|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
158-489 |
7.70e-162 |
|
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: 461.46 E-value: 7.70e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 158 RGLLNLGATCFMNCIVQALVHTPLLSDYFMSDRH--DCGSKSSHKCLVCEVSRLFQEF-YSGSRSPLSLHRLLHLIWNHA 234
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 235 KHLAGYEQQDAHEFFIATLDVLHRHCVKAKAEhesksnssgsgsgtnssnsssSHCYGQCNCIIDQIFTGMLQSDVVCQA 314
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNE---------------------ANDESHCNCIIHQTFSGSLQSSVTCQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 315 CNGVSTTYDPFWDISLDLGETTTH-------GGVTPKTLIDCLERYTRAEHLGSAAkIKCSTCKSYQESTKQFSLRTLPS 387
Cdd:cd02660 140 CGGVSTTVDPFLDLSLDIPNKSTPswalgesGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 388 VVSFHLKRFEHSA-LIDRKISSFIQFPVEFDMTPFMS-------EKKNAYGDFRFSLYAVVNHVGTIDTGHYTAYVRHQK 459
Cdd:cd02660 219 VLCFQLKRFEHSLnKTSRKIDTYVQFPLELNMTPYTSssigdtqDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGD 298
|
330 340 350
....*....|....*....|....*....|
gi 665410545 460 DTWVKCDDHVITMASLKQVLDSEGYLLFYH 489
Cdd:cd02660 299 GQWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
158-488 |
9.82e-75 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 238.11 E-value: 9.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 158 RGLLNLGATCFMNCIVQALVHTPLLSDYFMSDRHDCGSKSSHKC--LVCEVSRLFQEFYSGSR-SPLSLHRLLHLIWNHA 234
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 235 KHLAGYEQQDAHEFFIATLDVLHRhCVKAKAEHEsksnssgsgsgtnssnsssshcygqCNCIIDQIFTGMLQSDVVCQA 314
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE-DLNGNHSTE-------------------------NESLITDLFRGQLKSRLKCLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 315 CNGVSTTYDPFWDISLDLGETTTHGgvTPKTLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLPSVVSFHLK 394
Cdd:pfam00443 135 CGEVSETFEPFSDLSLPIPGDSAEL--KTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 395 RFEHSALIDRKISSFIQFPVEFDMTPFMSEKKNAYGDFR--FSLYAVVNHVGTIDTGHYTAYVRHQKDT-WVKCDDHVIT 471
Cdd:pfam00443 213 RFSYNRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLqdYRLVAVVVHSGSLSSGHYIAYIKAYENNrWYKFDDEKVT 292
|
330
....*....|....*...
gi 665410545 472 MASL-KQVLDSEGYLLFY 488
Cdd:pfam00443 293 EVDEeTAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
158-488 |
1.65e-66 |
|
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: 216.37 E-value: 1.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 158 RGLLNLGATCFMNCIVQALVHTPLLSDYFMSDRHDCGSKSSHKCLVCEVSRLFQEFYSGSRSPLSLHRLLHLIWNHAKHL 237
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 238 AGYEQQDAHEFFIATLDVLHRHC----VKAKAEHESKsnssgsgsgtnssnsssshcygQCNCIIDQIFTGMLQSDVVCQ 313
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKACldrfKKLKAVDPSS----------------------QETTLVQQIFGGYLRSQVKCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 314 ACNGVSTTYDPFWDISLDLgetttHGGvtpKTLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLPSVVSFHL 393
Cdd:cd02661 140 NCKHVSNTYDPFLDLSLDI-----KGA---DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 394 KRFehSALIDRKISSFIQFPVEFDMTPFMSEKKNayGDFRFSLYAVVNHVGT-IDTGHYTAYVRHQKDTWVKCDDHVITM 472
Cdd:cd02661 212 KRF--SNFRGGKINKQISFPETLDLSPYMSQPND--GPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYNMDDSKVSP 287
|
330
....*....|....*.
gi 665410545 473 ASLKQVLDSEGYLLFY 488
Cdd:cd02661 288 VSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
159-488 |
9.67e-60 |
|
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: 197.32 E-value: 9.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHtpllsdyfmsdrhdcgsksshkclvcevsrlfqefysgsrsplslhrllhliwnhakhla 238
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 239 gyEQQDAHEFFIATLDVLHRHCVKAKAEHESKSnssgsgsgtnssnsssshcygQCNCIIDQIFTGMLQSDVVCQACNGV 318
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKKSSKRTSDSS---------------------SLKSLIHDLFGGKLESTIVCLECGHE 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 319 STTYDPFWDISLDLGETTTHggvtPKTLIDCLERYTRAEHLGSAAKIKCStCKSYQESTKQFSLRTLPSVVSFHLKRFEH 398
Cdd:cd02257 78 SVSTEPELFLSLPLPVKGLP----QVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSF 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 399 SALIDR-KISSFIQFPVEFDMTPFMSEKKNAY----GDFRFSLYAVVNHVGT-IDTGHYTAYVRHQ-KDTWVKCDDHVIT 471
Cdd:cd02257 153 NEDGTKeKLNTKVSFPLELDLSPYLSEGEKDSdsdnGSYKYELVAVVVHSGTsADSGHYVAYVKDPsDGKWYKFNDDKVT 232
|
330 340
....*....|....*....|..
gi 665410545 472 MASLKQVLD-----SEGYLLFY 488
Cdd:cd02257 233 EVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
2.38e-58 |
|
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: 192.50 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHtpllsdyfmsdrhdcgsksshkclvcevsrlfqefysgsrsplslhrllhliwnhakhla 238
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 239 gyEQQDAHEFFIATLDVLHRhcvkakaehesksnssgsgsgtnssnsssshcygqcncIIDQIFTGMLQSDVVCQACNGV 318
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS--------------------------------------IIVDLFQGQLKSRLTCLTCGKT 60
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 319 STTYDPFWDISLDLGETTTHGgvTPKTLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLPSVVSFHLKRFEH 398
Cdd:cd02674 61 STTFEPFTYLSLPIPSGSGDA--PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 399 SALIDRKISSFIQFPVE-FDMTPFmSEKKNAYGDFRFSLYAVVNHVGTIDTGHYTAYVRH-QKDTWVKCDDHVITMASLK 476
Cdd:cd02674 139 SRGSTRKLTTPVTFPLNdLDLTPY-VDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNnETNDWYKFDDSRVTKVSES 217
|
330
....*....|..
gi 665410545 477 QVLDSEGYLLFY 488
Cdd:cd02674 218 SVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
2.49e-48 |
|
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: 167.95 E-value: 2.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHTPLLSDYFmsdrhdcgsKSSHKCLVCEVSRLFQEFysgsrsplslhrllhliwnhakhlA 238
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL---------SETPKELFSQVCRKAPQF------------------------K 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 239 GYEQQDAHEFFIATLDVLhrhcvkakaehesksnssgsgsgtnssnsssshcygqcNCIIDQIFTGMLQSDVVCQACNGV 318
Cdd:cd02667 48 GYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCESCGTV 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 319 STTYDPFWDISLDLGETTThggvTPKTLIDCLERYTRAEHLGSAAKIKCSTCksyQESTKQFSLRTLPSVVSFHLKRFEH 398
Cdd:cd02667 90 SLVYEPFLDLSLPRSDEIK----SECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQ 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 399 SAL-IDRKISSFIQFPVEFDMTPFMSEKKNAYGD---FRFSLYAVVNHVGTIDTGHYTAYV--RHQ-------------- 458
Cdd:cd02667 163 PRSaNLRKVSRHVSFPEILDLAPFCDPKCNSSEDkssVLYRLYGVVEHSGTMRSGHYVAYVkvRPPqqrlsdltkskpaa 242
|
330 340 350
....*....|....*....|....*....|....*.
gi 665410545 459 ------KDTWVKCDDHVITMASLKQVLDSEGYLLFY 488
Cdd:cd02667 243 deagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
156-481 |
7.72e-39 |
|
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: 143.94 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 156 GLRGLLNLGATCFMNCIVQALVHTPLLSDYFMS---DRHDCGSKSshkcLVCEVSRLFQEFYSgSRSPLSLHRLLHLI-- 230
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKS----VPLALQRLFLFLQL-SESPVKTTELTDKTrs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 231 --WnhaKHLAGYEQQDAHEFFIATLDVLHRHCVKAKAEHesksnssgsgsgtnssnsssshcygqcncIIDQIFTGMLQS 308
Cdd:cd02659 76 fgW---DSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEG-----------------------------LIKNLFGGKLVN 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 309 DVVCQACNGVSTTYDPFWDISLDlgettthggVTP-KTLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLPS 387
Cdd:cd02659 124 YIICKECPHESEREEYFLDLQVA---------VKGkKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 388 VVSFHLKRFEHSALIDR--KISSFIQFPVEFDMTPFMSE---------KKNAYGDFRFSLYAVVNHVGTIDTGHYTAYVR 456
Cdd:cd02659 195 VLTLQLKRFEFDFETMMriKINDRFEFPLELDMEPYTEKglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIK 274
|
330 340
....*....|....*....|....*.
gi 665410545 457 HQKDT-WVKCDDHVITMASLKQVLDS 481
Cdd:cd02659 275 DRDDGkWYKFNDDVVTPFDPNDAEEE 300
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
5.81e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 127.04 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHTPL---LSDYFMSdrhdcgsKSSHKCLVcevsrlfqefysGSRSPlslHRLLHLIWNHAK 235
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLltcLKDLFES-------ISEQKKRT------------GVISP---KKFITRLKRENE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 236 HLAGYEQQDAHEFFiatlDVLHRHCVK-AKAEHESKSNSSGSGSGTnssnssssHCYGQCNCIiDQIFTGMLQSDVVCQA 314
Cdd:cd02663 59 LFDNYMHQDAHEFL----NFLLNEIAEiLDAERKAEKANRKLNNNN--------NAEPQPTWV-HEIFQGILTNETRCLT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 315 CNGVSTTYDPFWDISLDLGETTThggvtpktLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLPSVVSFHLK 394
Cdd:cd02663 126 CETVSSRDETFLDLSIDVEQNTS--------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 395 RFEHSALIDR--KISSFIQFPVEfdMTPFMSEKKNAYGDFRFSLYAVVNHVG-TIDTGHYTAYVRHqKDTWVKCDDHVIT 471
Cdd:cd02663 198 RFKYDEQLNRyiKLFYRVVFPLE--LRLFNTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS-HGGWLLFDDETVE 274
|
330 340
....*....|....*....|....*
gi 665410545 472 MASLKQVLD--------SEGYLLFY 488
Cdd:cd02663 275 KIDENAVEEffgdspnqATAYVLFY 299
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
156-480 |
3.47e-29 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 121.90 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 156 GLRGLLNLGATCFMNCIVQALVHTPLLSD--YFMSDRHDCGSKSSHKCLvcevSRLFQEFYSGsRSPLSLHRLL-HLIWN 232
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALAL----QRLFYNLQTG-EEPVDTTELTrSFGWD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 233 HAKHlagYEQQDAHEFFIATLDVLHRHCVKAKAEHesksnssgsgsgtnssnsssshcygqcncIIDQIFTGMLQSDVVC 312
Cdd:COG5077 267 SDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVEN-----------------------------ALNGIFVGKMKSYIKC 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 313 QACNGVSTTYDPFWDISLDLGETtthggvtpKTLIDCLERYTRAEHLGSAAKIKCSTcKSYQESTKQFSLRTLPSVVSFH 392
Cdd:COG5077 315 VNVNYESARVEDFWDIQLNVKGM--------KNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 393 LKRFEHSALIDR--KISSFIQFPVEFDMTPFMSE--KKNAYGDFRFSLYAVVNHVGTIDTGHYTAYVRHQKDT-WVKCDD 467
Cdd:COG5077 386 LKRFEYDFERDMmvKINDRYEFPLEIDLLPFLDRdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGrWYKFDD 465
|
330
....*....|...
gi 665410545 468 HVITMASLKQVLD 480
Cdd:COG5077 466 TRVTRATEKEVLE 478
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-467 |
4.09e-29 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 117.14 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVH-TPLLSDYF-------MSDRHDCGSKSSHKCLVCE-VSRLFQEFYSGSRS---PLSLHRL 226
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMnLEFRKAVYecnstedAELKNMPPDKPHEPQTIIDqLQLIFAQLQFGNRSvvdPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 227 LHLiwnhakhlAGYEQQDAHEFFIATLDVLhrhcvKAKAEHESKSNSSGsgsgtnssnsssshcygqcncIIDQIFTGML 306
Cdd:cd02668 81 LGL--------DTGQQQDAQEFSKLFLSLL-----EAKLSKSKNPDLKN---------------------IVQDLFRGEY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 307 QSDVVCQACNGVSTTYDPFWDISLDLGETtthggvtpKTLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLP 386
Cdd:cd02668 127 SYVTQCSKCGRESSLPSKFYELELQLKGH--------KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 387 SVVSFHLKR--FEHSALIDRKISSFIQFPVEFDMTPFMSEKKNayGDFRFSLYAVVNHVGT-IDTGHYTAYVRH-QKDTW 462
Cdd:cd02668 199 PTLNFQLLRfvFDRKTGAKKKLNASISFPEILDMGEYLAESDE--GSYVYELSGVLIHQGVsAYSGHYIAHIKDeQTGEW 276
|
....*
gi 665410545 463 VKCDD 467
Cdd:cd02668 277 YKFND 281
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
322-488 |
2.43e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 113.05 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 322 YDPFWDISldlgETTTHggvTPK-TLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQFSLRTLPSVVSFHLKRFEHSA 400
Cdd:COG5560 659 YDPLWTIR----EIGAA---ERTiTLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVR 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 401 LIDRKISSFIQFPV-EFDMTPFMSEKKNAygDFRFSLYAVVNHVGTIDTGHYTAYVRHQKD-TWVKCDDHVITMASLKQV 478
Cdd:COG5560 732 SFRDKIDDLVEYPIdDLDLSGVEYMVDDP--RLIYDLYAVDNHYGGLSGGHYTAYARNFANnGWYLFDDSRITEVDPEDS 809
|
170
....*....|
gi 665410545 479 LDSEGYLLFY 488
Cdd:COG5560 810 VTSSAYVLFY 819
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
152-488 |
9.53e-26 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 107.67 E-value: 9.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 152 NQTIGLRGLLNLGATCFMNCIVQALVHTPllsdYFMSD-RHDCGSKSS--HKCLVCEvsrLFQEFYSGSRSPLSLHRLLH 228
Cdd:cd02671 19 ENLLPFVGLNNLGNTCYLNSVLQVLYFCP----GFKHGlKHLVSLISSveQLQSSFL---LNPEKYNDELANQAPRRLLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 229 LIWNHAKHLAGYEQQDAHEFFIATLDvlhrhCVKAkaehesksnssgsgsgtnssnsssshcygqcncIIDQIFTGMLQS 308
Cdd:cd02671 92 ALREVNPMYEGYLQHDAQEVLQCILG-----NIQE---------------------------------LVEKDFQGQLVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 309 DVVCQACNGVSTTYDPFWDISL-----DLGETTTHGGVTP------KTLIDCLERYTRAEHLGSAAKIKCSTCKSYQEST 377
Cdd:cd02671 134 RTRCLECETFTERREDFQDISVpvqesELSKSEESSEISPdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 378 KQFSLRTLPSVVSFHLKRFEHSALID------RKISSFIQFPveFDMTPF---MSEKKNAYGdfrfsLYAVVNHVG-TID 447
Cdd:cd02671 214 RSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTP--LKLSLEewsTKPKNDVYR-----LFAVVMHSGaTIS 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 665410545 448 TGHYTAYVRhqkdtWVKCDDHVITMASLKQVLD---------SEGYLLFY 488
Cdd:cd02671 287 SGHYTAYVR-----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
133-338 |
4.80e-25 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 109.20 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 133 TTKETNLLLANARRRLVRPNQTIGLRGLLNLGATCFMNCIVQALVHTPLLSDYFMSDRH-DCGSKSSHKCLVCEVSRLF- 210
Cdd:COG5560 241 TRNPDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYeESINEENPLGMHGSVASAYa 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 211 ---QEFYSGSRSPLSLHRLLHLIWNHAKHLAGYEQQDAHEFFIATLDVLH----RHCVKAKAEHESKSNSSGSGSGTNSS 283
Cdd:COG5560 321 dliKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHedlnRIIKKPYTSKPDLSPGDDVVVKKKAK 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 665410545 284 NSSSSHCYGQCNcIIDQIFTGMLQSDVVCQACNGVSTTYDPFWDISLDLGETTTH 338
Cdd:COG5560 401 ECWWEHLKRNDS-IITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVW 454
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
159-490 |
4.08e-23 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 99.11 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALV-HTPLLSDYFMSDrhdcgSKSShkclvcevsRLFQEFYSGSRSPLSLHRLLHL---IWNHA 234
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDL-----SKEL---------KVLKNVIRKPEPDLNQEEALKLftaLWSSK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 235 KHLAG-----YEQQDAHEFFIATLDVLHrhcvkakaehesksnssgsgsgtnssnsssshcygqcnciIDQIFTGMLQSD 309
Cdd:COG5533 67 EHKVGwippmGSQEDAHELLGKLLDELK----------------------------------------LDLVNSFTIRIF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 310 VVCQacNGVSTTYDPFWDISLDLGETTTHGGVtpKTLIDCLERYtraEHLGSAAK-IKCSTCKSYQESTKQ---FSLRTL 385
Cdd:COG5533 107 KTTK--DKKKTSTGDWFDIIIELPDQTWVNNL--KTLQEFIDNM---EELVDDETgVKAKENEELEVQAKQeyeVSFVKL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 386 PSVVSFHLKRFEHSaLIDRKISSFIQFPveFDMTPFMSEKKNAYGDFRFSLYAVVNHVGTIDTGHYTAYVRhQKDTWVKC 465
Cdd:COG5533 180 PKILTIQLKRFANL-GGNQKIDTEVDEK--FELPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK-KGGKWEKA 255
|
330 340
....*....|....*....|....*...
gi 665410545 466 DDHVITMASLKQVLDS---EGYLLFYHK 490
Cdd:COG5533 256 NDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
6.03e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 96.24 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHTPLLSDYFMSDRH--DCGSKSSHKCLVCEVSRLFQEFYSGSRSPLSLHRLLHLIWNHA-- 234
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENkfPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLKSENDPYQVGik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 235 ----KHLAGY--------EQQDAHEFFIATLDVLHRHCVKAkaehesksnssgsgsgtnssnsssshcyGQCNciIDQIF 302
Cdd:cd02658 81 psmfKALIGKghpefstmRQQDALEFLLHLIDKLDRESFKN----------------------------LGLN--PNDLF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 303 TGMLQSDVVCQACNGVSTTYDPFWDISLDL---------GETTTHGGVTpktLIDCLERYTRAEHLgsaaKIKCSTCKSY 373
Cdd:cd02658 131 KFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeEGELVYEPVP---LEDCLKAYFAPETI----EDFCSTCKEK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 374 QESTKQFSLRTLPSVVSFHLKRFEhsALID---RKISSFIQFPVEFdmtpfmsekknayGDFRFSLYAVVNHVGT-IDTG 449
Cdd:cd02658 204 TTATKTTGFKTFPDYLVINMKRFQ--LLENwvpKKLDVPIDVPEEL-------------GPGKYELIAFISHKGTsVHSG 268
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 665410545 450 HYTAYVR---HQKDTWVKCDDHVITMASLKQVLDSEGYLLFY 488
Cdd:cd02658 269 HYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
54-488 |
2.61e-16 |
|
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: 80.83 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 54 IQLYACLHC-IYFGCRG--AHITSHLRSKKHNVALELSHGTLYCYAcrdfiydarsREYALINRKLEakdlqkSIGWV-- 128
Cdd:cd02669 26 LNVYACLVCgKYFQGRGkgSHAYTHSLEDNHHVFLNLETLKFYCLP----------DNYEIIDSSLD------DIKYVln 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 129 PwVPTTKETNLLLANA--RRRLVRPNQTIGLRGLLNLGATCFMNCIVQALVHTPLLSDYFMSDRHDCGSKSSHKCLVCEV 206
Cdd:cd02669 90 P-TYTKEQISDLDRDPklSRDLDGKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 207 SRLFQEFYSGS--RSPLSLHRLLHLIWNHAKHLAGYEQQ-DAHEFFIATLDVLHRHCVKAKAEHESksnssgsgsgtnss 283
Cdd:cd02669 169 SELIRKIWNPRnfKGHVSPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGSKKPNSS-------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 284 nsssshcygqcncIIDQIFTGMLQ---------SDVVCQACNGVSTTYD------PFWDISLDLGETTTHGGVTPKTLI- 347
Cdd:cd02669 235 -------------IIHDCFQGKVQietqkikphAEEEGSKDKFFKDSRVkktsvsPFLLLTLDLPPPPLFKDGNEENIIp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 348 -----DCLERYTRaehlgsaakikcSTCKSYQESTKQFSLRTLPSVVSFHLKRFEHSALIDRKISSFIQFPVE-FDMTPF 421
Cdd:cd02669 302 qvplkQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDY 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 422 MSEKKNAYGDF-RFSLYAVVNHVGTIDT-GHYTAYVRHQK-DTWVKCDDHVITMASLKQVLDSEGYLLFY 488
Cdd:cd02669 370 VHFDKPSLNLStKYNLVANIVHEGTPQEdGTWRVQLRHKStNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
3.62e-16 |
|
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: 77.79 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHTPLLSDYfmsdrhdcgsksshkclvcevsrlfqefysgsrsplsLHRLLhliwnhakhla 238
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY-------------------------------------LEEFL----------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 239 gyEQQDAHEFFIATLDVLHRHCVkakaehesksnssgsgsgtnssnsssshcygqcnciidQIFTGMLQSDVVCQACNGV 318
Cdd:cd02662 33 --EQQDAHELFQVLLETLEQLLK--------------------------------------FPFDGLLASRIVCLQCGES 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 319 ST-TYDPFWDISLDLGEtttHGGVTPKTLIDCLERYTRAEHLGSAAKIKCSTcksyqestkqfSLRTLPSVVSFHLKRFE 397
Cdd:cd02662 73 SKvRYESFTMLSLPVPN---QSSGSGTTLEHCLDDFLSTEIIDDYKCDRCQT-----------VIVRLPQILCIHLSRSV 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 398 HSALID-RKISSFIQFPVEFDmtpfmsekknaygDFRFSLYAVVNHVGTIDTGHYTAYVRH------------------- 457
Cdd:cd02662 139 FDGRGTsTKNSCKVSFPERLP-------------KVLYRLRAVVVHYGSHSSGHYVCYRRKplfskdkepgsfvrmregp 205
|
330 340 350
....*....|....*....|....*....|....
gi 665410545 458 --QKDTWVKCDDHVITMASLKQVL-DSEGYLLFY 488
Cdd:cd02662 206 ssTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
6.84e-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 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: 75.45 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVHTPLLSD---YFMSDRHdcGSKSSHKCLVCEVSRLFQEFYSGSRS--PLSLHRLLHLiwnH 233
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPvpPIEFLQLLRM---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 234 AKHLA------GYEQQDAHEFFIATLDVLhRHCVKAKAEHESKsnssgsgsgtnssnsssshcygqcnciIDQIFTGMLQ 307
Cdd:cd02657 76 FPQFAekqnqgGYAQQDAEECWSQLLSVL-SQKLPGAGSKGSF---------------------------IDQLFGIELE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 308 SDVVCQAC-NGVSTTYDPFWDISLDLGETTT----HGGVTpKTLIDCLERytRAEHLGSAAKikcstcksYQEsTKQFSl 382
Cdd:cd02657 128 TKMKCTESpDEEEVSTESEYKLQCHISITTEvnylQDGLK-KGLEEEIEK--HSPTLGRDAI--------YTK-TSRIS- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 383 rTLPSVVSFHLKRFEHSALIDR--KISSFIQFPVEFDMTPFMSEKKNaygdfrFSLYAVVNHVG-TIDTGHYTAYVRH-Q 458
Cdd:cd02657 195 -RLPKYLTVQFVRFFWKRDIQKkaKILRKVKFPFELDLYELCTPSGY------YELVAVITHQGrSADSGHYVAWVRRkN 267
|
330 340 350
....*....|....*....|....*....|....*..
gi 665410545 459 KDTWVKCDDHVITMASLKQVLDSEG-------YLLFY 488
Cdd:cd02657 268 DGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-487 |
3.60e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 70.60 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALvhtpllsdyFMSdrhdcgsksSHKCLvcEVSRLFQEFYSGSRSPLSLHRLLHLIWNHAKHLA 238
Cdd:cd02664 1 GLINLGNTCYMNSVLQAL---------FMA---------KDFRR--QVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 239 GY-----------------EQQDAHEFFIATLDVLHrhcvkakaehesksnssgsgsgtnssnsssshcygqcnCIIDQI 301
Cdd:cd02664 61 EAppdyfleasrppwftpgSQQDCSEYLRYLLDRLH--------------------------------------TLIEKM 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 302 FTGMLQSDVVCQACNGVSTTYD--PFWDISLDLgettthggvtpktLIDCLERYTRAEHLGSAAKIKCSTCKSYQESTKQ 379
Cdd:cd02664 103 FGGKLSTTIRCLNCNSTSARTErfRDLDLSFPS-------------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 380 FSLRTLPSVVSFHLKRFE-------HSALIDR-KISSFIQFPVEFDMTPFMSEKKNAYGDFR-----------FSLYAVV 440
Cdd:cd02664 170 MKVTGAPEYLILTLLRFSydqkthvREKIMDNvSINEVLSLPVRVESKSSESPLEKKEEESGddgelvtrqvhYRLYAVV 249
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 665410545 441 NHVGT-IDTGHYTAYVRHQKDTwVKCDDHVITMASLKQVLDSEGYLLF 487
Cdd:cd02664 250 VHSGYsSESGHYFTYARDQTDA-DSTGQECPEPKDAEENDESKNWYLF 296
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
46-103 |
1.12e-09 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 54.19 E-value: 1.12e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410545 46 CFECGSYGiQLYACLHCIYFGC---RGAHITSHLRSKKHNVALELSHGTLYCYACRDFIYD 103
Cdd:pfam02148 1 CSLCGNTS-NLWLCLTCGHVGCgryQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHD 60
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
344-488 |
1.22e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 58.34 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 344 KTLIDCLERYT---RAEHLGSAAKIKCSTCKSYQEstkqfslrtLPSVVSFHLKRFEHSALIDRKISSFIQFPVEFDMTP 420
Cdd:cd02665 93 GNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQIIQQVP 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410545 421 FmsekknaygdfrfSLYAVVNHVGTIDTGHYTAYV-RHQKDTWVKCDDHVITMASLKQVL-DSEG-------YLLFY 488
Cdd:cd02665 164 Y-------------ELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVErDSFGggrnpsaYCLMY 227
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
311-488 |
2.13e-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 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: 54.84 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 311 VCQACNGVSTTYDPFWDISLDLGETTthgGVTPKTLIDCLERYTRAEHlgsaakiKCSTCKsYQESTKQFSLRTLPSVVS 390
Cdd:cd02673 83 VCIGCSFEENVSDVGNFLDVSMIDNK---LDIDELLISNFKTWSPIEK-------DCSSCK-CESAISSERIMTFPECLS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 391 FHLKRF--EHSALIDRKISSFIqfpvefdMTPFMSEKKNaygdfrFSLYAVVNHVG-TIDTGHYTAYVR--HQKDTWVKC 465
Cdd:cd02673 152 INLKRYklRIATSDYLKKNEEI-------MKKYCGTDAK------YSLVAVICHLGeSPYDGHYIAYTKelYNGSSWLYC 218
|
170 180
....*....|....*....|....*.
gi 665410545 466 DDHVITMASLKQVLD---SEGYLLFY 488
Cdd:cd02673 219 SDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
340-488 |
3.38e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 51.37 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 340 GVTPKTLIDCLERYTRaehlgsaakikcstcksyqesTKQFSLRtlPSVVSFHLKRFEHSALIDRKISSFIQFPVEFDMT 419
Cdd:cd02670 76 DGGGITLEQCLEQYFN---------------------NSVFAKA--PSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 420 PFM-----------SEKKNAY---------GDFRFSLYAVVNHVGT-IDTGHYTAYVRHQKDT------------WVKCD 466
Cdd:cd02670 133 DFVaddpracskcqLECRVCYddkdfsptcGKFKLSLCSAVCHRGTsLETGHYVAFVRYGSYSltetdneaynaqWVFFD 212
|
170 180 190
....*....|....*....|....*....|..
gi 665410545 467 DhvitMASLKQVLD----------SEGYLLFY 488
Cdd:cd02670 213 D----MADRDGVSNgfnipaarllEDPYMLFY 240
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
159-488 |
4.61e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 48.64 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 159 GLLNLGATCFMNCIVQALVH-TPL-------------LSDYFMSDRHDCGSKSSHKCL------VCEVSRLFQEF-YSGS 217
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTiKPLrdlvlnfdeskaeLASDYPTERRIGGREVSRSELqrsnqfVYELRSLFNDLiHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 218 RSPLSLHRLLHLIWNhakhlagyeQQDAHEFFIATLDVLhRHCVKAKAEHESKSNSSGSgsgtnssnsssshcyGQCNCI 297
Cdd:cd02666 83 RSVTPSKELAYLALR---------QQDVTECIDNVLFQL-EVALEPISNAFAGPDTEDD---------------KEQSDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 298 IDQIFTGML-QSDVVCQACNGVSTT--YDPFWDISLDLGETTTHGGVT--PKTLIDCLERYTRAEHLGSAAKIKCSTCKS 372
Cdd:cd02666 138 IKRLFSGKTkQQLVPESMGNQPSVRtkTERFLSLLVDVGKKGREIVVLlePKDLYDALDRYFDYDSLTKLPQRSQVQAQL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410545 373 YQESTKQF---SLRTLPSVVSfHLKRFEHSALIDRKISSFIQFPVEFDMTPFMSEKKNAYGDFRFSLYAVVNHVGTIDTG 449
Cdd:cd02666 218 AQPLQRELismDRYELPSSID-DIDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEASSG 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 665410545 450 HYTAYVR-HQKDTWVKCDDHVITMA-SLKQVLDSEG-----YLLFY 488
Cdd:cd02666 297 HYWVYIKdFEENVWRKYNDETVTVVpASEVFLFTLGntatpYFLVY 342
|
|
| |
