|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
1.53e-161 |
|
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: 478.91 E-value: 1.53e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATDFRRQVLSLNL---NGCNSLMKKLQHLFAFLAHTQREAYAPRI-FFEASRPPWFTPRS 521
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLprlGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyFLEASRPPWFTPGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 522 QQDCSEYLRFLLDRLHeeekilkvqashkpseilecsetslqevaskaavltetprtsdgekTLIEKMFGGKLRTHIRCL 601
Cdd:cd02664 81 QQDCSEYLRYLLDRLH----------------------------------------------TLIEKMFGGKLSTTIRCL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 602 NCRSTSQKVEAFTDLSLAFcpssslenmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficdslvnektigsp 681
Cdd:cd02664 115 NCNSTSARTERFRDLDLSF------------------------------------------------------------- 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 682 pnefycsentsvpnesnkilvnkdvpqkpggettPSVTDLLNYFLAPEILTGDNQYYCENCASLQNAEKTMQITEEPEYL 761
Cdd:cd02664 134 ----------------------------------PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYL 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 762 ILTLLRFSYDQKYHVRRKILDNVSLPLVLELPVKRITSFSslseswsvdvdftdlSENLAKKLKPSGTDEASCTKLVPYL 841
Cdd:cd02664 180 ILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKSS---------------ESPLEKKEEESGDDGELVTRQVHYR 244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 842 LSSVVVHSGISSESGHYYSYARNITSTDSSYQMYHqsealalassqshllgrdspsavFEQDLENKEMSKEWFLFNDSRV 921
Cdd:cd02664 245 LYAVVVHSGYSSESGHYFTYARDQTDADSTGQECP-----------------------EPKDAEENDESKNWYLFNDSRV 301
|
490 500
....*....|....*....|....*.
gi 193785252 922 TFTSFQSVQKITSRFPKDTAYVLLYK 947
Cdd:cd02664 302 TFSSFESVQNVTSRFPKDTPYILFYE 327
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
445-946 |
1.22e-47 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 172.63 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 445 TGLINLGNTCYMNSVIQALFMATDFRRQVLSL-------NLNGCNSLMKKLQHLF-AFLAHTQREAYAPRIFFEA--SRP 514
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRIsplsedsRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSlgKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 515 PWFTPRSQQDCSEYLRFLLDRLHEEEKilkvqashkpseilecsetslqevaskaavltetPRTSDGEKTLIEKMFGGKL 594
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------GNHSTENESLITDLFRGQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 595 RTHIRCLNCRSTSQKVEAFTDLSLAFCPSSSLenmsvqdpasspsiqdgglmqasvpgpseepvvyNPTTAAFICDSLvn 674
Cdd:pfam00443 127 KSRLKCLSCGEVSETFEPFSDLSLPIPGDSAE----------------------------------LKTASLQICFLQ-- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 675 ektigsppnefycsentsvpnesnkilvnkdvpqkpggettpsvtdllnyFLAPEILTGDNQYYCENCASLQNAEKTMQI 754
Cdd:pfam00443 171 --------------------------------------------------FSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 755 TEEPEYLILTLLRFSYDQKyhVRRKILDNVSLPLVLelpvkritsfsslseswsvdvdftDLSENLAKKLKPSGTDeasc 834
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYNRS--TWEKLNTEVEFPLEL------------------------DLSRYLAEELKPKTNN---- 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 835 tkLVPYLLSSVVVHSGiSSESGHYYSYARNitstdssyqmyhqsealalassqshllgrdspsavfeqdlenkEMSKEWF 914
Cdd:pfam00443 251 --LQDYRLVAVVVHSG-SLSSGHYIAYIKA-------------------------------------------YENNRWY 284
|
490 500 510
....*....|....*....|....*....|..
gi 193785252 915 LFNDSRVTFTSFQSVQKitsrfpKDTAYVLLY 946
Cdd:pfam00443 285 KFDDEKVTEVDEETAVL------SSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
446-947 |
9.56e-47 |
|
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: 168.05 E-value: 9.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMatdfrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftprSQQDC 525
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS-------------------------------------------------------EQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 526 SEYLRFLLDRLHEEEKILKVQASHKPSEilecsetslqevaskaavltetprtsdgeKTLIEKMFGGKLRTHIRCLNCRS 605
Cdd:cd02257 26 HEFLLFLLDKLHEELKKSSKRTSDSSSL-----------------------------KSLIHDLFGGKLESTIVCLECGH 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 606 TSQKVEAFTDLSLafcpssslenmsvqdpasspsiqdgglmqaSVPGPSEEPVvynpttaaficdslvnektigsppnef 685
Cdd:cd02257 77 ESVSTEPELFLSL------------------------------PLPVKGLPQV--------------------------- 99
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 686 ycsentsvpnesnkilvnkdvpqkpggettpSVTDLLNYFLAPEILTGDNQYYCENCaSLQNAEKTMQITEEPEYLILTL 765
Cdd:cd02257 100 -------------------------------SLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHL 147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 766 LRFSYDQKYhVRRKILDNVSLPLVLelpvkritsfsslseswsvdvdftDLSENLAKKLKPSGTDEASCTklvpYLLSSV 845
Cdd:cd02257 148 KRFSFNEDG-TKEKLNTKVSFPLEL------------------------DLSPYLSEGEKDSDSDNGSYK----YELVAV 198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 846 VVHSGISSESGHYYSYARNITstdssyqmyhqsealalassqshllgrdspsavfeqdlenkemSKEWFLFNDSRVTFTS 925
Cdd:cd02257 199 VVHSGTSADSGHYVAYVKDPS-------------------------------------------DGKWYKFNDDKVTEVS 235
|
490 500
....*....|....*....|..
gi 193785252 926 FQSVQKITSRfpKDTAYVLLYK 947
Cdd:cd02257 236 EEEVLEFGSL--SSSAYILFYE 255
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
443-949 |
2.33e-42 |
|
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: 158.19 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 443 GKTGLINLGNTCYMNSVIQALFMATDFRRQVLSLNLN----GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEASRPPWFT 518
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTedddDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 519 --PRSQQDCSEYLRFLLDRLheEEKilkvqashkpseilecsetslqevaSKAAvltetprtsdGEKTLIEKMFGGKLRT 596
Cdd:cd02659 81 lnTFEQHDVQEFFRVLFDKL--EEK-------------------------LKGT----------GQEGLIKNLFGGKLVN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 597 HIRCLNCRSTSQKVEAFTDLSLAFCPSSSLEnmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficDSLVNek 676
Cdd:cd02659 124 YIICKECPHESEREEYFLDLQVAVKGKKNLE------------------------------------------ESLDA-- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 677 tigsppnefycsentsvpnesnkilvnkdvpqkpggettpsvtdllnyFLAPEILTGDNQYYCENCASLQNAEKTMQITE 756
Cdd:cd02659 160 ------------------------------------------------YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 757 EPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLEL-PvkritsfsslseswsvdvdFTDlsENLAKKLKPSGTDEASCT 835
Cdd:cd02659 192 LPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMeP-------------------YTE--KGLAKKEGDSEKKDSESY 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 836 KlvpYLLSSVVVHSGISSeSGHYYSYARNITStdssyqmyhqsealalassqshllGRdspsavfeqdlenkemskeWFL 915
Cdd:cd02659 251 I---YELHGVLVHSGDAH-GGHYYSYIKDRDD------------------------GK-------------------WYK 283
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 193785252 916 FNDSRVTFTSFQSV--------------QKITSRFPKDT-AYVLLYKKQ 949
Cdd:cd02659 284 FNDDVVTPFDPNDAeeecfggeetqktyDSGPRAFKRTTnAYMLFYERK 332
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-946 |
7.12e-34 |
|
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: 132.40 E-value: 7.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 445 TGLINLGNTCYMNSVIQALFMATDFRRQVLSLN--LNGCNSLMKKL----QHLFAFLAHTqREAYAPRIFFEASRPPW-- 516
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREhsKDCCNEGFCMMcaleAHVERALASS-GPGSAPRIFSSNLKQISkh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 517 FTPRSQQDCSEYLRFLLDRLHEeekilkvqashkpseilecseTSLQEvaskaAVLTETPRTSDGEKTLIEKMFGGKLRT 596
Cdd:cd02661 81 FRIGRQEDAHEFLRYLLDAMQK---------------------ACLDR-----FKKLKAVDPSSQETTLVQQIFGGYLRS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 597 HIRCLNCRSTSQKVEAFTDLSLAFCPSSSLENMsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficdslvnek 676
Cdd:cd02661 135 QVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDA----------------------------------------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 677 tigsppnefycsentsvpnesnkilvnkdvpqkpggettpsvtdlLNYFLAPEILTGDNQYYCENCASLQNAEKTMQITE 756
Cdd:cd02661 168 ---------------------------------------------LEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHR 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 757 EPEYLILTLLRFSYDQkyhvRRKILDNVSLPLVLelpvkritsfsslseswsvdvdftDLSENLAKKLKPSgtdeasctk 836
Cdd:cd02661 203 APNVLTIHLKRFSNFR----GGKINKQISFPETL------------------------DLSPYMSQPNDGP--------- 245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 837 lVPYLLSSVVVHSGISSESGHYYSYArnitstdssyqmyhqsealalassqshllgrdspsavfeqdlenKEMSKEWFLF 916
Cdd:cd02661 246 -LKYKLYAVLVHSGFSPHSGHYYCYV--------------------------------------------KSSNGKWYNM 280
|
490 500 510
....*....|....*....|....*....|
gi 193785252 917 NDSRVTFTSFQSVQkitsrfpKDTAYVLLY 946
Cdd:cd02661 281 DDSKVSPVSIETVL-------SQKAYILFY 303
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
7.93e-29 |
|
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: 117.80 E-value: 7.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATdfrrqvlslnlngcnsLMKKLQHLFAFLAHTQRE--AYAPRIFFEASRP--PWFTPRS 521
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFEN----------------LLTCLKDLFESISEQKKRtgVISPKKFITRLKRenELFDNYM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 522 QQDCSEYLRFLLDRLheeekilkvqashkpSEILECSETSLQEVASKAAVLTETPrtsdgEKTLIEKMFGGKLRTHIRCL 601
Cdd:cd02663 65 HQDAHEFLNFLLNEI---------------AEILDAERKAEKANRKLNNNNNAEP-----QPTWVHEIFQGILTNETRCL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 602 NCRSTSQKVEAFTDLSLafcpssslenmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficdslvnektigsp 681
Cdd:cd02663 125 TCETVSSRDETFLDLSI--------------------------------------------------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 682 pnefycsentsvpnesnkilvnkDVPQKPggettpSVTDLLNYFLAPEILTGDNQYYCENCASLQNAEKTMQITEEPEYL 761
Cdd:cd02663 142 -----------------------DVEQNT------SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKIL 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 762 ILTLLRFSYDQKYHVRRKILDNVSLPLVLELPvkritsfsslseswsvdvDFTDLSENLAKKlkpsgtdeasctklvpYL 841
Cdd:cd02663 193 ALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF------------------NTTDDAENPDRL----------------YE 238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 842 LSSVVVHSGISSESGHYYSyarnitstdssyqmyhqsealaLASSQSHllgrdspsavfeqdlenkemskeWFLFNDSRV 921
Cdd:cd02663 239 LVAVVVHIGGGPNHGHYVS----------------------IVKSHGG-----------------------WLLFDDETV 273
|
490 500
....*....|....*....|....*..
gi 193785252 922 TFTSFQSVQKITSRFP-KDTAYVLLYK 947
Cdd:cd02663 274 EKIDENAVEEFFGDSPnQATAYVLFYQ 300
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
2.29e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 117.09 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATDFRRQVLS--LNLNGC-----NSLMKKLQHLFA-FLAHTQREAYAPRIFFEASrppWF 517
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrHSCTCLscspnSCLSCAMDEIFQeFYYSGDRSPYGPINLLYLS---WK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 518 TPR-----SQQDCSEYLRFLLDRLHEEEKILKVQASHKPSeileCsetslqevaskaavltetprtsdgeKTLIEKMFGG 592
Cdd:cd02660 79 HSRnlagySQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----C-------------------------NCIIHQTFSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 593 KLRTHIRCLNCRSTSQKVEAFTDLSLafcpssSLENMSVQDPASSPSiqdgglmqasvpgpseepvvynpttaaficdsl 672
Cdd:cd02660 130 SLQSSVTCQRCGGVSTTVDPFLDLSL------DIPNKSTPSWALGES--------------------------------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 673 vnektigsppnefycsentsvpnesnkilvnkdvpqkpGGETTPSVTDLLNYFLAPEILtGDNQYYCENCASLQNAEKTM 752
Cdd:cd02660 171 --------------------------------------GVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQL 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 753 QITEEPEYLILTLLRFSYDQkYHVRRKILDNVSLPLVLelpvkritsfsslseswsvdvDFTDLSENLAKKLKPSGTDEA 832
Cdd:cd02660 212 SIKKLPPVLCFQLKRFEHSL-NKTSRKIDTYVQFPLEL---------------------NMTPYTSSSIGDTQDSNSLDP 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 833 SCTklvpYLLSSVVVHSGiSSESGHYYSYARNitstdssyqmyhqsealalassqshllGRDspsavfeqdlenkemskE 912
Cdd:cd02660 270 DYT----YDLFAVVVHKG-TLDTGHYTAYCRQ---------------------------GDG-----------------Q 300
|
490 500 510
....*....|....*....|....*....|....*
gi 193785252 913 WFLFNDSRVTFTSFQSVQKitSRfpkdtAYVLLYK 947
Cdd:cd02660 301 WFKFDDAMITRVSEEEVLK--SQ-----AYLLFYH 328
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
2.13e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 105.83 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFmatdfrrqvlslnlngcnslmkklqhlfaflahtqreayapriffeasrppwftpRSQQDC 525
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS-------------------------------------------------------ADQQDA 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 526 SEYLRFLLDRLHeeekilkvqashkpseilecsetslqevaskaavltetprtsdgekTLIEKMFGGKLRTHIRCLNCRS 605
Cdd:cd02674 26 QEFLLFLLDGLH----------------------------------------------SIIVDLFQGQLKSRLTCLTCGK 59
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 606 TSQKVEAFTDLSLAfcpssslenmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficdslvnektigsppnef 685
Cdd:cd02674 60 TSTTFEPFTYLSLP------------------------------------------------------------------ 73
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 686 ycsentsvpnesnkilvnkdVPQKPGGETTPSVTDLLNYFLAPEILTGDNQYYCENCASLQNAEKTMQITEEPEYLILTL 765
Cdd:cd02674 74 --------------------IPSGSGDAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHL 133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 766 LRFSYDQKYhvRRKILDNVSLPLvlelpvkritsfsslseswsVDVDFTDLSenlakklkpsgtDEASCTKLVPYLLSSV 845
Cdd:cd02674 134 KRFSFSRGS--TRKLTTPVTFPL--------------------NDLDLTPYV------------DTRSFTGPFKYDLYAV 179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 846 VVHSGiSSESGHYYSYARNITSTDssyqmyhqsealalassqshllgrdspsavfeqdlenkemskeWFLFNDSRVTFTS 925
Cdd:cd02674 180 VNHYG-SLNGGHYTAYCKNNETND-------------------------------------------WYKFDDSRVTKVS 215
|
490 500
....*....|....*....|..
gi 193785252 926 FQSVQkitsrfpKDTAYVLLYK 947
Cdd:cd02674 216 ESSVV-------SSSAYILFYE 230
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-858 |
2.49e-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: 108.28 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATDFRRQVLSLNLN--------------GCNSLMKKLQHLFAFLAHTQREAYAPRIFFEA 511
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTedaelknmppdkphEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 512 SRppwFTPRSQQDCSEYLRFLLDRLheeekilkvqashkpseilecsETSLQEVASKAAvltetprtsdgeKTLIEKMFG 591
Cdd:cd02668 81 LG---LDTGQQQDAQEFSKLFLSLL----------------------EAKLSKSKNPDL------------KNIVQDLFR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 592 GKLRTHIRCLNCRSTSQKVEAFTDLSLafcpssslenmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficds 671
Cdd:cd02668 124 GEYSYVTQCSKCGRESSLPSKFYELEL----------------------------------------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 672 lvnektigsppnefycsentsvpnesnKILVNKdvpqkpggettpSVTDLLNYFLAPEILTGDNQYYCENCASLQNAEKT 751
Cdd:cd02668 151 ---------------------------QLKGHK------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRR 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 752 MQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLelpvkritsfsslseswsvdvdftDLSENLAKKlkpsgtDE 831
Cdd:cd02668 192 IRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEIL------------------------DMGEYLAES------DE 241
|
410 420
....*....|....*....|....*..
gi 193785252 832 ASCTklvpYLLSSVVVHSGISSESGHY 858
Cdd:cd02668 242 GSYV----YELSGVLIHQGVSAYSGHY 264
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-946 |
5.29e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 100.15 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFmATDFRRQVLSLNLNGcnslmkklqhLFAFLAHtqreayapriffeasRPPWFTPRSQQDC 525
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSETPKE----------LFSQVCR---------------KAPQFKGYQQQDS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 526 SEYLRFLLDRLheeekilkvqashkpseilecsetslqevaskaavltetprtsdgeKTLIEKMFGGKLRTHIRCLNCRS 605
Cdd:cd02667 55 HELLRYLLDGL----------------------------------------------RTFIDSIFGGELTSTIMCESCGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 606 TSQKVEAFTDLSLafcPSSSlenmsvqdpasspsiqdgglmqasvpgPSEEPVvynpttaaficdslvnektigsppnef 685
Cdd:cd02667 89 VSLVYEPFLDLSL---PRSD---------------------------EIKSEC--------------------------- 111
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 686 ycsentsvpnesnkilvnkdvpqkpggettpSVTDLLNYFLAPEILTGDNQYYCENCaslQNAEKTMQITEEPEYLILTL 765
Cdd:cd02667 112 -------------------------------SIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHL 157
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 766 LRFSYDQKyHVRRKILDNVSLPLVLELpvkritsfsslseswsvdVDFTDLSENLakklkPSGTDEasctklVPYLLSSV 845
Cdd:cd02667 158 KRFQQPRS-ANLRKVSRHVSFPEILDL------------------APFCDPKCNS-----SEDKSS------VLYRLYGV 207
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 846 VVHSGiSSESGHYYSYARNitstdssyqmyhqsealalassqSHLLGRDSPSAVF-EQDLENKEMSKEWFLFNDSRVtft 924
Cdd:cd02667 208 VEHSG-TMRSGHYVAYVKV-----------------------RPPQQRLSDLTKSkPAADEAGPGSGQWYYISDSDV--- 260
|
490 500
....*....|....*....|..
gi 193785252 925 sfQSVQkiTSRFPKDTAYVLLY 946
Cdd:cd02667 261 --REVS--LEEVLKSEAYLLFY 278
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
386-950 |
8.32e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 104.97 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 386 YHYSGFPDLYEPILEAIKDFPKPSEEKIKLILNQSAWTSQSNSLASclsRLSGKSETGKTGLINLGNTCYMNSVIQALFM 465
Cdd:COG5560 210 YRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDH---NRSINKEAGTCGLRNLGNTCYMNSALQCLMH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 466 ATDFRRQVLS------LNLNGCNSLMKKLQHLFAFL---AHTQR-EAYAPRIF------FEASrppwFTPRSQQDCSEYL 529
Cdd:COG5560 287 TWELRDYFLSdeyeesINEENPLGMHGSVASAYADLikqLYDGNlHAFTPSGFkktigsFNEE----FSGYDQQDSQEFI 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 530 RFLLDRLHEE-EKILKVQASHKPSeILECSETSLQEVASKAAVLTETPRTSdgektLIEKMFGGKLRTHIRCLNCRSTSQ 608
Cdd:COG5560 363 AFLLDGLHEDlNRIIKKPYTSKPD-LSPGDDVVVKKKAKECWWEHLKRNDS-----IITDLFQGMYKSTLTCPGCGSVSI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 609 KVEAFTDLSLA-------------FCPSSSLENMSVQDPASSPSI----------------------------------Q 641
Cdd:COG5560 437 TFDPFMDLTLPlpvsmvwkhtivvFPESGRRQPLKIELDASSTIRglkklvdaeygklgcfeikvmciyyggnynmlepA 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 642 DGGLMQASVP-------GPSEEPVVY------------------------NPTTAAFICDSLVNE--------------K 676
Cdd:COG5560 517 DKVLLQDIPQtdfvylyETNDNGIEVpvvhlriekgykskrlfgdpflqlNVLIKASIYDKLVKEfeellvlvemkktdV 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 677 TIGSppNEFYCSENTSVPNESNKILVNKDVP---------QKPGGET--------------------------------T 715
Cdd:COG5560 597 DLVS--EQVRLLREESSPSSWLKLETEIDTKreeqveeegQMNFNDAvvisceweekrylslfsydplwtireigaaerT 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 716 PSVTDLLNYFLAPEILTGDNQYYCENCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhvRRKILDNVSLPlvlelpvk 795
Cdd:COG5560 675 ITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYP-------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 796 ritsfsslseswsvdVDFTDLSENLAKKLKPSgtdeasctklVPYLLSSVVVHSGISSeSGHYYSYARNITstdssyqmy 875
Cdd:COG5560 745 ---------------IDDLDLSGVEYMVDDPR----------LIYDLYAVDNHYGGLS-GGHYTAYARNFA--------- 789
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193785252 876 hqsealalassqshllgrdspsavfeqdlenkemSKEWFLFNDSRVTFTSfqSVQKITSrfpkdTAYVLLYKKQH 950
Cdd:COG5560 790 ----------------------------------NNGWYLFDDSRITEVD--PEDSVTS-----SAYVLFYRRKS 823
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
423-885 |
2.97e-17 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 84.17 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 423 TSQSNSLASCLSRLSGKSetgKTGLINLGNTCYMNSVIQALFMATDFRRQVLSLnlngCNSLMKKLQHLFAFLahTQREA 502
Cdd:cd02671 6 APQPSSATSCEKRENLLP---FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVEQLQSSFL--LNPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 503 YAPrifFEASRPPwftprsqqdcseylRFLLDRLHEEEKILKVQASHKPSEILECSETSLQEvaskaavltetprtsdge 582
Cdd:cd02671 77 YND---ELANQAP--------------RRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 583 ktLIEKMFGGKLRTHIRCLNCRSTSQKVEAFTDLslafcpssslenmsvqdpasspsiqdgglmqaSVPGPSEEpvvynp 662
Cdd:cd02671 122 --LVEKDFQGQLVLRTRCLECETFTERREDFQDI--------------------------------SVPVQESE------ 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 663 ttaaficdslvnektigsPPNEFYCSENTSVPNESNKILvnKDVPQKpggettpsvtdllnyFLAPEILTGDNQYYCENC 742
Cdd:cd02671 162 ------------------LSKSEESSEISPDPKTEMKTL--KWAISQ---------------FASVERIVGEDKYFCENC 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 743 ASLQNAEKTMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLELpvkritsfsslseswsvDVDFTDLSENlak 822
Cdd:cd02671 207 HHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYGGLSKVNTPLLTPL-----------------KLSLEEWSTK--- 266
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193785252 823 klkpsgtdeascTKLVPYLLSSVVVHSGISSESGHYYSYARNITSTDSSYQMYHQSEALALAS 885
Cdd:cd02671 267 ------------PKNDVYRLFAVVMHSGATISSGHYTAYVRWLLFDDSEVKVTEEKDFLEALS 317
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
439-861 |
1.03e-14 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 79.14 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 439 KSETGKTGLINLGNTCYMNSVIQALFMATDFRRQVLSL---NLNGCNSLMKKLQHLFAFLaHTQREayaPRIFFEASRP- 514
Cdd:COG5077 188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIptdHPRGRDSVALALQRLFYNL-QTGEE---PVDTTELTRSf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 515 PWFTPRS--QQDCSEYLRFLLDRLHEEEKILKVqashkpseilecsETSLQEVaskaavltetprtsdgektliekmFGG 592
Cdd:COG5077 264 GWDSDDSfmQHDIQEFNRVLQDNLEKSMRGTVV-------------ENALNGI------------------------FVG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 593 KLRTHIRCLNCRSTSQKVEAFTDLSLAFCPSSSLEnmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficDSL 672
Cdd:COG5077 307 KMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQ------------------------------------------ESF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 673 VNektigsppnefycsentsvpnesnkilvnkdvpqkpggettpsvtdllnyFLAPEILTGDNQYYCENcASLQNAEKTM 752
Cdd:COG5077 345 RR--------------------------------------------------YIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 753 QITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLelpvkritsfsslseswsvdvdftDLSENLAKKLKPSgtDEA 832
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEI------------------------DLLPFLDRDADKS--ENS 427
|
410 420
....*....|....*....|....*....
gi 193785252 833 SCTklvpYLLSSVVVHSGISSEsGHYYSY 861
Cdd:COG5077 428 DAV----YVLYGVLVHSGDLHE-GHYYAL 451
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
5.78e-14 |
|
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: 73.90 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATDFRRQVLSLNLNG------CNSLMKKLQHLFAFLAHTQrEAYAPRIFFEASRP--PWF 517
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARrganqsSDNLTNALRDLFDTMDKKQ-EPVPPIEFLQLLRMafPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 518 TPRS------QQDCSEYLRFLLdrlheeekilkvqashkpseilecsetslqevaskaAVLTETPRTSDGEKTLIEKMFG 591
Cdd:cd02657 80 AEKQnqggyaQQDAEECWSQLL------------------------------------SVLSQKLPGAGSKGSFIDQLFG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 592 GKLRTHIRCL-NCRSTSQKVEAFTDLSLafcpsssleNMSVQDPASspSIQDgGLMQASvpgpSEEPVVYNPTTAAficd 670
Cdd:cd02657 124 IELETKMKCTeSPDEEEVSTESEYKLQC---------HISITTEVN--YLQD-GLKKGL----EEEIEKHSPTLGR---- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 671 slvnektigsppnefycsentsvpnesnkilvnkdvpqkpggettpsvtdllnyflapeiltgDNQYycencaslqnaEK 750
Cdd:cd02657 184 ---------------------------------------------------------------DAIY-----------TK 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 751 TMQITEEPEYLILTLLRFSYDQKYHVRRKILDNVSLPLVLELpvkritsfsslseswsvdVDFtdlsenlakkLKPSGTd 830
Cdd:cd02657 190 TSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDL------------------YEL----------CTPSGY- 240
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 831 easctklvpYLLSSVVVHSGISSESGHYYSYARnitstdssyqmyhqsealalassqshllgrdspsavfeQDLENKems 910
Cdd:cd02657 241 ---------YELVAVITHQGRSADSGHYVAWVR--------------------------------------RKNDGK--- 270
|
490 500 510
....*....|....*....|....*....|....*..
gi 193785252 911 keWFLFNDSRVTFTSFQSVQKITSRFPKDTAYVLLYK 947
Cdd:cd02657 271 --WIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-947 |
1.80e-11 |
|
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: 66.58 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATDFRRQVLSLNL----------NGCNSLMKKLQHlfAFLAH---------TQREAY--- 503
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfpsdvvdpaNDLNCQLIKLAD--GLLSGryskpaslkSENDPYqvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 504 -APRIF----------FEASRppwftprsQQDCSEYLRFLLDRLheeEKILKVQASHKPSEILecsetslqevaskaavl 572
Cdd:cd02658 79 iKPSMFkaligkghpeFSTMR--------QQDALEFLLHLIDKL---DRESFKNLGLNPNDLF----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 573 tetprtsdgeKTLIEKmfggklrtHIRCLNC---RSTSQKVeaftdlslafcpssslENMSVqdPasspsiqdgglMQAS 649
Cdd:cd02658 131 ----------KFMIED--------RLECLSCkkvKYTSELS----------------EILSL--P-----------VPKD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 650 VPGPSEEPVvynpttaaficdslvnektigsppnefycsentsvpnesnkiLVNKDVPQKpggettpsvtDLLNYFLAPE 729
Cdd:cd02658 164 EATEKEEGE------------------------------------------LVYEPVPLE----------DCLKAYFAPE 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 730 iltgDNQYYCENCASLQNAEKTMQITEEPEYLILTLLRFSYDQKYhVRRKILDNVSLPLVLeLPVKritsfsslseswsv 809
Cdd:cd02658 192 ----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENW-VPKKLDVPIDVPEEL-GPGK-------------- 251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 810 dvdftdlsenlakklkpsgtdeasctklvpYLLSSVVVHSGISSESGHYYSYARnitstdssyqmyhqsealalassqsh 889
Cdd:cd02658 252 ------------------------------YELIAFISHKGTSVHSGHYVAHIK-------------------------- 275
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 193785252 890 llgrdspsavfeQDLENKEmskEWFLFNDSRVtftsfqsVQKITSRFPKDTAYVLLYK 947
Cdd:cd02658 276 ------------KEIDGEG---KWVLFNDEKV-------VASQDPPEMKKLGYIYFYQ 311
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
446-536 |
5.38e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 52.50 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQALFMATDFRRQVLSLNLNGCNSLMKKLQHLFAFLahTQREAYApriFFEASRP-------PWFT 518
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKNVIRKPEPDL--NQEEALK---LFTALWSskehkvgWIPP 75
|
90
....*....|....*...
gi 193785252 519 PRSQQDCSEYLRFLLDRL 536
Cdd:COG5533 76 MGSQEDAHELLGKLLDEL 93
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-915 |
7.32e-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: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 446 GLINLGNTCYMNSVIQAlfmatdfrrqvlslnLNGCNSLMKKLQhlfaflahtqreayapriffeasrppWFTprSQQDC 525
Cdd:cd02662 1 GLVNLGNTCFMNSVLQA---------------LASLPSLIEYLE--------------------------EFL--EQQDA 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 526 SEYLRFLLDRLHEEEKILkvqashkpseilecsetslqevaskaavltetprtsdgektliekmFGGKLRTHIRCLNCRS 605
Cdd:cd02662 38 HELFQVLLETLEQLLKFP----------------------------------------------FDGLLASRIVCLQCGE 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 606 TSQ-KVEAFTDLSLAfcpssslenmsvqdpasspsiqdgglmqasvpgpseepvvynpttaaficdslvnektigsppne 684
Cdd:cd02662 72 SSKvRYESFTMLSLP----------------------------------------------------------------- 86
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 685 fycsentsvpnesnkilvnkdVPQKPGGETTpSVTDLLNYFLAPEILTGdnqYYCENCASLqnaektmqITEEPEYLILT 764
Cdd:cd02662 87 ---------------------VPNQSSGSGT-TLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIH 133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193785252 765 LLRFSYDQKYHVRRKIlDNVSLPlvLELPVKRitsfsslseswsvdvdftdlsenlakklkpsgtdeasctklvpYLLSS 844
Cdd:cd02662 134 LSRSVFDGRGTSTKNS-CKVSFP--ERLPKVL-------------------------------------------YRLRA 167
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193785252 845 VVVHSGiSSESGHYYSYARN-ITSTDSSYQMYhqSEALALASSQSHLLGRDSPSAVFEQDLENKEMSKEWFL 915
Cdd:cd02662 168 VVVHYG-SHSSGHYVCYRRKpLFSKDKEPGSF--VRMREGPSSTSHPWWRISDTTVKEVSESEVLEQKSAYM 236
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-479 |
9.53e-05 |
|
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: 45.95 E-value: 9.53e-05
10 20 30
....*....|....*....|....*....|....*
gi 193785252 445 TGLINLGNTCYMNSVIQALFMATDFRRQVLSLNLN 479
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDES 36
|
|
| |
