|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
28-446 |
5.82e-86 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 265.85 E-value: 5.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 28 VGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYV 107
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 108 PSFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilangpvpspprrggalleepelsdddranlmwkRYLEREDSKIV 187
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNG-----------------------------------------NHSTENESLIT 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 188 DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLT 267
Cdd:pfam00443 120 DLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 268 VQRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqrptasqml 347
Cdd:pfam00443 200 ISRLPPVLIIH--------------------------------------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 348 lnqgldLNRFSASRGSIKKSSVGVDFPLQ----RLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTG--WH 421
Cdd:pfam00443 211 ------LKRFSYNRSTWEKLNTEVEFPLEldlsRYLAEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnrWY 284
|
410 420
....*....|....*....|....*.
gi 966921373 422 VYNDSRVSPVS-ENQVASSEGYVLFY 446
Cdd:pfam00443 285 KFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-447 |
1.31e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 223.32 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 108
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSAD----------------------------------------------------------- 21
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 109 sfsgysQQDAQEFLKLLMERLHleinrrgrrappilangpvpspprrggalleepelsdddranlmwkryleredSKIVD 188
Cdd:cd02674 22 ------QQDAQEFLLFLLDGLH-----------------------------------------------------SIIVD 42
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 189 LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLTV 268
Cdd:cd02674 43 LFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTI 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 269 QRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqrptasqmll 348
Cdd:cd02674 123 SRLPKVLIIH---------------------------------------------------------------------- 132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 349 nqgldLNRFSASRGSIKKSSVGVDFPLQRLSLGDF--ASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQ--TGWHVYN 424
Cdd:cd02674 133 -----LKRFSFSRGSTRKLTTPVTFPLNDLDLTPYvdTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNetNDWYKFD 207
|
410 420
....*....|....*....|...
gi 966921373 425 DSRVSPVSENQVASSEGYVLFYQ 447
Cdd:cd02674 208 DSRVTKVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
27-446 |
1.28e-56 |
|
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: 189.41 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 27 HVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQE--VPGGGRAQELtEAFadVIGALWHPDSCEAVNPtrFRAVFQ 104
Cdd:cd02661 1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDccNEGFCMMCAL-EAH--VERALASSGPGSAPRI--FSSNLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 105 KYVPSFSGYSQQDAQEFLKLLMERLHleinrrgrrappilangpvPSPPRRGGALLEEPELSdddranlmwkryleREDS 184
Cdd:cd02661 76 QISKHFRIGRQEDAHEFLRYLLDAMQ-------------------KACLDRFKKLKAVDPSS--------------QETT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 185 KIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGfaggkvSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTK 264
Cdd:cd02661 123 LVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD------SLEDALEQFTKPEQLDGENKYKCERCKKKVKASK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 265 KLTVQRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqrptas 344
Cdd:cd02661 197 QLTIHRAPNVLTIH------------------------------------------------------------------ 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 345 qmllnqgldLNRFSASRGSikKSSVGVDFPlQRLSLGDFASDK-AGSPVYQLYALCNHSG-SVHYGHYTALCRCQTG-WH 421
Cdd:cd02661 211 ---------LKRFSNFRGG--KINKQISFP-ETLDLSPYMSQPnDGPLKYKLYAVLVHSGfSPHSGHYYCYVKSSNGkWY 278
|
410 420
....*....|....*....|....*
gi 966921373 422 VYNDSRVSPVSENQVASSEGYVLFY 446
Cdd:cd02661 279 NMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
29-447 |
3.45e-50 |
|
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: 171.13 E-value: 3.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSStrplrdfclrrdfrqevpgggraqelteafadvigalwhpdsceavnptrfravfqkyvp 108
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 109 sfsgySQQDAQEFLKLLMERLHLEINRRGRRappilangpvpspprrggalleepelsdddranlmwKRYLEREDSKIVD 188
Cdd:cd02257 21 -----EQQDAHEFLLFLLDKLHEELKKSSKR------------------------------------TSDSSSLKSLIHD 59
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 189 LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGfaGGKVSLRDCFNLFTKEEELESENAPVCDRCRqKTRSTKKLTV 268
Cdd:cd02257 60 LFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKG--LPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKI 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 269 QRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqrptasqmll 348
Cdd:cd02257 137 KKLPPVLIIH---------------------------------------------------------------------- 146
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 349 nqgldLNRFSASR-GSIKKSSVGVDFPLQ------RLSLGDFASDKAGSPVYQLYALCNHSG-SVHYGHYTALCRCQT-- 418
Cdd:cd02257 147 -----LKRFSFNEdGTKEKLNTKVSFPLEldlspyLSEGEKDSDSDNGSYKYELVAVVVHSGtSADSGHYVAYVKDPSdg 221
|
410 420 430
....*....|....*....|....*....|....
gi 966921373 419 GWHVYNDSRVSPVSENQV-----ASSEGYVLFYQ 447
Cdd:cd02257 222 KWYKFNDDKVTEVSEEEVlefgsLSSSAYILFYE 255
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
26-447 |
2.73e-43 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 162.75 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 26 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEV----PGGGRAQeLTEAFADVIGALWHPDScEAVNPTRFRA 101
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESIneenPLGMHGS-VASAYADLIKQLYDGNL-HAFTPSGFKK 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 102 VFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRappilangPVPSPPrrggALLEEPELSDDDRANLMWKRYLER 181
Cdd:COG5560 342 TIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKK--------PYTSKP----DLSPGDDVVVKKKAKECWWEHLKR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 182 EDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKV--------------------SLRDCFNLFTK 241
Cdd:COG5560 410 NDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIvvfpesgrrqplkieldassTIRGLKKLVDA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 242 EEELE--SENAPVC---DRCRQKTRSTKKLTVQRFPR---------------ILVLHilifrFLLLLGYLPYILFPHP-- 299
Cdd:COG5560 490 EYGKLgcFEIKVMCiyyGGNYNMLEPADKVLLQDIPQtdfvylyetndngieVPVVH-----LRIEKGYKSKRLFGDPfl 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 300 ----------------------------------------------------PCFQRIEFSL------------------ 309
Cdd:COG5560 565 qlnvlikasiydklvkefeellvlvemkktdvdlvseqvrllreesspsswlKLETEIDTKReeqveeegqmnfndavvi 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 310 -----GKACHTLFHKllPVFWEWGEDSFQDRSP----------------PQ-----------RPTASQMLLNQGLD---- 353
Cdd:COG5560 645 sceweEKRYLSLFSY--DPLWTIREIGAAERTItlqdclnefskpeqlgLSdswycpgckefRQASKQMELWRLPMilii 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 354 -LNRFSASRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPV-YQLYALCNHSGSVHYGHYTALCR--CQTGWHVYNDSRVS 429
Cdd:COG5560 723 hLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLiYDLYAVDNHYGGLSGGHYTAYARnfANNGWYLFDDSRIT 802
|
570
....*....|....*...
gi 966921373 430 PVSENQVASSEGYVLFYQ 447
Cdd:COG5560 803 EVDPEDSVTSSAYVLFYR 820
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-447 |
8.47e-40 |
|
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: 144.45 E-value: 8.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRrdfrqevpgggraqelteafadvigalwhpdsceavNPTRFRAVFQKYVP 108
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE------------------------------------TPKELFSQVCRKAP 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 109 SFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilangpvpspprrggalleepelsdddranlmwkryleredskivd 188
Cdd:cd02667 45 QFKGYQQQDSHELLRYLLDGLRTFIDS----------------------------------------------------- 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 189 LFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFagGKVSLRDCFNLFTKEEELESENAPVCDRCrqkTRSTKKLTV 268
Cdd:cd02667 72 IFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK--SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLI 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 269 QRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqrptasqmll 348
Cdd:cd02667 147 SKLPPVLVIH---------------------------------------------------------------------- 156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 349 nqgldLNRFSA-SRGSIKKSSVGVDFPlQRLSLGDFASDKAGSP------VYQLYALCNHSGSVHYGHYTALCRC----- 416
Cdd:cd02667 157 -----LKRFQQpRSANLRKVSRHVSFP-EILDLAPFCDPKCNSSedkssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqq 230
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 966921373 417 ------------------QTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 447
Cdd:cd02667 231 rlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-446 |
9.82e-40 |
|
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: 145.59 E-value: 9.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRrDFRQEVPGGGRAQ-----ELTEAFADvigaLWHPDSCEAVNPTRFRAVF 103
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLS-DRHSCTCLSCSPNsclscAMDEIFQE----FYYSGDRSPYGPINLLYLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 104 QKYVPSFSGYSQQDAQEFLKLLMERLHleiNRRGRRAPPILANGPVPSPPRRggalleepelsdddranlmwkrylered 183
Cdd:cd02660 77 WKHSRNLAGYSQQDAHEFFQFLLDQLH---THYGGDKNEANDESHCNCIIHQ---------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 184 skivdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIP----KKGFAGGKV-----SLRDCFNLFTKEEELESeNAPVCD 254
Cdd:cd02660 126 -----TFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnkstPSWALGESGvsgtpTLSDCLDRFTRPEKLGD-FAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 255 RCRQKTRSTKKLTVQRFPRILVLHilifrfllllgylpyilfphppcFQRIEFSLgkacHTLFHKLlpvfwewgedsfqd 334
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQ-----------------------LKRFEHSL----NKTSRKI-------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 335 RSPPQRPTAsqmllnqgLDLNRFSASRGSIKKSSvgvdfplqrlslgdfaSDKAGSPVYQLYALCNHSGSVHYGHYTALC 414
Cdd:cd02660 239 DTYVQFPLE--------LNMTPYTSSSIGDTQDS----------------NSLDPDYTYDLFAVVVHKGTLDTGHYTAYC 294
|
410 420 430
....*....|....*....|....*....|...
gi 966921373 415 RCQTG-WHVYNDSRVSPVSENQVASSEGYVLFY 446
Cdd:cd02660 295 RQGDGqWFKFDDAMITRVSEEEVLKSQAYLLFY 327
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-447 |
4.77e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 112.79 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSstrplrdfclrrdfrqevpgggrAQELTEAFADVIGALWHPDSCEAV-NPTRFRAVFQKYV 107
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-----------------------FENLLTCLKDLFESISEQKKRTGViSPKKFITRLKREN 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 108 PSFSGYSQQDAQEFLKLLMERL--HLEINRRGRRAPPILANGPVPSPPRRggalleepelsdddranlmWkryleredsk 185
Cdd:cd02663 58 ELFDNYMHQDAHEFLNFLLNEIaeILDAERKAEKANRKLNNNNNAEPQPT-------------------W---------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 186 IVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKgfaggkVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKK 265
Cdd:cd02663 109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 266 LTVQRFPRILVLHilifrfllllgylpyilfphppcFQRIEFSLGKACHT-LFHKllpvfwewgedsfqdrsppqrptas 344
Cdd:cd02663 183 MKIKKLPKILALH-----------------------LKRFKYDEQLNRYIkLFYR------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 345 qmllnqgldlnrfsasrgsikkssvgVDFPLQ-RL-SLGDFASDkaGSPVYQLYALCNHSGS-VHYGHYTALCRCQTGWH 421
Cdd:cd02663 215 --------------------------VVFPLElRLfNTTDDAEN--PDRLYELVAVVVHIGGgPNHGHYVSIVKSHGGWL 266
|
410 420 430
....*....|....*....|....*....|....
gi 966921373 422 VYNDSRVSPVSENQV--------ASSEGYVLFYQ 447
Cdd:cd02663 267 LFDDETVEKIDENAVeeffgdspNQATAYVLFYQ 300
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
26-449 |
5.38e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 105.03 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 26 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPG-GGRAQELTEAFAdvigaLWHPDSCEAVNPTRFRAVFQ 104
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDnKSVPLALQRLFL-----FLQLSESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 105 KYVPSFSGYSQQDAQEFLKLLMERLhleinrrgrrappilangpvpspprrggallEEpelsdddranlMWKRyLEREDS 184
Cdd:cd02659 76 FGWDSLNTFEQHDVQEFFRVLFDKL-------------------------------EE-----------KLKG-TGQEGL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 185 kIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPkkgfagGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTK 264
Cdd:cd02659 113 -IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK------GKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 265 KLTVQRFPRILVLHilifrfllllgylpyilfphppcFQRIEFSLGKACHTlfhKLLPVFwewgedSFQDRsppqrptas 344
Cdd:cd02659 186 GVCFKKLPPVLTLQ-----------------------LKRFEFDFETMMRI---KINDRF------EFPLE--------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 345 qmllnqgLDLNRFsasrgsIKKSSVGVDfplqrlslGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTG--WHV 422
Cdd:cd02659 225 -------LDMEPY------TEKGLAKKE--------GDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDgkWYK 283
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 966921373 423 YNDSRVSPVSENQVA----------------------SSEGYVLFYQLM 449
Cdd:cd02659 284 FNDDVVTPFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFYERK 332
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-447 |
4.68e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 99.49 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTrplRDFclRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPT--RFRAVFQky 106
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMA---KDF--RRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPdyFLEASRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 107 vPSFSGYSQQDAQEFLKLLMERLHLEINRrgrrappilangpvpspprrggalleepelsdddranlmwkryleredski 186
Cdd:cd02664 74 -PWFTPGSQQDCSEYLRYLLDRLHTLIEK--------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 187 vdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPkkgfaggkvSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKL 266
Cdd:cd02664 102 --MFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP---------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEM 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 267 TVQRFPRILVLhilifrfllllgylpyilfphppcfQRIEFSLGKACHtLFHKLLpvfwewgedsfqdrsppqrptaSQM 346
Cdd:cd02664 171 KVTGAPEYLIL-------------------------TLLRFSYDQKTH-VREKIM----------------------DNV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 347 LLNQGLDLNRFSASRGSikkssvgvdFPLQRLSLGDFASDKAG---SPVYQLYALCNHSG-SVHYGHYTALCRCQTG--- 419
Cdd:cd02664 203 SINEVLSLPVRVESKSS---------ESPLEKKEEESGDDGELvtrQVHYRLYAVVVHSGySSESGHYFTYARDQTDads 273
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 966921373 420 -------------------WHVYNDSRVSPVSENQV-------ASSEGYVLFYQ 447
Cdd:cd02664 274 tgqecpepkdaeendesknWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFYE 327
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-447 |
1.88e-20 |
|
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: 91.62 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRPL--RDFCLRRDFRQEV--PgggrAQELTEAFADVIGAL-------------WHPDSC 91
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFqwRYDDLENKFPSDVvdP----ANDLNCQLIKLADGLlsgryskpaslksENDPYQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 92 EAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPpilangpvpspprrggalleepelsdddra 171
Cdd:cd02658 77 VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNP------------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 172 nlmwkryleredSKIVDLFVGQLkscLKCQACGYRSTTFEVFCDLSLPIPK--KGFAG------GKVSLRDCFNLFTKEE 243
Cdd:cd02658 127 ------------NDLFKFMIEDR---LECLSCKKVKYTSELSEILSLPVPKdeATEKEegelvyEPVPLEDCLKAYFAPE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 244 ELESEnapvCDRCRQKTRSTKKLTVQRFPRILVLHIlifrfllllgylpyilfphppcfQRIEFSLGkachtlfhkllpv 323
Cdd:cd02658 192 TIEDF----CSTCKEKTTATKTTGFKTFPDYLVINM-----------------------KRFQLLEN------------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 324 fWewgedsfqdrsppqRPtasqmllnqgldlnrfsasrgsiKKSSVGVDFPlqrlslgdfasDKAGSPVYQLYALCNHSG 403
Cdd:cd02658 232 -W--------------VP-----------------------KKLDVPIDVP-----------EELGPGKYELIAFISHKG 262
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 966921373 404 -SVHYGHYTALCR----CQTGWHVYNDSRVSPVSENQVASSEGYVLFYQ 447
Cdd:cd02658 263 tSVHSGHYVAHIKkeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-446 |
9.11e-20 |
|
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: 89.79 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIG------ALWHPDSCEAVNPTRFRAV 102
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDqlqlifAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 103 FqkyvpSFSGYSQQDAQEFLKLLMERLhleinrrgrrappilangpvpspprrggalleEPELSDDDRANLmwkrylere 182
Cdd:cd02668 81 L-----GLDTGQQQDAQEFSKLFLSLL--------------------------------EAKLSKSKNPDL--------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 183 dSKIV-DLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIpkKGFAggkvSLRDCFNLFTKEEELESENAPVCDRCRQKTR 261
Cdd:cd02668 115 -KNIVqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--KGHK----TLEECIDEFLKEEQLTGDNQYFCESCNSKTD 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 262 STKKLTVQRFPrilvlhilifrfllllgylPYILFphppCFQRIEFslgkachtlfhkllpvfwewgedsfqDRSPPQRp 341
Cdd:cd02668 188 ATRRIRLTTLP-------------------PTLNF----QLLRFVF--------------------------DRKTGAK- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 342 tasqmllnqgldlnrfsasrgsiKKSSVGVDFPLQrLSLGDFASD-KAGSPVYQLYALCNHSG-SVHYGHYTA-LCRCQT 418
Cdd:cd02668 218 -----------------------KKLNASISFPEI-LDMGEYLAEsDEGSYVYELSGVLIHQGvSAYSGHYIAhIKDEQT 273
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 966921373 419 G-WHVYNDSRVSPVSENQV---------------------ASSEGYVLFY 446
Cdd:cd02668 274 GeWYKFNDEDVEEMPGKPLklgnsedpakprkseikkgthSSRTAYMLVY 323
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-446 |
4.52e-16 |
|
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: 78.53 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRPLRDfCLRRDFRQEVPGGGRAQELTEAFADVIGALwhPDSCEAVNPTRFRAVFQKYVP 108
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRD-ALKNYNPARRGANQSSDNLTNALRDLFDTM--DKKQEPVPPIEFLQLLRMAFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 109 SFS------GYSQQDAQEFLKLLMERLhleinrrgRRAPPILAngpvpspprrggalleepelsdddranlmwkryleRE 182
Cdd:cd02657 78 QFAekqnqgGYAQQDAEECWSQLLSVL--------SQKLPGAG-----------------------------------SK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 183 DSKIVDLFVGQLKSCLKCQACGY-RSTTFEVFCDLSLPIpkkgfaGGKVslrDCFNLFTK-EEELESENAPVCDRCRQKT 260
Cdd:cd02657 115 GSFIDQLFGIELETKMKCTESPDeEEVSTESEYKLQCHI------SITT---EVNYLQDGlKKGLEEEIEKHSPTLGRDA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 261 RSTKKLTVQRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqr 340
Cdd:cd02657 186 IYTKTSRISRLPKYLTVQ-------------------------------------------------------------- 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 341 ptasqmllnqgldLNRFSASRGSIKKSSV--GVDFPLQrLSLGDFASdkaGSPVYQLYALCNHSG-SVHYGHYTALCRCQ 417
Cdd:cd02657 204 -------------FVRFFWKRDIQKKAKIlrKVKFPFE-LDLYELCT---PSGYYELVAVITHQGrSADSGHYVAWVRRK 266
|
410 420 430
....*....|....*....|....*....|....*...
gi 966921373 418 TG--WHVYNDSRVSPVSENQVASSEG-------YVLFY 446
Cdd:cd02657 267 NDgkWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
28-446 |
2.37e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 70.69 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 28 VGLRNLGNTCFLNAVLQCLSstrplrdFClrRDFRQEVP---GGGRAQELTEAFADVIGALWHpDSCEAVNPTRFRAVFQ 104
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLY-------FC--PGFKHGLKhlvSLISSVEQLQSSFLLNPEKYN-DELANQAPRRLLNALR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 105 KYVPSFSGYSQQDAQEFLKLLMERLHleinrrgrrappilangpvpspprrggALLEEpelsdddranlmwkrylereds 184
Cdd:cd02671 95 EVNPMYEGYLQHDAQEVLQCILGNIQ---------------------------ELVEK---------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 185 kivdLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVS-------------LRDCFNLFTKEEELESENAP 251
Cdd:cd02671 126 ----DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESseispdpktemktLKWAISQFASVERIVGEDKY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 252 VCDRCRQKTRSTKKLTVQRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgeds 331
Cdd:cd02671 202 FCENCHHYTEAERSLLFDKLPEVITIH----------------------------------------------------- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 332 fqdrsppqrptasqmllnqgldLNRFSASR------GSIKKSSVGVDFPLqRLSLGDFaSDKAGSPVYQLYALCNHSG-S 404
Cdd:cd02671 229 ----------------------LKCFAANGsefdcyGGLSKVNTPLLTPL-KLSLEEW-STKPKNDVYRLFAVVMHSGaT 284
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 966921373 405 VHYGHYTALCRcqtgWHVYNDSRV---------SPVSENQVASSEGYVLFY 446
Cdd:cd02671 285 ISSGHYTAYVR----WLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
29-447 |
9.72e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 67.78 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRPLRDFClrrdfrqevpgggraQELTEafadvigalwhpdsceavnptrfravfqkyvp 108
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------EEFLE-------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 109 sfsgysQQDAQEFLKLLMERLHLEinrrgrrappilangpvPSPPRRGgalleepelsdddranLMWKRyleredskivd 188
Cdd:cd02662 34 ------QQDAHELFQVLLETLEQL-----------------LKFPFDG----------------LLASR----------- 63
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 189 lfvgqlkscLKCQACGYRST-TFEVFCDLSLPIPKKGFAGGkVSLRDCFNLFTKEEELESenaPVCDRCrqktrstkKLT 267
Cdd:cd02662 64 ---------IVCLQCGESSKvRYESFTMLSLPVPNQSSGSG-TTLEHCLDDFLSTEIIDD---YKCDRC--------QTV 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 268 VQRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsfqdrsppqrptasqml 347
Cdd:cd02662 123 IVRLPQILCIH--------------------------------------------------------------------- 133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 348 lnqgldLNRFSAS-RGSIKKSSVGVDFPLqRLSlgdfasdkagSPVYQLYALCNHSGSVHYGHYTALCR----------- 415
Cdd:cd02662 134 ------LSRSVFDgRGTSTKNSCKVSFPE-RLP----------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepg 196
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 966921373 416 ---------CQTG--WHVYNDSRVSPVSENQV-ASSEGYVLFYQ 447
Cdd:cd02662 197 sfvrmregpSSTShpWWRISDTTVKEVSESEVlEQKSAYMLFYE 240
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
29-446 |
3.68e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 66.75 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 29 GLRNLGNTCFLNAVLQCLSSTRP------LRDFCLRRDFRQEVPGGGRAQELTEAFAdVIGALWHPDSceavnptrfrav 102
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldellDDLSKELKVLKNVIRKPEPDLNQEEALK-LFTALWSSKE------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 103 fQKYVPSFSGYSQQDAQEFLKLLMERLHLE-INRRGRRAPPILANgpvpspprrggalleepelsdddranlmwkryler 181
Cdd:COG5533 68 -HKVGWIPPMGSQEDAHELLGKLLDELKLDlVNSFTIRIFKTTKD----------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 182 edskivdlfvgqlksclkcqacgYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLF---------TKEEELESENApv 252
Cdd:COG5533 112 -----------------------KKKTSTGDWFDIIIELPDQTWVNNLKTLQEFIDNMeelvddetgVKAKENEELEV-- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 253 cdRCRQKTRSTKKltvqRFPRILVLHilifrfllllgylpyilfphppcfqriefslgkachtlfhkllpvfwewgedsf 332
Cdd:COG5533 167 --QAKQEYEVSFV----KLPKILTIQ------------------------------------------------------ 186
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 333 qdrsppqrptasqmllnqgldLNRFSASRGSIK-KSSVGVDFPLQrlslgdFASDKAGSPV----YQLYALCNHSGSVHY 407
Cdd:COG5533 187 ---------------------LKRFANLGGNQKiDTEVDEKFELP------VKHDQILNIVketyYDLVGFVLHQGSLEG 239
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 966921373 408 GHYTALCRCQTGWHVYNDSRVSPVSENQ---VASSEGYVLFY 446
Cdd:COG5533 240 GHYIAYVKKGGKWEKANDSDVTPVSEEEainEKAKNAYLYFY 281
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
26-144 |
1.41e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 63.11 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 26 GHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVpgGGRAQELTEAFADVIGALWhpdsceavNPTRFRAV--- 102
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENI--KDRKSELVKRLSELIRKIW--------NPRNFKGHvsp 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 966921373 103 --FQKYVPS-----FSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPIL 144
Cdd:cd02669 188 heLLQAVSKvskkkFSITEQSDPVEFLSWLLNTLHKDLGGSKKPNSSII 236
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
25-436 |
1.55e-10 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 63.74 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 25 SGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVigalwhPDSCEAVNPTRFRAVFQ 104
Cdd:COG5077 191 TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNL------QTGEEPVDTTELTRSFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 105 kyVPSFSGYSQQDAQEFLKLLMERLhlEINRRGRrappilangPVpspprrggalleepelsdddranlmwkrylereDS 184
Cdd:COG5077 265 --WDSDDSFMQHDIQEFNRVLQDNL--EKSMRGT---------VV---------------------------------EN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 185 KIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIpkKGFAggkvSLRDCFNLFTKEEELESENAPVCDRcRQKTRSTK 264
Cdd:COG5077 299 ALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--KGMK----NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 265 KLTVQRFPRILVLHilifrfllllgylpyilfphppcFQRIEFSlgkachtlfhkllpvfwewgedsfqdrsppqrptas 344
Cdd:COG5077 372 GVIFESLPPVLHLQ-----------------------LKRFEYD------------------------------------ 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 345 qMLLNQGLDLN-RFsasrgsikkssvgvDFPLQ--RLSLGDFASDKAGSP--VYQLYALCNHSGSVHYGHYTALCRCQTG 419
Cdd:COG5077 393 -FERDMMVKINdRY--------------EFPLEidLLPFLDRDADKSENSdaVYVLYGVLVHSGDLHEGHYYALLKPEKD 457
|
410
....*....|....*....
gi 966921373 420 --WHVYNDSRVSPVSENQV 436
Cdd:COG5077 458 grWYKFDDTRVTRATEKEV 476
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
28-162 |
3.70e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 51.72 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 28 VGLRNLGNTCFLNAVLQCLSSTRPLRDFCL---------------------RRDFRQEVPGGGR-AQELTEAFADVIGAL 85
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLnfdeskaelasdypterriggREVSRSELQRSNQfVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966921373 86 WHpdsceAVNPTRFRAvfqkyvpsFSGYSQQDAQEFLKLLMERLHLEINRRGrrappilaNGPVPSPPRRGGALLEE 162
Cdd:cd02666 82 TR-----SVTPSKELA--------YLALRQQDVTECIDNVLFQLEVALEPIS--------NAFAGPDTEDDKEQSDL 137
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
28-278 |
2.46e-04 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 43.03 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 28 VGLRNLGNTCFLNAVLQCLSSTRPLR-------------DFCLrrdfrqevpgggraqeLTEAfadviGALWHP--DS-- 90
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRnlalshlateclkEHCL----------------LCEL-----GFLFDMleKAkg 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 91 --CEAVNptrfravFQKyvpSFSGYSQQDA--------------------QEFLKLLMERLHLEinrrGRRAPPILANGP 148
Cdd:pfam13423 60 knCQASN-------FLR---ALSSIPEASAlglldedretnsaislssliQSFNRFLLDQLSSE----ENSTPPNPSPAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966921373 149 VPspprrggalleepelsdddranlmwkryleredskIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGG 228
Cdd:pfam13423 126 SP-----------------------------------LEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYPRKPSSNN 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 966921373 229 KVSLRDCFnlftkEEELES------ENAPVCDRCRQKTRSTKKLTVQRFPRILVLH 278
Cdd:pfam13423 171 KKPPNQTF-----SSILKSsleretTTKAWCEKCKRYQPLESRRTVRNLPPVLSLN 221
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
391-446 |
3.21e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 39.05 E-value: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966921373 391 PVYQLYALCNHSG-SVHYGHYTALCRCQTG---WHVYNDSRVSPVSENQV---ASSEGYVLFY 446
Cdd:cd02673 182 AKYSLVAVICHLGeSPYDGHYIAYTKELYNgssWLYCSDDEIRPVSKNDVstnARSSGYLIFY 244
|
|
| |
