|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
181-523 |
7.59e-139 |
|
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: 409.84 E-value: 7.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 181 RGLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSLEDCkrRTTERLCLICDINTVFSAM-YSGDRNPYSPAQFLYSWWQ 259
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCL--SCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 260 HSANLASYEQQDAHEFFISMLDAIHEKEGITKNGSkGNGGDCQCIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISlnL 339
Cdd:cd02660 79 HSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA-NDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLS--L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 340 DINISLTEKGKKLTKQNADdnMSTLLGCLDLFTRPEKLGSDQkLYCQNCKERQNALKQMSISKLPLVLTLHVKRFEHSfV 419
Cdd:cd02660 156 DIPNKSTPSWALGESGVSG--TPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 420 KKLSRKIDRYLQFPFSLDMTPYLSSSILRAKYGNrifnfggdESDTFSKFEIFAVVTHSGTLESGHYVTFVRLRK-QWYR 498
Cdd:cd02660 232 NKTSRKIDTYVQFPLELNMTPYTSSSIGDTQDSN--------SLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDgQWFK 303
|
330 340
....*....|....*....|....*
gi 657400764 499 CDDAWITKVDEATVRASQCYMIFYV 523
Cdd:cd02660 304 FDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
181-522 |
8.73e-78 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 251.21 E-value: 8.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 181 RGLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSLEDCKRRTTerLCLICDINTVFSAMYSGDRN-PYSPAQFLYSWWQ 259
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKD--INLLCALRDLFKALQKNSKSsSVSPKMFKKSLGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 260 HSANLASYEQQDAHEFFISMLDAIHEKegitknGSKGNGGDCQCIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISLNL 339
Cdd:pfam00443 79 LNPDFSGYKQQDAQEFLLFLLDGLHED------LNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 340 DINISLTEKgkkltkqnaddnmSTLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFEHSfv 419
Cdd:pfam00443 153 PGDSAELKT-------------ASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 420 KKLSRKIDRYLQFPFSLDMTPYLSSSILrakygnrifnfggDESDTFSKFEIFAVVTHSGTLESGHYVTFVR--LRKQWY 497
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLAEELK-------------PKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKayENNRWY 284
|
330 340
....*....|....*....|....*.
gi 657400764 498 RCDDAWITKVDEAT-VRASQCYMIFY 522
Cdd:pfam00443 285 KFDDEKVTEVDEETaVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
181-523 |
1.64e-73 |
|
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: 239.48 E-value: 1.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 181 RGLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSLeDCKRrttERLCLICDINTVFSAMYSGDRNPYSPAQFLYSWWQH 260
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSK-DCCN---EGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 261 SANLASYEQQDAHEFFISMLDAIHE-------KEGITKNGSKGNGgdcqcIAHRVFYGQLRSEVTCMACGFTSTTYDPFL 333
Cdd:cd02661 78 SKHFRIGRQEDAHEFLRYLLDAMQKacldrfkKLKAVDPSSQETT-----LVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 334 DISLnlDINisltekgkkltkqnaddNMSTLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKR 413
Cdd:cd02661 153 DLSL--DIK-----------------GADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 414 FEHSFvkklSRKIDRYLQFPFSLDMTPYLSSSilrakygnrifnfgGDESDtfsKFEIFAVVTHSGT-LESGHYVTFVR- 491
Cdd:cd02661 214 FSNFR----GGKINKQISFPETLDLSPYMSQP--------------NDGPL---KYKLYAVLVHSGFsPHSGHYYCYVKs 272
|
330 340 350
....*....|....*....|....*....|..
gi 657400764 492 LRKQWYRCDDAWITKVDEATVRASQCYMIFYV 523
Cdd:cd02661 273 SNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
182-523 |
1.26e-58 |
|
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: 198.48 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHappfrdyflsgghsledckrrtterlclicdintvfsamysgdrnpyspaqflyswwqhs 261
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 262 anlasyEQQDAHEFFISMLDAIHEKEGITKNGSKgNGGDCQCIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISLNLDI 341
Cdd:cd02257 21 ------EQQDAHEFLLFLLDKLHEELKKSSKRTS-DSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 342 NisltekgkkltkqnaDDNMSTLLGCLDLFTRPEKLGSDQKLYCqNCKERQNALKQMSISKLPLVLTLHVKRFEHSFVKK 421
Cdd:cd02257 94 K---------------GLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGT 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 422 lSRKIDRYLQFPFSLDMTPYLSSSilrakygnrifNFGGDESDTFSKFEIFAVVTHSGTL-ESGHYVTFVR--LRKQWYR 498
Cdd:cd02257 158 -KEKLNTKVSFPLELDLSPYLSEG-----------EKDSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKdpSDGKWYK 225
|
330 340 350
....*....|....*....|....*....|
gi 657400764 499 CDDAWITKVDEATV-----RASQCYMIFYV 523
Cdd:cd02257 226 FNDDKVTEVSEEEVlefgsLSSSAYILFYE 255
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
7.04e-54 |
|
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: 184.80 E-value: 7.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHappfrdyflsgghsledckrrtterlclicdintvfsamysgdrnpyspaqflyswwqhs 261
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 262 anlasyEQQDAHEFFISMLDAIHEkegitkngskgnggdcqcIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISLNLDi 341
Cdd:cd02674 21 ------DQQDAQEFLLFLLDGLHS------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP- 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 342 nisltEKGKKLTKQnaddnmsTLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFEHSFVKK 421
Cdd:cd02674 76 -----SGSGDAPKV-------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 422 lsRKIDRYLQFPFS-LDMTPYLSSSILRakygnrifnfggdesdTFSKFEIFAVVTHSGTLESGHYVTFVR--LRKQWYR 498
Cdd:cd02674 144 --RKLTTPVTFPLNdLDLTPYVDTRSFT----------------GPFKYDLYAVVNHYGSLNGGHYTAYCKnnETNDWYK 205
|
330 340
....*....|....*....|....
gi 657400764 499 CDDAWITKVDEATVRASQCYMIFY 522
Cdd:cd02674 206 FDDSRVTKVSESSVVSSSAYILFY 229
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
179-526 |
1.60e-53 |
|
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: 187.08 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 179 GLRGLNSLGSTCFMNSVLQALLHAPPFRDYFLSgghslEDCKRRTTERLCLICDINTVFSAMYSGDR--NPYSPAQFLYS 256
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYS-----IPPTEDDDDNKSVPLALQRLFLFLQLSESpvKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 257 -WWQhsaNLASYEQQDAHEFFISMLDAIHEKegitkngSKGNGGDcQCIAhRVFYGQLRSEVTCMACGFTSTTYDPFLDI 335
Cdd:cd02659 76 fGWD---SLNTFEQHDVQEFFRVLFDKLEEK-------LKGTGQE-GLIK-NLFGGKLVNYIICKECPHESEREEYFLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 336 SLNldinisltekgkkltkqnaDDNMSTLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFE 415
Cdd:cd02659 144 QVA-------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 416 HSFVKKLSRKIDRYLQFPFSLDMTPYLSSSILRAKYGNRifnfgGDESDTfSKFEIFAVVTHSGTLESGHYVTFVRLRK- 494
Cdd:cd02659 205 FDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGDSE-----KKDSES-YIYELHGVLVHSGDAHGGHYYSYIKDRDd 278
|
330 340 350
....*....|....*....|....*....|...
gi 657400764 495 -QWYRCDDAWITKVDEATVrASQCYMIFYVQKT 526
Cdd:cd02659 279 gKWYKFNDDVVTPFDPNDA-EEECFGGEETQKT 310
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
1.11e-47 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 169.49 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYFlsgghsledcKRRTTERLCLICdintVFSAMYSGdrnpyspaqflyswwqhs 261
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL----------SETPKELFSQVC----RKAPQFKG------------------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 262 anlasYEQQDAHEFFISMLDAIhekegITkngskgnggdcqcIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISL-NLD 340
Cdd:cd02667 49 -----YQQQDSHELLRYLLDGL-----RT-------------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLpRSD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 341 INISLTekgkkltkqnaddnmsTLLGCLDLFTRPEKLGSDQKLYCQNCkerQNALKQMSISKLPLVLTLHVKRF---EHS 417
Cdd:cd02667 106 EIKSEC----------------SIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFqqpRSA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 418 FVKKLSRKIDrylqFPFSLDMTPYLSSsilrakygnrifNFGGDESDTFSKFEIFAVVTHSGTLESGHYVTFVRLRK--- 494
Cdd:cd02667 167 NLRKVSRHVS----FPEILDLAPFCDP------------KCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRPpqq 230
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 657400764 495 --------------------QWYRCDDAWITKVDEATVRASQCYMIFY 522
Cdd:cd02667 231 rlsdltkskpaadeagpgsgQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
2.96e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 146.69 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPF---RDYFlsggHSLEDCKRRTterlclicdintvfsamysgdrNPYSPAQFLYSWW 258
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYFENLLtclKDLF----ESISEQKKRT----------------------GVISPKKFITRLK 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 259 QHSANLASYEQQDAHEFF-------ISMLDAIHEKEGITKNGSKGNGGDCQ--CIaHRVFYGQLRSEVTCMACGFTSTTY 329
Cdd:cd02663 55 RENELFDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQptWV-HEIFQGILTNETRCLTCETVSSRD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 330 DPFLDISLNLDINISLTEkgkkltkqnaddnmstllgCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTL 409
Cdd:cd02663 134 ETFLDLSIDVEQNTSITS-------------------CLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILAL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 410 HVKRFEHSfvKKLSRKIDRYLQFPFSLDMtpylsssilrakygnRIFNFGGDESDTFSKFEIFAVVTHSG-TLESGHYVT 488
Cdd:cd02663 195 HLKRFKYD--EQLNRYIKLFYRVVFPLEL---------------RLFNTTDDAENPDRLYELVAVVVHIGgGPNHGHYVS 257
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 657400764 489 FVRLRKQWYRCDDAWITKVDEATV-------RASQC-YMIFY 522
Cdd:cd02663 258 IVKSHGGWLLFDDETVEKIDENAVeeffgdsPNQATaYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-517 |
3.75e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 132.93 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYFL----SGGHSLEDCKRRTTERLCLICD-INTVFSAMYSGDRNPYSPAQFLys 256
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnsTEDAELKNMPPDKPHEPQTIIDqLQLIFAQLQFGNRSVVDPSGFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 257 wwqHSANLASYEQQDAHEFFISMLDAIHEKEgitkngSKGNGGDCQCIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDIS 336
Cdd:cd02668 79 ---KALGLDTGQQQDAQEFSKLFLSLLEAKL------SKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 337 LNLDINISLTEkgkkltkqnaddnmstllgCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFEH 416
Cdd:cd02668 150 LQLKGHKTLEE-------------------CIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 417 SFVKKLSRKIDRYLQFPFSLDMTPYLSssilrakygnrifnfggDESDTFSKFEIFAVVTHSGT-LESGHYVTFVR--LR 493
Cdd:cd02668 211 DRKTGAKKKLNASISFPEILDMGEYLA-----------------ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKdeQT 273
|
330 340
....*....|....*....|....
gi 657400764 494 KQWYRCDDawiTKVDEATVRASQC 517
Cdd:cd02668 274 GEWYKFND---EDVEEMPGKPLKL 294
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
6.03e-32 |
|
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: 126.93 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRD---YFLSGGHSLEdckrrtteRLCLICDINtvfSAMYSGDRNPYSPAQFLYSWW 258
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVE--------QLQSSFLLN---PEKYNDELANQAPRRLLNALR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 259 QHSANLASYEQQDAHEFFISMLDAIHEkegitkngskgnggdcqcIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISLN 338
Cdd:cd02671 95 EVNPMYEGYLQHDAQEVLQCILGNIQE------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 339 LDINISLTEKGKKLTKQNADDNMSTLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFEHSF 418
Cdd:cd02671 157 VQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 419 VKKLS----RKIDRYLQFPFSLDMtpylsssilrakygnrifnFGGDESDTFSKFEIFAVVTHSG-TLESGHYVTFVRlr 493
Cdd:cd02671 237 SEFDCygglSKVNTPLLTPLKLSL-------------------EEWSTKPKNDVYRLFAVVMHSGaTISSGHYTAYVR-- 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 657400764 494 kqWYRCDDAWITKVDE---------ATVRASQCYMIFY 522
Cdd:cd02671 296 --WLLFDDSEVKVTEEkdflealspNTSSTSTPYLLFY 331
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
1.84e-30 |
|
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: 122.60 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSLEDCKRRTTERLclicdINTVFSAMYSGDRNPYSPAQFLYSWWQHS 261
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKL-----QLLQAHLMHTQRRAEAPPDYFLEASRPPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 262 ANLASyeQQDAHEFFISMLDAIHEkegitkngskgnggdcqcIAHRVFYGQLRSEVTCMACGFTSTTYDPFLDISLNLdi 341
Cdd:cd02664 76 FTPGS--QQDCSEYLRYLLDRLHT------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSF-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 342 nisltekgkkltkqnaddnmSTLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFEHSFVKK 421
Cdd:cd02664 134 --------------------PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTH 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 422 LSRKIDRYLQFPFSLDMTPYLSSSILRAKYGNRIFNFGGDESDTFSK--FEIFAVVTHSGT-LESGHYVTFVR------- 491
Cdd:cd02664 194 VREKIMDNVSINEVLSLPVRVESKSSESPLEKKEEESGDDGELVTRQvhYRLYAVVVHSGYsSESGHYFTYARdqtdads 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 657400764 492 ---------------LRKQWYRCDDAWITKVDEATVRASQC-------YMIFY 522
Cdd:cd02664 274 tgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
179-526 |
5.20e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 123.45 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 179 GLRGLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSlEDCKRrtTERLCLICDINTVFSAM----YSGDRNPYSPAQFL 254
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYE-ESINE--ENPLGMHGSVASAYADLikqlYDGNLHAFTPSGFK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 255 YSWWQHSANLASYEQQDAHEFFISMLDAIHE------KEGITKNGSKGNGGDC-------QC----------IAHRVFYG 311
Cdd:COG5560 341 KTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEdlnriiKKPYTSKPDLSPGDDVvvkkkakECwwehlkrndsIITDLFQG 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 312 QLRSEVTCMACGFTSTTYDPFLDIS------------------------------------------------------- 336
Cdd:COG5560 421 MYKSTLTCPGCGSVSITFDPFMDLTlplpvsmvwkhtivvfpesgrrqplkieldasstirglkklvdaeygklgcfeik 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 337 ---------------------------------------------------------------LNLDINIS--------- 344
Cdd:COG5560 501 vmciyyggnynmlepadkvllqdipqtdfvylyetndngievpvvhlriekgykskrlfgdpfLQLNVLIKasiydklvk 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 345 --------------------------------------LTEKGKKLTKQ-------NADDNMS----------------- 362
Cdd:COG5560 581 efeellvlvemkktdvdlvseqvrllreesspsswlklETEIDTKREEQveeegqmNFNDAVVisceweekrylslfsyd 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 363 ---------------TLLGCLDLFTRPEKLGSDQKLYCQNCKERQNALKQMSISKLPLVLTLHVKRFehSFVKKLSRKID 427
Cdd:COG5560 661 plwtireigaaertiTLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRF--SSVRSFRDKID 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 428 RYLQFP-FSLDMT----PYLSSSILrakygnrifnfggdesdtfskFEIFAVVTHSGTLESGHYVTFVR--LRKQWYRCD 500
Cdd:COG5560 739 DLVEYPiDDLDLSgveyMVDDPRLI---------------------YDLYAVDNHYGGLSGGHYTAYARnfANNGWYLFD 797
|
570 580
....*....|....*....|....*.
gi 657400764 501 DAWITKVDEATVRASQCYMIFYVQKT 526
Cdd:COG5560 798 DSRITEVDPEDSVTSSAYVLFYRRKS 823
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
182-525 |
2.04e-26 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 109.51 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQAL-LHAPPFRDYFLSGGHSLEDCKR--RTTERLCLICDINTVFSAMYSGDR---NPYSPaqfly 255
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNviRKPEPDLNQEEALKLFTALWSSKEhkvGWIPP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 256 swwqhsanlaSYEQQDAHEFFISMLDAIhekeGITKNGSKGnggdcqciahrVFYGQLRSEvtcmacgFTSTTYDPFLDI 335
Cdd:COG5533 76 ----------MGSQEDAHELLGKLLDEL----KLDLVNSFT-----------IRIFKTTKD-------KKKTSTGDWFDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 336 slnldiNISLTEkgkkltkQNADDNMSTLLGCLDLFtrpEKLGSDQKLYCQNCKERQNALKQM----SISKLPLVLTLHV 411
Cdd:COG5533 124 ------IIELPD-------QTWVNNLKTLQEFIDNM---EELVDDETGVKAKENEELEVQAKQeyevSFVKLPKILTIQL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 412 KRFEHSFVKklsRKIDRYLQFPFSLdmtPYLSSSILrakygnrifnfgGDESDTFskFEIFAVVTHSGTLESGHYVTFVR 491
Cdd:COG5533 188 KRFANLGGN---QKIDTEVDEKFEL---PVKHDQIL------------NIVKETY--YDLVGFVLHQGSLEGGHYIAYVK 247
|
330 340 350
....*....|....*....|....*....|....*..
gi 657400764 492 LRKQWYRCDDAWITKV---DEATVRASQCYMIFYVQK 525
Cdd:COG5533 248 KGGKWEKANDSDVTPVseeEAINEKAKNAYLYFYERI 284
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
179-513 |
2.79e-24 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 108.80 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 179 GLRGLNSLGSTCFMNSVLQALLhappFRDYFLSGGHSLEDCKRRTTERLCLIcdINTVFSAMYSGDrNPYSPAQFLYSW- 257
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLF----FIAKFRKDVYGIPTDHPRGRDSVALA--LQRLFYNLQTGE-EPVDTTELTRSFg 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 258 WQhsaNLASYEQQDAHEFFISMLDAIHEKEGITKNGSKGNGgdcqciahrVFYGQLRSEVTCMACGFTSTTYDPFLDISL 337
Cdd:COG5077 265 WD---SDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNG---------IFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 338 NLDinisltekgkkltkqnaddNMSTLLGCLDLFTRPEKLGSDQKLYCQNcKERQNALKQMSISKLPLVLTLHVKRFEHS 417
Cdd:COG5077 333 NVK-------------------GMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 418 FVKKLSRKIDRYLQFPFSLDMTPYLSSSILRAKYGNRIFNFGGdesdtfskfeifaVVTHSGTLESGHYVTFVRLRK--Q 495
Cdd:COG5077 393 FERDMMVKINDRYEFPLEIDLLPFLDRDADKSENSDAVYVLYG-------------VLVHSGDLHEGHYYALLKPEKdgR 459
|
330
....*....|....*...
gi 657400764 496 WYRCDDawiTKVDEATVR 513
Cdd:COG5077 460 WYKFDD---TRVTRATEK 474
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
1.22e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 102.02 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSLEDCKRRTTErlCLICDINTVFSAMYSGD----------RNPY--- 248
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPAN--DLNCQLIKLADGLLSGRyskpaslkseNDPYqvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 249 -SPAQFLYSWWQHSANLASYEQQDAHEFFISMLDAIhEKEGITKNGSKGNggdcqciahRVFYGQLRSEVTCMACGFTST 327
Cdd:cd02658 79 iKPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKL-DRESFKNLGLNPN---------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 328 TYDPFLDISLNLDINISLTEKGKKLTKQNADdnmstLLGCLDLFTRPEKLgsdqKLYCQNCKERQNALKQMSISKLPLVL 407
Cdd:cd02658 149 TSELSEILSLPVPKDEATEKEEGELVYEPVP-----LEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 408 TLHVKRFEHSfVKKLSRKIDRYLQFPfslDMtpylsssILRAKYgnrifnfggdesdtfskfEIFAVVTHSGT-LESGHY 486
Cdd:cd02658 220 VINMKRFQLL-ENWVPKKLDVPIDVP---EE-------LGPGKY------------------ELIAFISHKGTsVHSGHY 270
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 657400764 487 VTFVR----LRKQWYRCDDAWITKVDEATVRASQCYMIFY 522
Cdd:cd02658 271 VAHIKkeidGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-509 |
4.30e-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 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: 97.40 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRD----YFLSGGHSLEDCKRRTTErlclicdINTVFSAMySGDRNPYSPAQFLYSW 257
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalknYNPARRGANQSSDNLTNA-------LRDLFDTM-DKKQEPVPPIEFLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 258 WQHSANLAS------YEQQDAHEFFISMLDAIhekegitKNGSKGNGGDCQCIAhRVFYGQLRSEVTCMACGF-TSTTYD 330
Cdd:cd02657 73 RMAFPQFAEkqnqggYAQQDAEECWSQLLSVL-------SQKLPGAGSKGSFID-QLFGIELETKMKCTESPDeEEVSTE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 331 PFLdiSLNLDINISLTekgkkltkqnaddnMSTLLGCLdlftrpeKLGSDQKLYCQNCKERQNALKQMS--ISKLPLVLT 408
Cdd:cd02657 145 SEY--KLQCHISITTE--------------VNYLQDGL-------KKGLEEEIEKHSPTLGRDAIYTKTsrISRLPKYLT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 409 LHVKRF--EHSFVKKLsrKIDRYLQFPFSLDMTPYLSSSilrakygnrifnfggdesdtfSKFEIFAVVTHSG-TLESGH 485
Cdd:cd02657 202 VQFVRFfwKRDIQKKA--KILRKVKFPFELDLYELCTPS---------------------GYYELVAVITHQGrSADSGH 258
|
330 340
....*....|....*....|....*.
gi 657400764 486 YVTFVR--LRKQWYRCDDAWITKVDE 509
Cdd:cd02657 259 YVAWVRrkNDGKWIKFDDDKVSEVTE 284
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-522 |
1.84e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 90.89 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYflsgghsledckrrtterlclicdintvfsamysgdrnpyspaqflyswwqhs 261
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEY----------------------------------------------------- 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 262 anLASY-EQQDAHEFFISMLDAIHEKEGITkngskgnggdcqciahrvFYGQLRSEVTCMACGFTST-TYDPFLDISLNL 339
Cdd:cd02662 28 --LEEFlEQQDAHELFQVLLETLEQLLKFP------------------FDGLLASRIVCLQCGESSKvRYESFTMLSLPV 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 340 dinisltekgkkltKQNADDNMSTLLGCLDLFTRPEKLgSDQKlyCQNCkerqnalkQMSISKLPLVLTLHVKRF---EH 416
Cdd:cd02662 88 --------------PNQSSGSGTTLEHCLDDFLSTEII-DDYK--CDRC--------QTVIVRLPQILCIHLSRSvfdGR 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 417 SFVKKLSRKIdrylQFPfsldmtpylssSILRAKygnrifnfggdesdtfsKFEIFAVVTHSGTLESGHYVTFVRLR--- 493
Cdd:cd02662 143 GTSTKNSCKV----SFP-----------ERLPKV-----------------LYRLRAVVVHYGSHSSGHYVCYRRKPlfs 190
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 657400764 494 -------------------KQWYRCDDAWITKVDEATVR-ASQCYMIFY 522
Cdd:cd02662 191 kdkepgsfvrmregpsstsHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
168-522 |
5.81e-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: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 168 KDLRGKSCFPeGLRGLNSLGSTCFMNSVLQALLHAPPFRDYFLSgGHSLEDCKRRTTErlcLICDINTVFSAMYsgdrNP 247
Cdd:cd02669 108 RDLDGKPYLP-GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLL-YENYENIKDRKSE---LVKRLSELIRKIW----NP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 248 Y------SPAQFLYSWWQHSANLASYEQQ-DAHEFFISMLDAIHekegitkNGSKGNGGDCQCIAHRVFYGQLRSEVT-- 318
Cdd:cd02669 179 RnfkghvSPHELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLH-------KDLGGSKKPNSSIIHDCFQGKVQIETQki 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 319 -------CMACGFTSTTYD------PFLDISLNLD-INISLTEKGKKLTKQnaddnmSTLLGCLDLFTRPEklgsdqkly 384
Cdd:cd02669 252 kphaeeeGSKDKFFKDSRVkktsvsPFLLLTLDLPpPPLFKDGNEENIIPQ------VPLKQLLKKYDGKT--------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 385 cqnCKERQNALKQMSISKLPLVLTLHVKRFE-HSFVKKLSRKIdryLQFPFS-LDMTPYLSSsilrakygnrifnfggDE 462
Cdd:cd02669 317 ---ETELKDSLKRYLISRLPKYLIFHIKRFSkNNFFKEKNPTI---VNFPIKnLDLSDYVHF----------------DK 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657400764 463 SDTF--SKFEIFAVVTHSGT-LESGHYVTFVR--LRKQWYRCDDAWITKVDEATVRASQCYMIFY 522
Cdd:cd02669 375 PSLNlsTKYNLVANIVHEGTpQEDGTWRVQLRhkSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
182-501 |
4.06e-14 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 73.46 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYFLSggHSLEDCKRRTterlCLICDINTVFSAMYSGDRNPYSPAQFLY---SWW 258
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEH----CLLCELGFLFDMLEKAKGKNCQASNFLRalsSIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 259 QHSA-NLASYEQQDAHEFFIS---------MLDAIHEKEGITKNGSKGNGGDCQciahRVFYGQLRSEVTCMACGFTSTT 328
Cdd:pfam13423 76 EASAlGLLDEDRETNSAISLSsliqsfnrfLLDQLSSEENSTPPNPSPAESPLE----QLFGIDAETTIRCSNCGHESVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 329 YDPFLDISLNLdinisltekGKKLTKQNADDNMSTLLGCLDLFTRPEKLgsdQKLYCQNCKERQNALKQMSISKLPLVLT 408
Cdd:pfam13423 152 ESSTHVLDLIY---------PRKPSSNNKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 409 LHVKRfeHSFVKKLSRKIDRYLQFPFSLDMTPylsssilRAKYGNRIFnfggdesdtfsKFEIFAVVTH-SGTLESGHYV 487
Cdd:pfam13423 220 LNAAL--TNEEWRQLWKTPGWLPPEIGLTLSD-------DLQGDNEIV-----------KYELRGVVVHiGDSGTSGHLV 279
|
330 340
....*....|....*....|...
gi 657400764 488 TFVR---------LRKQWYRCDD 501
Cdd:pfam13423 280 SFVKvadseledpTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
182-523 |
1.72e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 59.81 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 182 GLNSLGSTCFMNSVLQALLHAPPFRDYFLSGGHSLEDCK------RRTTER----------LCLICDINTVFSAMYSGDR 245
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELAsdypteRRIGGRevsrselqrsNQFVYELRSLFNDLIHSNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 246 NPYSPAQFLyswwqhsANLAsYEQQDAHEFFISMLDAIHEKEGITKNGSKGNGGDCQCIA----HRVFYGQLRSEVTCMA 321
Cdd:cd02666 83 RSVTPSKEL-------AYLA-LRQQDVTECIDNVLFQLEVALEPISNAFAGPDTEDDKEQsdliKRLFSGKTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 322 CGFTSTTYDPF-LDISLNLDInisltekGKKLTKQNADDNMSTLLGCLD-LFtrpeklgsdqklycqnckerqnalKQMS 399
Cdd:cd02666 155 MGNQPSVRTKTeRFLSLLVDV-------GKKGREIVVLLEPKDLYDALDrYF------------------------DYDS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 400 ISKLPLVLTLHVKRFEHSFVKKLSrkIDRYLQfPFSLDMTPYLSSSILR------AKYGNRIFNFGGDESDTFSKF---- 469
Cdd:cd02666 204 LTKLPQRSQVQAQLAQPLQRELIS--MDRYEL-PSSIDDIDELIREAIQsesslvRQAQNELAELKHEIEKQFDDLksyg 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657400764 470 -EIFAVVTHSGTLESGHYVTFVRLRKQ--WYRCDDAWITKVDEATV------RASQCYMIFYV 523
Cdd:cd02666 281 yRLHAVFIHRGEASSGHYWVYIKDFEEnvWRKYNDETVTVVPASEVflftlgNTATPYFLVYV 343
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
57-117 |
2.90e-07 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 48.03 E-value: 2.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657400764 57 CSFCNGCEkRVFLCLICSSFCCLD----HTLLHIQtENGHDLFVDVERCELYCGVCCDQIYDPDF 117
Cdd:pfam02148 1 CSLCGNTS-NLWLCLTCGHVGCGRyqnsHALEHYE-ETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-522 |
8.68e-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: 50.61 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 269 QQDAHEFFISMLDAIHEkegITKNGSKGNGGDCQCIAH----RVFYGQLRSEVTCMACGFTSTTYDP--FLDIS---LNL 339
Cdd:cd02673 33 QQDAHEFLLTLLEAIDD---IMQVNRTNVPPSNIEIKRlnplEAFKYTIESSYVCIGCSFEENVSDVgnFLDVSmidNKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 340 DINISLTEKGKKLTKQNADdnmstllgcldlftrpeklgsdqklyCQNCKErQNALKQMSISKLPLVLTLHVKRFehsfv 419
Cdd:cd02673 110 DIDELLISNFKTWSPIEKD--------------------------CSSCKC-ESAISSERIMTFPECLSINLKRY----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 420 kKLSRKIDRYLQfPFSLDMTPYLSssilrakygnrifnfggdesdTFSKFEIFAVVTHSG-TLESGHYVTFVR---LRKQ 495
Cdd:cd02673 158 -KLRIATSDYLK-KNEEIMKKYCG---------------------TDAKYSLVAVICHLGeSPYDGHYIAYTKelyNGSS 214
|
250 260 270
....*....|....*....|....*....|
gi 657400764 496 WYRCDDAWITKVDEATVRA---SQCYMIFY 522
Cdd:cd02673 215 WLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
400-522 |
8.11e-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: 239135 [Multi-domain] Cd Length: 241 Bit Score: 47.91 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 400 ISKLPLVLTLHVKRF--EHSFVKKLSRKIDrylqFPFSLDMTPYLSSSILRAKYGN---RIFNFGGDESDTFSKFEIF-- 472
Cdd:cd02670 95 FAKAPSCLIICLKRYgkTEGKAQKMFKKIL----IPDEIDIPDFVADDPRACSKCQlecRVCYDDKDFSPTCGKFKLSlc 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657400764 473 AVVTHSGT-LESGHYVTFVR-------------LRKQWYRCDD----AWITKVDEATVRASQC--YMIFY 522
Cdd:cd02670 171 SAVCHRGTsLETGHYVAFVRygsysltetdneaYNAQWVFFDDmadrDGVSNGFNIPAARLLEdpYMLFY 240
|
|
| |
