|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
446-801 |
2.20e-103 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 320.93 E-value: 2.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 446 VGLENIGNCCYMNCILQCLVGTHDLVRMFLDntyLNFINFDSSRGSKGLLAKNFAILVNNMHrhgaftpPNVRTIPVQTI 525
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLR---ISPLSEDSRYNKDINLLCALRDLFKALQ-------KNSKSSSVSPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 526 QFKKICGHINPMYSDSMQQDCQEFCQFLLDGLHEDLNQNGSKKhlkqlsdeeermrekmsirkasalewerflltDFSAI 605
Cdd:pfam00443 71 MFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE--------------------------------NESLI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 606 IDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKTCNIL----DCFREFTKCERLGVDEQWSCPKCLKKQPSTKQL 681
Cdd:pfam00443 119 TDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 682 KITRLPKKLIINLKRFD---NQMNKNNVFVQYPYSLDLTPYWARDFNheaivnediptRGQVPPFRYRLYGVACHSGSLY 758
Cdd:pfam00443 199 KISRLPPVLIIHLKRFSynrSTWEKLNTEVEFPLELDLSRYLAEELK-----------PKTNNLQDYRLVAVVVHSGSLS 267
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398364885 759 GGHYTSYVYKGPKKGWYFFDDSLYRPITFSTEFITPSAYVLFY 801
Cdd:pfam00443 268 SGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
7.16e-87 |
|
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: 274.55 E-value: 7.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVgthdlvrmfldntylnfinfdssrgskgllaknfailvnnmhrhgaftppnvrtipvqtiq 526
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLS------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 527 fkkicghinpmysdSMQQDCQEFCQFLLDGLHedlnqngskkhlkqlsdeeermrekmsirkasalewerflltdfSAII 606
Cdd:cd02674 20 --------------ADQQDAQEFLLFLLDGLH--------------------------------------------SIIV 41
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 607 DLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKT----CNILDCFREFTKCERLGVDEQWSCPKCLKKQPSTKQLK 682
Cdd:cd02674 42 DLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGdapkVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLT 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 683 ITRLPKKLIINLKRFDNQ---MNKNNVFVQYPYS-LDLTPYwardfnheaivnedIPTRGQVPPFRYRLYGVACHSGSLY 758
Cdd:cd02674 122 ISRLPKVLIIHLKRFSFSrgsTRKLTTPVTFPLNdLDLTPY--------------VDTRSFTGPFKYDLYAVVNHYGSLN 187
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 398364885 759 GGHYTSYVYKGPKKGWYFFDDSLYRPITFSTEfITPSAYVLFYE 802
Cdd:cd02674 188 GGHYTAYCKNNETNDWYKFDDSRVTKVSESSV-VSSSAYILFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
447-802 |
1.82e-63 |
|
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: 213.11 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVgthdlvrmfldntylnfinfdssrgskgllaknfailvnnmhrhgaftppnvrtipvqtiq 526
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 527 fkkicghinpmysdSMQQDCQEFCQFLLDGLHEDLNQNGSKKHLKQLSDeeermrekmsirkasalewerflltdfSAII 606
Cdd:cd02257 20 --------------SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLK---------------------------SLIH 58
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 607 DLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVP--RVKTCNILDCFREFTKCERLGVDEQWSCPKClKKQPSTKQLKIT 684
Cdd:cd02257 59 DLFGGKLESTIVCLECGHESVSTEPELFLSLPLPvkGLPQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIK 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 685 RLPKKLIINLKRF----DNQMNKNNVFVQYPYSLDLTPYwardfnheaIVNEDIPTRGQVPPFRYRLYGVACHSG-SLYG 759
Cdd:cd02257 138 KLPPVLIIHLKRFsfneDGTKEKLNTKVSFPLELDLSPY---------LSEGEKDSDSDNGSYKYELVAVVVHSGtSADS 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 398364885 760 GHYTSYVYKGPKKGWYFFDDSLYRPITFSTEFI----TPSAYVLFYE 802
Cdd:cd02257 209 GHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEfgslSSSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-801 |
3.35e-49 |
|
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: 175.93 E-value: 3.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLdntylnfinfdSSRGSKGLLAKNFAIL------VNNMHRHGAftppNVRTI 520
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL-----------SREHSKDCCNEGFCMMcaleahVERALASSG----PGSAP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 521 PVQTIQFKKICGHInpmySDSMQQDCQEFCQFLLDGLHedlnqngskkhlkqlsdeeermreKMSIRKASALEWERFLLT 600
Cdd:cd02661 68 RIFSSNLKQISKHF----RIGRQEDAHEFLRYLLDAMQ------------------------KACLDRFKKLKAVDPSSQ 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 601 DFSAIIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKTcnILDCFREFTKCERLGVDEQWSCPKCLKKQPSTKQ 680
Cdd:cd02661 120 ETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADS--LEDALEQFTKPEQLDGENKYKCERCKKKVKASKQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 681 LKITRLPKKLIINLKRF-DNQMNKNNVFVQYPYSLDLTPYWardfnheaivnedipTRGQVPPFRYRLYGVACHSG-SLY 758
Cdd:cd02661 198 LTIHRAPNVLTIHLKRFsNFRGGKINKQISFPETLDLSPYM---------------SQPNDGPLKYKLYAVLVHSGfSPH 262
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 398364885 759 GGHYTSYVyKGPKKGWYFFDDSLYRPITFSTEFITPsAYVLFY 801
Cdd:cd02661 263 SGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLSQK-AYILFY 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-801 |
4.35e-47 |
|
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: 170.63 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLDNTYLNFINFDSSRGSKGL-LAKNFAILVNNMHRHGaFTPPNVRTIpVQTI 525
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSCLSCaMDEIFQEFYYSGDRSP-YGPINLLYL-SWKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 526 QfKKICGhinpmYSdsmQQDCQEFCQFLLDGLHEDlnqngSKKHLKQLSDEEermrekmsirkasalewerflltDFSAI 605
Cdd:cd02660 80 S-RNLAG-----YS---QQDAHEFFQFLLDQLHTH-----YGGDKNEANDES-----------------------HCNCI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 606 ID-LFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVP-------------RVKTCNILDCFREFTKCERLGVDeQWSCPKC 671
Cdd:cd02660 123 IHqTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnkstpswalgesgVSGTPTLSDCLDRFTRPEKLGDF-AYKCSGC 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 672 LKKQPSTKQLKITRLPKKLIINLKRFDNQMNKNNV----FVQYPYSLDLTPYWARDFNHEAIVNEDIPTrgqvppFRYRL 747
Cdd:cd02660 202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRkidtYVQFPLELNMTPYTSSSIGDTQDSNSLDPD------YTYDL 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 398364885 748 YGVACHSGSLYGGHYTSYVYKGpKKGWYFFDDSLYRPITFStEFITPSAYVLFY 801
Cdd:cd02660 276 FAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEE-EVLKSQAYLLFY 327
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-804 |
2.37e-40 |
|
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: 151.64 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 446 VGLENIGNCCYMNCILQCLVGTHDlvrmFLDNTYLNFINFDSSRGSKGLLAKNFAILVNNMHRHGAFTPpnvrtipVQTI 525
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPE----FRNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTT-------ELTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 526 QFKKICGhiNPMYSdSMQQDCQEFCQFLLDglhedlnqngskkhlkqlsdeeeRMREKMsirKASALEwerflltdfSAI 605
Cdd:cd02659 72 KTRSFGW--DSLNT-FEQHDVQEFFRVLFD-----------------------KLEEKL---KGTGQE---------GLI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 606 IDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKtcNILDCFREFTKCERLGVDEQWSCPKCLKKQPSTKQLKITR 685
Cdd:cd02659 114 KNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKK--NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 686 LPKKLIINLKRFD-----NQMNKNNVFVQYPYSLDLTPYWARDFNHEAIVNEDIPTrgqvPPFRYRLYGVACHSGSLYGG 760
Cdd:cd02659 192 LPPVLTLQLKRFEfdfetMMRIKINDRFEFPLELDMEPYTEKGLAKKEGDSEKKDS----ESYIYELHGVLVHSGDAHGG 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398364885 761 HYTSYVYKGPKKGWYFFDDSLYRPITFSTE--------------FITP-------SAYVLFYERI 804
Cdd:cd02659 268 HYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqktyDSGPrafkrttNAYMLFYERK 332
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
447-641 |
1.96e-39 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 156.97 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLDNTYLNFINFDSSRGSKGLLAKNFAILVNNMH--RHGAFTPpnvrtipvqt 524
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYdgNLHAFTP---------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 525 IQFKKICGHINPMYSDSMQQDCQEFCQFLLDGLHEDLNQNGSKKHLKQ--LSDEEErmrekMSIRKASALEWERFLLTDF 602
Cdd:COG5560 337 SGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKpdLSPGDD-----VVVKKKAKECWWEHLKRND 411
|
170 180 190
....*....|....*....|....*....|....*....
gi 398364885 603 SAIIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPR 641
Cdd:COG5560 412 SIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPV 450
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
4.27e-36 |
|
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: 138.21 E-value: 4.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLvgthdlvrmFLDNTYlnfinfdssrgskGLLAKNFAILVNNMHRHGAFTPPNVRTIpvqtiq 526
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL---------YFENLL-------------TCLKDLFESISEQKKRTGVISPKKFITR------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 527 FKKIcghiNPMYSDSMQQDCQEFCQFLLDGLHEDLNQngskkhlkqlsdEEERMREKMSIRKASALEWERflltdfSAII 606
Cdd:cd02663 53 LKRE----NELFDNYMHQDAHEFLNFLLNEIAEILDA------------ERKAEKANRKLNNNNNAEPQP------TWVH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 607 DLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPrvKTCNILDCFREFTKCERLGVDEQWSCPKCLKKQPSTKQLKITRL 686
Cdd:cd02663 111 EIFQGILTNETRCLTCETVSSRDETFLDLSIDVE--QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 687 PKKLIINLKRF--DNQMNKN-NVFVQYPYSLDLTPYWARDFnheaivNEDiptrgqvpPFR-YRLYGVACHSGS-LYGGH 761
Cdd:cd02663 189 PKILALHLKRFkyDEQLNRYiKLFYRVVFPLELRLFNTTDD------AEN--------PDRlYELVAVVVHIGGgPNHGH 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 398364885 762 YTSYVYKgpKKGWYFFDDSLYRPI--TFSTEFITPS-----AYVLFYE 802
Cdd:cd02663 255 YVSIVKS--HGGWLLFDDETVEKIdeNAVEEFFGDSpnqatAYVLFYQ 300
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
1.03e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 136.75 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLDNtylnfinfdssrgSKGLLAknfailvnnmhrhgaftppnvrTIPVQTIQ 526
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------PKELFS----------------------QVCRKAPQ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 527 FKkicghinpmysDSMQQDCQEFCQFLLDGLhedlnqngskkhlkqlsdeeermrekmsirkasalewerflltdfSAII 606
Cdd:cd02667 46 FK-----------GYQQQDSHELLRYLLDGL---------------------------------------------RTFI 69
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 607 D-LFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKT--CNILDCFREFTKCERLGVDEQWSCPKCLKkqpSTKQLKI 683
Cdd:cd02667 70 DsIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKseCSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLI 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 684 TRLPKKLIINLKRF----DNQMNKNNVFVQYPYSLDLTPYWARDFNHEAIVNEdiptrgqvppFRYRLYGVACHSGSLYG 759
Cdd:cd02667 147 SKLPPVLVIHLKRFqqprSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSS----------VLYRLYGVVEHSGTMRS 216
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364885 760 GHYTSYVY--------------------KGPKKG-WYFFDDSLYRPITFStEFITPSAYVLFYE 802
Cdd:cd02667 217 GHYVAYVKvrppqqrlsdltkskpaadeAGPGSGqWYYISDSDVREVSLE-EVLKSEAYLLFYE 279
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-786 |
1.50e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 117.14 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLDNTYLNFINFDSSRGSK--------GLLAKNFAILVNNmhRHGAFTPPNVr 518
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKphepqtiiDQLQLIFAQLQFG--NRSVVDPSGF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 519 tipVQTIQFkkicghinpmySDSMQQDCQEFCQFLLDGLHEDLNQNGSKKhLKQLsdeeermrekmsirkasalewerfl 598
Cdd:cd02668 78 ---VKALGL-----------DTGQQQDAQEFSKLFLSLLEAKLSKSKNPD-LKNI------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 599 ltdfsaIIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKTcnILDCFREFTKCERLGVDEQWSCPKCLKKQPST 678
Cdd:cd02668 118 ------VQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT--LEECIDEFLKEEQLTGDNQYFCESCNSKTDAT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 679 KQLKITRLPKKLIINLKRF-----DNQMNKNNVFVQYPYSLDLTPYWARDFNHEaivnediptrgqvppFRYRLYGVACH 753
Cdd:cd02668 190 RRIRLTTLPPTLNFQLLRFvfdrkTGAKKKLNASISFPEILDMGEYLAESDEGS---------------YVYELSGVLIH 254
|
330 340 350
....*....|....*....|....*....|....
gi 398364885 754 SG-SLYGGHYTSYVYKGPKKGWYFFDDSLYRPIT 786
Cdd:cd02668 255 QGvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMP 288
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
9.85e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 114.34 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLD--NTYLNFINFDS-------SRGSKGLLAKNFAILVNNMHRHGAFTppnv 517
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDleNKFPSDVVDPAndlncqlIKLADGLLSGRYSKPASLKSENDPYQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 518 rtIPVQTIQFKKICGHINPMYSDSMQQDCQEFCQFLLDGLHEDLNQNGSKKhlkqlsdeeermrekmsirkasalewerf 597
Cdd:cd02658 77 --VGIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLN----------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 598 lltdfsaIIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKTCN------------ILDCFREFTKCERLgvdeQ 665
Cdd:cd02658 126 -------PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEkeegelvyepvpLEDCLKAYFAPETI----E 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 666 WSCPKCLKKQPSTKQLKITRLPKKLIINLKRFdnQMNKNNVfvqyPYSLDltpywardfnheaiVNEDIPtrGQVPPFRY 745
Cdd:cd02658 195 DFCSTCKEKTTATKTTGFKTFPDYLVINMKRF--QLLENWV----PKKLD--------------VPIDVP--EELGPGKY 252
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364885 746 RLYGVACHSG-SLYGGHYTSYVYKG--PKKGWYFFDDS-LYrpITFSTEFITPSAYVLFYE 802
Cdd:cd02658 253 ELIAFISHKGtSVHSGHYVAHIKKEidGEGKWVLFNDEkVV--ASQDPPEMKKLGYIYFYQ 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
4.25e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 112.97 E-value: 4.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRMFLDNTYLNFINFDSSRGSKGLLaknFAILvnnMHRHGAFTPPnvrtipvqTIQ 526
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLL---QAHL---MHTQRRAEAP--------PDY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 527 FKKICghINPMYSDSMQQDCQEFCQFLLDGLHEdlnqngskkhlkqlsdeeerMREKMsirkasalewerflltdfsaii 606
Cdd:cd02664 67 FLEAS--RPPWFTPGSQQDCSEYLRYLLDRLHT--------------------LIEKM---------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 607 dlFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKtcnilDCFREFTKCERLGVDEQWSCPKCLKKQPSTKQLKITRL 686
Cdd:cd02664 103 --FGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQ-----DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 687 PKKLIINLKRF--DNQMNK-----NNVFvqYPYSLDLTPYWARDFNhEAIVNEDIPTRG--------QVPpfrYRLYGVA 751
Cdd:cd02664 176 PEYLILTLLRFsyDQKTHVrekimDNVS--INEVLSLPVRVESKSS-ESPLEKKEEESGddgelvtrQVH---YRLYAVV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364885 752 CHSG-SLYGGHYTSY------------VYKGPK--------KGWYFFDDSLYRPITFSTEF----ITPS--AYVLFYE 802
Cdd:cd02664 250 VHSGySSESGHYFTYardqtdadstgqECPEPKdaeendesKNWYLFNDSRVTFSSFESVQnvtsRFPKdtPYILFYE 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
649-803 |
4.69e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 114.98 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 649 DCFREFTKCERLGVDEQWSCPKCLKKQPSTKQLKITRLPKKLIINLKRFDNQM---NKNNVFVQYP-YSLDLTPYWARDF 724
Cdd:COG5560 679 DCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRsfrDKIDDLVEYPiDDLDLSGVEYMVD 758
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364885 725 NheaivnediptrgqvPPFRYRLYGVACHSGSLYGGHYTSYVYKGPKKGWYFFDDSLYRPITfSTEFITPSAYVLFYER 803
Cdd:COG5560 759 D---------------PRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVD-PEDSVTSSAYVLFYRR 821
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-801 |
8.30e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 103.43 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 446 VGLENIGNCCYMNCILQCLvgthdlvrMFLDNTYLNFINFDSSRGSKGLLAKNFAILVNNMHRHGAFTPPnvRTIpVQTI 525
Cdd:cd02671 25 VGLNNLGNTCYLNSVLQVL--------YFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYNDELANQAP--RRL-LNAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 526 QfkkicgHINPMYSDSMQQDCQEFCQFLLDGLHEdlnqngskkhlkqlsdeeermrekmsirkasALEWerflltdfsai 605
Cdd:cd02671 94 R------EVNPMYEGYLQHDAQEVLQCILGNIQE-------------------------------LVEK----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 606 idLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPV-----------------PRVKTCNILDCFREFTKCERLGVDEQWSC 668
Cdd:cd02671 126 --DFQGQLVLRTRCLECETFTERREDFQDISVPVqeselskseesseispdPKTEMKTLKWAISQFASVERIVGEDKYFC 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 669 PKCLKKQPSTKQLKITRLPKKLIINLKRFDNQ---------MNKNNVFVQYPYSLDLtpywardfnHEAIVNEDIPTrgq 739
Cdd:cd02671 204 ENCHHYTEAERSLLFDKLPEVITIHLKCFAANgsefdcyggLSKVNTPLLTPLKLSL---------EEWSTKPKNDV--- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364885 740 vppfrYRLYGVACHSG-SLYGGHYTSYVykgpkkGWYFFDDSLYRpITFSTEF---------ITPSAYVLFY 801
Cdd:cd02671 272 -----YRLFAVVMHSGaTISSGHYTAYV------RWLLFDDSEVK-VTEEKDFlealspntsSTSTPYLLFY 331
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
2.57e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 85.11 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLVRmFLDNtylnFINfdssrgskgllaknfailvnnmhrhgaftppnvrtipvqtiq 526
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIE-YLEE----FLE------------------------------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 527 fkkicghinpmysdsmQQDCQEFCQFLLDGLHEDLNQngskkhlkqlsdeeermrekmsirkasalewerflltdfsaii 606
Cdd:cd02662 34 ----------------QQDAHELFQVLLETLEQLLKF------------------------------------------- 54
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 607 dLFQGQYASRLQCQVCEHTST-TYQTFSVLSVPVP---RVKTCNILDCFREFTKCERLgvdEQWSCPKClkkqpstkQLK 682
Cdd:cd02662 55 -PFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPnqsSGSGTTLEHCLDDFLSTEII---DDYKCDRC--------QTV 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 683 ITRLPKKLIINLKR--FDNQMN--KNNVFVQYPYSLdltpywardfnheaivnediptrgqvPPFRYRLYGVACHSGSLY 758
Cdd:cd02662 123 IVRLPQILCIHLSRsvFDGRGTstKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHS 176
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364885 759 GGHYTSY--------------------VYKGPKKGWYFFDDSLYRPITFSTEFITPSAYVLFYE 802
Cdd:cd02662 177 SGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQKSAYMLFYE 240
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
446-780 |
1.02e-17 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 88.39 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 446 VGLENIGNCCYMNCILQCLVGTHdlvrMFLDNTYLNFINFDSSRGSKGLLAKNfailvnnmhrhgAFTPPNVRTIPVQTI 525
Cdd:COG5077 194 VGLRNQGATCYMNSLLQSLFFIA----KFRKDVYGIPTDHPRGRDSVALALQR------------LFYNLQTGEEPVDTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 526 QFKKICGHINpmySDS-MQQDCQEFCQFLLDGLhedlnqngskkhlkqlsdeEERMREkmsirkaSALEwerflltdfSA 604
Cdd:COG5077 258 ELTRSFGWDS---DDSfMQHDIQEFNRVLQDNL-------------------EKSMRG-------TVVE---------NA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 605 IIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKtcNILDCFREFTKCERLGVDEQWSCPKcLKKQPSTKQLKIT 684
Cdd:COG5077 300 LNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 685 RLPKKLIINLKRFD-----NQMNKNNVFVQYPYSLDLTPYWARDFNheaivnediptRGQVPPFRYRLYGVACHSGSLYG 759
Cdd:COG5077 377 SLPPVLHLQLKRFEydferDMMVKINDRYEFPLEIDLLPFLDRDAD-----------KSENSDAVYVLYGVLVHSGDLHE 445
|
330 340
....*....|....*....|.
gi 398364885 760 GHYTSYVYKGPKKGWYFFDDS 780
Cdd:COG5077 446 GHYYALLKPEKDGRWYKFDDT 466
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
595-802 |
7.24e-13 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 69.46 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 595 ERFLLTD----FSAIIDLFQGQYASRLQCQ------VCEHTSTTYQTFSVLSVPVPRVKTCNILDcFREFTK---CERLg 661
Cdd:cd02672 54 ESCLLCElgylFSTLIQNFTRFLLETISQDqlgtpfSCGTSRNSVSLLYTLSLPLGSTKTSKEST-FLQLLKrslDLEK- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 662 VDEQWsCPKCLKKQPSTKQLKITRLP----KKLIINLKRFDNqmNKNNVFVQYPYSLDLTPYWAR-DFNHEAIVNEDIPT 736
Cdd:cd02672 132 VTKAW-CDTCCKYQPLEQTTSIRHLPdillLVLVINLSVTNG--EFDDINVVLPSGKVMQNKVSPkAIDHDKLVKNRGQE 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364885 737 RGQVppfrYRLYGVACH-SGSLYGGHYTSYVYKGPKK----GWYFFDDSLYRPitfstefITPSAYVLFYE 802
Cdd:cd02672 209 SIYK----YELVGYVCEiNDSSRGQHNVVFVIKVNEEsthgRWYLFNDFLVTP-------VSELAYILLYQ 268
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-802 |
2.45e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 68.51 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 447 GLENIGNCCYMNCILQCLVGTHDLvrmfldNTYLNFINFDSSRGSK--GLLAKNFAILVNNMHR-HGAFTP-PNVRTIPV 522
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPEL------RDALKNYNPARRGANQssDNLTNALRDLFDTMDKkQEPVPPiEFLQLLRM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 523 QTIQFKKIcgHINPMYsdsMQQDCQEFCQFLLDGLHEDLNQNGSKKhlkqlsdeeermrekmsirkasalewerflltdf 602
Cdd:cd02657 75 AFPQFAEK--QNQGGY---AQQDAEECWSQLLSVLSQKLPGAGSKG---------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 603 SAIIDLFQGQYASRLQCQVCEH-TSTTYQTFSVLSVPVPRVKTCN-----ILDCFRE--FTKCERLGVDEQWscpkclkk 674
Cdd:cd02657 116 SFIDQLFGIELETKMKCTESPDeEEVSTESEYKLQCHISITTEVNylqdgLKKGLEEeiEKHSPTLGRDAIY-------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 675 qpsTKQLKITRLPKKLIINLKRF-----DNQMNKNNVFVQYPYSLDLTPYWArdfnheaivnediptrgqvPPFRYRLYG 749
Cdd:cd02657 188 ---TKTSRISRLPKYLTVQFVRFfwkrdIQKKAKILRKVKFPFELDLYELCT-------------------PSGYYELVA 245
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364885 750 VACHSG-SLYGGHYTSYVYKGPKKGWYFFDDSlyRPITFSTEFI--------TPSAYVLFYE 802
Cdd:cd02657 246 VITHQGrSADSGHYVAWVRRKNDGKWIKFDDD--KVSEVTEEDIlklsgggdWHIAYILLYK 305
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
524-802 |
3.32e-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 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: 239138 [Multi-domain] Cd Length: 245 Bit Score: 58.31 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 524 TIQFKKICGHINPMYSDSMQQDCQEFCQFLLDGLhEDLNQNgskkhlkqlsdeeERMREKMSIRKASALEwerflltdfs 603
Cdd:cd02673 14 TMQALSSIGKINTEFDNDDQQDAHEFLLTLLEAI-DDIMQV-------------NRTNVPPSNIEIKRLN---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 604 aIIDLFQGQYASRLQCQVCEHTSTTYQTFSVLSVPVPRVKTCNILDC---FREFTKCERlgvdeqwSCPKClKKQPSTKQ 680
Cdd:cd02673 70 -PLEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNKLDIDELLisnFKTWSPIEK-------DCSSC-KCESAISS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 681 LKITRLPKKLIINLKRFDnqmnknnvfVQYPYSLDLTPywardfnheaivNEDIPTRGQVPPFRYRLYGVACHSG-SLYG 759
Cdd:cd02673 141 ERIMTFPECLSINLKRYK---------LRIATSDYLKK------------NEEIMKKYCGTDAKYSLVAVICHLGeSPYD 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 398364885 760 GHYTSY---VYKGPKkgWYFFDDSLYRPITFST--EFITPSAYVLFYE 802
Cdd:cd02673 200 GHYIAYtkeLYNGSS--WLYCSDDEIRPVSKNDvsTNARSSGYLIFYD 245
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
671-802 |
5.83e-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 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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 57.54 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 671 CLKKQPSTKQLKitRLPKKLIINLKRF---DNQMNKNNVFVQYPYSLDLTPYWARDFNHEAIVN----------EDIPTR 737
Cdd:cd02670 85 CLEQYFNNSVFA--KAPSCLIICLKRYgktEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQlecrvcyddkDFSPTC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 738 GqvpPFRYRLYGVACHSG-SLYGGHYTSYVYKGPKKG-----------WYFFDDSLYRP-----ITFSTEFITPSAYVLF 800
Cdd:cd02670 163 G---KFKLSLCSAVCHRGtSLETGHYVAFVRYGSYSLtetdneaynaqWVFFDDMADRDgvsngFNIPAARLLEDPYMLF 239
|
..
gi 398364885 801 YE 802
Cdd:cd02670 240 YQ 241
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
159-280 |
1.65e-08 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 52.85 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 159 HGDALLLIDVRPRSEFVRAHIKCKNIICIDPASFKDSFTDQQiesvslitsPHSDITFFSNRDKFKFIILYTDTQLHNnf 238
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIL---------EFEELLKRLGLDKDKPVVVYCRSGNRS-- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 398364885 239 qQRQTRILAKILSQNsvikplsgtkILILENGFSNWVKLGGA 280
Cdd:smart00450 70 -AKAAWLLRELGFKN----------VYLLDGGYKEWSAAGPP 100
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
547-781 |
7.80e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 54.97 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 547 QEFCQFLLDglhedlnqngskkhlkQLSDEEERMREKMSirkasalewerfllTDFSAIIDLFQGQYASRLQCQVCEHTS 626
Cdd:pfam13423 100 QSFNRFLLD----------------QLSSEENSTPPNPS--------------PAESPLEQLFGIDAETTIRCSNCGHES 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 627 TTYQTFSVLSVPVPRVKTCN--------ILDCFREFTkcERLGVDEQWsCPKCLKKQPSTKQLKITRLPKKLIINLKRFD 698
Cdd:pfam13423 150 VRESSTHVLDLIYPRKPSSNnkkppnqtFSSILKSSL--ERETTTKAW-CEKCKRYQPLESRRTVRNLPPVLSLNAALTN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 699 NQMN---KNNVFVqyPYSLDLTPYWARDFNHEAIVnediptrgqvppfrYRLYGVACH-SGSLYGGHYTSYV-------Y 767
Cdd:pfam13423 227 EEWRqlwKTPGWL--PPEIGLTLSDDLQGDNEIVK--------------YELRGVVVHiGDSGTSGHLVSFVkvadselE 290
|
250
....*....|....
gi 398364885 768 KGPKKGWYFFDDSL 781
Cdd:pfam13423 291 DPTESQWYLFNDFL 304
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
158-275 |
5.45e-06 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 45.55 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 158 FHGDALLLIDVRPRSEFVRAHIkcKNIICIDPASFkdsftdqQIESVSLITSPHSDItffsNRDKFKFIILYTDTqlhnn 237
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHI--PGAVNVPLSSL-------SLPPLPLLELLEKLL----ELLKDKPIVVYCNS----- 62
|
90 100 110
....*....|....*....|....*....|....*...
gi 398364885 238 fqQRQTRILAKILSQnsvikpLSGTKILILENGFSNWV 275
Cdd:pfam00581 63 --GNRAAAAAALLKA------LGYKNVYVLDGGFEAWK 92
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
739-801 |
2.72e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 43.32 E-value: 2.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 739 QVPpfrYRLYGVACHSGSLYGGHYTSYVYKGPKKGWYFFDDSLYRPITFST-------EFITPSAYVLFY 801
Cdd:cd02665 161 QVP---YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEverdsfgGGRNPSAYCLMY 227
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-779 |
5.30e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 43.46 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 445 IVGLENIGNCCYMNCILQCLVGTHDLVRMFLDNTylnfiNFDSSRGSKGLLAKNFAILVNNMHRHGAFTppnvRTI-PVQ 523
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE-----NYENIKDRKSELVKRLSELIRKIWNPRNFK----GHVsPHE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 524 TIQFKKICGHINpmYSDSMQQDCQEFCQFLLDGLHEDLNQnGSKKHLKQLSDEEermREKMSIRKASALEWErfllTDFS 603
Cdd:cd02669 190 LLQAVSKVSKKK--FSITEQSDPVEFLSWLLNTLHKDLGG-SKKPNSSIIHDCF---QGKVQIETQKIKPHA----EEEG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 604 AIIDLFQGQYAsrlqcqvcehTSTTYQTFSVLS--VP-------------VPRVKTCNILDCFReftkcerlGVDEQWSc 668
Cdd:cd02669 260 SKDKFFKDSRV----------KKTSVSPFLLLTldLPppplfkdgneeniIPQVPLKQLLKKYD--------GKTETEL- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364885 669 pkclkkQPSTKQLKITRLPKKLIINLKRFDN---QMNKNNVFVQYPYS-LDLTPYWARDFNheaivnediptrGQVPPFR 744
Cdd:cd02669 321 ------KDSLKRYLISRLPKYLIFHIKRFSKnnfFKEKNPTIVNFPIKnLDLSDYVHFDKP------------SLNLSTK 382
|
330 340 350
....*....|....*....|....*....|....*.
gi 398364885 745 YRLYGVACHSGSLYG-GHYTSYVYKGPKKGWYFFDD 779
Cdd:cd02669 383 YNLVANIVHEGTPQEdGTWRVQLRHKSTNKWFEIQD 418
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
745-780 |
5.76e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 42.86 E-value: 5.76e-04
10 20 30
....*....|....*....|....*....|....*.
gi 398364885 745 YRLYGVACHSGSLYGGHYTSYVYKGPKKGWYFFDDS 780
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDE 316
|
|
| |
