|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-518 |
3.51e-105 |
|
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: 320.59 E-value: 3.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFMASDFRHCVLRLT---ENNSQPLMTKLQWLFAFLEHSQRPAISPEN-FLSASWTPWFSPGT 121
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNlprLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 122 QQDCSEYLKYLLDRLHeeektgtricqklkqsslpspqeelpssnaTSVERMFGGKIVTRICCLHCLNVSSREEAFTDLS 201
Cdd:cd02664 81 QQDCSEYLRYLLDRLH------------------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 202 LAFPppersrhrrlgsvmlptedvraqeltlaprapgaqrqrkhcitgdaprtgldiegvdtvgnggqsgqekvereqag 281
Cdd:cd02664 131 LSFP---------------------------------------------------------------------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 282 kekevaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreqacgpegsrSVLDLVNY 361
Cdd:cd02664 135 ------------------------------------------------------------------------SVQDLLNY 142
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 362 FLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVTIPLLLRLPL---------- 431
Cdd:cd02664 143 FLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVrveskssesp 222
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 432 ----AGGQGQA---------YDLCSVVVHSGVSSESGHYYCYAR-----EGAARPAPVLGSTERPEPENQWYLFNDTRVS 493
Cdd:cd02664 223 lekkEEESGDDgelvtrqvhYRLYAVVVHSGYSSESGHYFTYARdqtdaDSTGQECPEPKDAEENDESKNWYLFNDSRVT 302
|
490 500
....*....|....*....|....*
gi 1958653818 494 FSSFESVSNVTSFFPKDTAYVLFYR 518
Cdd:cd02664 303 FSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
45-517 |
7.33e-34 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 131.03 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 45 IGLINLGNTCYVNSVLQALFMASDFRHCVLRL-------TENNSQPLMTKLQWLF-AFLEHSQRPAISPENFLSA--SWT 114
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 115 PWFSPGTQQDCSEYLKYLLDRLHEEEKTGTricqKLKQSSLPSpqeelpssnatsveRMFGGKIVTRICCLHCLNVSSRE 194
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNGNH----STENESLIT--------------DLFRGQLKSRLKCLSCGEVSETF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 195 EAFTDLSlafpppersrhrrlgsvmlptedvraqeltlaprapgaqrqrkhcitgdaprtgLDIEGVDTVGNGGQSGQEK 274
Cdd:pfam00443 143 EPFSDLS------------------------------------------------------LPIPGDSAELKTASLQICF 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 275 VEreqagkekevaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreqacgpegsrs 354
Cdd:pfam00443 169 LQ------------------------------------------------------------------------------ 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 355 vldlvnyFLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTmrRRKILDDVTIPLLLRLplagg 434
Cdd:pfam00443 171 -------FSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDL----- 236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 435 qgqaYDLCSVVVHSGVSSES----------------GHYYCYAregaarpapvlgsteRPEPENQWYLFNDTRVSFSSFE 498
Cdd:pfam00443 237 ----SRYLAEELKPKTNNLQdyrlvavvvhsgslssGHYIAYI---------------KAYENNRWYKFDDEKVTEVDEE 297
|
490
....*....|....*....
gi 1958653818 499 SVSNvtsffpKDTAYVLFY 517
Cdd:pfam00443 298 TAVL------SSSAYILFY 310
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-518 |
6.21e-33 |
|
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: 129.30 E-value: 6.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 43 GKIGLINLGNTCYVNSVLQALFMASDFRHCVLRLTEN----NSQPLMTKLQWLFAFLEHSQRPAISPENFLSASWTPWFS 118
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 119 --PGTQQDCSEYLKYLLDRLHEeektgtricqKLKQSSLPSpqeelpssnatSVERMFGGKIVTRICCLHCLNVSSREEA 196
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKLEE----------KLKGTGQEG-----------LIKNLFGGKLVNYIICKECPHESEREEY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 197 FTDLSLAfpppersrhrrlgsVMlptedvraqeltlaprapgaqrqrkhcitgdaprtgldiegvdtvgnGGQSGQEKVE 276
Cdd:cd02659 140 FLDLQVA--------------VK-----------------------------------------------GKKNLEESLD 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 277 Reqagkekevaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreqacgpegsrsvl 356
Cdd:cd02659 159 A------------------------------------------------------------------------------- 159
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 357 dlvnyFLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVTIPLLLRL------P 430
Cdd:cd02659 160 -----YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMepytekG 234
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 431 LAGGQGQAYDLCSVVVHSGV--------SSESGHYYCYAregaarpapvlgsteRPEPENQWYLFNDTRvsfssfesvsn 502
Cdd:cd02659 235 LAKKEGDSEKKDSESYIYELhgvlvhsgDAHGGHYYSYI---------------KDRDDGKWYKFNDDV----------- 288
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958653818 503 VTSF-------------------------FPKDT-AYVLFYR 518
Cdd:cd02659 289 VTPFdpndaeeecfggeetqktydsgpraFKRTTnAYMLFYE 330
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
46-518 |
4.52e-30 |
|
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: 118.74 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFMasdfrhcvlrltennsqplmtklqwlfaflehsqrpaispenflsaswtpwfspgTQQDC 125
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 126 SEYLKYLLDRLHEEEKTGtricqklkqsslpSPQEELPSSNATSVERMFGGKIVTRICCLHCLNVSSREEAFTDLSLAFP 205
Cdd:cd02257 26 HEFLLFLLDKLHEELKKS-------------SKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 206 PPersrhrrlgsvmlptedvraqeltlaprapgaqrqrkhcitgdaprtgldiegvdtvgnggqsgqekvereqagkeke 285
Cdd:cd02257 93 VK------------------------------------------------------------------------------ 94
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 286 vaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreqacgPEGSRSVLDLVNYFLSP 365
Cdd:cd02257 95 ---------------------------------------------------------------GLPQVSLEDCLEKFFKE 111
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 366 ERLTAENRYYCESCaSLQDAEKVVELSQGPCYLILTLLRFSFDlRTMRRRKILDDVTIPLLLRL----------PLAGGQ 435
Cdd:cd02257 112 EILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLspylsegekdSDSDNG 189
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 436 GQAYDLCSVVVHSGVSSESGHYYCYAREGaarpapvlgsterpePENQWYLFNDTRVSFSSFESVSNVTSFfpKDTAYVL 515
Cdd:cd02257 190 SYKYELVAVVVHSGTSADSGHYVAYVKDP---------------SDGKWYKFNDDKVTEVSEEEVLEFGSL--SSSAYIL 252
|
...
gi 1958653818 516 FYR 518
Cdd:cd02257 253 FYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-489 |
4.08e-24 |
|
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: 103.65 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFMASDFRHCVLRL--------------TENNSQPLMTKLQWLFAFLEHSQRPAISPENFLSA 111
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECnstedaelknmppdKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 112 SWtpwFSPGTQQDCSEYLKYLLDRLHEeektgtricqKLKQSSLPSPQeelpssnaTSVERMFGGKIVTRICCLHCLNVS 191
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLLEA----------KLSKSKNPDLK--------NIVQDLFRGEYSYVTQCSKCGRES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 192 SREEAFTDLSLAFppperSRHRRLgsvmlptedvraqeltlaprapgaqrqrKHCITGdaprtgldiegvdtvgnggqsg 271
Cdd:cd02668 140 SLPSKFYELELQL-----KGHKTL----------------------------EECIDE---------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 272 qekvereqagkekevaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreqacgpeg 351
Cdd:cd02668 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 352 srsvldlvnyFLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVTIPLLL---- 427
Cdd:cd02668 165 ----------FLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILdmge 234
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958653818 428 RLPLAGGQGQAYDLCSVVVHSGVSSESGHYYCYAREgaarpapvlgsterpEPENQWYLFND 489
Cdd:cd02668 235 YLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKD---------------EQTGEWYKFND 281
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-517 |
6.90e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 99.27 E-value: 6.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQAL--------FMasdfrhcvlrLTENNSQPLMTKLQWLFAFLEH-------SQRPAISPENFLS 110
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLthtpplanYL----------LSREHSKDCCNEGFCMMCALEAhveralaSSGPGSAPRIFSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 111 A--SWTPWFSPGTQQDCSEYLKYLLDRLHeeeKTGTRICQKLKQSSlpspqeelPSSNATS-VERMFGGKIVTRICCLHC 187
Cdd:cd02661 73 NlkQISKHFRIGRQEDAHEFLRYLLDAMQ---KACLDRFKKLKAVD--------PSSQETTlVQQIFGGYLRSQVKCLNC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 188 LNVSSREEAFTDLSLafpppersrhrrlgsvmlptedvraqeltlaprapgaqrqrkhcitgdaprtglDIEGVDTVGng 267
Cdd:cd02661 142 KHVSNTYDPFLDLSL------------------------------------------------------DIKGADSLE-- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 268 gqsgqekvereqagkekevaedreeegpreeekeegeekdkekkedekekeaedgkekegDSLgpgtrkdaatpprEQac 347
Cdd:cd02661 166 ------------------------------------------------------------DAL-------------EQ-- 170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 348 gpegsrsvldlvnyFLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDlrtmRRRKILDDVTIPLLL 427
Cdd:cd02661 171 --------------FTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF----RGGKINKQISFPETL 232
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 428 RL-PL---AGGQGQAYDLCSVVVHSGVSSESGHYYCYARegaarpapvlgsterpEPENQWYLFNDTRVSFSSFESVSNv 503
Cdd:cd02661 233 DLsPYmsqPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVK----------------SSNGKWYNMDDSKVSPVSIETVLS- 295
|
490
....*....|....
gi 1958653818 504 tsffpkDTAYVLFY 517
Cdd:cd02661 296 ------QKAYILFY 303
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-517 |
6.24e-22 |
|
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: 96.61 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFMASdfrhcvlrltennsqpLMTKLQWLF-AFLEHSQRPA-ISPENFLSASWT--PWFSPGT 121
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFeSISEQKKRTGvISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 122 QQDCSEYLKYLLDRLHE---EEKTGTRICQKLKQSSLPSPQEelpssnaTSVERMFGGKIVTRICCLHCLNVSSREEAFT 198
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEildAERKAEKANRKLNNNNNAEPQP-------TWVHEIFQGILTNETRCLTCETVSSRDETFL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 199 DLSLafpppersrhrrlgsvmlptedvraqeltlaprapgaqrqrkhcitgdaprtglDIEgvdtvgnggqsgqekvere 278
Cdd:cd02663 138 DLSI------------------------------------------------------DVE------------------- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 279 qagkekevaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreQACgpegsrSVLDL 358
Cdd:cd02663 145 ------------------------------------------------------------------QNT------SITSC 152
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 359 VNYFLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRTMRRRKILDDVTIPLLLRLP----LAGG 434
Cdd:cd02663 153 LRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLFnttdDAEN 232
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 435 QGQAYDLCSVVVHSGVSSESGHYYCYAREGaarpapvlgsterpepeNQWYLFNDtrvSFSSFESVSNVTSFF----PKD 510
Cdd:cd02663 233 PDRLYELVAVVVHIGGGPNHGHYVSIVKSH-----------------GGWLLFDD---ETVEKIDENAVEEFFgdspNQA 292
|
....*..
gi 1958653818 511 TAYVLFY 517
Cdd:cd02663 293 TAYVLFY 299
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
43-520 |
1.32e-19 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 93.41 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 43 GKIGLINLGNTCYVNSVLQALFMASDFRHCVL------RLTENNSQPLMTKLQWLFAFL---EHSQR-PAISPENFLS-- 110
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLsdeyeeSINEENPLGMHGSVASAYADLikqLYDGNlHAFTPSGFKKti 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 111 ASWTPWFSPGTQQDCSEYLKYLLDRLHEEEktgTRICQKlKQSSLPSPQEELP---------------SSNATSVERMFG 175
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDL---NRIIKK-PYTSKPDLSPGDDvvvkkkakecwwehlKRNDSIITDLFQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 176 GKIVTRICCLHCLNVSSREEAFTDLSLAFPPPERSRHrrlgSVMLPTEDVRAQELTLAPRAPGAQRQRK----------- 244
Cdd:COG5560 420 GMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKH----TIVVFPESGRRQPLKIELDASSTIRGLKklvdaeygklg 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 245 ---------------------------------HCITGDAPRTGLDIEGVDTVGNGGQ-------------------SGQ 272
Cdd:COG5560 496 cfeikvmciyyggnynmlepadkvllqdipqtdFVYLYETNDNGIEVPVVHLRIEKGYkskrlfgdpflqlnvlikaSIY 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 273 EKVEREQAGKEKEVAEDREEEGPREEEKEEGEEKDKEKKEDEKEKEAEDGKEKEGDSLGPGTRKDAATPPRE-------- 344
Cdd:COG5560 576 DKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEweekryls 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 345 ----QACGPE-----GSRSVL--DLVNYFLSPERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDLRtmR 413
Cdd:COG5560 656 lfsyDPLWTIreigaAERTITlqDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRS--F 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 414 RRKILDDVTIPlLLRLPLAGGQGQ------AYDLcSVVVHSGVSSESGHYYCYAREGAarpapvlgsterpepENQWYLF 487
Cdd:COG5560 734 RDKIDDLVEYP-IDDLDLSGVEYMvddprlIYDL-YAVDNHYGGLSGGHYTAYARNFA---------------NNGWYLF 796
|
570 580 590
....*....|....*....|....*....|....*..
gi 1958653818 488 NDTRvsfssfesvsnVTSFFPKDT----AYVLFYRQR 520
Cdd:COG5560 797 DDSR-----------ITEVDPEDSvtssAYVLFYRRK 822
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-518 |
4.55e-18 |
|
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: 83.49 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFmasdfrhcvlrltennsqplmtklqwlfaflehsqrpaispenflsaswtpwfspGTQQDC 125
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 126 SEYLKYLLDRLHeeektgtricqklkqsSLpspqeelpssnatsVERMFGGKIVTRICCLHCLNVSSREEAFTDLSLAfp 205
Cdd:cd02674 26 QEFLLFLLDGLH----------------SI--------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLP-- 73
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 206 ppersrhrrlgsvmLPTEDVRAQELTLaprapgaqrqrKHCITGdaprtgldiegvdtvgnggqsgqekvereqagkeke 285
Cdd:cd02674 74 --------------IPSGSGDAPKVTL-----------EDCLRL------------------------------------ 92
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 286 vaedreeegpreeekeegeekdkekkedekekeaedgkekegdslgpgtrkdaatppreqacgpegsrsvldlvnyFLSP 365
Cdd:cd02674 93 ----------------------------------------------------------------------------FTKE 96
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 366 ERLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFSFDlrTMRRRKILDDVTIPL--LLRLPLAGGQGQA----Y 439
Cdd:cd02674 97 ETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPLndLDLTPYVDTRSFTgpfkY 174
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958653818 440 DLCsVVVHSGVSSESGHYYCYARegaarpapvlgsteRPEPeNQWYLFNDTRVSFSSFESVSNvtsffpkDTAYVLFYR 518
Cdd:cd02674 175 DLY-AVVNHYGSLNGGHYTAYCK--------------NNET-NDWYKFDDSRVTKVSESSVVS-------SSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-211 |
5.33e-17 |
|
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: 82.42 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQAL--------FMASDFRHCVLRLTENNSQpLMTKLQWLFA-FLEHSQRPAISPENFLSASWTPW 116
Cdd:cd02660 2 GLINLGATCFMNVILQALlhnpllrnYFLSDRHSCTCLSCSPNSC-LSCAMDEIFQeFYYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 117 FSPGT--QQDCSEYLKYLLDRLHEEEKTGTRICQKLKQSSLPspqeelpssnatsVERMFGGKIVTRICCLHCLNVSSRE 194
Cdd:cd02660 81 RNLAGysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCI-------------IHQTFSGSLQSSVTCQRCGGVSTTV 147
|
170
....*....|....*..
gi 1958653818 195 EAFTDLSLAFPPPERSR 211
Cdd:cd02660 148 DPFLDLSLDIPNKSTPS 164
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-210 |
1.45e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 71.26 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFmasdfrhcvlrltennSQPLMTKLqwlfaFLEhsqrpaiSPENFLS--ASWTPWFSPGTQQ 123
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS----------------QTPALREL-----LSE-------TPKELFSqvCRKAPQFKGYQQQ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 124 DCSEYLKYLLDRLHeeektgtricqklkqsslpspqeelpssnaTSVERMFGGKIVTRICCLHCLNVSSREEAFTDLSLA 203
Cdd:cd02667 53 DSHELLRYLLDGLR------------------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP 102
|
....*..
gi 1958653818 204 FPPPERS 210
Cdd:cd02667 103 RSDEIKS 109
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-205 |
2.16e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 71.20 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALF-----------MASDFRHCVLRLTEN-NSQplMTKLqwLFAFLEH----------SQRP-- 101
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFsipsfqwryddLENKFPSDVVDPANDlNCQ--LIKL--ADGLLSGryskpaslksENDPyq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 102 -AISPENF--LSASWTPWFSPGTQQDCSEYLKYLLDRLHeeektgtricQKLKQSSLPSPQEelpssnatsverMFGGKI 178
Cdd:cd02658 77 vGIKPSMFkaLIGKGHPEFSTMRQQDALEFLLHLIDKLD----------RESFKNLGLNPND------------LFKFMI 134
|
170 180
....*....|....*....|....*..
gi 1958653818 179 VTRICCLHCLNVSSREEAFTDLSLAFP 205
Cdd:cd02658 135 EDRLECLSCKKVKYTSELSEILSLPVP 161
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
38-202 |
1.04e-12 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 71.44 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 38 AKSDTGKIGLINLGNTCYVNSVLQALFMASDFRHCVLRLTENNSQP---LMTKLQWLFAFLEHSQRPAISPENFLSASWT 114
Cdd:COG5077 187 SKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGrdsVALALQRLFYNLQTGEEPVDTTELTRSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 115 PwFSPGTQQDCSEYLKYLLDRLhEEEKTGTRICQKLKQsslpspqeelpssnatsverMFGGKIVTRICCLHCLNVSSRE 194
Cdd:COG5077 267 S-DDSFMQHDIQEFNRVLQDNL-EKSMRGTVVENALNG--------------------IFVGKMKSYIKCVNVNYESARV 324
|
....*...
gi 1958653818 195 EAFTDLSL 202
Cdd:COG5077 325 EDFWDIQL 332
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
45-250 |
1.10e-12 |
|
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: 69.54 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 45 IGLINLGNTCYVNSVLQALFMASDFRHCVLRLTENNSQplMTKLQWLFAFLE---HSQRPAISPENFLSA--SWTPWFSP 119
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISS--VEQLQSSFLLNPekyNDELANQAPRRLLNAlrEVNPMYEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 120 GTQQDCSEYLKYLLDRLHEeektgtricqklkqsslpspqeelpssnatSVERMFGGKIVTRICCLHCLNVSSREEAFTD 199
Cdd:cd02671 103 YLQHDAQEVLQCILGNIQE------------------------------LVEKDFQGQLVLRTRCLECETFTERREDFQD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958653818 200 LSLAFPPPERSRHRRlGSVMLPTEDVRAQELTLAPrapgAQRQRKHCITGD 250
Cdd:cd02671 153 ISVPVQESELSKSEE-SSEISPDPKTEMKTLKWAI----SQFASVERIVGE 198
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-185 |
6.74e-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 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: 57.73 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFMASDFRHCVLRLTEN------NSQPLMTKLQWLFAFLEHSQRPaISPENFLSASWT--PWF 117
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPArrganqSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958653818 118 SPGT------QQDCSEYLKYLLDRLheeektgtricqklkQSSLPspqeeLPSSNATSVERMFGGKIVTRICCL 185
Cdd:cd02657 80 AEKQnqggyaQQDAEECWSQLLSVL---------------SQKLP-----GAGSKGSFIDQLFGIELETKMKCT 133
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-212 |
1.63e-08 |
|
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: 55.84 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALfmASdfrhcvlrltennsqplmtkLQWLFAFLehsqrpaispENFLSaswtpwfspgtQQDC 125
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL--AS--------------------LPSLIEYL----------EEFLE-----------QQDA 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 126 SEYLKYLLDRLHeeektgtricQKLKQSslpspqeelpssnatsvermFGGKIVTRICCLHCLNVSS-REEAFTDLSLAf 204
Cdd:cd02662 38 HELFQVLLETLE----------QLLKFP--------------------FDGLLASRIVCLQCGESSKvRYESFTMLSLP- 86
|
....*...
gi 1958653818 205 PPPERSRH 212
Cdd:cd02662 87 VPNQSSGS 94
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
46-136 |
1.91e-06 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 49.80 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 46 GLINLGNTCYVNSVLQALFMASD----------FRHCVLRLTENNSQPLMTKLQWLFAFlehsqrPAISPENFLSASWTP 115
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPkldellddlsKELKVLKNVIRKPEPDLNQEEALKLF------TALWSSKEHKVGWIP 74
|
90 100
....*....|....*....|.
gi 1958653818 116 wfSPGTQQDCSEYLKYLLDRL 136
Cdd:COG5533 75 --PMGSQEDAHELLGKLLDEL 93
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
45-178 |
7.75e-06 |
|
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: 48.26 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 45 IGLINLGNTCYVNSVLQALFMASDFRHCVLRLTENN-------------------------SQPLMTKLQWLFAFLEHSQ 99
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKaelasdypterriggrevsrselqrSNQFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958653818 100 RPAISPENFLSaswtpwFSPGTQQDCSEYLKYLLDRLHEEEKTGTricqklkQSSLPSPQEELPSSNaTSVERMFGGKI 178
Cdd:cd02666 82 TRSVTPSKELA------YLALRQQDVTECIDNVLFQLEVALEPIS-------NAFAGPDTEDDKEQS-DLIKRLFSGKT 146
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
43-207 |
1.64e-04 |
|
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: 44.23 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 43 GKIGLINLGNTCYVNSVLQALFMASDFR-HCVL----RLTENNSQPLMTKLQWLF-------AFLEHsqrpaISPENFLS 110
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRnFFLLyenyENIKDRKSELVKRLSELIrkiwnprNFKGH-----VSPHELLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958653818 111 A----SWTPwFSPGTQQDCSEYLKYLLDRLH--------EEEKTGTRICQ-KLKQSSLPSPQEELPSSNATSVERMFGGK 177
Cdd:cd02669 193 AvskvSKKK-FSITEQSDPVEFLSWLLNTLHkdlggskkPNSSIIHDCFQgKVQIETQKIKPHAEEEGSKDKFFKDSRVK 271
|
170 180 190
....*....|....*....|....*....|
gi 1958653818 178 IVTRICCLHclnvssreeaftdLSLAFPPP 207
Cdd:cd02669 272 KTSVSPFLL-------------LTLDLPPP 288
|
|
| |
