|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
145-684 |
9.72e-66 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 223.09 E-value: 9.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 145 TGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGL---VRTDKKPALCKSYQKLISEVWHKKRPSYVVPTSLSHGIKLVN 221
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLsedSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 222 PMFRGYAQQDTQEFLRCLMDQLHEELKepmvaavaaltdardsdssdtderrdgdrspsedeflscdsssdrgegdgqgr 301
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 302 gggsskaemellisdeaGRAISEKErmkdrkfswgqqrtnseqvdedadvdtamasldeqsreaqppsprstspcqtpep 381
Cdd:pfam00443 108 -----------------GNHSTENE------------------------------------------------------- 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 382 dneahirsssrpcspvhhhheghsklsssppraspvrmgpsyvlkkaqvpstggrrrkeqsyrSVISDVFNGSVLSLVQC 461
Cdd:pfam00443 116 ---------------------------------------------------------------SLITDLFRGQLKSRLKC 132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 462 LTCDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyssqgwlafiveyirrfvvsctpswfWGPVVTL 541
Cdd:pfam00443 133 LSCGEVSETFEPFSDLSLPIPGDSA------------------------------------------------ELKTASL 164
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 542 EDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEgLDLRPFLAKE 621
Cdd:pfam00443 165 QICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEE 243
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81876818 622 ---CTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVH-ETVVQNVEAYVLFY 684
Cdd:pfam00443 244 lkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-685 |
2.90e-57 |
|
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: 196.35 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 445 SVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAklhsaiyqnvpakpgacgdsyssqgwlafiveyirr 524
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 525 fvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSH 604
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 605 VSFPLEGLDLRPFLAKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFY 684
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 81876818 685 R 685
Cdd:cd02674 230 E 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
73-688 |
4.90e-38 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 153.12 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 73 TVNLTTFRVWCYACEREVFLE--QRLAVHLASSSARLSEQdSPPPSHPLkavpiavaDEGESESEDDDLKPRGLTGMKNL 150
Cdd:COG5560 201 LGLDSFFRRYRVLASDGRVLHplTRLELFEDRSVLLLSKI-TRNPDWLV--------DSIVDDHNRSINKEAGTCGLRNL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 151 GNSCYMNAALQALSNCPPLTQFFLECG---GLVRTDKKP---ALCKSYQKLISEVwHKKRPSYVVPTSLSHGIKLVNPMF 224
Cdd:COG5560 272 GNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGFKKTIGSFNEEF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 225 RGYAQQDTQEFLRCLMDQLHEELKEPMVAAVAALTDARDSDSSDT--------DERRDGDRSPSEDEFLSCDSS------ 290
Cdd:COG5560 351 SGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkakecwWEHLKRNDSIITDLFQGMYKStltcpg 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 291 ---------------------------------SDRGEGDGQGRGGGSSKAEMELLISDEAGRA------ISEKERMKDR 331
Cdd:COG5560 431 cgsvsitfdpfmdltlplpvsmvwkhtivvfpeSGRRQPLKIELDASSTIRGLKKLVDAEYGKLgcfeikVMCIYYGGNY 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 332 KFSWGQQRTNSEQVDEDADVdtamasldeqsREAQPPSPRSTSPCqtpepdneAHIRSSSRPCSPVHHhheGHSKLSSSP 411
Cdd:COG5560 511 NMLEPADKVLLQDIPQTDFV-----------YLYETNDNGIEVPV--------VHLRIEKGYKSKRLF---GDPFLQLNV 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 412 PRASPVRMGPSYVLKKAQVPSTGGRRRKEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLH 491
Cdd:COG5560 569 LIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEW 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 492 SaiyqnvpakpgacGDSYssqgwlafiveyirRFVVSCTPSW------FWGPVVTLEDCLAAFFAADELKGDNMYSCERC 565
Cdd:COG5560 649 E-------------EKRY--------------LSLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGC 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 566 KKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEGLDLRPFLAKECTSQVTtYDLLSVICHHGTAGSGH 645
Cdd:COG5560 702 KEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLI-YDLYAVDNHYGGLSGGH 780
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 81876818 646 YIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFYRKSS 688
Cdd:COG5560 781 YTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
812-896 |
3.57e-28 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 108.60 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 812 AEESPAVIYCISMHWFREWEAFVKGKDSEPPGPIDNSRIAQVKGS--GHIQLKQGADCGQISEETWTYLSSLYGGGPEIA 889
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*..
gi 81876818 890 IRQSVAQ 896
Cdd:smart00695 81 PRKVVCQ 87
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
704-787 |
8.61e-24 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 95.89 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 704 MREPSLLRFYVSREWLNKFNTFAE------PGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQSVWEHLYSRFGGGPAvn 777
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
90
....*....|
gi 81876818 778 HLYVCSICQV 787
Cdd:smart00695 79 PIPRKVVCQG 88
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
819-891 |
2.81e-20 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 85.88 E-value: 2.81e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81876818 819 IYCISMHWFREWEAFVKGKdSEPPGPIDNSRIAQVKGSGHI--QLKQGADCGQISEETWTYLSSLYGGGPEIAIR 891
Cdd:pfam06337 4 VYLISSKWLNKWKSYVKEP-NNEPGPIDNSDLLDDESNGQLkpNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
540-671 |
6.74e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 89.16 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 540 TLEDCLAAFFAADELKGDNMYSCERcKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYS--FKVSSHVSFPLEgLDLRPF 617
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDmmVKINDRYEFPLE-IDLLPF 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 81876818 618 L---AKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHE 671
Cdd:COG5077 417 LdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATE 473
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
712-782 |
4.49e-15 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 70.86 E-value: 4.49e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81876818 712 FYVSREWLNKFNTFAE-----PGPITNHTFLC--SHGGIPPNKYHYIDdlVVILPQSVWEHLYSRFGGGPAVNHLYVC 782
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLDdeSNGQLKPNLQEGVD--YVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
30-90 |
5.50e-15 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 69.98 E-value: 5.50e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81876818 30 CQSCGVAGpNLWACLqvTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFRVWCYACEREV 90
Cdd:pfam02148 1 CSLCGNTS-NLWLCL--TCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-247 |
4.88e-07 |
|
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: 53.09 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 39 NLWACLqVTCPYV-GCGESfaDHSSIHAQVKKHNLTVNLTTFRVWCYACEREVF---LEQrLAVHLASSSARLSEQDSPP 114
Cdd:cd02669 27 NVYACL-VCGKYFqGRGKG--SHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIdssLDD-IKYVLNPTYTKEQISDLDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 115 PSHPLKAVpiavadegesesEDDDLKPrGLTGMKNLGNSCYMNAALQALSNCPPLTQFFL-ECGGLVRTDKKPALCKSYQ 193
Cdd:cd02669 103 DPKLSRDL------------DGKPYLP-GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDRKSELVKRLS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 81876818 194 KLISEVWHKKR-PSYVVPTSLSHGIKLV-NPMFRGYAQQDTQEFLRCLMDQLHEEL 247
Cdd:cd02669 170 ELIRKIWNPRNfKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL 225
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-81 |
6.60e-05 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 41.20 E-value: 6.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 81876818 29 TCQSCGVAGpNLWACLqvTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFRV 81
Cdd:smart00290 1 RCSVCGTIE-NLWLCL--TCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
145-684 |
9.72e-66 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 223.09 E-value: 9.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 145 TGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGL---VRTDKKPALCKSYQKLISEVWHKKRPSYVVPTSLSHGIKLVN 221
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLsedSRYNKDINLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 222 PMFRGYAQQDTQEFLRCLMDQLHEELKepmvaavaaltdardsdssdtderrdgdrspsedeflscdsssdrgegdgqgr 301
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 302 gggsskaemellisdeaGRAISEKErmkdrkfswgqqrtnseqvdedadvdtamasldeqsreaqppsprstspcqtpep 381
Cdd:pfam00443 108 -----------------GNHSTENE------------------------------------------------------- 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 382 dneahirsssrpcspvhhhheghsklsssppraspvrmgpsyvlkkaqvpstggrrrkeqsyrSVISDVFNGSVLSLVQC 461
Cdd:pfam00443 116 ---------------------------------------------------------------SLITDLFRGQLKSRLKC 132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 462 LTCDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyssqgwlafiveyirrfvvsctpswfWGPVVTL 541
Cdd:pfam00443 133 LSCGEVSETFEPFSDLSLPIPGDSA------------------------------------------------ELKTASL 164
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 542 EDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEgLDLRPFLAKE 621
Cdd:pfam00443 165 QICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEE 243
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81876818 622 ---CTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVH-ETVVQNVEAYVLFY 684
Cdd:pfam00443 244 lkpKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-685 |
2.90e-57 |
|
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: 196.35 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 445 SVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAklhsaiyqnvpakpgacgdsyssqgwlafiveyirr 524
Cdd:cd02674 38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 525 fvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSH 604
Cdd:cd02674 82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 605 VSFPLEGLDLRPFLAKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFY 684
Cdd:cd02674 150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
|
.
gi 81876818 685 R 685
Cdd:cd02674 230 E 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
435-685 |
1.32e-48 |
|
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: 173.05 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 435 GRRRKEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyssqgw 514
Cdd:cd02257 45 KRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL---------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 515 lafiveyirrfvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKlRNGVKYCKVLCLPEILCVHLKRFRH- 593
Cdd:cd02257 97 ----------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSFn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 594 EVMYSFKVSSHVSFPLEgLDLRPFLAKECTSQV-----TTYDLLSVICHHGTAG-SGHYIAYCQNVINGQWYEFDDQYVT 667
Cdd:cd02257 154 EDGTKEKLNTKVSFPLE-LDLSPYLSEGEKDSDsdngsYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVT 232
|
250 260
....*....|....*....|...
gi 81876818 668 EVHETVVQNV-----EAYVLFYR 685
Cdd:cd02257 233 EVSEEEVLEFgslssSAYILFYE 255
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-684 |
3.25e-43 |
|
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: 159.36 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 445 SVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGkedlaklhsaiyqnvpakpgacgdsyssqgwlafiveyirr 524
Cdd:cd02661 122 TLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG----------------------------------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 525 fvvsctpswfwgpVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFrhEVMYSFKVSSH 604
Cdd:cd02661 161 -------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 605 VSFPLEgLDLRPFLAKEcTSQVTTYDLLSVICHHGT-AGSGHYIAYCQNvINGQWYEFDDQYVTEVHETVVQNVEAYVLF 683
Cdd:cd02661 226 ISFPET-LDLSPYMSQP-NDGPLKYKLYAVLVHSGFsPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILF 302
|
.
gi 81876818 684 Y 684
Cdd:cd02661 303 Y 303
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
446-684 |
8.44e-41 |
|
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: 153.30 E-value: 8.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 446 VISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIyqnvpakpgacgdsyssqgwlafiveyirrf 525
Cdd:cd02660 122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGES------------------------------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 526 VVSCTPswfwgpvvTLEDCLAaFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSF-KVSSH 604
Cdd:cd02660 171 GVSGTP--------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSrKIDTY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 605 VSFPLEgLDLRPFLAKECTSQVT--------TYDLLSVICHHGTAGSGHYIAYCQNViNGQWYEFDDQYVTEVHETVVQN 676
Cdd:cd02660 242 VQFPLE-LNMTPYTSSSIGDTQDsnsldpdyTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLK 319
|
....*...
gi 81876818 677 VEAYVLFY 684
Cdd:cd02660 320 SQAYLLFY 327
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
73-688 |
4.90e-38 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 153.12 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 73 TVNLTTFRVWCYACEREVFLE--QRLAVHLASSSARLSEQdSPPPSHPLkavpiavaDEGESESEDDDLKPRGLTGMKNL 150
Cdd:COG5560 201 LGLDSFFRRYRVLASDGRVLHplTRLELFEDRSVLLLSKI-TRNPDWLV--------DSIVDDHNRSINKEAGTCGLRNL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 151 GNSCYMNAALQALSNCPPLTQFFLECG---GLVRTDKKP---ALCKSYQKLISEVwHKKRPSYVVPTSLSHGIKLVNPMF 224
Cdd:COG5560 272 GNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGFKKTIGSFNEEF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 225 RGYAQQDTQEFLRCLMDQLHEELKEPMVAAVAALTDARDSDSSDT--------DERRDGDRSPSEDEFLSCDSS------ 290
Cdd:COG5560 351 SGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkakecwWEHLKRNDSIITDLFQGMYKStltcpg 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 291 ---------------------------------SDRGEGDGQGRGGGSSKAEMELLISDEAGRA------ISEKERMKDR 331
Cdd:COG5560 431 cgsvsitfdpfmdltlplpvsmvwkhtivvfpeSGRRQPLKIELDASSTIRGLKKLVDAEYGKLgcfeikVMCIYYGGNY 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 332 KFSWGQQRTNSEQVDEDADVdtamasldeqsREAQPPSPRSTSPCqtpepdneAHIRSSSRPCSPVHHhheGHSKLSSSP 411
Cdd:COG5560 511 NMLEPADKVLLQDIPQTDFV-----------YLYETNDNGIEVPV--------VHLRIEKGYKSKRLF---GDPFLQLNV 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 412 PRASPVRMGPSYVLKKAQVPSTGGRRRKEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLH 491
Cdd:COG5560 569 LIKASIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREESSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEW 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 492 SaiyqnvpakpgacGDSYssqgwlafiveyirRFVVSCTPSW------FWGPVVTLEDCLAAFFAADELKGDNMYSCERC 565
Cdd:COG5560 649 E-------------EKRY--------------LSLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGC 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 566 KKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEGLDLRPFLAKECTSQVTtYDLLSVICHHGTAGSGH 645
Cdd:COG5560 702 KEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPRLI-YDLYAVDNHYGGLSGGH 780
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 81876818 646 YIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFYRKSS 688
Cdd:COG5560 781 YTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-688 |
1.64e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 135.08 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 447 ISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLaklhsaiyqnvpakpgacgdsyssqgwlafiveyirrfv 526
Cdd:cd02659 113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 527 vsctpswfwgpvvtlEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRH--EVMYSFKVSSH 604
Cdd:cd02659 154 ---------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 605 VSFPLEgLDLRPFLAKEC----------TSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEV----- 669
Cdd:cd02659 219 FEFPLE-LDMEPYTEKGLakkegdsekkDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFdpnda 297
|
250 260 270
....*....|....*....|....*....|....*.
gi 81876818 670 -------HETVVQNVE----------AYVLFYRKSS 688
Cdd:cd02659 298 eeecfggEETQKTYDSgprafkrttnAYMLFYERKS 333
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-685 |
4.98e-33 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 129.04 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 442 SYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDlaklhsaiyqnvpakpgacgdsyssqgwlafivey 521
Cdd:cd02667 64 GLRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK----------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 522 irrfvvsctpswfwgPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRngvKYCKVLCLPEILCVHLKRFRHEVMYSF-K 600
Cdd:cd02667 109 ---------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 601 VSSHVSFPlEGLDLRPFLAKECTSQVTT----YDLLSVICHHGTAGSGHYIAY---------------------CQNVIN 655
Cdd:cd02667 171 VSRHVSFP-EILDLAPFCDPKCNSSEDKssvlYRLYGVVEHSGTMRSGHYVAYvkvrppqqrlsdltkskpaadEAGPGS 249
|
250 260 270
....*....|....*....|....*....|
gi 81876818 656 GQWYEFDDQYVTEVHETVVQNVEAYVLFYR 685
Cdd:cd02667 250 GQWYYISDSDVREVSLEEVLKSEAYLLFYE 279
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
439-668 |
1.55e-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: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 439 KEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEdlaklhsaiyqnvpakpgacgdsyssqgwlafi 518
Cdd:cd02668 110 KNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK--------------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 519 veyirrfvvsctpswfwgpvvTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKR--FRHEVM 596
Cdd:cd02668 157 ---------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRfvFDRKTG 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81876818 597 YSFKVSSHVSFPLEgLDLRPFLAkECTSQVTTYDLLSVICHHGT-AGSGHYIAYCQNVINGQWYEFDDQYVTE 668
Cdd:cd02668 216 AKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-684 |
2.56e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 115.87 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 447 ISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGkedlaklHSAIyqnvpakpgacgdsyssqgwlafiveyirrfv 526
Cdd:cd02663 109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTSI-------------------------------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 527 vsctpswfwgpvvtlEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYS--FKVSSH 604
Cdd:cd02663 150 ---------------TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 605 VSFPLEgldLRPF-LAKECTSQVTTYDLLSVICHHG-TAGSGHYIAYCQnvINGQWYEFDDQYVTEVHETVVQNV----- 677
Cdd:cd02663 215 VVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFfgdsp 289
|
250
....*....|
gi 81876818 678 ---EAYVLFY 684
Cdd:cd02663 290 nqaTAYVLFY 299
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
812-896 |
3.57e-28 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 108.60 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 812 AEESPAVIYCISMHWFREWEAFVKGKDSEPPGPIDNSRIAQVKGS--GHIQLKQGADCGQISEETWTYLSSLYGGGPEIA 889
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGprLKEHLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80
|
....*..
gi 81876818 890 IRQSVAQ 896
Cdd:smart00695 81 PRKVVCQ 87
|
|
| DUSP |
smart00695 |
Domain in ubiquitin-specific proteases; |
704-787 |
8.61e-24 |
|
Domain in ubiquitin-specific proteases;
Pssm-ID: 197831 Cd Length: 88 Bit Score: 95.89 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 704 MREPSLLRFYVSREWLNKFNTFAE------PGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQSVWEHLYSRFGGGPAvn 777
Cdd:smart00695 1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
|
90
....*....|
gi 81876818 778 HLYVCSICQV 787
Cdd:smart00695 79 PIPRKVVCQG 88
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
535-684 |
2.41e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 97.05 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 535 WGPVVTLEDCLAAFFAADELKGdnmYSCERCKklrngvkyCKVLCLPEILCVHLKRFR-HEVMYSFKVSSHVSFPlegld 613
Cdd:cd02662 92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 614 lrpflakECTSQVTtYDLLSVICHHGTAGSGHYIAY--------------------CQNVINGQWYEFDDQYVTEVHE-T 672
Cdd:cd02662 156 -------ERLPKVL-YRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSEsE 227
|
170
....*....|..
gi 81876818 673 VVQNVEAYVLFY 684
Cdd:cd02662 228 VLEQKSAYMLFY 239
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
445-685 |
2.05e-21 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 96.41 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 445 SVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPgkedlaklhsaiyqnvpakpgacgdsyssqgwlafiveyirr 524
Cdd:cd02664 97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------------------------------------ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 525 fvvsctpswfwgpvvTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFR------------ 592
Cdd:cd02664 135 ---------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydqkthvrekim 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 593 HEVMY----SFKVSSHVSFPLEGLDLRPFLAKECTSQVTT---YDLLSVICHHGTAG-SGHYIAYCQNV----------- 653
Cdd:cd02664 200 DNVSInevlSLPVRVESKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSGYSSeSGHYFTYARDQtdadstgqecp 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 81876818 654 ---------INGQWYEFDDQYVTEVHETVVQNVE-------AYVLFYR 685
Cdd:cd02664 280 epkdaeendESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
819-891 |
2.81e-20 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 85.88 E-value: 2.81e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81876818 819 IYCISMHWFREWEAFVKGKdSEPPGPIDNSRIAQVKGSGHI--QLKQGADCGQISEETWTYLSSLYGGGPEIAIR 891
Cdd:pfam06337 4 VYLISSKWLNKWKSYVKEP-NNEPGPIDNSDLLDDESNGQLkpNLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
540-671 |
6.74e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 89.16 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 540 TLEDCLAAFFAADELKGDNMYSCERcKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYS--FKVSSHVSFPLEgLDLRPF 617
Cdd:COG5077 339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDmmVKINDRYEFPLE-IDLLPF 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 81876818 618 L---AKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHE 671
Cdd:COG5077 417 LdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATE 473
|
|
| DUSP |
pfam06337 |
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
712-782 |
4.49e-15 |
|
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.
Pssm-ID: 399383 Cd Length: 80 Bit Score: 70.86 E-value: 4.49e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81876818 712 FYVSREWLNKFNTFAE-----PGPITNHTFLC--SHGGIPPNKYHYIDdlVVILPQSVWEHLYSRFGGGPAVNHLYVC 782
Cdd:pfam06337 5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLDdeSNGQLKPNLQEGVD--YVIVPEEVWEFLVEWYGGGPEIKRNVVN 80
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
30-90 |
5.50e-15 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 69.98 E-value: 5.50e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81876818 30 CQSCGVAGpNLWACLqvTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFRVWCYACEREV 90
Cdd:pfam02148 1 CSLCGNTS-NLWLCL--TCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
447-685 |
7.68e-15 |
|
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: 76.59 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 447 ISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIyqnvpakpgacgdsyssqgwlafivEYIRrfv 526
Cdd:cd02658 126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGEL-------------------------VYEP--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 527 vsctpswfwgpvVTLEDCLAAFFAADELKgdnmYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMY-SFKVSSHV 605
Cdd:cd02658 178 ------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 606 SFPLEgldLRPflAKectsqvttYDLLSVICHHGT-AGSGHYIAYCQNVIN--GQWYEFDDQYVtevheTVVQNVE---- 678
Cdd:cd02658 242 DVPEE---LGP--GK--------YELIAFISHKGTsVHSGHYVAHIKKEIDgeGKWVLFNDEKV-----VASQDPPemkk 303
|
....*...
gi 81876818 679 -AYVLFYR 685
Cdd:cd02658 304 lGYIYFYQ 311
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
442-685 |
7.82e-15 |
|
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: 76.86 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 442 SYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGAcgdsyssqgwlafivey 521
Cdd:cd02671 118 NIQELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKTEMK----------------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 522 irrfvvsctpswfwgpvvTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRF--RHEVMYSF 599
Cdd:cd02671 181 ------------------TLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFaaNGSEFDCY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 600 KVSSHVSFPLegldLRPF---LAKECTSQVT-TYDLLSVICHHG-TAGSGHYIAYCqnvingQWYEFDDQYVTEVHE--- 671
Cdd:cd02671 243 GGLSKVNTPL----LTPLklsLEEWSTKPKNdVYRLFAVVMHSGaTISSGHYTAYV------RWLLFDDSEVKVTEEkdf 312
|
250 260
....*....|....*....|
gi 81876818 672 ------TVVQNVEAYVLFYR 685
Cdd:cd02671 313 lealspNTSSTSTPYLLFYK 332
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
580-685 |
4.78e-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: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 580 LPEILCVHLKRF--RHEVMYSFKVSSHVSFPLEgLDLRPFLakeCTSQVttYDLLSVICHHG-TAGSGHYIAYCQNVING 656
Cdd:cd02657 196 LPKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDG 269
|
90 100 110
....*....|....*....|....*....|....*....
gi 81876818 657 QWYEFDDQYVTEVHEtvvQNVE----------AYVLFYR 685
Cdd:cd02657 270 KWIKFDDDKVSEVTE---EDILklsgggdwhiAYILLYK 305
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
144-292 |
1.79e-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 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: 69.54 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 144 LTGMKNLGNSCYMNAALQALSNCPPLTQ--FFLECGGLVRTDKKPALCKSYQKLISEvwHKKRPsyvvPTSLSHGIKLVN 221
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHglKHLVSLISSVEQLQSSFLLNPEKYNDE--LANQA----PRRLLNALREVN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81876818 222 PMFRGYAQQDTQEFLRCLMDQLHEELKEPMVAAVAALTDARDSDSsdTDERRDGDRSPS----EDEFLSCDSSSD 292
Cdd:cd02671 98 PMYEGYLQHDAQEVLQCILGNIQELVEKDFQGQLVLRTRCLECET--FTERREDFQDISvpvqESELSKSEESSE 170
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
580-686 |
2.54e-12 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 68.29 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 580 LPEILCVHLKRFRHEVMYSfKVSSHVSFPLEgLDLRpFLAKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQnvINGQWY 659
Cdd:COG5533 179 LPKILTIQLKRFANLGGNQ-KIDTEVDEKFE-LPVK-HDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK--KGGKWE 253
|
90 100 110
....*....|....*....|....*....|
gi 81876818 660 EFDDQYVTEVHETVVQNV---EAYVLFYRK 686
Cdd:COG5533 254 KANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
537-685 |
3.82e-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 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: 69.27 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 537 PVVTLEDCLAAFFAadelkgdnmyscERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEGLDLRP 616
Cdd:cd02669 301 PQVPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSD 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81876818 617 FLAKECTSQ--VTTYDLLSVICHHGT-AGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFYR 685
Cdd:cd02669 369 YVHFDKPSLnlSTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
146-243 |
5.24e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 64.33 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 146 GMKNLGNSCYMNAALQALSNCPPLTQFFLEcgglvrtdkKPALcksyqkLISEVWHKKrpsyvvptslshgiklvnPMFR 225
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------TPKE------LFSQVCRKA------------------PQFK 47
|
90
....*....|....*...
gi 81876818 226 GYAQQDTQEFLRCLMDQL 243
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL 65
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
146-248 |
1.54e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 63.50 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 146 GMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKK-PALC------KSYQKLISEVWHKKRPSYVVPTSLSHGIK 218
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVdPANDlncqliKLADGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 81876818 219 ------LV---NPMFRGYAQQDTQEFLRCLMDQLHEELK 248
Cdd:cd02658 81 psmfkaLIgkgHPEFSTMRQQDALEFLLHLIDKLDRESF 119
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
146-248 |
4.13e-08 |
|
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: 55.80 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 146 GMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPA--LCKSYQKLISEVWHKKRPsyVVPTSLSHGIKLVNPM 223
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
|
90 100 110
....*....|....*....|....*....|.
gi 81876818 224 F------RGYAQQDTQEFLRCLMDQLHEELK 248
Cdd:cd02657 79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLP 109
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
146-244 |
5.56e-08 |
|
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: 55.58 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 146 GMKNLGNSCYMNAALQALSNCpplTQFFLECGGLVRTDKKP--ALCKSYQKLISEVWHKKRPSYVVPTSLSHGIKlvNPM 223
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMA---KDFRRQVLSLNLPRLGDsqSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR--PPW 75
|
90 100
....*....|....*....|.
gi 81876818 224 FRGYAQQDTQEFLRCLMDQLH 244
Cdd:cd02664 76 FTPGSQQDCSEYLRYLLDRLH 96
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
562-684 |
2.05e-07 |
|
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: 53.29 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 562 CERCKKLRNGVKYCKVLCLPEI----LCVHLKRF-------RHEVMYSFKVSSHVSFPLEgldLRPFLAKECTSQ-VTTY 629
Cdd:cd02672 137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI---DHDKLVKNRGQEsIYKY 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81876818 630 DLLSVICH--HGTAGsGHY----IAYCQNVINGQWYEFDDQYVTEVHETvvqnveAYVLFY 684
Cdd:cd02672 214 ELVGYVCEinDSSRG-QHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
539-684 |
3.36e-07 |
|
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: 52.53 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 539 VTLEDCLAAFFAADELKGDnmysCERCKKlRNGVKYCKVLCLPEILCVHLKRFRhevmYSFKVSSHVSfpleglDLRPFL 618
Cdd:cd02673 110 DIDELLISNFKTWSPIEKD----CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDYLK------KNEEIM 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81876818 619 aKECTSQVTTYDLLSVICHHG-TAGSGHYIAYCQNVING-QWYEFDDQYVTEVHE-TVVQNV--EAYVLFY 684
Cdd:cd02673 175 -KKYCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNGsSWLYCSDDEIRPVSKnDVSTNArsSGYLIFY 244
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
39-247 |
4.88e-07 |
|
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: 53.09 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 39 NLWACLqVTCPYV-GCGESfaDHSSIHAQVKKHNLTVNLTTFRVWCYACEREVF---LEQrLAVHLASSSARLSEQDSPP 114
Cdd:cd02669 27 NVYACL-VCGKYFqGRGKG--SHAYTHSLEDNHHVFLNLETLKFYCLPDNYEIIdssLDD-IKYVLNPTYTKEQISDLDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 115 PSHPLKAVpiavadegesesEDDDLKPrGLTGMKNLGNSCYMNAALQALSNCPPLTQFFL-ECGGLVRTDKKPALCKSYQ 193
Cdd:cd02669 103 DPKLSRDL------------DGKPYLP-GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDRKSELVKRLS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 81876818 194 KLISEVWHKKR-PSYVVPTSLSHGIKLV-NPMFRGYAQQDTQEFLRCLMDQLHEEL 247
Cdd:cd02669 170 ELIRKIWNPRNfKGHVSPHELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTLHKDL 225
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
629-674 |
5.38e-07 |
|
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: 52.88 E-value: 5.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 81876818 629 YDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVV 674
Cdd:cd02666 281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
146-243 |
7.30e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 51.73 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 146 GMKNLGNSCYMNAALQALS-NCPPLTQFFLECGGLVRT-------DKKPALCKSYQKLISEVWhkkrpsyvvpTSLSHGI 217
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALW----------SSKEHKV 70
|
90 100
....*....|....*....|....*.
gi 81876818 218 KLVNPMfrgYAQQDTQEFLRCLMDQL 243
Cdd:COG5533 71 GWIPPM---GSQEDAHELLGKLLDEL 93
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
562-663 |
1.33e-06 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 51.12 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 562 CERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEvmYSFKVSSHVSFPLEgLDLRPFLAKECTSQVTTYDLLSVICH-HGT 640
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
|
90 100 110
....*....|....*....|....*....|
gi 81876818 641 AGSGHYIAYC-------QNVINGQWYEFDD 663
Cdd:pfam13423 273 GTSGHLVSFVkvadselEDPTESQWYLFND 302
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
146-172 |
2.32e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 46.98 E-value: 2.32e-05
10 20
....*....|....*....|....*..
gi 81876818 146 GMKNLGNSCYMNAALQALSNCPPLTQF 172
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY 27
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
580-684 |
2.76e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 46.40 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 580 LPEILCVHLKRFRHEVMYSFKVSSHVSFPlegldlrpflakECTSQVTtYDLLSVICHHGTAGSGHYIAYCQNVINGQWY 659
Cdd:cd02665 128 LPPVLTFELSRFEFNQGRPEKIHDKLEFP------------QIIQQVP-YELHAVLVHEGQANAGHYWAYIYKQSRQEWE 194
|
90 100 110
....*....|....*....|....*....|...
gi 81876818 660 EFDDQYVTEVHETVVQ--------NVEAYVLFY 684
Cdd:cd02665 195 KYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
29-81 |
6.60e-05 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 41.20 E-value: 6.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 81876818 29 TCQSCGVAGpNLWACLqvTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFRV 81
Cdd:smart00290 1 RCSVCGTIE-NLWLCL--TCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
531-685 |
8.90e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 45.21 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 531 PSWFWGPVVTLEDCLAAFFAADELKGdnmyscerckklrngvkyckvlcLPEILCVHLKRFRHEVMYSFKVSSHVsFPLE 610
Cdd:cd02670 72 PDDDDGGGITLEQCLEQYFNNSVFAK-----------------------APSCLIICLKRYGKTEGKAQKMFKKI-LIPD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81876818 611 GLDLRPFLA----------KECTSQVTTYD-----------LLSVICHHGTA-GSGHYIAY-----------CQNVINGQ 657
Cdd:cd02670 128 EIDIPDFVAddpracskcqLECRVCYDDKDfsptcgkfklsLCSAVCHRGTSlETGHYVAFvrygsysltetDNEAYNAQ 207
|
170 180 190
....*....|....*....|....*....|....*
gi 81876818 658 WYEFDD-------QYVTEVHETVVQNvEAYVLFYR 685
Cdd:cd02670 208 WVFFDDmadrdgvSNGFNIPAARLLE-DPYMLFYQ 241
|
|
| |
