|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-613 |
1.71e-148 |
|
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: 435.00 E-value: 1.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNL---NGCNSLMKKLQHLFAFLAHTQREAYAPRI-FFEASRPPWFTPRS 187
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLprlGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 188 QQDCSEYLRFLLDRLHeeekilrvqsshkpsegldcaetclqevtskvavptespgtgdsekTLIEKMFGGKLRTHICCL 267
Cdd:cd02664 81 QQDCSEYLRYLLDRLH----------------------------------------------TLIEKMFGGKLSTTIRCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 268 NCGSTSHKVEAFTDLSLAFCpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlgsp 347
Cdd:cd02664 115 NCNSTSARTERFRDLDLSFP------------------------------------------------------------ 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 348 pvefhcaesssvpeesakiliskdvpqnpggesttSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYL 427
Cdd:cd02664 135 -----------------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 428 ILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRTASFsslsqswsvdvdftdINENLPKKLKPSGTEEAFCPKLVPYL 507
Cdd:cd02664 180 ILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS---------------SESPLEKKEEESGDDGELVTRQVHYR 244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 508 LSSVVVHSGVSSESGHYYSYARNITGTESSYQMCPQseslalapsqscllgvespntviEQDLENKEMSQEWFLFNDSRV 587
Cdd:cd02664 245 LYAVVVHSGYSSESGHYFTYARDQTDADSTGQECPE-----------------------PKDAEENDESKNWYLFNDSRV 301
|
490 500
....*....|....*....|....*.
gi 568957738 588 TFTSFQSVQKITSRFPKDTAYVLLYK 613
Cdd:cd02664 302 TFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
111-612 |
3.30e-37 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 141.43 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 111 TGLINLGNTCYMNSVLQALFMATEFRRQVLSL-------NLNGCNSLMKKLQHLF-AFLAHTQREAYAPRIFFEA--SRP 180
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 181 PWFTPRSQQDCSEYLRFLLDRLHEEEKilrvqsshkpsegldcaetclqevtskvavptesPGTGDSEKTLIEKMFGGKL 260
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------GNHSTENESLITDLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 261 RTHICCLNCGSTSHKVEAFTDLSLAFCPSPSVEDLSFQDTASLPsaqddglmqtsvadpeeepvvynpataafvcdsvvn 340
Cdd:pfam00443 127 KSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQ------------------------------------ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 341 qrvlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQI 420
Cdd:pfam00443 171 --------------------------------------------------FSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 421 TEEPEYLILTLLRFSYDQKyhVRRKILDNVSLPLVLelpvkrtasfsslsqswsvDVDFTDINENLPKKLKP-------- 492
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLEL-------------------DLSRYLAEELKPKTNNLqdyrlvav 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 493 ---SGTEEafcpklvpyllssvvvhsgvsseSGHYYSYARNitgtessyqmcpqseslalapsqscllgvespntvieqd 569
Cdd:pfam00443 260 vvhSGSLS-----------------------SGHYIAYIKA--------------------------------------- 277
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568957738 570 lenkEMSQEWFLFNDSRVTFTSFQSVQKitsrfpKDTAYVLLY 612
Cdd:pfam00443 278 ----YENNRWYKFDDEKVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
112-613 |
2.31e-36 |
|
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: 137.23 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMatefrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftprSQQDC 191
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 192 SEYLRFLLDRLHEEEKILRVQSSHKpsegldcaetclqevtskvavptespgtgDSEKTLIEKMFGGKLRTHICCLNCGS 271
Cdd:cd02257 26 HEFLLFLLDKLHEELKKSSKRTSDS-----------------------------SSLKSLIHDLFGGKLESTIVCLECGH 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 272 TSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlgsppvef 351
Cdd:cd02257 77 ESVSTEPELFLSL------------------------------------------------------------------- 89
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 352 hcaesssvpeesakiliskDVPQNPGGESttSVTDLLNYFLAPEVLTGENQYYCESCaSLQNAEKTMQITEEPEYLILTL 431
Cdd:cd02257 90 -------------------PLPVKGLPQV--SLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHL 147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 432 LRFSYDQKYhVRRKILDNVSLPLVLelpvkrtasfsslsqswsvdvdftdineNLPKKLKPSGTEEAFCPKLVPYLLSSV 511
Cdd:cd02257 148 KRFSFNEDG-TKEKLNTKVSFPLEL----------------------------DLSPYLSEGEKDSDSDNGSYKYELVAV 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 512 VVHSGVSSESGHYYSYARNITgtessyqmcpqseslalapsqscllgvespntvieqdlenkemSQEWFLFNDSRVTFTS 591
Cdd:cd02257 199 VVHSGTSADSGHYVAYVKDPS-------------------------------------------DGKWYKFNDDKVTEVS 235
|
490 500
....*....|....*....|..
gi 568957738 592 FQSVQKITSRfpKDTAYVLLYK 613
Cdd:cd02257 236 EEEVLEFGSL--SSSAYILFYE 255
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
109-617 |
2.27e-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: 131.23 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 109 GKTGLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN----GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEASRPPWFT 184
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 185 --PRSQQDCSEYLRFLLDRLheEEKilrvqsshkpsegldcaetclqevtskvavpteSPGTGdsEKTLIEKMFGGKLRT 262
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKL--EEK---------------------------------LKGTG--QEGLIKNLFGGKLVN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 263 HICCLNCGSTSHKVEAFTDLSLAFCPSPSVEDlSFQDtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqr 342
Cdd:cd02659 124 YIICKECPHESEREEYFLDLQVAVKGKKNLEE-SLDA------------------------------------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 343 vlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQITE 422
Cdd:cd02659 160 ------------------------------------------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 423 EPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLELpvkrtasfsslsqswSVDVDFTDINENLPKKLKPSGTEEAfcpK 502
Cdd:cd02659 192 LPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDM---------------EPYTEKGLAKKEGDSEKKDSESYIY---E 253
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 503 LVPYLLssvvvhSGVSSESGHYYSYARNITgtessyqmcpqseslalapsqscllgvespntvieqdlenkemSQEWFLF 582
Cdd:cd02659 254 LHGVLV------HSGDAHGGHYYSYIKDRD-------------------------------------------DGKWYKF 284
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 568957738 583 NDSRVTFTSFQSV--------------QKITSRFPKDT-AYVLLYKKQSR 617
Cdd:cd02659 285 NDDVVTPFDPNDAeeecfggeetqktyDSGPRAFKRTTnAYMLFYERKSP 334
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-458 |
1.59e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 110.44 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 111 TGLINLGNTCYMNSVLQALFMATEFRRQVLSLN--LNGCNSLMKKL----QHLFAFLAHTqREAYAPRIFFEASRPPW-- 182
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREhsKDCCNEGFCMMcaleAHVERALASS-GPGSAPRIFSSNLKQISkh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 183 FTPRSQQDCSEYLRFLLDRLHEeekilrvqsshkpsegldcaeTCLQEvtskvAVPTESPGTGDSEKTLIEKMFGGKLRT 262
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQK---------------------ACLDR-----FKKLKAVDPSSQETTLVQQIFGGYLRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 263 HICCLNCGSTSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqr 342
Cdd:cd02661 135 QVKCLNCKHVSNTYDPFLDLSL---------------------------------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 343 vlgsppvefhcaesssvpeesakiliskDVPQNPggesttSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITE 422
Cdd:cd02661 157 ----------------------------DIKGAD------SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHR 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 568957738 423 EPEYLILTLLRFSYDQkyhvRRKILDNVSLPLVLEL 458
Cdd:cd02661 203 APNVLTIHLKRFSNFR----GGKINKQISFPETLDL 234
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-458 |
6.49e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 109.05 E-value: 6.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN--------------GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEA 177
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTedaelknmppdkphEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 178 SRppwFTPRSQQDCSEYLRFLLDRLheeekilrvqsshkpsegldcaETCLQEVTSKVAvptespgtgdseKTLIEKMFG 257
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLL----------------------EAKLSKSKNPDL------------KNIVQDLFR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 258 GKLRTHICCLNCGSTSHKVEAFTDLslafcpspsveDLSFQDTASLPSAQDDglmqtsvadpeeepvvynpataafvcds 337
Cdd:cd02668 124 GEYSYVTQCSKCGRESSLPSKFYEL-----------ELQLKGHKTLEECIDE---------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 338 vvnqrvlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKT 417
Cdd:cd02668 165 -----------------------------------------------------FLKEEQLTGDNQYFCESCNSKTDATRR 191
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568957738 418 MQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL 458
Cdd:cd02668 192 IRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDM 232
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-459 |
4.79e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 105.85 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATefrrqvlslnlngcnsLMKKLQHLFAFLAHTQRE--AYAPRIFFEASRP--PWFTPRS 187
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 188 QQDCSEYLRFLLDRLHEeekilrvqsshkpsegldcaetCLQEVTSKVAVPTESPG--TGDSEKTLIEKMFGGKLRTHIC 265
Cdd:cd02663 65 HQDAHEFLNFLLNEIAE----------------------ILDAERKAEKANRKLNNnnNAEPQPTWVHEIFQGILTNETR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 266 CLNCGSTSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlg 345
Cdd:cd02663 123 CLTCETVSSRDETFLDLSI------------------------------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 346 sppvefhcaesssvpeesakiliskDVPQNpggestTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPE 425
Cdd:cd02663 142 -------------------------DVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPK 190
|
330 340 350
....*....|....*....|....*....|....
gi 568957738 426 YLILTLLRFSYDQKYHVRRKILDNVSLPLVLELP 459
Cdd:cd02663 191 ILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-456 |
1.40e-21 |
|
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: 96.29 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLS--LNLNGC-----NSLMKKLQHLFA-FLAHTQREAYAPRIFFEASrppWF 183
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrHSCTCLscspnSCLSCAMDEIFQeFYYSGDRSPYGPINLLYLS---WK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 184 TPR-----SQQDCSEYLRFLLDRLHEEEKILRVQSSHKPseglDCaeTClqevtskvavptespgtgdsektLIEKMFGG 258
Cdd:cd02660 79 HSRnlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDES----HC--NC-----------------------IIHQTFSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 259 KLRTHICCLNCGSTSHKVEAFTDLSLAFcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsv 338
Cdd:cd02660 130 SLQSSVTCQRCGGVSTTVDPFLDLSLDI---------------------------------------------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 339 vnqrvlgsppvefhcaESSSVPEESAKILiskdvpqnpGGESTTSVTDLLNYFLAPEVLtGENQYYCESCASLQNAEKTM 418
Cdd:cd02660 158 ----------------PNKSTPSWALGES---------GVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQL 211
|
330 340 350
....*....|....*....|....*....|....*...
gi 568957738 419 QITEEPEYLILTLLRFSYDQkYHVRRKILDNVSLPLVL 456
Cdd:cd02660 212 SIKKLPPVLCFQLKRFEHSL-NKTSRKIDTYVQFPLEL 248
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
52-454 |
5.91e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 94.95 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 52 YHYSGFPDLYEPILEAVKDFPKPSEEKIKLILNQSAWTSQSNALASclsRLSGKSETGKTGLINLGNTCYMNSVLQALFM 131
Cdd:COG5560 210 YRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDH---NRSINKEAGTCGLRNLGNTCYMNSALQCLMH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 132 ATEFRRQVLS------LNLNGCNSLMKKLQHLFAFL---AHTQR-EAYAPRIF------FEASrppwFTPRSQQDCSEYL 195
Cdd:COG5560 287 TWELRDYFLSdeyeesINEENPLGMHGSVASAYADLikqLYDGNlHAFTPSGFkktigsFNEE----FSGYDQQDSQEFI 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 196 RFLLDRLHEE-EKILRVQSSHKPS--EGLDcaetclqEVTSKVAVPT--ESPGTGDSektLIEKMFGGKLRTHICCLNCG 270
Cdd:COG5560 363 AFLLDGLHEDlNRIIKKPYTSKPDlsPGDD-------VVVKKKAKECwwEHLKRNDS---IITDLFQGMYKSTLTCPGCG 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 271 STSHKVEAFTDLSL------------AFCP--------------SPSVEDLSFQDTASLP-------------------- 304
Cdd:COG5560 433 SVSITFDPFMDLTLplpvsmvwkhtiVVFPesgrrqplkieldaSSTIRGLKKLVDAEYGklgcfeikvmciyyggnynm 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 305 -SAQDDGLMQ-----------TSVADPEEEPVVYNPATAAFvcdsvVNQRVLGSPPVEFH-------------------- 352
Cdd:COG5560 513 lEPADKVLLQdipqtdfvylyETNDNGIEVPVVHLRIEKGY-----KSKRLFGDPFLQLNvlikasiydklvkefeellv 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 353 ---------CAESSSVP---EESA----------------KILISKDVPQNP---------------------------- 376
Cdd:COG5560 588 lvemkktdvDLVSEQVRllrEESSpsswlkleteidtkreEQVEEEGQMNFNdavvisceweekrylslfsydplwtire 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 377 --GGESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhvRRKILDNVSLPL 454
Cdd:COG5560 668 igAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPI 745
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-458 |
4.75e-19 |
|
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: 87.83 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFmATEFRRQVLSLNLNGcnslmkklqhLFAFLAHtqreayapriffeasRPPWFTPRSQQDC 191
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSETPKE----------LFSQVCR---------------KAPQFKGYQQQDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 192 SEYLRFLLDRLheeekilrvqsshkpsegldcaetclqevtskvavptespgtgdseKTLIEKMFGGKLRTHICCLNCGS 271
Cdd:cd02667 55 HELLRYLLDGL----------------------------------------------RTFIDSIFGGELTSTIMCESCGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 272 TSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadPEEEPVvynpataafvcdsvvnqrvlgsppvef 351
Cdd:cd02667 89 VSLVYEPFLDLSL----------------------------------PRSDEI--------------------------- 107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 352 hcaesssvpeesakiliskdvpqnpggESTTSVTDLLNYFLAPEVLTGENQYYCESCaslQNAEKTMQITEEPEYLILTL 431
Cdd:cd02667 108 ---------------------------KSECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHL 157
|
330 340
....*....|....*....|....*..
gi 568957738 432 LRFSYDQKyHVRRKILDNVSLPLVLEL 458
Cdd:cd02667 158 KRFQQPRS-ANLRKVSRHVSFPEILDL 183
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-613 |
2.51e-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: 84.65 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFmatefrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftpRSQQDC 191
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 192 SEYLRFLLDRLHeeekilrvqsshkpsegldcaetclqevtskvavptespgtgdsekTLIEKMFGGKLRTHICCLNCGS 271
Cdd:cd02674 26 QEFLLFLLDGLH----------------------------------------------SIIVDLFQGQLKSRLTCLTCGK 59
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 272 TSHKVEAFTDLSLAfcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlgsppvef 351
Cdd:cd02674 60 TSTTFEPFTYLSLP------------------------------------------------------------------ 73
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 352 hcaesssvpeesakiliskdVPQNPGGESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTL 431
Cdd:cd02674 74 --------------------IPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHL 133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 432 LRFSYDQKYhvRRKILDNVSLPLVLELPvkrtasfsslsQSWSVDVDFTDINE-NLPKKLKPSGTEEAfcpklvpyllss 510
Cdd:cd02674 134 KRFSFSRGS--TRKLTTPVTFPLNDLDL-----------TPYVDTRSFTGPFKyDLYAVVNHYGSLNG------------ 188
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 511 vvvhsgvssesGHYYSYARNitgtessyqmcpqseslalapsqscllgvespntvieqdlenkEMSQEWFLFNDSRVTFT 590
Cdd:cd02674 189 -----------GHYTAYCKN-------------------------------------------NETNDWYKFDDSRVTKV 214
|
490 500
....*....|....*....|...
gi 568957738 591 SFQSVQkitsrfpKDTAYVLLYK 613
Cdd:cd02674 215 SESSVV-------SSSAYILFYE 230
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
105-458 |
5.60e-11 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 66.05 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 105 KSETGKTGLINLGNTCYMNSVLQALFMATEFRRQVLSL---NLNGCNSLMKKLQHLFAFLaHTQREayaPRIFFEASRP- 180
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIptdHPRGRDSVALALQRLFYNL-QTGEE---PVDTTELTRSf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 181 PWFTPRS--QQDCSEYLRFLLDRLheeEKILRvqsshkpsegldcaetclqevtskvavptespgtGDSEKTLIEKMFGG 258
Cdd:COG5077 264 GWDSDDSfmQHDIQEFNRVLQDNL---EKSMR----------------------------------GTVVENALNGIFVG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 259 KLRTHICCLNCGSTSHKVEAFTDLSLAFCPSPSVEDlSFQDtaslpsaqddglmqtsvadpeeepvvynpataafvcdsv 338
Cdd:COG5077 307 KMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE-SFRR--------------------------------------- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 339 vnqrvlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCEScASLQNAEKTM 418
Cdd:COG5077 347 ----------------------------------------------------YIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568957738 419 QITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL 458
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDL 413
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-207 |
2.67e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 62.34 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNL----------NGCNSLMKKLQHlfAFLAH---------TQREAY--- 169
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfpsdvvdpaNDLNCQLIKLAD--GLLSGryskpaslkSENDPYqvg 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568957738 170 -APRIF----------FEASRppwftprsQQDCSEYLRFLLDRLHEEEK 207
Cdd:cd02658 79 iKPSMFkaligkghpeFSTMR--------QQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-234 |
3.57e-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 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: 61.58 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLNG------CNSLMKKLQHLFAFLAHTQrEAYAPRIFFEASRP--PWF 183
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARrganqsSDNLTNALRDLFDTMDKKQ-EPVPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568957738 184 TPRS------QQDCSEYLRFLLDRLHEEEKILRVQSSH-------KPSEGLDCAETCLQEVTSK 234
Cdd:cd02657 80 AEKQnqggyaQQDAEECWSQLLSVLSQKLPGAGSKGSFidqlfgiELETKMKCTESPDEEEVST 143
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-454 |
8.86e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 60.68 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLSLnlngCNSLMKKLQHLFAFLA-----HTQREAYAPRIFFEASRP--PWFT 184
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVEQLQSSFLLnpekyNDELANQAPRRLLNALREvnPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 185 PRSQQDCSEYLRFLLDrlheeekilrvqsshkpsegldcaetCLQEvtskvavptespgtgdsektLIEKMFGGKLRTHI 264
Cdd:cd02671 102 GYLQHDAQEVLQCILG--------------------------NIQE--------------------LVEKDFQGQLVLRT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 265 CCLNCGSTSHKVEAFTDLSLafcPSPSVEDLSFQDTaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvl 344
Cdd:cd02671 136 RCLECETFTERREDFQDISV---PVQESELSKSEES-------------------------------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 345 gsppvefhcaeSSSVPEESAKILISKDVPQNpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQITEEP 424
Cdd:cd02671 169 -----------SEISPDPKTEMKTLKWAISQ---------------FASVERIVGEDKYFCENCHHYTEAERSLLFDKLP 222
|
330 340 350
....*....|....*....|....*....|
gi 568957738 425 EYLILTLLRFSYDQKYHVRRKILDNVSLPL 454
Cdd:cd02671 223 EVITIHLKCFAANGSEFDCYGGLSKVNTPL 252
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
112-202 |
3.43e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 52.50 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLNGCNSLMKKLQHLFAFLahTQREAYApriFFEASRP-------PWFT 184
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKNVIRKPEPDL--NQEEALK---LFTALWSskehkvgWIPP 75
|
90
....*....|....*...
gi 568957738 185 PRSQQDCSEYLRFLLDRL 202
Cdd:COG5533 76 MGSQEDAHELLGKLLDEL 93
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
112-221 |
3.51e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 48.90 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957738 112 GLINLGNTCYMNSVLQAlfmatefrrqvlslnLNGCNSLMKKLQhlfaflahtqreayapriffeasrppWFTprSQQDC 191
Cdd:cd02662 1 GLVNLGNTCFMNSVLQA---------------LASLPSLIEYLE--------------------------EFL--EQQDA 37
|
90 100 110
....*....|....*....|....*....|
gi 568957738 192 SEYLRFLLDRLHeeekilrvQSSHKPSEGL 221
Cdd:cd02662 38 HELFQVLLETLE--------QLLKFPFDGL 59
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
111-145 |
6.30e-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: 49.03 E-value: 6.30e-06
10 20 30
....*....|....*....|....*....|....*
gi 568957738 111 TGLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN 145
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDES 36
|
|
| |
