|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
4.57e-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: 304.98 E-value: 4.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 320
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 321 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNTSV 400
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS------------------------------------IIVDLFQGQLKSRLTCLTCGKTST 62
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 401 TFDPFWDLSVPLPSSSR----CKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETR-- 474
Cdd:cd02674 63 TFEPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRgs 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 475 WSKLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDaLSENHLVS 554
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK-VSESSVVS 221
|
....*....
gi 665392821 555 SSAYILFYE 563
Cdd:cd02674 222 SSAYILFYE 230
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
240-562 |
3.28e-100 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 305.91 E-value: 3.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 240 CGLRNIGNTCFMNSVIQCLSHTQELTRFL--RSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHT-VTPMELKRAFSTKH 316
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLlrISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 317 RMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCG 396
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE------------------------NESLITDLFRGQLKSRLKCLSCG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 397 NTSVTFDPFWDLSVPLPSSSRCKLEA----CLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSE 472
Cdd:pfam00443 137 EVSETFEPFSDLSLPIPGDSAELKTAslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 473 TR--WSKLSNIVEFPTsdsELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSD 545
Cdd:pfam00443 217 NRstWEKLNTEVEFPL---ELDLSRYlaeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTE 293
|
330
....*....|....*..
gi 665392821 546 ALSENHLVSSSAYILFY 562
Cdd:pfam00443 294 VDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
241-563 |
3.55e-72 |
|
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: 231.22 E-value: 3.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkrafstkhrmys 320
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 321 dyNQQDAQEFLRFFLDSLHSALNSGVKGEtlniddnlsdnkkadltweWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSV 400
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRT-------------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 401 TFDPFWDLSVPLP--SSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtRRKCTKSFTIQRFPKYLVIHLKRFSETRW--- 475
Cdd:cd02257 80 STEPELFLSLPLPvkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDgtk 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 476 SKLSNIVEFPtsdSELNMGSY-------GANSNSNVHYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSDAL 547
Cdd:cd02257 159 EKLNTKVSFP---LELDLSPYlsegekdSDSDNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVS 235
|
330 340
....*....|....*....|
gi 665392821 548 SE----NHLVSSSAYILFYE 563
Cdd:cd02257 236 EEevleFGSLSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
240-562 |
9.04e-71 |
|
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: 229.47 E-value: 9.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 240 CGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMY 319
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 320 SDYNQQDAQEFLRFFLDSLHSA-LNSGVKGETLNIDDNlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCTTCGNT 398
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAcLDRFKKLKAVDPSSQ-----------------ETTLVQQIFGGYLRSQVKCLNCKHV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 399 SVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKL 478
Cdd:cd02661 145 SNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 479 SNIVEFPtsdSELNMGSYGANSNSN-VHYSLYAISNHMG-STAGGHYVALCKHPvSRKWHEFNDNIVSdALSENHLVSSS 556
Cdd:cd02661 223 NKQISFP---ETLDLSPYMSQPNDGpLKYKLYAVLVHSGfSPHSGHYYCYVKSS-NGKWYNMDDSKVS-PVSIETVLSQK 297
|
....*.
gi 665392821 557 AYILFY 562
Cdd:cd02661 298 AYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-562 |
1.38e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 184.88 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSH-HgsrSLSTKDQQILH----EFAKLIQEMW-TANVHTVTPMELKRAFST 314
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDrH---SCTCLSCSPNSclscAMDEIFQEFYySGDRSPYGPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 315 KHRMYSDYNQQDAQEFLRFFLDSLHSAlNSGVKGETlniddnlSDNKkadltwewytrHENSLVRDLFVGQLKSTLKCTT 394
Cdd:cd02660 79 HSRNLAGYSQQDAHEFFQFLLDQLHTH-YGGDKNEA-------NDES-----------HCNCIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 395 CGNTSVTFDPFWDLSVPLPSSSRC-------------KLEACLDLFIREEVLdGDEMPTCAKCKTRRKCTKSFTIQRFPK 461
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 462 YLVIHLKRF---SETRWSKLSNIVEFPTsdsELNMGSYGANS----------NSNVHYSLYAISNHMGSTAGGHYVALCK 528
Cdd:cd02660 219 VLCFQLKRFehsLNKTSRKIDTYVQFPL---ELNMTPYTSSSigdtqdsnslDPDYTYDLFAVVVHKGTLDTGHYTAYCR 295
|
330 340 350
....*....|....*....|....*....|....
gi 665392821 529 HPVSrKWHEFNDNIVSdALSENHLVSSSAYILFY 562
Cdd:cd02660 296 QGDG-QWFKFDDAMIT-RVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
8.93e-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: 181.05 E-value: 8.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRflrshhgsrslstkdqqilhefakLIQEmwtanvhtvTPMELKRAFSTKHRMYS 320
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRE------------------------LLSE---------TPKELFSQVCRKAPQFK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 321 DYNQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsdnkkadltwewytrheNSLVRDLFVGQLKSTLKCTTCGNTSV 400
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL------------------------------------RTFIDSIFGGELTSTIMCESCGTVSL 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 401 TFDPFWDLSVPL--PSSSRCKLEACLDLFIREEVLDGDEMPTCAKCKtrrKCTKSFTIQRFPKYLVIHLKRFSETRWS-- 476
Cdd:cd02667 92 VYEPFLDLSLPRsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT---KAKKQYLISKLPPVLVIHLKRFQQPRSAnl 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 477 -KLSNIVEFPtsdSELNMGSY------GANSNSNVHYSLYAISNHMGSTAGGHYVA----------LCKH---------- 529
Cdd:cd02667 169 rKVSRHVSFP---EILDLAPFcdpkcnSSEDKSSVLYRLYGVVEHSGTMRSGHYVAyvkvrppqqrLSDLtkskpaadea 245
|
330 340 350
....*....|....*....|....*....|....*
gi 665392821 530 -PVSRKWHEFNDNIVSdALSENHLVSSSAYILFYE 563
Cdd:cd02667 246 gPGSGQWYYISDSDVR-EVSLEEVLKSEAYLLFYE 279
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
235-415 |
5.87e-48 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 178.92 E-value: 5.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 235 KSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILH-----EFAKLIQEMWTANVHTVTPMELK 309
Cdd:COG5560 261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHgsvasAYADLIKQLYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 310 RAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGE-----TLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVG 384
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPytskpDLSPGDDVVVKKKAKECWWEHLKRNDSIITDLFQG 420
|
170 180 190
....*....|....*....|....*....|.
gi 665392821 385 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS 415
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTLPLPVS 451
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
9.63e-46 |
|
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: 163.75 E-value: 9.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFL--------RSHHGSRSLSTKDQQ-ILHEFAKLIQEMWTANVHTVTPMELKRA 311
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnstedAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 312 FStkhrmYSDYNQQDAQEFLRFFLDSLHSALNSgvkgetlniddnlSDNKKAdltwewytrheNSLVRDLFVGQLKSTLK 391
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEAKLSK-------------SKNPDL-----------KNIVQDLFRGEYSYVTQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 392 CTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS 471
Cdd:cd02668 132 CSKCGRESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 472 ETRWS----KLSNIVEFPtsdSELNMGSYGANSNSNVH-YSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFNDNIVSD 545
Cdd:cd02668 210 FDRKTgakkKLNASISFP---EILDMGEYLAESDEGSYvYELSGVLIHQGVSAySGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
330 340 350
....*....|....*....|....*....|....*...
gi 665392821 546 --------------------ALSENHLVSSSAYILFYE 563
Cdd:cd02668 287 mpgkplklgnsedpakprksEIKKGTHSSRTAYMLVYK 324
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
238-564 |
1.43e-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: 163.58 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 238 GLCGLRNIGNTCFMNSVIQCLSHTQELtRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHR 317
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEF-RNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 318 MYSDYNQQDAQEFLRFFLDSLHSALnsgvKGetlniddnlsdnkkadltwewyTRHENsLVRDLFVGQLKSTLKCTTCGN 397
Cdd:cd02659 80 SLNTFEQHDVQEFFRVLFDKLEEKL----KG----------------------TGQEG-LIKNLFGGKLVNYIICKECPH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 398 TSVTFDPFWDLSVPLpssSRCK-LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF-----S 471
Cdd:cd02659 133 ESEREEYFLDLQVAV---KGKKnLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfeT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 472 ETRwSKLSNIVEFPtsdSELNMGSY------------GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFN 539
Cdd:cd02659 210 MMR-IKINDRFEFP---LELDMEPYtekglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFN 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 665392821 540 DNIVS-----DALSEN----------------HLVSSSAYILFYER 564
Cdd:cd02659 286 DDVVTpfdpnDAEEECfggeetqktydsgpraFKRTTNAYMLFYER 331
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
2.11e-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: 162.09 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTrflrshhgsrslSTKD--QQILHEFAKliqemwtanVHTVTPMELKRAFSTKHRM 318
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLT------------CLKDlfESISEQKKR---------TGVISPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 319 YSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKADLTWewytrhenslVRDLFVGQLKSTLKCTTCGNT 398
Cdd:cd02663 60 FDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNETRCLTCETV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 399 SVTFDPFWDLSVPLPSSsrCKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRF--SET--R 474
Cdd:cd02663 130 SSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkyDEQlnR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 475 WSKLSNIVEFPTsdsELNM-GSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHpvSRKWHEFNDNIVsDALSENHL 552
Cdd:cd02663 208 YIKLFYRVVFPL---ELRLfNTTDDAENPDRLYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETV-EKIDENAV 281
|
330
....*....|....*....
gi 665392821 553 V--------SSSAYILFYE 563
Cdd:cd02663 282 EeffgdspnQATAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
4.17e-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: 134.54 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRslsTKDQQILheFAKLIQEMWTANVHTVTPMELKRAF--STKHRM 318
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPR---LGDSQSV--MKKLQLLQAHLMHTQRRAEAPPDYFleASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 319 YSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCGNT 398
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLHT------------------------------------LIEKMFGGKLSTTIRCLNCNST 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 399 SVTFD--PFWDLSVPLpsssrckLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFS----- 471
Cdd:cd02664 120 SARTErfRDLDLSFPS-------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkt 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 472 ETRWSKLSNI-----VEFPTSDS-----------ELNMGSYGANSNSNVHYSLYAISNHMG-STAGGHYVALCKHPVSRK 534
Cdd:cd02664 193 HVREKIMDNVsinevLSLPVRVEskssesplekkEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQTDAD 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 665392821 535 --------------------WHEFNDNIVSDALSE---NHLV---SSSAYILFYE 563
Cdd:cd02664 273 stgqecpepkdaeendesknWYLFNDSRVTFSSFEsvqNVTSrfpKDTPYILFYE 327
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
2.54e-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: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--QQILHEFAKLIQEM-----------WTANVHT---VT 304
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKLADGLlsgryskpaslKSENDPYqvgIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 305 PMELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTwewytrhenslvrDLFVG 384
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDK---------------LDRESFKNLGLNPN-------------DLFKF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 385 QLKSTLKCTTCGNTSVTFDPFWDLSVPLPSS------------SRCKLEACLDLFIREEVLDGdempTCAKCKTRRKCTK 452
Cdd:cd02658 133 MIEDRLECLSCKKVKYTSELSEILSLPVPKDeatekeegelvyEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 453 SFTIQRFPKYLVIHLKRFS-ETRW--SKLSNIVEFPtsdSELNMGSygansnsnvhYSLYAISNHMG-STAGGHYVALCK 528
Cdd:cd02658 209 TTGFKTFPDYLVINMKRFQlLENWvpKKLDVPIDVP---EELGPGK----------YELIAFISHKGtSVHSGHYVAHIK 275
|
330 340 350
....*....|....*....|....*....|....*...
gi 665392821 529 HPVSR--KWHEFNDNIVsdALSEN-HLVSSSAYILFYE 563
Cdd:cd02658 276 KEIDGegKWVLFNDEKV--VASQDpPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
5.18e-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: 125.52 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQEL-TRFLRSHHGSRSLSTKDQQILHEFAKLIQEMwTANVHTVTPMELKRAFSTKHRMY 319
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELrDALKNYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 320 SD------YNQQDAQEFLRFFLDSLHSALNSGVKgetlniddnlsdnkkadltwewytrhENSLVRDLFVGQLKSTLKCT 393
Cdd:cd02657 80 AEkqnqggYAQQDAEECWSQLLSVLSQKLPGAGS--------------------------KGSFIDQLFGIELETKMKCT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 394 TCGN-TSVTFDPFWDLSVPLPSSSRCK-LEACLDLFIREEV------LDGDEMPTcakcKTRRkctksftIQRFPKYLVI 465
Cdd:cd02657 134 ESPDeEEVSTESEYKLQCHISITTEVNyLQDGLKKGLEEEIekhsptLGRDAIYT----KTSR-------ISRLPKYLTV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 466 HLKRF----SETRWSKLSNIVEFPtsdseLNMGSYGANSNSNVhYSLYAISNHMGSTA-GGHYVALCKHPVSRKWHEFND 540
Cdd:cd02657 203 QFVRFfwkrDIQKKAKILRKVKFP-----FELDLYELCTPSGY-YELVAVITHQGRSAdSGHYVAWVRRKNDGKWIKFDD 276
|
330 340 350
....*....|....*....|....*....|...
gi 665392821 541 NIVS-------DALS---ENHlvssSAYILFYE 563
Cdd:cd02657 277 DKVSevteediLKLSgggDWH----IAYILLYK 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
420-564 |
4.31e-30 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 125.77 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 420 LEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWS--KLSNIVEFPTSDSELNMGSYg 497
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPIDDLDLSGVEY- 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665392821 498 ANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENhLVSSSAYILFYER 564
Cdd:COG5560 756 MVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPED-SVTSSAYVLFYRR 821
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
238-563 |
9.38e-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: 118.96 E-value: 9.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 238 GLCGLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANV--HTVTPMELKRAFSTK 315
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 316 -HRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKadLTWEWYTRHENSLvrdlfvGQLKSTLKCTT 394
Cdd:cd02669 198 sKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSIIHDCFQGKVQ--IETQKIKPHAEEE------GSKDKFFKDSR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 395 CGNTSVTfdPFWDLSVPLPSSSrckleacldLFIRE------------EVLDGDEMPTCAKCKTRRkctKSFTIQRFPKY 462
Cdd:cd02669 270 VKKTSVS--PFLLLTLDLPPPP---------LFKDGneeniipqvplkQLLKKYDGKTETELKDSL---KRYLISRLPKY 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 463 LVIHLKRFSETRWSKLSN--IVEFPTSDSELN--MGSYGANSNSNVHYSLYAISNHMGSTAG-GHYVALCKHPVSRKWHE 537
Cdd:cd02669 336 LIFHIKRFSKNNFFKEKNptIVNFPIKNLDLSdyVHFDKPSLNLSTKYNLVANIVHEGTPQEdGTWRVQLRHKSTNKWFE 415
|
330 340
....*....|....*....|....*.
gi 665392821 538 FNDNIVSDALSENHLVSSSaYILFYE 563
Cdd:cd02669 416 IQDLNVKEVLPQLIFLSES-YIQIWE 440
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-563 |
4.16e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 109.76 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFLrshhgsrslstkdQQILhefakliqemwtanvhtvtpmelkrafstkhrmys 320
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-------------EEFL----------------------------------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 321 dyNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLKSTLKCTTCG-NTS 399
Cdd:cd02662 33 --EQQDAHELFQVLLETLEQ------------------------------------LLKFPFDGLLASRIVCLQCGeSSK 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 400 VTFDPFWDLSVPLPSSSR---CKLEACLDLFIREEVLDGdemPTCAKCKTrrkctksfTIQRFPKYLVIHLKRFSETRW- 475
Cdd:cd02662 75 VRYESFTMLSLPVPNQSSgsgTTLEHCLDDFLSTEIIDD---YKCDRCQT--------VIVRLPQILCIHLSRSVFDGRg 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 476 --SKLSNIVEFPtsdSELnmgsygansnSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRK------------------- 534
Cdd:cd02662 144 tsTKNSCKVSFP---ERL----------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstsh 210
|
330 340 350
....*....|....*....|....*....|
gi 665392821 535 -WHEFNDNIVSDALSENHLVSSSAYILFYE 563
Cdd:cd02662 211 pWWRISDTTVKEVSESEVLEQKSAYMLFYE 240
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
228-562 |
1.35e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 110.75 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 228 ASSSRDEKSEGLCGLRNIGNTCFMNSVIQCLSHTQELTRFLrsHHGSRSLSTKDQqiLHEFAKLIQEMWTANVHTVTPME 307
Cdd:cd02671 13 TSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHGL--KHLVSLISSVEQ--LQSSFLLNPEKYNDELANQAPRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 308 LKRAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSalnsgvkgetlniddnlsdnkkadltwewytrhensLVRDLFVGQLK 387
Cdd:cd02671 89 LLNALREVNPMYEGYLQHDAQEVLQCILGNIQE------------------------------------LVEKDFQGQLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 388 STLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDL-----------------FIREEVLDGDEMPTCAKCKTRRKC 450
Cdd:cd02671 133 LRTRCLECETFTERREDFQDISVPVQESELSKSEESSEIspdpktemktlkwaisqFASVERIVGEDKYFCENCHHYTEA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 451 TKSFTIQRFPKYLVIHLKRFSETRW--------SKLSNIVEFPTSDSELNMGSyganSNSNVHYSLYAISNHMGST-AGG 521
Cdd:cd02671 213 ERSLLFDKLPEVITIHLKCFAANGSefdcygglSKVNTPLLTPLKLSLEEWST----KPKNDVYRLFAVVMHSGATiSSG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 665392821 522 HYVAlckhpvSRKWHEFNDNIVS--------DALSENHLVSSSAYILFY 562
Cdd:cd02671 289 HYTA------YVRWLLFDDSEVKvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
241-565 |
1.64e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 106.42 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCL--------SHTQELTRFLRS----HHGSRSLSTKDQQIlhefaKLIQEMWTANVHTVTPmel 308
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILalylpkldELLDDLSKELKVlknvIRKPEPDLNQEEAL-----KLFTALWSSKEHKVGW--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 309 krafstKHRMYSdynQQDAQEFLRFFLDSLhsalnsgvkgetlNIDDnlsdnkkadltwewytrhenslvrdlfVGQLKS 388
Cdd:COG5533 73 ------IPPMGS---QEDAHELLGKLLDEL-------------KLDL---------------------------VNSFTI 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 389 TLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDEmPTCAKCKT------RRKCTKSFTIQRFPKY 462
Cdd:COG5533 104 RIFKTTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMEELVDD-ETGVKAKEneelevQAKQEYEVSFVKLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 463 LVIHLKRFS-ETRWSKLSNIVefptsDSELNMG---SYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKhpVSRKWHEF 538
Cdd:COG5533 183 LTIQLKRFAnLGGNQKIDTEV-----DEKFELPvkhDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKA 255
|
330 340
....*....|....*....|....*....
gi 665392821 539 NDNIVSDALSEN--HLVSSSAYILFYERT 565
Cdd:COG5533 256 NDSDVTPVSEEEaiNEKAKNAYLYFYERI 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
234-546 |
3.27e-21 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 98.40 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 234 EKSEGLCGLRNIGNTCFMNSVIQCLSHTQeltRFLRSHHG--SRSLSTKDQqILHEFAKLIQEMWTANvHTVTPMELKRA 311
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIA---KFRKDVYGipTDHPRGRDS-VALALQRLFYNLQTGE-EPVDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 312 F---STKHRMysdynQQDAQEFLRFFLDSLhsalnsgvkgetlniddnlsDNKKADltwewyTRHENSLvRDLFVGQLKS 388
Cdd:COG5077 263 FgwdSDDSFM-----QHDIQEFNRVLQDNL--------------------EKSMRG------TVVENAL-NGIFVGKMKS 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 389 TLKCTTCGNTSVTFDPFWDLSVPLPSSSrcKLEACLDLFIREEVLDGDempTCAKCKTR--RKCTKSFTIQRFPKYLVIH 466
Cdd:COG5077 311 YIKCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLHLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 467 LKRFS---ET-RWSKLSNIVEFPtsdSELNMGSY-----GANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHE 537
Cdd:COG5077 386 LKRFEydfERdMMVKINDRYEFP---LEIDLLPFldrdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYK 462
|
....*....
gi 665392821 538 FNDNIVSDA 546
Cdd:COG5077 463 FDDTRVTRA 471
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-562 |
8.72e-14 |
|
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: 72.91 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLSTKD--------------------QQILHEFAKLIQEMWTANV 300
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDypterriggrevsrselqrsNQFVYELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 301 HTVTPmelkrafsTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDnkkadltwewytrhENSLVRD 380
Cdd:cd02666 83 RSVTP--------SKELAYLALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKE--------------QSDLIKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 381 LFVGQLKSTL-KCTTCGNTSVTFDPFWDLSVPL----------PSSSRCKLEACLDLFIREEVL-----DGDEMPTCAKC 444
Cdd:cd02666 141 LFSGKTKQQLvPESMGNQPSVRTKTERFLSLLVdvgkkgreivVLLEPKDLYDALDRYFDYDSLtklpqRSQVQAQLAQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 445 KTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTSDSELNMGSYGANSNSNVhYSLYAISNHMGSTAGGHYV 524
Cdd:cd02666 221 LQRELISMDRYELPSSIDDIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYG-YRLHAVFIHRGEASSGHYW 299
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 665392821 525 ALCKHPVSRKWHEFNDNIVSDALSE---NHLVSSSA--YILFY 562
Cdd:cd02666 300 VYIKDFEENVWRKYNDETVTVVPASevfLFTLGNTAtpYFLVY 342
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
241-540 |
8.74e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 69.22 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLSHTQELTRFLRSHHGSRSLstKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTK----- 315
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECL--KEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIpeasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 316 -HRMYSDYNQQDA-------QEFLRFFLDSLHSalnsgvkgETLNIDDNLSDNKkadltwewytrhenSLVRDLFVGQLK 387
Cdd:pfam13423 80 lGLLDEDRETNSAislssliQSFNRFLLDQLSS--------EENSTPPNPSPAE--------------SPLEQLFGIDAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 388 STLKCTTCGNTSVTFDPF--WDLSVPLPSSSRCKLEACLDL-------FIREEVLDGdempTCAKCK------TRRkctk 452
Cdd:pfam13423 138 TTIRCSNCGHESVRESSThvLDLIYPRKPSSNNKKPPNQTFssilkssLERETTTKA----WCEKCKryqpleSRR---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 453 sfTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTsdsELNMGSYGANSNSN--VHYSLYAISNHMGSTAG-GHYVALCKH 529
Cdd:pfam13423 210 --TVRNLPPVLSLNAALTNEEWRQLWKTPGWLPP---EIGLTLSDDLQGDNeiVKYELRGVVVHIGDSGTsGHLVSFVKV 284
|
330
....*....|....*...
gi 665392821 530 PVSR-------KWHEFND 540
Cdd:pfam13423 285 ADSEledptesQWYLFND 302
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
242-563 |
5.06e-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: 57.15 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 242 LRNIGNTCFMNSVIQCLShtqeltrflrshhgsrSLStkdqQILHEFAkliqemwtanvhtvtpmelkrafstkhrmysD 321
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS----------------SIG----KINTEFD-------------------------------N 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 322 YNQQDAQEFLRFFLDSlhsalnsgvkgetlnIDDNLSDNKKADLTWEWYTRHENSLvrDLFVGQLKSTLKCTTCGNTSVT 401
Cdd:cd02673 31 DDQQDAHEFLLTLLEA---------------IDDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 402 FDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDemptCAKCKtrrkCTKSFTIQR---FPKYLVIHLKRFsetrwsKL 478
Cdd:cd02673 94 SDVGNFLDVSMIDNKLDIDELLISNFKTWSPIEKD----CSSCK----CESAISSERimtFPECLSINLKRY------KL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 479 SNIVEFPTSDSELNMGSYGANSNSnvhYSLYAISNHMG-STAGGHYVALCKHPVS-RKWHEFNDNIV----SDALSENhl 552
Cdd:cd02673 160 RIATSDYLKKNEEIMKKYCGTDAK---YSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIrpvsKNDVSTN-- 234
|
330
....*....|.
gi 665392821 553 VSSSAYILFYE 563
Cdd:cd02673 235 ARSSGYLIFYD 245
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
241-562 |
6.86e-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: 50.63 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 241 GLRNIGNTCFMNSVIQCLshtqeltrflrshhgsrslstkdqqilhefakliqemwtanvhtvtpmelkraFSTkhrmys 320
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSL-----------------------------------------------------FSQ------ 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 321 dynQQDAQEFLRFFLDSLHSALNSGVKGETlniDDNLSDNKKADLTWEwytrhenslvRDLFVGQLKST--LKCTTCGNT 398
Cdd:cd02665 22 ---QQDVSEFTHLLLDWLEDAFQAAAEAIS---PGEKSKNPMVQLFYG----------TFLTEGVLEGKpfCNCETFGQY 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 399 SVTFDPFWDLsvplpsssrcklEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKsftiqrFPKYLVIHLKRFS--ETRWS 476
Cdd:cd02665 86 PLQVNGYGNL------------HECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEfnQGRPE 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392821 477 KLSNIVEFPtsdSELNmgsygansnsNVHYSLYAISNHMGSTAGGHYVA-LCKHPVSRkWHEFND---------NIVSDA 546
Cdd:cd02665 148 KIHDKLEFP---QIIQ----------QVPYELHAVLVHEGQANAGHYWAyIYKQSRQE-WEKYNDisvtessweEVERDS 213
|
330
....*....|....*.
gi 665392821 547 LSEnhLVSSSAYILFY 562
Cdd:cd02665 214 FGG--GRNPSAYCLMY 227
|
|
| |
