|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-946 |
1.58e-146 |
|
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: 440.00 E-value: 1.58e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNL---NGCNSLMKKLQHLFAFLAHTQREAYAPRI-FFEASRPPWFTPRS 521
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLprlGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 522 QQDCSEYLRFLLDRLHeeekilriqsshkpseglgctetclqevtnkvavpsespstggsekTLIEKMFGGKLRTHICCL 601
Cdd:cd02664 81 QQDCSEYLRYLLDRLH----------------------------------------------TLIEKMFGGKLSTTIRCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 602 NCRSTSHKVEAFTDLSLAFCpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsp 681
Cdd:cd02664 115 NCNSTSARTERFRDLDLSFP------------------------------------------------------------ 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 682 pvefpcaknssvpgesakilvskdvpqnpggesttSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYL 761
Cdd:cd02664 135 -----------------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 762 ILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRTSLSSLSEGwsadadftdvnenlAKKLKPSGTEEAFCPKLVPYLL 841
Cdd:cd02664 180 ILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKSSESPL--------------EKKEEESGDDGELVTRQVHYRL 245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 842 SSVVVHSGVSSESGHYYSYARNITGTESSYQMRPQseslsltpsqssllggespntviEQDLENKEMSQEWFLFNDSRVT 921
Cdd:cd02664 246 YAVVVHSGYSSESGHYFTYARDQTDADSTGQECPE-----------------------PKDAEENDESKNWYLFNDSRVT 302
|
490 500
....*....|....*....|....*
gi 1716952116 922 FTSFQSVQKITSRFPKDTAYVLFYK 946
Cdd:cd02664 303 FSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
445-945 |
8.44e-38 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 144.12 E-value: 8.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 445 TGLINLGNTCYMNSVLQALFMATEFRRQVLSL-------NLNGCNSLMKKLQHLF-AFLAHTQREAYAPRIFFEA--SRP 514
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 515 PWFTPRSQQDCSEYLRFLLDRLHEEekilriqsshkpSEGLGCTEtclqevtnkvavpsespstggsEKTLIEKMFGGKL 594
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHED------------LNGNHSTE----------------------NESLITDLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 595 RTHICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSSFQDPASLPsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvn 674
Cdd:pfam00443 127 KSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQ------------------------------------ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 675 errlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQI 754
Cdd:pfam00443 171 --------------------------------------------------FSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 755 TEEPEYLILTLLRFSYDQKyhVRRKILDNVSLPLVLelpvkrtSLSSLSEgwsadadfTDVNENLAKKLK--------PS 826
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLEL-------DLSRYLA--------EELKPKTNNLQDyrlvavvvHS 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 827 GTEEafcpklvpyllssvvvhsgvsseSGHYYSYARNitgtessyqmrpqseslsltpsqssllggespntvieqdlenk 906
Cdd:pfam00443 264 GSLS-----------------------SGHYIAYIKA------------------------------------------- 277
|
490 500 510
....*....|....*....|....*....|....*....
gi 1716952116 907 EMSQEWFLFNDSRVTFTSFQSVQKitsrfpKDTAYVLFY 945
Cdd:pfam00443 278 YENNRWYKFDDEKVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
446-946 |
1.05e-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: 139.16 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMatefrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftprSQQDC 525
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 526 SEYLRFLLDRLHEEEKILRIQSSHKPSEglgctetclqevtnkvavpsespstggseKTLIEKMFGGKLRTHICCLNCRS 605
Cdd:cd02257 26 HEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------------------KSLIHDLFGGKLESTIVCLECGH 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 606 TSHKVEAFTDLSLafcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvef 685
Cdd:cd02257 77 ESVSTEPELFLSL------------------------------------------------------------------- 89
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 686 pcaknssvpgesakilvskDVPQNPGGESttSVTDLLNYFLAPEVLTGENQYYCESCaSLQNAEKTMQITEEPEYLILTL 765
Cdd:cd02257 90 -------------------PLPVKGLPQV--SLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHL 147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 766 LRFSYDQKYhVRRKILDNVSLPLVLelpvkrtslsslsegwsadadftdvneNLAKKLKPSGTEEAFCPKLVPYLLSSVV 845
Cdd:cd02257 148 KRFSFNEDG-TKEKLNTKVSFPLEL---------------------------DLSPYLSEGEKDSDSDNGSYKYELVAVV 199
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 846 VHSGVSSESGHYYSYARNITgtessyqmrpqseslsltpsqssllggespntvieqdlenkemSQEWFLFNDSRVTFTSF 925
Cdd:cd02257 200 VHSGTSADSGHYVAYVKDPS-------------------------------------------DGKWYKFNDDKVTEVSE 236
|
490 500
....*....|....*....|.
gi 1716952116 926 QSVQKITSRfpKDTAYVLFYK 946
Cdd:cd02257 237 EEVLEFGSL--SSSAYILFYE 255
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-950 |
9.89e-35 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 135.85 E-value: 9.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 443 GKTGLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN----GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEASRPPWFT 518
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 519 --PRSQQDCSEYLRFLLDRLheEEKilriqsshkpseglgctetclqevtnkvavpseSPSTGgsEKTLIEKMFGGKLRT 596
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKL--EEK---------------------------------LKGTG--QEGLIKNLFGGKLVN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 597 HICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSsFQDpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvner 676
Cdd:cd02659 124 YIICKECPHESEREEYFLDLQVAVKGKKNLEES-LDA------------------------------------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 677 rlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKTMQITE 756
Cdd:cd02659 160 ------------------------------------------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 757 EPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL-PVKRTSLSSLSEGWSADADFTDVNEnLAKKLKPSGTEEAfcpk 835
Cdd:cd02659 192 LPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMePYTEKGLAKKEGDSEKKDSESYIYE-LHGVLVHSGDAHG---- 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 836 lvpyllssvvvhsgvssesGHYYSYARNITgtessyqmrpqseslsltpsqssllggespntvieqdlenkemSQEWFLF 915
Cdd:cd02659 267 -------------------GHYYSYIKDRD-------------------------------------------DGKWYKF 284
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1716952116 916 NDSRVTFTSFQSV--------------QKITSRFPKDT-AYVLFYKKQSR 950
Cdd:cd02659 285 NDDVVTPFDPNDAeeecfggeetqktyDSGPRAFKRTTnAYMLFYERKSP 334
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-945 |
1.14e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 114.30 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 445 TGLINLGNTCYMNSVLQALFMATEFRRQVLSLN--LNGCNSLMKKL----QHLFAFLAHTqREAYAPRIFFEASRPPW-- 516
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREhsKDCCNEGFCMMcaleAHVERALASS-GPGSAPRIFSSNLKQISkh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 517 FTPRSQQDCSEYLRFLLDRLHEeekilriqsshkpseglgcteTCLQEVTNKVAVPSESPSTggsekTLIEKMFGGKLRT 596
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQK---------------------ACLDRFKKLKAVDPSSQET-----TLVQQIFGGYLRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 597 HICCLNCRSTSHKVEAFTDLSLAFCPSPSVEDSsfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvner 676
Cdd:cd02661 135 QVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDA----------------------------------------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 677 rlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdlLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITE 756
Cdd:cd02661 168 ---------------------------------------------LEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHR 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 757 EPEYLILTLLRFSYDQkyhvRRKILDNVSLPLVLELpvkRTSLSSLSEGwsadadftdvnenlakklkpsgteeafcpkL 836
Cdd:cd02661 203 APNVLTIHLKRFSNFR----GGKINKQISFPETLDL---SPYMSQPNDG------------------------------P 245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 837 VPYLLSSVVVHSGVSSESGHYYSYARNITGTessyqmrpqseslsltpsqssllggespntvieqdlenkemsqeWFLFN 916
Cdd:cd02661 246 LKYKLYAVLVHSGFSPHSGHYYCYVKSSNGK--------------------------------------------WYNMD 281
|
490 500
....*....|....*....|....*....
gi 1716952116 917 DSRVTFTSFQSVQkitsrfpKDTAYVLFY 945
Cdd:cd02661 282 DSKVSPVSIETVL-------SQKAYILFY 303
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-792 |
2.82e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 107.89 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN--------------GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEA 511
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTedaelknmppdkphEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 512 SRppwFTPRSQQDCSEYLRFLLDRLheeekilriqsshkpseglgctETCLQEVTNKVAvpsespstggseKTLIEKMFG 591
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLL----------------------EAKLSKSKNPDL------------KNIVQDLFR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 592 GKLRTHICCLNCRSTSHKVEAFTDLSLafcpspsvedsSFQDPASLPSAQDDglmqtsvtdaeeepvvcnpaaaafvcds 671
Cdd:cd02668 124 GEYSYVTQCSKCGRESSLPSKFYELEL-----------QLKGHKTLEECIDE---------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 672 vvnerrlgsppvefpcaknssvpgesakilvskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCESCASLQNAEKT 751
Cdd:cd02668 165 -----------------------------------------------------FLKEEQLTGDNQYFCESCNSKTDATRR 191
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1716952116 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 |
3.03e-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: 107.40 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATefrrqvlslnlngcnsLMKKLQHLFAFLAHTQRE--AYAPRIFFEASRP--PWFTPRS 521
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 522 QQDCSEYLRFLLDRLHEeekilriqsshkpseglgctetCLQEVTNKVAVPSESPSTGGSE--KTLIEKMFGGKLRTHIC 599
Cdd:cd02663 65 HQDAHEFLNFLLNEIAE----------------------ILDAERKAEKANRKLNNNNNAEpqPTWVHEIFQGILTNETR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 600 CLNCRSTSHKVEAFTDLSLafcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlg 679
Cdd:cd02663 123 CLTCETVSSRDETFLDLSI------------------------------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 680 sppvefpcaknssvpgesakilvskDVPQNpggestTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPE 759
Cdd:cd02663 142 -------------------------DVEQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPK 190
|
330 340 350
....*....|....*....|....*....|....
gi 1716952116 760 YLILTLLRFSYDQKYHVRRKILDNVSLPLVLELP 793
Cdd:cd02663 191 ILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF 224
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-946 |
4.64e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 98.60 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLS--LNLNGC-----NSLMKKLQHLFA-FLAHTQREAYAPRIFFEASrppWF 517
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrHSCTCLscspnSCLSCAMDEIFQeFYYSGDRSPYGPINLLYLS---WK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 518 TPR-----SQQDCSEYLRFLLDRLHEEEKILRIQSSHKPSeglgCTetCLqevtnkvavpsespstggsektlIEKMFGG 592
Cdd:cd02660 79 HSRnlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CN--CI-----------------------IHQTFSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 593 KLRTHICCLNCRSTSHKVEAFTDLSLAFcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsv 672
Cdd:cd02660 130 SLQSSVTCQRCGGVSTTVDPFLDLSLDI---------------------------------------------------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 673 vnerrlgsppvefpcaKNSSVPGESAKILvskdvpqnpGGESTTSVTDLLNYFLAPEVLtGENQYYCESCASLQNAEKTM 752
Cdd:cd02660 158 ----------------PNKSTPSWALGES---------GVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 753 QITEEPEYLILTLLRFSYDQkYHVRRKILDNVSLPLVLELpvkrTSLSSLSEGWSADADFtdvnenlakkLKPSGTEEAF 832
Cdd:cd02660 212 SIKKLPPVLCFQLKRFEHSL-NKTSRKIDTYVQFPLELNM----TPYTSSSIGDTQDSNS----------LDPDYTYDLF 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 833 cpKLVPYllssvvvhsGVSSESGHYYSYARNITGtessyqmrpqseslsltpsqssllggespntvieqdlenkemsqEW 912
Cdd:cd02660 277 --AVVVH---------KGTLDTGHYTAYCRQGDG--------------------------------------------QW 301
|
490 500 510
....*....|....*....|....*....|....
gi 1716952116 913 FLFNDSRVTFTSFQSVQKitSRfpkdtAYVLFYK 946
Cdd:cd02660 302 FKFDDAMITRVSEEEVLK--SQ-----AYLLFYH 328
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-946 |
3.79e-20 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 90.42 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFmatefrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftpRSQQDC 525
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 526 SEYLRFLLDRLHeeekilriqsshkpseglgctetclqevtnkvavpsespstggsekTLIEKMFGGKLRTHICCLNCRS 605
Cdd:cd02674 26 QEFLLFLLDGLH----------------------------------------------SIIVDLFQGQLKSRLTCLTCGK 59
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 606 TSHKVEAFTDLSLAfcpspsvedssfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvef 685
Cdd:cd02674 60 TSTTFEPFTYLSLP------------------------------------------------------------------ 73
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 686 pcaknssvpgesakilvskdVPQNPGGESTTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTL 765
Cdd:cd02674 74 --------------------IPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHL 133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 766 LRFSYDQKYhvRRKILDNVSLPLvlelpvkrtSLSSLSEgWSADADFTDVNE-NLAKKLKPSGTEEAfcpklvpyllssv 844
Cdd:cd02674 134 KRFSFSRGS--TRKLTTPVTFPL---------NDLDLTP-YVDTRSFTGPFKyDLYAVVNHYGSLNG------------- 188
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 845 vvhsgvssesGHYYSYARNitgtessyqmrpqseslsltpsqssllggespntvieqdlenkEMSQEWFLFNDSRVTFTS 924
Cdd:cd02674 189 ----------GHYTAYCKN-------------------------------------------NETNDWYKFDDSRVTKVS 215
|
490 500
....*....|....*....|..
gi 1716952116 925 FQSVQkitsrfpKDTAYVLFYK 946
Cdd:cd02674 216 ESSVV-------SSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-945 |
1.39e-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: 90.14 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFmATEFRRQVLSLNLNGcnslmkklqhLFAFLAHtqreayapriffeasRPPWFTPRSQQDC 525
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSETPKE----------LFSQVCR---------------KAPQFKGYQQQDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 526 SEYLRFLLDRLheeekilriqsshkpseglgctetclqevtnkvavpsespstggseKTLIEKMFGGKLRTHICCLNCRS 605
Cdd:cd02667 55 HELLRYLLDGL----------------------------------------------RTFIDSIFGGELTSTIMCESCGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 606 TSHKVEAFTDLSLafcpsPSVEDSsfqdpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvef 685
Cdd:cd02667 89 VSLVYEPFLDLSL-----PRSDEI-------------------------------------------------------- 107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 686 pcaknssvpgesakilvskdvpqnpggESTTSVTDLLNYFLAPEVLTGENQYYCESCaslQNAEKTMQITEEPEYLILTL 765
Cdd:cd02667 108 ---------------------------KSECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHL 157
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 766 LRFSYDQKyHVRRKILDNVSLPLVLELpvkrtslsslsegwsadADFTDVNENLAKklkpsgTEEAFCPKLVPYLlssvv 845
Cdd:cd02667 158 KRFQQPRS-ANLRKVSRHVSFPEILDL-----------------APFCDPKCNSSE------DKSSVLYRLYGVV----- 208
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 846 vHSGVSSESGHYYSYARnitgtessyqMRPQSESLSLTPSQSsllggespntviEQDLENKEMSQEWFLFNDSRVtftsf 925
Cdd:cd02667 209 -EHSGTMRSGHYVAYVK----------VRPPQQRLSDLTKSK------------PAADEAGPGSGQWYYISDSDV----- 260
|
490 500
....*....|....*....|
gi 1716952116 926 QSVQkiTSRFPKDTAYVLFY 945
Cdd:cd02667 261 REVS--LEEVLKSEAYLLFY 278
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
386-949 |
9.60e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 88.79 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 386 YHYSGFPDLYEPILEAVKDFPKPTEEKIKLILNQSAWTSQSNALASclsRLSGKSETGKTGLINLGNTCYMNSVLQALFM 465
Cdd:COG5560 210 YRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDH---NRSINKEAGTCGLRNLGNTCYMNSALQCLMH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 466 ATEFRRQVLS------LNLNGCNSLMKKLQHLFAFL---AHTQR-EAYAPRIF------FEASrppwFTPRSQQDCSEYL 529
Cdd:COG5560 287 TWELRDYFLSdeyeesINEENPLGMHGSVASAYADLikqLYDGNlHAFTPSGFkktigsFNEE----FSGYDQQDSQEFI 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 530 RFLLDRLHEE-EKILRIQSSHKPSEGLGctetcLQEVTNKVAVPSESPSTGGSEkTLIEKMFGGKLRTHICCLNCRSTSH 608
Cdd:COG5560 363 AFLLDGLHEDlNRIIKKPYTSKPDLSPG-----DDVVVKKKAKECWWEHLKRND-SIITDLFQGMYKSTLTCPGCGSVSI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 609 KVEAFTDLSLafcPSPS----------VEDSSFQDP----ASLPS------------AQDDGLMQTSVTD---------- 652
Cdd:COG5560 437 TFDPFMDLTL---PLPVsmvwkhtivvFPESGRRQPlkieLDASStirglkklvdaeYGKLGCFEIKVMCiyyggnynml 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 653 ----------------------AEEEPVVC-----------------------NPAAAAFVCDSVVNE-----RRLGSPP 682
Cdd:COG5560 514 epadkvllqdipqtdfvylyetNDNGIEVPvvhlriekgykskrlfgdpflqlNVLIKASIYDKLVKEfeellVLVEMKK 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 683 V-------EFPCAKNSSVPGESAKILVSKDVPQ---------------------------------NPGG--------ES 714
Cdd:COG5560 594 TdvdlvseQVRLLREESSPSSWLKLETEIDTKReeqveeegqmnfndavvisceweekrylslfsyDPLWtireigaaER 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 715 TTSVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhvRRKILDNVSLPLvlelpv 794
Cdd:COG5560 674 TITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPI------ 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 795 krtslsslsegwsadadftdvnenlaKKLKPSGTEEAFCPKLVPYLLsSVVVHSGVSSESGHYYSYARNITgtessyqmr 874
Cdd:COG5560 746 --------------------------DDLDLSGVEYMVDDPRLIYDL-YAVDNHYGGLSGGHYTAYARNFA--------- 789
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1716952116 875 pqseslsltpsqssllggespntvieqdlenkemSQEWFLFNDSRVTFTSfqSVQKITSrfpkdTAYVLFYKKQS 949
Cdd:COG5560 790 ----------------------------------NNGWYLFDDSRITEVD--PEDSVTS-----SAYVLFYRRKS 823
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
390-792 |
1.15e-10 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 66.05 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 390 GFPDLYEP--ILEAVKDFPKPTEEKIKLI-LNQSAWTSQSNALASCLSRLSGKSETGKTGLINLGNTCYMNSVLQALFMA 466
Cdd:COG5077 136 GFTNFIDLnkLIEPSPGRPPFLEEGTLVItVYVRVLKDPTGVLWHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 467 TEFRRQVLSL---NLNGCNSLMKKLQHLFAFLaHTQREayaPRIFFEASRP-PWFTPRS--QQDCSEYLRFLLDRLheeE 540
Cdd:COG5077 216 AKFRKDVYGIptdHPRGRDSVALALQRLFYNL-QTGEE---PVDTTELTRSfGWDSDDSfmQHDIQEFNRVLQDNL---E 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 541 KILRiqsshkpseglgctetclqevtnkvavpsespstggseKTLIEKM----FGGKLRTHICCLNCRSTSHKVEAFTDL 616
Cdd:COG5077 289 KSMR--------------------------------------GTVVENAlngiFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 617 SLAFCPSPSVEDsSFQDpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrlgsppvefpcaknssvpge 696
Cdd:COG5077 331 QLNVKGMKNLQE-SFRR--------------------------------------------------------------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 697 sakilvskdvpqnpggesttsvtdllnyFLAPEVLTGENQYYCEScASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHV 776
Cdd:COG5077 347 ----------------------------YIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDM 397
|
410
....*....|....*.
gi 1716952116 777 RRKILDNVSLPLVLEL 792
Cdd:COG5077 398 MVKINDRYEFPLEIDL 413
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-541 |
3.26e-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: 62.73 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNL----------NGCNSLMKKLQHlfAFLAH---------TQREAY--- 503
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfpsdvvdpaNDLNCQLIKLAD--GLLSGryskpaslkSENDPYqvg 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1716952116 504 -APRIF----------FEASRppwftprsQQDCSEYLRFLLDRLHEEEK 541
Cdd:cd02658 79 iKPSMFkaligkghpeFSTMR--------QQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-788 |
9.69e-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: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLnlngCNSLMKKLQHLFAFLA-----HTQREAYAPRIFFEASRP--PWFT 518
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVEQLQSSFLLnpekyNDELANQAPRRLLNALREvnPMYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 519 PRSQQDCSEYLRFLLDrlheeekilriqsshkpseglgctetCLQEvtnkvavpsespstggsektLIEKMFGGKLRTHI 598
Cdd:cd02671 102 GYLQHDAQEVLQCILG--------------------------NIQE--------------------LVEKDFQGQLVLRT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 599 CCLNCRSTSHKVEAFTDLSLafcPSPSVEDSSFQDpaslpsaqddglmqtsvtdaeeepvvcnpaaaafvcdsvvnerrl 678
Cdd:cd02671 136 RCLECETFTERREDFQDISV---PVQESELSKSEE--------------------------------------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 679 gsppvefpcaknssvpgesakilvSKDVPQNPGGESTTsVTDLLNYFLAPEVLTGENQYYCESCASLQNAEKTMQITEEP 758
Cdd:cd02671 168 ------------------------SSEISPDPKTEMKT-LKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLP 222
|
330 340 350
....*....|....*....|....*....|
gi 1716952116 759 EYLILTLLRFSYDQKYHVRRKILDNVSLPL 788
Cdd:cd02671 223 EVITIHLKCFAANGSEFDCYGGLSKVNTPL 252
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-568 |
1.42e-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: 60.42 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLNG------CNSLMKKLQHLFAFLAHTQrEAYAPRIFFEASRP--PWF 517
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARrganqsSDNLTNALRDLFDTMDKKQ-EPVPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1716952116 518 TPRS------QQDCSEYLRFLLDRLHEE-----------EKILRIQSSHKpsegLGCTETCLQEVTNK 568
Cdd:cd02657 80 AEKQnqggyaQQDAEECWSQLLSVLSQKlpgagskgsfiDQLFGIELETK----MKCTESPDEEEVST 143
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
446-536 |
5.52e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 52.50 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQALFMATEFRRQVLSLNLNGCNSLMKKLQHLFAFLahTQREAYApriFFEASRP-------PWFT 518
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKNVIRKPEPDL--NQEEALK---LFTALWSskehkvgWIPP 75
|
90
....*....|....*...
gi 1716952116 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 |
6.74e-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: 48.52 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1716952116 446 GLINLGNTCYMNSVLQAlfmatefrrqvlslnLNGCNSLMKKLQhlfaflahtqreayapriffeasrppWFTprSQQDC 525
Cdd:cd02662 1 GLVNLGNTCFMNSVLQA---------------LASLPSLIEYLE--------------------------EFL--EQQDA 37
|
90 100 110
....*....|....*....|....*....|
gi 1716952116 526 SEYLRFLLDRLHeeekilriQSSHKPSEGL 555
Cdd:cd02662 38 HELFQVLLETLE--------QLLKFPFDGL 59
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-479 |
8.61e-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: 8.61e-06
10 20 30
....*....|....*....|....*....|....*
gi 1716952116 445 TGLINLGNTCYMNSVLQALFMATEFRRQVLSLNLN 479
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDES 36
|
|
| |
