|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
1.63e-144 |
|
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: 1.63e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNL---NGCNSLMKKLQHLFAFLAHTQREAYAPRI-FFEASRPPWFTPRS 521
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLprlGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 522 QQDCSEYLRFLLDRLHeeekilrvqsshkpsegldcaetclqevtskvavptespgtgdsekTLIEKMFGGKLRTHICCL 601
Cdd:cd02664 81 QQDCSEYLRYLLDRLH----------------------------------------------TLIEKMFGGKLSTTIRCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 602 NCGSTSHKVEAFTDLSLAFCpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlgsp 681
Cdd:cd02664 115 NCNSTSARTERFRDLDLSFP------------------------------------------------------------ 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 682 pvefhcaesssvpeesakiliskdvpqnpggesttSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYL 761
Cdd:cd02664 135 -----------------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 762 ILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRTASFsslsqswsvdvdftdINENLPKKLKPSGTEEAFCPKLVPYL 841
Cdd:cd02664 180 ILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS---------------SESPLEKKEEESGDDGELVTRQVHYR 244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 842 LSSVVVHSGVSSESGHYYSYARNITGTESSYQMCPQseslalapsqscllgvespntviEQDLENKEMSQEWFLFNDSRV 921
Cdd:cd02664 245 LYAVVVHSGYSSESGHYFTYARDQTDADSTGQECPE-----------------------PKDAEENDESKNWYLFNDSRV 301
|
490 500
....*....|....*....|....*.
gi 34784763 922 TFTSFQSVQKITSRFPKDTAYVLLYK 947
Cdd:cd02664 302 TFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
445-946 |
5.23e-37 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 141.81 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 445 TGLINLGNTCYMNSVLQALFMATEFRRQVLSL-------NLNGCNSLMKKLQHLF-AFLAHTQREAYAPRIFFEA--SRP 514
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 515 PWFTPRSQQDCSEYLRFLLDRLHEEEKilrvqsshkpsegldcaetclqevtskvavptesPGTGDSEKTLIEKMFGGKL 594
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------GNHSTENESLITDLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 595 RTHICCLNCGSTSHKVEAFTDLSLAFCPSPSVEDLSFQDTASLPsaqddglmqtsvadpeeepvvynpataafvcdsvvn 674
Cdd:pfam00443 127 KSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQ------------------------------------ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 675 qrvlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQI 754
Cdd:pfam00443 171 --------------------------------------------------FSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 755 TEEPEYLILTLLRFSYDQKyhVRRKILDNVSLPLVLelpvkrtasfsslsqswsvDVDFTDINENLPKKLKP-------- 826
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLEL-------------------DLSRYLAEELKPKTNNLqdyrlvav 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 827 ---SGTEEafcpklvpyllssvvvhsgvsseSGHYYSYARNitgtessyqmcpqseslalapsqscllgvespntvieqd 903
Cdd:pfam00443 260 vvhSGSLS-----------------------SGHYIAYIKA--------------------------------------- 277
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 34784763 904 lenkEMSQEWFLFNDSRVTFTSFQSVQKitsrfpKDTAYVLLY 946
Cdd:pfam00443 278 ----YENNRWYKFDDEKVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
446-947 |
6.01e-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: 6.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMatefrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftprSQQDC 525
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 526 SEYLRFLLDRLHEEEKILRVQSSHKpsegldcaetclqevtskvavptespgtgDSEKTLIEKMFGGKLRTHICCLNCGS 605
Cdd:cd02257 26 HEFLLFLLDKLHEELKKSSKRTSDS-----------------------------SSLKSLIHDLFGGKLESTIVCLECGH 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 606 TSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlgsppvef 685
Cdd:cd02257 77 ESVSTEPELFLSL------------------------------------------------------------------- 89
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 686 hcaesssvpeesakiliskDVPQNPGGESttSVTDLLNYFLAPEVLTGENQYYCESCaSLQNAEKTMQITEEPEYLILTL 765
Cdd:cd02257 90 -------------------PLPVKGLPQV--SLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHL 147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 766 LRFSYDQKYhVRRKILDNVSLPLVLelpvkrtasfsslsqswsvdvdftdineNLPKKLKPSGTEEAFCPKLVPYLLSSV 845
Cdd:cd02257 148 KRFSFNEDG-TKEKLNTKVSFPLEL----------------------------DLSPYLSEGEKDSDSDNGSYKYELVAV 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 846 VVHSGVSSESGHYYSYARNITgtessyqmcpqseslalapsqscllgvespntvieqdlenkemSQEWFLFNDSRVTFTS 925
Cdd:cd02257 199 VVHSGTSADSGHYVAYVKDPS-------------------------------------------DGKWYKFNDDKVTEVS 235
|
490 500
....*....|....*....|..
gi 34784763 926 FQSVQKITSRfpKDTAYVLLYK 947
Cdd:cd02257 236 EEEVLEFGSL--SSSAYILFYE 255
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-951 |
3.01e-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: 131.61 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 443 GKTGLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN----GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEASRPPWFT 518
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 519 --PRSQQDCSEYLRFLLDRLheEEKilrvqsshkpsegldcaetclqevtskvavpteSPGTGdsEKTLIEKMFGGKLRT 596
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKL--EEK---------------------------------LKGTG--QEGLIKNLFGGKLVN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 597 HICCLNCGSTSHKVEAFTDLSLAFCPSPSVEDlSFQDtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqr 676
Cdd:cd02659 124 YIICKECPHESEREEYFLDLQVAVKGKKNLEE-SLDA------------------------------------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 677 vlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQITE 756
Cdd:cd02659 160 ------------------------------------------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 757 EPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL-PvkrtasfsslsqswsvDVDFTDINENLPKKLKPSGTEEAfcp 835
Cdd:cd02659 192 LPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMeP----------------YTEKGLAKKEGDSEKKDSESYIY--- 252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 836 KLVPYLLssvvvhSGVSSESGHYYSYARNITgtessyqmcpqseslalapsqscllgvespntvieqdlenkemSQEWFL 915
Cdd:cd02659 253 ELHGVLV------HSGDAHGGHYYSYIKDRD-------------------------------------------DGKWYK 283
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 34784763 916 FNDSRVTFTSFQSV--------------QKITSRFPKDT-AYVLLYKKQSR 951
Cdd:cd02659 284 FNDDVVTPFDPNDAeeecfggeetqktyDSGPRAFKRTTnAYMLFYERKSP 334
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-792 |
1.70e-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: 110.83 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 445 TGLINLGNTCYMNSVLQALFMATEFRRQVLSLN--LNGCNSLMKKL----QHLFAFLAHTqREAYAPRIFFEASRPPW-- 516
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREhsKDCCNEGFCMMcaleAHVERALASS-GPGSAPRIFSSNLKQISkh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 517 FTPRSQQDCSEYLRFLLDRLHEeekilrvqsshkpsegldcaeTCLQEvtskvAVPTESPGTGDSEKTLIEKMFGGKLRT 596
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQK---------------------ACLDR-----FKKLKAVDPSSQETTLVQQIFGGYLRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 597 HICCLNCGSTSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqr 676
Cdd:cd02661 135 QVKCLNCKHVSNTYDPFLDLSL---------------------------------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 677 vlgsppvefhcaesssvpeesakiliskDVPQNPggesttSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITE 756
Cdd:cd02661 157 ----------------------------DIKGAD------SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHR 202
|
330 340 350
....*....|....*....|....*....|....*.
gi 34784763 757 EPEYLILTLLRFSYDQkyhvRRKILDNVSLPLVLEL 792
Cdd:cd02661 203 APNVLTIHLKRFSNFR----GGKINKQISFPETLDL 234
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-792 |
4.37e-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: 110.20 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN--------------GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEA 511
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTedaelknmppdkphEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 512 SRppwFTPRSQQDCSEYLRFLLDRLheeekilrvqsshkpsegldcaETCLQEVTSKVAvptespgtgdseKTLIEKMFG 591
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLL----------------------EAKLSKSKNPDL------------KNIVQDLFR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 592 GKLRTHICCLNCGSTSHKVEAFTDLslafcpspsveDLSFQDTASLPSAQDDglmqtsvadpeeepvvynpataafvcds 671
Cdd:cd02668 124 GEYSYVTQCSKCGRESSLPSKFYEL-----------ELQLKGHKTLEECIDE---------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 672 vvnqrvlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKT 751
Cdd:cd02668 165 -----------------------------------------------------FLKEEQLTGDNQYFCESCNSKTDATRR 191
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 34784763 752 MQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL 792
Cdd:cd02668 192 IRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDM 232
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-793 |
4.19e-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: 107.01 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATefrrqvlslnlngcnsLMKKLQHLFAFLAHTQRE--AYAPRIFFEASRP--PWFTPRS 521
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 522 QQDCSEYLRFLLDRLHEeekilrvqsshkpsegldcaetCLQEVTSKVAVPTESPG--TGDSEKTLIEKMFGGKLRTHIC 599
Cdd:cd02663 65 HQDAHEFLNFLLNEIAE----------------------ILDAERKAEKANRKLNNnnNAEPQPTWVHEIFQGILTNETR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 600 CLNCGSTSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlg 679
Cdd:cd02663 123 CLTCETVSSRDETFLDLSI------------------------------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 680 sppvefhcaesssvpeesakiliskDVPQNpggestTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPE 759
Cdd:cd02663 142 -------------------------DVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPK 190
|
330 340 350
....*....|....*....|....*....|....
gi 34784763 760 YLILTLLRFSYDQKYHVRRKILDNVSLPLVLELP 793
Cdd:cd02663 191 ILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-790 |
2.01e-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: 96.67 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLS--LNLNGC-----NSLMKKLQHLFA-FLAHTQREAYAPRIFFEASrppWF 517
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrHSCTCLscspnSCLSCAMDEIFQeFYYSGDRSPYGPINLLYLS---WK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 518 TPR-----SQQDCSEYLRFLLDRLHEEEKILRVQSSHKPseglDCaeTClqevtskvavptespgtgdsektLIEKMFGG 592
Cdd:cd02660 79 HSRnlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDES----HC--NC-----------------------IIHQTFSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 593 KLRTHICCLNCGSTSHKVEAFTDLSLAFcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsv 672
Cdd:cd02660 130 SLQSSVTCQRCGGVSTTVDPFLDLSLDI---------------------------------------------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 673 vnqrvlgsppvefhcaESSSVPEESAKILiskdvpqnpGGESTTSVTDLLNYFLAPEVLtGENQYYCESCASLQNAEKTM 752
Cdd:cd02660 158 ----------------PNKSTPSWALGES---------GVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQL 211
|
330 340 350
....*....|....*....|....*....|....*...
gi 34784763 753 QITEEPEYLILTLLRFSYDQkYHVRRKILDNVSLPLVL 790
Cdd:cd02660 212 SIKKLPPVLCFQLKRFEHSL-NKTSRKIDTYVQFPLEL 248
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
386-788 |
5.48e-20 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 96.11 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 386 YHYSGFPDLYEPILEAVKDFPKPSEEKIKLILNQSAWTSQSNALASclsRLSGKSETGKTGLINLGNTCYMNSVLQALFM 465
Cdd:COG5560 210 YRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDH---NRSINKEAGTCGLRNLGNTCYMNSALQCLMH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 466 ATEFRRQVLS------LNLNGCNSLMKKLQHLFAFL---AHTQR-EAYAPRIF------FEASrppwFTPRSQQDCSEYL 529
Cdd:COG5560 287 TWELRDYFLSdeyeesINEENPLGMHGSVASAYADLikqLYDGNlHAFTPSGFkktigsFNEE----FSGYDQQDSQEFI 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 530 RFLLDRLHEE-EKILRVQSSHKPS--EGLDcaetclqEVTSKVAVPT--ESPGTGDSektLIEKMFGGKLRTHICCLNCG 604
Cdd:COG5560 363 AFLLDGLHEDlNRIIKKPYTSKPDlsPGDD-------VVVKKKAKECwwEHLKRNDS---IITDLFQGMYKSTLTCPGCG 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 605 STSHKVEAFTDLSL------------AFCP--------------SPSVEDLSFQDTASLP-------------------- 638
Cdd:COG5560 433 SVSITFDPFMDLTLplpvsmvwkhtiVVFPesgrrqplkieldaSSTIRGLKKLVDAEYGklgcfeikvmciyyggnynm 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 639 -SAQDDGLMQ-----------TSVADPEEEPVVYNPATAAFvcdsvVNQRVLGSPPVEFH-------------------- 686
Cdd:COG5560 513 lEPADKVLLQdipqtdfvylyETNDNGIEVPVVHLRIEKGY-----KSKRLFGDPFLQLNvlikasiydklvkefeellv 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 687 ---------CAESSSVP---EESA----------------KILISKDVPQNP---------------------------- 710
Cdd:COG5560 588 lvemkktdvDLVSEQVRllrEESSpsswlkleteidtkreEQVEEEGQMNFNdavvisceweekrylslfsydplwtire 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 711 --GGESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhvRRKILDNVSLPL 788
Cdd:COG5560 668 igAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPI 745
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-792 |
8.55e-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: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFmATEFRRQVLSLNLNGcnslmkklqhLFAFLAHtqreayapriffeasRPPWFTPRSQQDC 525
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSETPKE----------LFSQVCR---------------KAPQFKGYQQQDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 526 SEYLRFLLDRLheeekilrvqsshkpsegldcaetclqevtskvavptespgtgdseKTLIEKMFGGKLRTHICCLNCGS 605
Cdd:cd02667 55 HELLRYLLDGL----------------------------------------------RTFIDSIFGGELTSTIMCESCGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 606 TSHKVEAFTDLSLafcpspsvedlsfqdtaslpsaqddglmqtsvadPEEEPVvynpataafvcdsvvnqrvlgsppvef 685
Cdd:cd02667 89 VSLVYEPFLDLSL----------------------------------PRSDEI--------------------------- 107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 686 hcaesssvpeesakiliskdvpqnpggESTTSVTDLLNYFLAPEVLTGENQYYCESCaslQNAEKTMQITEEPEYLILTL 765
Cdd:cd02667 108 ---------------------------KSECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHL 157
|
330 340
....*....|....*....|....*..
gi 34784763 766 LRFSYDQKyHVRRKILDNVSLPLVLEL 792
Cdd:cd02667 158 KRFQQPRS-ANLRKVSRHVSFPEILDL 183
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
2.24e-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: 85.42 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFmatefrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftpRSQQDC 525
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 526 SEYLRFLLDRLHeeekilrvqsshkpsegldcaetclqevtskvavptespgtgdsekTLIEKMFGGKLRTHICCLNCGS 605
Cdd:cd02674 26 QEFLLFLLDGLH----------------------------------------------SIIVDLFQGQLKSRLTCLTCGK 59
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 606 TSHKVEAFTDLSLAfcpspsvedlsfqdtaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvlgsppvef 685
Cdd:cd02674 60 TSTTFEPFTYLSLP------------------------------------------------------------------ 73
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 686 hcaesssvpeesakiliskdVPQNPGGESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTL 765
Cdd:cd02674 74 --------------------IPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHL 133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 766 LRFSYDQKYhvRRKILDNVSLPLVLELPvkrtasfsslsQSWSVDVDFTDINE-NLPKKLKPSGTEEAfcpklvpyllss 844
Cdd:cd02674 134 KRFSFSRGS--TRKLTTPVTFPLNDLDL-----------TPYVDTRSFTGPFKyDLYAVVNHYGSLNG------------ 188
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 845 vvvhsgvssesGHYYSYARNitgtessyqmcpqseslalapsqscllgvespntvieqdlenkEMSQEWFLFNDSRVTFT 924
Cdd:cd02674 189 -----------GHYTAYCKN-------------------------------------------NETNDWYKFDDSRVTKV 214
|
490 500
....*....|....*....|...
gi 34784763 925 SFQSVQkitsrfpKDTAYVLLYK 947
Cdd:cd02674 215 SESSVV-------SSSAYILFYE 230
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
439-792 |
9.25e-11 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 66.43 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 439 KSETGKTGLINLGNTCYMNSVLQALFMATEFRRQVLSL---NLNGCNSLMKKLQHLFAFLaHTQREayaPRIFFEASRP- 514
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIptdHPRGRDSVALALQRLFYNL-QTGEE---PVDTTELTRSf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 515 PWFTPRS--QQDCSEYLRFLLDRLheeEKILRvqsshkpsegldcaetclqevtskvavptespgtGDSEKTLIEKMFGG 592
Cdd:COG5077 264 GWDSDDSfmQHDIQEFNRVLQDNL---EKSMR----------------------------------GTVVENALNGIFVG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 593 KLRTHICCLNCGSTSHKVEAFTDLSLAFCPSPSVEDlSFQDtaslpsaqddglmqtsvadpeeepvvynpataafvcdsv 672
Cdd:COG5077 307 KMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQE-SFRR--------------------------------------- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 673 vnqrvlgsppvefhcaesssvpeesakiliskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCEScASLQNAEKTM 752
Cdd:COG5077 347 ----------------------------------------------------YIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 34784763 753 QITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL 792
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDL 413
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-541 |
3.67e-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: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNL----------NGCNSLMKKLQHlfAFLAH---------TQREAY--- 503
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfpsdvvdpaNDLNCQLIKLAD--GLLSGryskpaslkSENDPYqvg 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 34784763 504 -APRIF----------FEASRppwftprsQQDCSEYLRFLLDRLHEEEK 541
Cdd:cd02658 79 iKPSMFkaligkghpeFSTMR--------QQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-568 |
5.70e-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: 61.96 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLNG------CNSLMKKLQHLFAFLAHTQrEAYAPRIFFEASRP--PWF 517
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARrganqsSDNLTNALRDLFDTMDKKQ-EPVPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34784763 518 TPRS------QQDCSEYLRFLLDRLHEEEKILRVQSSH-------KPSEGLDCAETCLQEVTSK 568
Cdd:cd02657 80 AEKQnqggyaQQDAEECWSQLLSVLSQKLPGAGSKGSFidqlfgiELETKMKCTESPDEEEVST 143
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-788 |
8.33e-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: 61.45 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLnlngCNSLMKKLQHLFAFLA-----HTQREAYAPRIFFEASRP--PWFT 518
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVEQLQSSFLLnpekyNDELANQAPRRLLNALREvnPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 519 PRSQQDCSEYLRFLLDrlheeekilrvqsshkpsegldcaetCLQEvtskvavptespgtgdsektLIEKMFGGKLRTHI 598
Cdd:cd02671 102 GYLQHDAQEVLQCILG--------------------------NIQE--------------------LVEKDFQGQLVLRT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 599 CCLNCGSTSHKVEAFTDLSLafcPSPSVEDLSFQDTaslpsaqddglmqtsvadpeeepvvynpataafvcdsvvnqrvl 678
Cdd:cd02671 136 RCLECETFTERREDFQDISV---PVQESELSKSEES-------------------------------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 679 gsppvefhcaeSSSVPEESAKILISKDVPQNpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQITEEP 758
Cdd:cd02671 169 -----------SEISPDPKTEMKTLKWAISQ---------------FASVERIVGEDKYFCENCHHYTEAERSLLFDKLP 222
|
330 340 350
....*....|....*....|....*....|
gi 34784763 759 EYLILTLLRFSYDQKYHVRRKILDNVSLPL 788
Cdd:cd02671 223 EVITIHLKCFAANGSEFDCYGGLSKVNTPL 252
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
446-536 |
5.53e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 52.50 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLNGCNSLMKKLQHLFAFLahTQREAYApriFFEASRP-------PWFT 518
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKNVIRKPEPDL--NQEEALK---LFTALWSskehkvgWIPP 75
|
90
....*....|....*...
gi 34784763 519 PRSQQDCSEYLRFLLDRL 536
Cdd:COG5533 76 MGSQEDAHELLGKLLDEL 93
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-555 |
5.99e-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: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34784763 446 GLINLGNTCYMNSVLQAlfmatefrrqvlslnLNGCNSLMKKLQhlfaflahtqreayapriffeasrppWFTprSQQDC 525
Cdd:cd02662 1 GLVNLGNTCFMNSVLQA---------------LASLPSLIEYLE--------------------------EFL--EQQDA 37
|
90 100 110
....*....|....*....|....*....|
gi 34784763 526 SEYLRFLLDRLHeeekilrvQSSHKPSEGL 555
Cdd:cd02662 38 HELFQVLLETLE--------QLLKFPFDGL 59
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-479 |
9.08e-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: 9.08e-06
10 20 30
....*....|....*....|....*....|....*
gi 34784763 445 TGLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN 479
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDES 36
|
|
| |
