|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-419 |
5.62e-173 |
|
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: 487.27 E-value: 5.62e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 78 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRH--RCEMPSPELCLVCEMSSLFREL-YSGNPSPHVPYKLLHLVWIHA 154
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 155 RHLAGYRQQDAHEFLIAALDVLHRHCKGDDvgKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLP 234
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDK--NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 235 GSCTSFWPmspgresslNGESHIPGITTLTDCLRRFTRPEHLGSSAkIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFE 314
Cdd:cd02660 159 NKSTPSWA---------LGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 315 HSA-KQRRKITTYISFPLELDMTPFMASSKetrvngQLQLPTNSANNENKYSLFAVVNHQGTLESGHYTSFIRHHRDQWF 393
Cdd:cd02660 229 HSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQWF 302
|
330 340
....*....|....*....|....*.
gi 223005910 394 KCDDAVITKASIKDVLDSEGYLLFYH 419
Cdd:cd02660 303 KFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
78-418 |
7.26e-86 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 264.69 E-value: 7.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 78 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELC--LVCEMSSLFRELYSGNPSPHV-PYKLLHLVWIHA 154
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 155 RHLAGYRQQDAHEFLIAALDVLHRhckgddvgkvASNPNHCN---CIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISL 231
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHE----------DLNGNHSTeneSLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 232 DLPGSctsfwpmspgresslngeSHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFK 311
Cdd:pfam00443 151 PIPGD------------------SAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 312 RFEHSAKQRRKITTYISFPLELDMTPFMASSKETRvngqlqlptnsANNENKYSLFAVVNHQGTLESGHYTSFIRHHRD- 390
Cdd:pfam00443 213 RFSYNRSTWEKLNTEVEFPLELDLSRYLAEELKPK-----------TNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENn 281
|
330 340
....*....|....*....|....*....
gi 223005910 391 QWFKCDDAVITKAS-IKDVLDSEGYLLFY 418
Cdd:pfam00443 282 RWYKFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-418 |
9.32e-78 |
|
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: 243.72 E-value: 9.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 78 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHL 157
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 158 AGYRQQDAHEFLIAALDVLHRHC----KGDDVGKVASNPnhcNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDl 233
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKACldrfKKLKAVDPSSQE---TTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 234 pgsctsfwpmspgresslngeshIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRF 313
Cdd:cd02661 158 -----------------------IKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 314 ehSAKQRRKITTYISFPLELDMTPFMassketrvngqlqlpTNSANNENKYSLFAVVNHQGT-LESGHYTSFIRHHRDQW 392
Cdd:cd02661 215 --SNFRGGKINKQISFPETLDLSPYM---------------SQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNGKW 277
|
330 340
....*....|....*....|....*.
gi 223005910 393 FKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02661 278 YNMDDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
79-418 |
5.63e-72 |
|
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: 227.37 E-value: 5.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspelclvcemsslfrelysgnpsphvpykllhlvwiharhla 158
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 159 gyRQQDAHEFLIAALDVLHRHCKGddVGKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSct 238
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVK-- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 239 sfwpmspgresslngeshIPGITTLTDCLRRFTRPEHLGSSAKIKCgSCQSYQESTKQLTMKKLPVVACFHFKRFEH-SA 317
Cdd:cd02257 95 ------------------GLPQVSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFnED 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 318 KQRRKITTYISFPLELDMTPFMASSKEtrvngqlqlPTNSANNENKYSLFAVVNHQGTL-ESGHYTSFIRHH-RDQWFKC 395
Cdd:cd02257 156 GTKEKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYKF 226
|
330 340
....*....|....*....|....*...
gi 223005910 396 DDAVITKASIKDVLD-----SEGYLLFY 418
Cdd:cd02257 227 NDDKVTEVSEEEVLEfgslsSSAYILFY 254
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
2.39e-68 |
|
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: 216.77 E-value: 2.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspelclvcemsslfrelysgnpsphvpykllhlvwiharhla 158
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 159 gyRQQDAHEFLIAALDVLHRhckgddvgkvasnpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCT 238
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 239 SFWPMspgresslngeshipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHSAK 318
Cdd:cd02674 80 DAPKV------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 319 QRRKITTYISFPLE-LDMTPFmassketrvngqlqLPTNSANNENKYSLFAVVNHQGTLESGHYTSFIRH-HRDQWFKCD 396
Cdd:cd02674 142 STRKLTTPVTFPLNdLDLTPY--------------VDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNnETNDWYKFD 207
|
330 340
....*....|....*....|..
gi 223005910 397 DAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02674 208 DSRVTKVSESSVVSSSAYILFY 229
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
2.59e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 179.50 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPILRDFFLsdrhrcemPSPELCL--VCEMSSLFRelysgnpsphvpykllhlvwiharh 156
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLS--------ETPKELFsqVCRKAPQFK------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 157 laGYRQQDAHEFLIAALDVLhrhckgddvgkvasnpnhcNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlpgs 236
Cdd:cd02667 48 --GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 237 ctsfwpmspgRESSLNGEshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCqsyQESTKQLTMKKLPVVACFHFKRFEHS 316
Cdd:cd02667 103 ----------RSDEIKSE------CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 317 AKQR-RKITTYISFPLELDMTPFMASSKEtrvngqlqlpTNSANNENKYSLFAVVNHQGTLESGHYTSFIRHH------- 388
Cdd:cd02667 164 RSANlRKVSRHVSFPEILDLAPFCDPKCN----------SSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrls 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 223005910 389 ---------------RDQWFKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02667 234 dltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
76-411 |
2.95e-49 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 170.52 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 76 GLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRcEMPSPELCLVCEMSSLFRELYSGnpspHVPYKLLHLVWIHAR 155
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLS----ESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 156 H----LAGYRQQDAHEFLIAALDVLhrhckgDDVGKVASNPNhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISL 231
Cdd:cd02659 76 FgwdsLNTFEQHDVQEFFRVLFDKL------EEKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 232 DlpgsctsfwpmspgresslngeshIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFK 311
Cdd:cd02659 146 A------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 312 RFEHS--AKQRRKITTYISFPLELDMTPFMASSketrVNGQLQLPTNSANNENKYSLFAVVNHQGTLESGHYTSFIRHHR 389
Cdd:cd02659 202 RFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD 277
|
330 340
....*....|....*....|...
gi 223005910 390 D-QWFKCDDAVITKASIKDVLDS 411
Cdd:cd02659 278 DgKWYKFNDDVVTPFDPNDAEEE 300
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
1.88e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 135.52 E-value: 1.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspeLCLVCEMSSLFRELYSGNPSPHV--PYKLLHLVWIHARH 156
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF---------------------ENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 157 LAGYRQQDAHEFL-------IAALDVLHRHCKGDDVGKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 229
Cdd:cd02663 60 FDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 230 SLDLPGSctsfwpmspgresslngeshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFH 309
Cdd:cd02663 140 SIDVEQN------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 310 FKRFEHSAKQRR--KITTYISFPLEldmtpfmassketrvngqLQLPTNSANNEN---KYSLFAVVNHQG-TLESGHYTS 383
Cdd:cd02663 196 LKRFKYDEQLNRyiKLFYRVVFPLE------------------LRLFNTTDDAENpdrLYELVAVVVHIGgGPNHGHYVS 257
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 223005910 384 FIRHHrDQWFKCDDAVITKASIKDVLD--------SEGYLLFY 418
Cdd:cd02663 258 IVKSH-GGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-406 |
8.44e-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: 129.08 E-value: 8.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPILRDFFLS---------DRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLlhl 149
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaelKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 150 vwIHARHLAGYRQQDAHEFLIAALDVLHRhCKGDDVGKVASNpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 229
Cdd:cd02668 78 --VKALGLDTGQQQDAQEFSKLFLSLLEA-KLSKSKNPDLKN------IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 230 SLDLPGSctsfwpmspgresslngeshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFH 309
Cdd:cd02668 149 ELQLKGH------------------------KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 310 FKRFEHSAK--QRRKITTYISFPLELDMTPFMASSKEtrvngqlqlptnsanNENKYSLFAVVNHQGT-LESGHYTSFIR 386
Cdd:cd02668 205 LLRFVFDRKtgAKKKLNASISFPEILDMGEYLAESDE---------------GSYVYELSGVLIHQGVsAYSGHYIAHIK 269
|
330 340
....*....|....*....|.
gi 223005910 387 H-HRDQWFKCDDAVITKASIK 406
Cdd:cd02668 270 DeQTGEWYKFNDEDVEEMPGK 290
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
1.85e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 116.65 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMP--SPELCLVCEMSSLFRELYSG-------NPSPHVPYKLlHL 149
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQV-GI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 150 VWIHARHLAGY--------RQQDAHEFLIAALDVLHRHCKGDDVgkvaSNPNhcnciidQIFTGGLQSDVTCQACHGVST 221
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESFKNLG----LNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 222 TIDPCWDISLDLPgsctsfwpMSPGRESSLNGESHIPgiTTLTDCLRRFTRPEHLgssaKIKCGSCQSYQESTKQLTMKK 301
Cdd:cd02658 149 TSELSEILSLPVP--------KDEATEKEEGELVYEP--VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 302 LPVVACFHFKRFEHSA-KQRRKITTYISFPLELDmtpfmassketrvNGqlqlptnsannenKYSLFAVVNHQGT-LESG 379
Cdd:cd02658 215 FPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG-------------PG-------------KYELIAFISHKGTsVHSG 268
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 223005910 380 HYTSFIR---HHRDQWFKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02658 269 HYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
75-418 |
2.04e-29 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 121.53 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 75 IGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELC-----LVCEMSSLFRELYSGNPSPHVPYKLLHL 149
Cdd:COG5560 263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLgmhgsVASAYADLIKQLYDGNLHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 150 VWIHARHLAGYRQQDAHEFLIAALDVLHRH---------------CKGDDVgKVASNPNHC-------NC-IIDQIFTGG 206
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDlnriikkpytskpdlSPGDDV-VVKKKAKECwwehlkrNDsIITDLFQGM 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 207 LQSDVTCQACHGV------------------------------------------STTI-------------DPC----- 226
Cdd:COG5560 422 YKSTLTCPGCGSVsitfdpfmdltlplpvsmvwkhtivvfpesgrrqplkieldaSSTIrglkklvdaeygkLGCfeikv 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 227 -------------------------WD----------------------------------------------------- 228
Cdd:COG5560 502 mciyyggnynmlepadkvllqdipqTDfvylyetndngievpvvhlriekgykskrlfgdpflqlnvlikasiydklvke 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 229 ---------------------ISLDLPGSCTSFW-----PMSPGRESSLNGES--------------------------- 255
Cdd:COG5560 582 feellvlvemkktdvdlvseqVRLLREESSPSSWlkletEIDTKREEQVEEEGqmnfndavvisceweekrylslfsydp 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 256 ---------HIPGITtLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHSAKQRRKITTY 326
Cdd:COG5560 662 lwtireigaAERTIT-LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDL 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 327 ISFPL-ELDMTPFMASSKETRVNgqlqlptnsannenkYSLFAVVNHQGTLESGHYTSFIRHHRDQ-WFKCDDAVITKAS 404
Cdd:COG5560 741 VEYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFDDSRITEVD 805
|
570
....*....|....
gi 223005910 405 IKDVLDSEGYLLFY 418
Cdd:COG5560 806 PEDSVTSSAYVLFY 819
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
4.23e-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 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: 115.51 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPILRDFFL-SDRHRCEMPSPELCLVCEMSSLFRELySGNPSPHVPYKLLHLVWIHARHL 157
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 158 A------GYRQQDAHEFLIAALDVLHRHCKGDDvgkvaSNPNHcnciIDQIFTGGLQSDVTCQACHGVSttidpcwdisl 231
Cdd:cd02657 80 AekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG-----SKGSF----IDQLFGIELETKMKCTESPDEE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 232 dlpgsctsfwPMSPGRESSLNgeSHIpGITTLTDCLrrFTRPEHlGSSAKIKCGSCQSYQES--TKQLTMKKLPVVACFH 309
Cdd:cd02657 140 ----------EVSTESEYKLQ--CHI-SITTEVNYL--QDGLKK-GLEEEIEKHSPTLGRDAiyTKTSRISRLPKYLTVQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 310 FKRF--EHSAKQRRKITTYISFPLELDMTPFMassketrvngqlqlpTNSANnenkYSLFAVVNHQG-TLESGHYTSFIR 386
Cdd:cd02657 204 FVRFfwKRDIQKKAKILRKVKFPFELDLYELC---------------TPSGY----YELVAVITHQGrSADSGHYVAWVR 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 223005910 387 H-HRDQWFKCDDAVITKASIKDVLDSEG-------YLLFY 418
Cdd:cd02657 265 RkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
73-418 |
2.17e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 116.26 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 73 FTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLS---DRHRCEMPSPelcLVCEMSSLFRELYS-----GNPSPHvpy 144
Cdd:cd02669 115 YLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKDRKSE---LVKRLSELIRKIWNprnfkGHVSPH--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 145 KLLHLVWIHARHLAGYRQQ-DAHEFLIAALDVLHRHCKgddvGKVASNPNhcncIIDQIFTGGLQ-----------SDVT 212
Cdd:cd02669 189 ELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLG----GSKKPNSS----IIHDCFQGKVQietqkikphaeEEGS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 213 CQACHG----VSTTIDPCWDISLDLPgsctsfwPMSPGRESslNGESHIPGItTLTDCLRRFTrpehlGSsakikcgSCQ 288
Cdd:cd02669 261 KDKFFKdsrvKKTSVSPFLLLTLDLP-------PPPLFKDG--NEENIIPQV-PLKQLLKKYD-----GK-------TET 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 289 SYQESTKQLTMKKLPVVACFHFKRFEHSAKQRRKITTYISFPLE-LDMTPFMASsketrvngqlqlPTNSANNENKYSLF 367
Cdd:cd02669 319 ELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDYVHF------------DKPSLNLSTKYNLV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 223005910 368 AVVNHQGT-LESGHYTSFIRHH-RDQWFKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02669 387 ANIVHEGTpQEDGTWRVQLRHKsTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
3.09e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 111.14 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPilrDFFLSDRHRCEMPSP--ELCLVCEmssLFRELYSGNPSPHVPYKLLHLVWIHARH 156
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSveQLQSSFL---LNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 157 LAGYRQQDAHEFLIAALDVLHRhckgddvgkvasnpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGS 236
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 237 CTsfwpmSPGRESSLNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHS 316
Cdd:cd02671 161 EL-----SKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 317 AKQR------RKITTYISFPLELDMtpFMASSKETRvngqlqlptnsanneNKYSLFAVVNHQG-TLESGHYTSFIRhhr 389
Cdd:cd02671 236 GSEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR--- 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 223005910 390 dqWFKCDDAVITKASIKDVLD---------SEGYLLFY 418
Cdd:cd02671 296 --WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
76-410 |
2.98e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 109.19 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 76 GLRGLINLGNTCFMNCIVQALTHTPILRD--FFLSDRHrcemPSPELCLVCEMSSLFRELYSGNpsphVPYKLLHLV--- 150
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDH----PRGRDSVALALQRLFYNLQTGE----EPVDTTELTrsf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 151 -WIHARHlagYRQQDAHEFLIAALDVLHRHCKGDDVGKVasnpnhcnciIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 229
Cdd:COG5077 264 gWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENA----------LNGIFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 230 SLDLPGSctsfwpmspgresslngeshipgiTTLTDCLRRFTRPEHLGSSakiKCGSCQSY--QESTKQLTMKKLPVVAC 307
Cdd:COG5077 331 QLNVKGM------------------------KNLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLH 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 308 FHFKRFEHSAK--QRRKITTYISFPLELDMTPFMasSKETRvngqlqlptNSANNENKYSLFAVVNHQGTLESGHYTSFI 385
Cdd:COG5077 384 LQLKRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDAD---------KSENSDAVYVLYGVLVHSGDLHEGHYYALL 452
|
330 340
....*....|....*....|....*.
gi 223005910 386 RHHRD-QWFKCDDAVITKASIKDVLD 410
Cdd:COG5077 453 KPEKDgRWYKFDDTRVTRATEKEVLE 478
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
7.41e-25 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 104.11 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLV--WIHARh 156
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRppWFTPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 157 lagyRQQDAHEFLIAALDVLHrhckgddvgkvasnpnhcnCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPgs 236
Cdd:cd02664 80 ----SQQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 237 ctsfwpmspgresslngeshipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHS 316
Cdd:cd02664 135 -------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 317 AKQ--RRKITTYISFPLELDMtPFMASSKETRVNGQLQLPTNSANNEN-----KYSLFAVVNHQGT-LESGHYTSFIRH- 387
Cdd:cd02664 190 QKThvREKIMDNVSINEVLSL-PVRVESKSSESPLEKKEEESGDDGELvtrqvHYRLYAVVVHSGYsSESGHYFTYARDq 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 223005910 388 --------------------HRDQWFKCDDAVITKASIKDVLDSEG-------YLLFY 418
Cdd:cd02664 269 tdadstgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
5.74e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 99.75 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALthtpilrdfflsdrhrcempspelclvcemSSLfrelysgnpsphvPYKLLHLVWIHArhla 158
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------------------ASL-------------PSLIEYLEEFLE---- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 159 gyrQQDAHEFLIAALDVLHRHCKgddvgkvasNPnhcnciidqiFTGGLQSDVTCQACHGVST-TIDPCWDISLDLPgsc 237
Cdd:cd02662 34 ---QQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 238 tsfwpmspgresslngESHIPGITTLTDCLRRFTRPEHLGSsakIKCGSCQsyqestkqLTMKKLPVVACFHFKRFEHSA 317
Cdd:cd02662 89 ----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDG 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 318 K-QRRKITTYISFPLELdmtpfmassketrvngqlqlptnsanNENKYSLFAVVNHQGTLESGHYTSFIRHH-------- 388
Cdd:cd02662 142 RgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkep 195
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 223005910 389 -------------RDQWFKCDDAVITKASIKDVL-DSEGYLLFY 418
Cdd:cd02662 196 gsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
79-420 |
8.92e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 100.26 E-value: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALT-HTP-----ILRDFF----LSDRHRCEMPSPELClvcEMSSLFRELysgnpsphVPYKLLH 148
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPkldelLDDLSKelkvLKNVIRKPEPDLNQE---EALKLFTAL--------WSSKEHK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 149 LVWIHARhlagYRQQDAHEFLIAALDvlhrHCKGDDVGKVAsnpnhcnciIDQIFTGGlqsdvtcqacHGVSTTIDPCWD 228
Cdd:COG5533 70 VGWIPPM----GSQEDAHELLGKLLD----ELKLDLVNSFT---------IRIFKTTK----------DKKKTSTGDWFD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 229 ISLDLPgsctsfwpmspgRESSLNGEshipgiTTLTDCLRRFtrpEHLGSSAK-IKCGSCQSYQESTKQL---TMKKLPV 304
Cdd:COG5533 123 IIIELP------------DQTWVNNL------KTLQEFIDNM---EELVDDETgVKAKENEELEVQAKQEyevSFVKLPK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 305 VACFHFKRFEHSAkQRRKITTYISFPLELdmtPFMASsketrvngqlqlPTNSANNENKYSLFAVVNHQGTLESGHYTSF 384
Cdd:COG5533 182 ILTIQLKRFANLG-GNQKIDTEVDEKFEL---PVKHD------------QILNIVKETYYDLVGFVLHQGSLEGGHYIAY 245
|
330 340 350
....*....|....*....|....*....|....*....
gi 223005910 385 IRhHRDQWFKCDDAVITKASIKDVLDS---EGYLLFYHK 420
Cdd:COG5533 246 VK-KGGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
79-397 |
4.33e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 78.47 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQALTHTPILRDFFLSdrHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHAR--- 155
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 156 -HLAGYRQQDAHEFLIAAL-DVLHR---HCKGDDVGKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDIS 230
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 231 LDLPgsctsfWPMSPGresslngeSHIPGITTLTDCLRRFTRPEhlgSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHF 310
Cdd:pfam13423 160 LIYP------RKPSSN--------NKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 311 KRfeHSAKQRRKITTYISFPLELDMTpfmassketrvngqLQLPTNSANNENKYSLFAVVNH-QGTLESGHYTSFIR--- 386
Cdd:pfam13423 223 AL--TNEEWRQLWKTPGWLPPEIGLT--------------LSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVKvad 286
|
330
....*....|....*.
gi 223005910 387 -----HHRDQWFKCDD 397
Cdd:pfam13423 287 seledPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
1.31e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 62.51 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 79 GLINLGNTCFMNCIVQAL-THTPiLRDFFL----------SDRH-------RCEMPSPELC---LVCEMSSLFRELYSGN 137
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKP-LRDLVLnfdeskaelaSDYPterriggREVSRSELQRsnqFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 138 PSPHVPYKLLHLvwiharhlAGYRQQDAHEFLIAALDVLHRHCKGDDVGKVASNP---NHCNCIIDQIFTGGL-QSDVTC 213
Cdd:cd02666 82 TRSVTPSKELAY--------LALRQQDVTECIDNVLFQLEVALEPISNAFAGPDTeddKEQSDLIKRLFSGKTkQQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 214 QACHGVSTTIDPCWDISLDLPgsCTSFWPMSPGRESSlngeshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQ-E 292
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLVD--VGKKGREIVVLLEP----------KDLYDALDRYFDYDSLTKLPQRSQVQAQLAQpL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 293 STKQLTMKKlpvvacfhfkRFEHSAKQRrkITTYISFPLELDMTPFMASSKETRVNGQLQLPTNSANNENKYSLFAVVNH 372
Cdd:cd02666 222 QRELISMDR----------YELPSSIDD--IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYGYRLHAVFIH 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 223005910 373 QGTLESGHYTSFIRHHRDQ--WFKCDDAVITKASIKDVLDSEG-----YLLFY 418
Cdd:cd02666 290 RGEASSGHYWVYIKDFEENvwRKYNDETVTVVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
162-418 |
1.10e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 58.69 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 162 QQDAHEFL---IAALDVL---HRHCKGDDVGKVAS-NPNhcnciidQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlp 234
Cdd:cd02673 33 QQDAHEFLltlLEAIDDImqvNRTNVPPSNIEIKRlNPL-------EAFKYTIESSYVCIGCSFEENVSDVGNFLDVS-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 235 gsctsfwpMSPGRESSlngeshipgITTLTDCLRRFTRPEHLGSSAKikcgsCQSYQESTKQLTMKKLPVVacfHFKRFe 314
Cdd:cd02673 104 --------MIDNKLDI---------DELLISNFKTWSPIEKDCSSCK-----CESAISSERIMTFPECLSI---NLKRY- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 315 hsaKQRRKITTYisfpleldmtpfMASSKETRVNGQLQLPtnsannenKYSLFAVVNHQG-TLESGHYTSFIR--HHRDQ 391
Cdd:cd02673 158 ---KLRIATSDY------------LKKNEEIMKKYCGTDA--------KYSLVAVICHLGeSPYDGHYIAYTKelYNGSS 214
|
250 260 270
....*....|....*....|....*....|
gi 223005910 392 WFKCDDAVITKASIKDVLD---SEGYLLFY 418
Cdd:cd02673 215 WLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
259-418 |
2.35e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 48.32 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 259 GITTLTDCLRRFT---RPEHLGSSAKIKCGSCQSYQEstkqltmkkLPVVACFHFKRFEHSAKQRRKITTYISFPLELdm 335
Cdd:cd02665 91 GYGNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQII-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 336 tpfmassketrvngqlqlptnsanNENKYSLFAVVNHQGTLESGHYTSFI-RHHRDQWFKCDDAVITKASIKDVL-DSEG 413
Cdd:cd02665 160 ------------------------QQVPYELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVErDSFG 215
|
170
....*....|..
gi 223005910 414 -------YLLFY 418
Cdd:cd02665 216 ggrnpsaYCLMY 227
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
300-418 |
4.67e-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: 47.52 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005910 300 KKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKETRVNGQLQLPTNSANNEN-------KYSLFAVVNH 372
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVCYDDKDFsptcgkfKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223005910 373 QGT-LESGHYTSFIR------------HHRDQWFKCDD-----AVITKASIKDVLDSE-GYLLFY 418
Cdd:cd02670 176 RGTsLETGHYVAFVRygsysltetdneAYNAQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| |
