTWEWYTRHENSLvrDLFVGQLKSTLKCTTCGNTSVT 786
Cdd:cd02673 31 DDQQDAHEFLLTLLEA---------------IDDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 787 FDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDemptCAKCKtrrkCTKSFTIQR---FPKYLVIHLKRFsetrwsKL 863
Cdd:cd02673 94 SDVGNFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSCK----CESAISSERimtFPECLSINLKRY------KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 864 SNIVEFPTSDSELNMGSYGANSNSnvhYSLYAISNHMG-STAGGHYVALCKHPVS-RKWHEFNDNIV----SDALSENhl 937
Cdd:cd02673 160 RIATSDYLKKNEEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIrpvsKNDVSTN-- 234
|
330
....*....|.
gi 665392823 938 VSSSAYILFYE 948
Cdd:cd02673 235 ARSSGYLIFYD 245
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
626-947 |
3.53e-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: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 626 GLRNIGNTCFMNSVIQCLshtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkraFSTkhrmys 705
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-----------------------------------------------------FSQ------ 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 706 dynQQDAQEFLRFFLDSLHSALNSGVKGETlniDDNLSDNKKADLTWEwytrhenslvRDLFVGQLKST--LKCTTCGNT 783
Cdd:cd02665 22 ---QQDVSEFTHLLLDWLEDAFQAAAEAIS---PGEKSKNPMVQLFYG----------TFLTEGVLEGKpfCNCETFGQY 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 784 SVTFDPFWDLsvplpsssrcklEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKsftiqrFPKYLVIHLKRFS--ETRWS 861
Cdd:cd02665 86 PLQVNGYGNL------------HECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEfnQGRPE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392823 862 KLSNIVEFPtsdSELNmgsygansnsNVHYSLYAISNHMGSTAGGHYVA-LCKHPVSRkWHEFND---------NIVSDA 931
Cdd:cd02665 148 KIHDKLEFP---QIIQ----------QVPYELHAVLVHEGQANAGHYWAyIYKQSRQE-WEKYNDisvtessweEVERDS 213
|
330
....*....|....*.
gi 665392823 932 LSEnhLVSSSAYILFY 947
Cdd:cd02665 214 FGG--GRNPSAYCLMY 227
|
|
| |
