|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-419 |
6.18e-171 |
|
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: 482.26 E-value: 6.18e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 78 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRH--RCEMPSPELCLVCEMSSLFREL-YSGNPSPHVPYKLLHLVWIHA 154
Cdd:cd02660 1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHscTCLSCSPNSCLSCAMDEIFQEFyYSGDRSPYGPINLLYLSWKHS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 155 RHLAGYRQQDAHEFLIAALDVLHRHCKGDDvgKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLP 234
Cdd:cd02660 81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDK--NEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 235 GSCTSFWPmspgressvNGESHIPGITTLTDCLRRFTRPEHLGSSAkIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFE 314
Cdd:cd02660 159 NKSTPSWA---------LGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 315 HSA-KQRRKITTYISFPLELDMTPFMASSKesrmngQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHHKDQWF 393
Cdd:cd02660 229 HSLnKTSRKIDTYVQFPLELNMTPYTSSSI------GDTQDSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQWF 302
|
330 340
....*....|....*....|....*.
gi 223005906 394 KCDDAVITKASIKDVLDSEGYLLFYH 419
Cdd:cd02660 303 KFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
78-418 |
4.65e-85 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 262.76 E-value: 4.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 78 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELC--LVCEMSSLFRELYSGNPSPHV-PYKLLHLVWIHA 154
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSSSVsPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 155 RHLAGYRQQDAHEFLIAALDVLHRHCKGddvgkaaNNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLP 234
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEDLNG-------NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 235 GSctsfwpmspgressvngeSHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFE 314
Cdd:pfam00443 154 GD------------------SAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 315 HSAKQRRKITTYISFPLELDMTPFMASSKESRMngqlqlptnsgNNENKYSLFAVVNHQGTLESGHYTSFIRHHKD-QWF 393
Cdd:pfam00443 216 YNRSTWEKLNTEVEFPLELDLSRYLAEELKPKT-----------NNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENnRWY 284
|
330 340
....*....|....*....|....*.
gi 223005906 394 KCDDAVITKAS-IKDVLDSEGYLLFY 418
Cdd:pfam00443 285 KFDDEKVTEVDeETAVLSSSAYILFY 310
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
78-418 |
2.11e-76 |
|
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: 240.26 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 78 RGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHL 157
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 158 AGYRQQDAHEFLIAALDVLHRHC-KGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlpgs 236
Cdd:cd02661 82 RIGRQEDAHEFLRYLLDAMQKAClDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 237 ctsfwpmspgressvngeshIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFehS 316
Cdd:cd02661 158 --------------------IKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--S 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 317 AKQRRKITTYISFPLELDMTPFMasskesrmngqlqlpTNSGNNENKYSLFAVVNHQGT-LESGHYTSFIRHHKDQWFKC 395
Cdd:cd02661 216 NFRGGKINKQISFPETLDLSPYM---------------SQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSNGKWYNM 280
|
330 340
....*....|....*....|...
gi 223005906 396 DDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02661 281 DDSKVSPVSIETVLSQKAYILFY 303
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
79-418 |
1.82e-70 |
|
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: 223.13 E-value: 1.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspelclvcemsslfrelysgnpsphvpykllhlvwiharhla 158
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 159 gyRQQDAHEFLIAALDVLHRHCKGddVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPgsct 238
Cdd:cd02257 21 --EQQDAHEFLLFLLDKLHEELKK--SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP---- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 239 sfwpmspgressVNGESHIpgitTLTDCLRRFTRPEHLGSSAKIKCgSCQSYQESTKQLTMNKLPVVACFHFKRFEH-SA 317
Cdd:cd02257 93 ------------VKGLPQV----SLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSFnED 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 318 KQRRKITTYISFPLELDMTPFMASSKEsrmngqlqlPTNSGNNENKYSLFAVVNHQGTL-ESGHYTSFIRHH-KDQWFKC 395
Cdd:cd02257 156 GTKEKLNTKVSFPLELDLSPYLSEGEK---------DSDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPsDGKWYKF 226
|
330 340
....*....|....*....|....*...
gi 223005906 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 |
4.41e-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: 216.38 E-value: 4.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspelclvcemsslfrelysgnpsphvpykllhlvwiharhla 158
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 159 gyRQQDAHEFLIAALDVLHRhckgddvgkaannpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCT 238
Cdd:cd02674 21 --DQQDAQEFLLFLLDGLHS-------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 239 SFWPMspgressvngeshipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAK 318
Cdd:cd02674 80 DAPKV------------------TLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRG 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 319 QRRKITTYISFPLE-LDMTPFmasskesrmngqlqLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRH-HKDQWFKCD 396
Cdd:cd02674 142 STRKLTTPVTFPLNdLDLTPY--------------VDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNnETNDWYKFD 207
|
330 340
....*....|....*....|..
gi 223005906 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 |
6.13e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 181.05 E-value: 6.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPILRDFFLsdrhrcemPSPELCL--VCEMSSLFRelysgnpsphvpykllhlvwiharh 156
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLS--------ETPKELFsqVCRKAPQFK------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 157 laGYRQQDAHEFLIAALDVLhrhckgddvgkaannpnhcNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlpgs 236
Cdd:cd02667 48 --GYQQQDSHELLRYLLDGL-------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 237 ctsfwpmspgRESSVNGEshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCqsyQESTKQLTMNKLPVVACFHFKRFEHS 316
Cdd:cd02667 103 ----------RSDEIKSE------CSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 317 AKQR-RKITTYISFPLELDMTPFMASSKESrmngqlqlptNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHH------- 388
Cdd:cd02667 164 RSANlRKVSRHVSFPEILDLAPFCDPKCNS----------SEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVRppqqrls 233
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 223005906 389 ---------------KDQWFKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02667 234 dltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
76-411 |
1.91e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 165.89 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 76 GLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRcEMPSPELCLVCEMSSLFRELYSGnpspHVPYKLLHLVWIHAR 155
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPT-EDDDDNKSVPLALQRLFLFLQLS----ESPVKTTELTDKTRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 156 H----LAGYRQQDAHEFLIAALDVLHRHCKGDDVGKaannpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISL 231
Cdd:cd02659 76 FgwdsLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEG----------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 232 DlpgsctsfwpmspgressvngeshIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFK 311
Cdd:cd02659 146 A------------------------VKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 312 RFEHS--AKQRRKITTYISFPLELDMTPFMASSkesrMNGQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIR-HH 388
Cdd:cd02659 202 RFEFDfeTMMRIKINDRFEFPLELDMEPYTEKG----LAKKEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKdRD 277
|
330 340
....*....|....*....|...
gi 223005906 389 KDQWFKCDDAVITKASIKDVLDS 411
Cdd:cd02659 278 DGKWYKFNDDVVTPFDPNDAEEE 300
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
3.37e-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: 134.74 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHtpilrdfflsdrhrcempspeLCLVCEMSSLFRELYSGNPSPHV--PYKLLHLVWIHARH 156
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF---------------------ENLLTCLKDLFESISEQKKRTGVisPKKFITRLKRENEL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 157 LAGYRQQDAHEFL-------IAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 229
Cdd:cd02663 60 FDNYMHQDAHEFLnfllneiAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 230 SLDLPGSctsfwpmspgressvngeshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFH 309
Cdd:cd02663 140 SIDVEQN------------------------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 310 FKRFEHSAKQRR--KITTYISFPLEldmtpfmasskesrmngqLQLPTNSGNNEN---KYSLFAVVNHQG-TLESGHYTS 383
Cdd:cd02663 196 LKRFKYDEQLNRyiKLFYRVVFPLE------------------LRLFNTTDDAENpdrLYELVAVVVHIGgGPNHGHYVS 257
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 223005906 384 FIRHHkDQWFKCDDAVITKASIKDVLD--------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 |
4.03e-33 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 127.15 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPILRDFFLS---------DRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLlhl 149
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaelKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 150 vwIHARHLAGYRQQDAHEFLIAALDVLHRHCKgddvgkAANNPNHCNcIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDI 229
Cdd:cd02668 78 --VKALGLDTGQQQDAQEFSKLFLSLLEAKLS------KSKNPDLKN-IVQDLFRGEYSYVTQCSKCGRESSLPSKFYEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 230 SLDLPGSctsfwpmspgressvngeshipgiTTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFH 309
Cdd:cd02668 149 ELQLKGH------------------------KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 310 FKRFEHSAK--QRRKITTYISFPLELDMTPFMASSKEsrmngqlqlptnsGNNEnkYSLFAVVNHQGT-LESGHYTSFIR 386
Cdd:cd02668 205 LLRFVFDRKtgAKKKLNASISFPEILDMGEYLAESDE-------------GSYV--YELSGVLIHQGVsAYSGHYIAHIK 269
|
330 340
....*....|....*....|.
gi 223005906 387 H-HKDQWFKCDDAVITKASIK 406
Cdd:cd02668 270 DeQTGEWYKFNDEDVEEMPGK 290
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
75-418 |
1.82e-32 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 130.39 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 75 IGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELC-----LVCEMSSLFRELYSGNPSPHVPYKLLHL 149
Cdd:COG5560 263 AGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLgmhgsVASAYADLIKQLYDGNLHAFTPSGFKKT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 150 VWIHARHLAGYRQQDAHEFLIAALDVLHRH---------------CKGDDVgKAANNPNHC-------NC-IIDQIFTGG 206
Cdd:COG5560 343 IGSFNEEFSGYDQQDSQEFIAFLLDGLHEDlnriikkpytskpdlSPGDDV-VVKKKAKECwwehlkrNDsIITDLFQGM 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 207 LQSDVTCQACHGVSTTIDPCWDISLDLPGSCT-----SFWPMSPGR---------ESSV--------------------- 251
Cdd:COG5560 422 YKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwkhtiVVFPESGRRqplkieldaSSTIrglkklvdaeygklgcfeikv 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 252 -----NGES-----------------------------------HIP--------------------------------- 258
Cdd:COG5560 502 mciyyGGNYnmlepadkvllqdipqtdfvylyetndngievpvvHLRiekgykskrlfgdpflqlnvlikasiydklvke 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 259 -----------------------------GITTLTDC------------------------------------------- 266
Cdd:COG5560 582 feellvlvemkktdvdlvseqvrllreesSPSSWLKLeteidtkreeqveeegqmnfndavvisceweekrylslfsydp 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 267 -------------------LRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYI 327
Cdd:COG5560 662 lwtireigaaertitlqdcLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLV 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 328 SFPL-ELDMTPFMASSKESRMNgqlqlptnsgnnenkYSLFAVVNHQGTLESGHYTSFIRHHKDQ-WFKCDDAVITKASI 405
Cdd:COG5560 742 EYPIdDLDLSGVEYMVDDPRLI---------------YDLYAVDNHYGGLSGGHYTAYARNFANNgWYLFDDSRITEVDP 806
|
570
....*....|...
gi 223005906 406 KDVLDSEGYLLFY 418
Cdd:COG5560 807 EDSVTSSAYVLFY 819
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
7.15e-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: 115.11 E-value: 7.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMP--SPELCLVCEMSSLFRELYSG-------NPSPHVPYKLlHL 149
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQLIKLADGLLSGryskpasLKSENDPYQV-GI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 150 VWIHARHLAGY--------RQQDAHEFLIAALDVLHRHCKGddvgKAANNPNhcnciidQIFTGGLQSDVTCQACHGVST 221
Cdd:cd02658 80 KPSMFKALIGKghpefstmRQQDALEFLLHLIDKLDRESFK----NLGLNPN-------DLFKFMIEDRLECLSCKKVKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 222 TIDPCWDISLDLPgsctsfwpMSPGRESSVNGESHIPgiTTLTDCLRRFTRPEHLgssaKIKCGSCQSYQESTKQLTMNK 301
Cdd:cd02658 149 TSELSEILSLPVP--------KDEATEKEEGELVYEP--VPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 302 LPVVACFHFKRFEHSA-KQRRKITTYISFPLELDmtpfmasskesrmngqlqlptnSGnnenKYSLFAVVNHQGT-LESG 379
Cdd:cd02658 215 FPDYLVINMKRFQLLEnWVPKKLDVPIDVPEELG----------------------PG----KYELIAFISHKGTsVHSG 268
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 223005906 380 HYTSFIR---HHKDQWFKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02658 269 HYVAHIKkeiDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
1.77e-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 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: 113.97 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPILRDFFL-SDRHRCEMPSPELCLVCEMSSLFRELySGNPSPHVPYKLLHLVWIHARHL 157
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnYNPARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 158 A------GYRQQDAHEFLIAALDVLHRHCKGDDVGKAAnnpnhcnciIDQIFTGGLQSDVTCQACHGVSttidpcwdisl 231
Cdd:cd02657 80 AekqnqgGYAQQDAEECWSQLLSVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 232 dlpgsctsfwPMSPGRESSVNgeSHIpGITTLTDCLrrFTRPEHlGSSAKIKCGSCQSYQES--TKQLTMNKLPVVACFH 309
Cdd:cd02657 140 ----------EVSTESEYKLQ--CHI-SITTEVNYL--QDGLKK-GLEEEIEKHSPTLGRDAiyTKTSRISRLPKYLTVQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 310 FKRF--EHSAKQRRKITTYISFPLELDMTPFMasskesrmngqlqlpTNSGNnenkYSLFAVVNHQG-TLESGHYTSFIR 386
Cdd:cd02657 204 FVRFfwKRDIQKKAKILRKVKFPFELDLYELC---------------TPSGY----YELVAVITHQGrSADSGHYVAWVR 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 223005906 387 H-HKDQWFKCDDAVITKASIKDVLDSEG-------YLLFY 418
Cdd:cd02657 265 RkNDGKWIKFDDDKVSEVTEEDILKLSGggdwhiaYILLY 304
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
73-418 |
3.78e-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: 115.49 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 73 FTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLS---DRHRCEMPSPelcLVCEMSSLFRELYS-----GNPSPHvpy 144
Cdd:cd02669 115 YLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyenYENIKDRKSE---LVKRLSELIRKIWNprnfkGHVSPH--- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 145 KLLHLVWIHARHLAGYRQQ-DAHEFLIAALDVLHRHCKgddvGKAANNPNhcncIIDQIFTGGLQ-----------SDVT 212
Cdd:cd02669 189 ELLQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLG----GSKKPNSS----IIHDCFQGKVQietqkikphaeEEGS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 213 CQACHG----VSTTIDPCWDISLDLPgsctsfwPMSPGResSVNGESHIPGItTLTDCLRRFTrpehlGSsakikcgSCQ 288
Cdd:cd02669 261 KDKFFKdsrvKKTSVSPFLLLTLDLP-------PPPLFK--DGNEENIIPQV-PLKQLLKKYD-----GK-------TET 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 289 SYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYISFPLE-LDMTPFMASskesrmngqlqlPTNSGNNENKYSLF 367
Cdd:cd02669 319 ELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKnLDLSDYVHF------------DKPSLNLSTKYNLV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 223005906 368 AVVNHQGT-LESGHYTSFIRHHK-DQWFKCDDAVITKASIKDVLDSEGYLLFY 418
Cdd:cd02669 387 ANIVHEGTpQEDGTWRVQLRHKStNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
2.91e-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: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPilrDFFLSDRHRCEMPSP--ELCLVCEmssLFRELYSGNPSPHVPYKLLHLVWIHARH 156
Cdd:cd02671 26 GLNNLGNTCYLNSVLQVLYFCP---GFKHGLKHLVSLISSveQLQSSFL---LNPEKYNDELANQAPRRLLNALREVNPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 157 LAGYRQQDAHEFLIAALDVLHRhckgddvgkaannpnhcncIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGS 236
Cdd:cd02671 100 YEGYLQHDAQEVLQCILGNIQE-------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 237 CTsfwpmSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHS 316
Cdd:cd02671 161 EL-----SKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 317 AKQR------RKITTYISFPLELDMtpFMASSKESRmngqlqlptnsgnneNKYSLFAVVNHQG-TLESGHYTSFIRhhk 389
Cdd:cd02671 236 GSEFdcygglSKVNTPLLTPLKLSL--EEWSTKPKN---------------DVYRLFAVVMHSGaTISSGHYTAYVR--- 295
|
330 340 350
....*....|....*....|....*....|....*...
gi 223005906 390 dqWFKCDDAVITKASIKDVLD---------SEGYLLFY 418
Cdd:cd02671 296 --WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
76-410 |
7.62e-27 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 113.81 E-value: 7.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 76 GLRGLINLGNTCFMNCIVQALTHTPILRD--FFLSDRHrcemPSPELCLVCEMSSLFRELYSGNpsphVPYKLLHLV--- 150
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDH----PRGRDSVALALQRLFYNLQTGE----EPVDTTELTrsf 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 151 -WIHARHlagYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNpnhcnciidqIFTGGLQSDVTCQACHGVSTTIDPCWDI 229
Cdd:COG5077 264 gWDSDDS---FMQHDIQEFNRVLQDNLEKSMRGTVVENALNG----------IFVGKMKSYIKCVNVNYESARVEDFWDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 230 SLDLPGSctsfwpmspgressvngeshipgiTTLTDCLRRFTRPEHLGSSakiKCGSCQSY--QESTKQLTMNKLPVVAC 307
Cdd:COG5077 331 QLNVKGM------------------------KNLQESFRRYIQVETLDGD---NRYNAEKHglQDAKKGVIFESLPPVLH 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 308 FHFKRFEHSAK--QRRKITTYISFPLELDMTPFMasSKESRmngqlqlptNSGNNENKYSLFAVVNHQGTLESGHYTSFI 385
Cdd:COG5077 384 LQLKRFEYDFErdMMVKINDRYEFPLEIDLLPFL--DRDAD---------KSENSDAVYVLYGVLVHSGDLHEGHYYALL 452
|
330 340
....*....|....*....|....*.
gi 223005906 386 RHHKD-QWFKCDDAVITKASIKDVLD 410
Cdd:COG5077 453 KPEKDgRWYKFDDTRVTRATEKEVLE 478
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
1.27e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 103.73 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLV--WIHARh 156
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASRppWFTPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 157 lagyRQQDAHEFLIAALDVLHrhckgddvgkaannpnhcnCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPgs 236
Cdd:cd02664 80 ----SQQDCSEYLRYLLDRLH-------------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 237 ctsfwpmspgressvngeshipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHS 316
Cdd:cd02664 135 -------------------------SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 317 AKQ--RRKITTYISFPLELDMtPFMASSKESRMNGQLQLPTNSGNNEN-----KYSLFAVVNHQGT-LESGHYTSFIRHH 388
Cdd:cd02664 190 QKThvREKIMDNVSINEVLSL-PVRVESKSSESPLEKKEEESGDDGELvtrqvHYRLYAVVVHSGYsSESGHYFTYARDQ 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 223005906 389 KDQ---------------------WFKCDDAVITKASIKDVLDSEG-------YLLFY 418
Cdd:cd02664 269 TDAdstgqecpepkdaeendesknWYLFNDSRVTFSSFESVQNVTSrfpkdtpYILFY 326
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
79-420 |
4.26e-24 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 101.42 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALT-HTP-----ILRDFF----LSDRHRCEMPSPELClvcEMSSLFRELysgnpsphVPYKLLH 148
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPkldelLDDLSKelkvLKNVIRKPEPDLNQE---EALKLFTAL--------WSSKEHK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 149 LVWIHARhlagYRQQDAHEFLIAALDVLhrhckgddvgkaaNNPNHcNCIIDQIF-TGGlqsdvtcqacHGVSTTIDPCW 227
Cdd:COG5533 70 VGWIPPM----GSQEDAHELLGKLLDEL-------------KLDLV-NSFTIRIFkTTK----------DKKKTSTGDWF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 228 DISLDLPgsctsfwpmspgRESSVNGEshipgiTTLTDCLRRFtrpEHLGSSAK-IKCGSCQSYQESTKQLTMN---KLP 303
Cdd:COG5533 122 DIIIELP------------DQTWVNNL------KTLQEFIDNM---EELVDDETgVKAKENEELEVQAKQEYEVsfvKLP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 304 VVACFHFKRFEHSAkQRRKITTYISFPLELdmtPFMASskesrmngqlqlPTNSGNNENKYSLFAVVNHQGTLESGHYTS 383
Cdd:COG5533 181 KILTIQLKRFANLG-GNQKIDTEVDEKFEL---PVKHD------------QILNIVKETYYDLVGFVLHQGSLEGGHYIA 244
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 223005906 384 FIRhHKDQWFKCDDAVITKASIKDVLDS---EGYLLFYHK 420
Cdd:COG5533 245 YVK-KGGKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
4.51e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 97.44 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALthtpilrdfflsdrhrcempspelclvcemSSLfrelysgnpsphvPYKLLHLVWIHArhla 158
Cdd:cd02662 1 GLVNLGNTCFMNSVLQAL------------------------------ASL-------------PSLIEYLEEFLE---- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 159 gyrQQDAHEFLIAALDVLHRHCKgddvgkaanNPnhcnciidqiFTGGLQSDVTCQACHGVST-TIDPCWDISLDLPgsc 237
Cdd:cd02662 34 ---QQDAHELFQVLLETLEQLLK---------FP----------FDGLLASRIVCLQCGESSKvRYESFTMLSLPVP--- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 238 tsfwpmspgressvngESHIPGITTLTDCLRRFTRPEHLGSsakIKCGSCQsyqestkqLTMNKLPVVACFHFKRFEHSA 317
Cdd:cd02662 89 ----------------NQSSGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDG 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 318 K-QRRKITTYISFPLELdmtpfmasskesrmngqlqlptnsgnNENKYSLFAVVNHQGTLESGHYTSFIRHH-------- 388
Cdd:cd02662 142 RgTSTKNSCKVSFPERL--------------------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPlfskdkep 195
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 223005906 389 -------------KDQWFKCDDAVITKASIKDVL-DSEGYLLFY 418
Cdd:cd02662 196 gsfvrmregpsstSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
79-397 |
3.30e-15 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 75.77 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQALTHTPILRDFFLSdrHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHAR--- 155
Cdd:pfam13423 2 GLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEasa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 156 -HLAGYRQQDAHEFLIAAL-DVLHR---HCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDIS 230
Cdd:pfam13423 80 lGLLDEDRETNSAISLSSLiQSFNRfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 231 LDLPgsctsfWPMSPGressvngeSHIPGITTLTDCLRRFTRPEhlgSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHF 310
Cdd:pfam13423 160 LIYP------RKPSSN--------NKKPPNQTFSSILKSSLERE---TTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 311 KRfeHSAKQRRKITTYISFPLELDMTpfmasskesrmngqLQLPTNSGNNENKYSLFAVVNH-QGTLESGHYTSFIR--- 386
Cdd:pfam13423 223 AL--TNEEWRQLWKTPGWLPPEIGLT--------------LSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVKvad 286
|
330
....*....|....*.
gi 223005906 387 -----HHKDQWFKCDD 397
Cdd:pfam13423 287 seledPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
79-418 |
6.37e-12 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 66.36 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 79 GLINLGNTCFMNCIVQAL-THTPiLRDFFL----------SDRH-------RCEMPSPELC---LVCEMSSLFRELYSGN 137
Cdd:cd02666 3 GLDNIGNTCYLNSLLQYFfTIKP-LRDLVLnfdeskaelaSDYPterriggREVSRSELQRsnqFVYELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 138 PSPHVPYKLLHLvwiharhlAGYRQQDAHEFLIAALDVLHRHCKGD---DVGKAANNPNHCNCIIDQIFTGGL-QSDVTC 213
Cdd:cd02666 82 TRSVTPSKELAY--------LALRQQDVTECIDNVLFQLEVALEPIsnaFAGPDTEDDKEQSDLIKRLFSGKTkQQLVPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 214 QACHGVSTTIDPCWDISLDLPgsCTSFWPMSPGRESSVngeshipgitTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQ-E 292
Cdd:cd02666 154 SMGNQPSVRTKTERFLSLLVD--VGKKGREIVVLLEPK----------DLYDALDRYFDYDSLTKLPQRSQVQAQLAQpL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 293 STKQLTMNKlpvvacfhfkRFEHSAKQRRKI---TTYISFPLELDMTPFMASSKESRMNGQLQlptnsGNNENKYSLFAV 369
Cdd:cd02666 222 QRELISMDR----------YELPSSIDDIDElirEAIQSESSLVRQAQNELAELKHEIEKQFD-----DLKSYGYRLHAV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 223005906 370 VNHQGTLESGHYTSFIRHHKDQ--WFKCDDAVITKASIKDVLDSEG-----YLLFY 418
Cdd:cd02666 287 FIHRGEASSGHYWVYIKDFEENvwRKYNDETVTVVPASEVFLFTLGntatpYFLVY 342
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
162-418 |
2.01e-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: 57.92 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 162 QQDAHEFL---IAALDVLHRHcKGDDVGKAANNPNHCNCIidQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDlpgsct 238
Cdd:cd02673 33 QQDAHEFLltlLEAIDDIMQV-NRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVS------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 239 sfwpMSPGRESSvngeshipgITTLTDCLRRFTRPEHlgssakiKCGSCQSYQESTKQLTMNkLPVVACFHFKRFehsaK 318
Cdd:cd02673 104 ----MIDNKLDI---------DELLISNFKTWSPIEK-------DCSSCKCESAISSERIMT-FPECLSINLKRY----K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 319 QRRKITTYisfpleldmtpfMASSKESRMNGQLQLPtnsgnnenKYSLFAVVNHQG-TLESGHYTSFIR--HHKDQWFKC 395
Cdd:cd02673 159 LRIATSDY------------LKKNEEIMKKYCGTDA--------KYSLVAVICHLGeSPYDGHYIAYTKelYNGSSWLYC 218
|
250 260
....*....|....*....|....*.
gi 223005906 396 DDAVITKASIKDVLD---SEGYLLFY 418
Cdd:cd02673 219 SDDEIRPVSKNDVSTnarSSGYLIFY 244
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
300-418 |
2.69e-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: 48.29 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 300 NKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKESRMNGQLQLPT-------NSGNNENKYSLFAVVNH 372
Cdd:cd02670 96 AKAPSCLIICLKRYGKTEGKAQKMFKKILIPDEIDIPDFVADDPRACSKCQLECRVcyddkdfSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223005906 373 QGT-LESGHYTSFIRHHKD------------QWFKCDD-----AVITKASIKDVLDSE-GYLLFY 418
Cdd:cd02670 176 RGTsLETGHYVAFVRYGSYsltetdneaynaQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
259-418 |
1.29e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 46.40 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 259 GITTLTDCLRRFT---RPEHLGSSAKIKCGSCQSYQEstkqltmnkLPVVACFHFKRFEHSAKQRRKITTYISFPLELdm 335
Cdd:cd02665 91 GYGNLHECLEAAMfegEVELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEFNQGRPEKIHDKLEFPQII-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223005906 336 tpfmasskesrmngqlqlptnsgnNENKYSLFAVVNHQGTLESGHYTSFI-RHHKDQWFKCDDAVITKASIKDVL-DSEG 413
Cdd:cd02665 160 ------------------------QQVPYELHAVLVHEGQANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVErDSFG 215
|
170
....*....|..
gi 223005906 414 -------YLLFY 418
Cdd:cd02665 216 ggrnpsaYCLMY 227
|
|
| |
