|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
86-477 |
1.25e-135 |
|
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: 418.20 E-value: 1.25e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 86 RYVGLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEyvqqpahiKEQRKKAEQSIPCQLQKLFLLLQTSENDSLETKD--L 163
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIP--------PTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 164 TQSFGWTSNEAYDQHDVQELCRLMFDALEHKWKGTEHEKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKPfga 243
Cdd:cd02659 73 TRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKG--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 244 ihaYKSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVLD 323
Cdd:cd02659 150 ---KKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 324 LNDYVNKEkrsttssawqqigknkSENEEDDMELgspnpkrctpgvqspnryqgsenvcvgqpidhaavddivKTSGDNV 403
Cdd:cd02659 227 MEPYTEKG----------------LAKKEGDSEK---------------------------------------KDSESYI 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 404 YELFSVMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEI-EKSFGGHPSGWN--------QSNTNAYMLMYRR 474
Cdd:cd02659 252 YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeEECFGGEETQKTydsgprafKRTTNAYMLFYER 331
|
...
gi 32563999 475 IDP 477
Cdd:cd02659 332 KSP 334
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
88-472 |
4.44e-72 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 243.50 E-value: 4.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 88 VGLVNQAMTCYLNSLVQSLYMTPEFRNamydweYVQQPAHIKEQRKKA-EQSIPCQLQK-LFLLLQTSENDSLETKDLTQ 165
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRD------YLLRISPLSEDSRYNkDINLLCALRDlFKALQKNSKSSSVSPKMFKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 166 SFGWTSNE--AYDQHDVQELCRLMFDALEHKWKG---TEHEKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKP 240
Cdd:pfam00443 75 SLGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 241 FGAIHAYKSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRfdFDYNTMHRIKLNDKMTFPD 320
Cdd:pfam00443 155 DSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKR--FSYNRSTWEKLNTEVEFPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 321 VLDLNDYVNKEkrsttssawqqigKNKSENEEDDmelgspnpkrctpgvqspnryqgsenvcvgqpidhaavddivktsg 400
Cdd:pfam00443 233 ELDLSRYLAEE-------------LKPKTNNLQD---------------------------------------------- 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32563999 401 dnvYELFSVMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVdfaTPLEIEKSFgghpsgwnqSNTNAYMLMY 472
Cdd:pfam00443 254 ---YRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKV---TEVDEETAV---------LSSSAYILFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
87-584 |
1.19e-65 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 243.24 E-value: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 87 YVGLVNQAMTCYLNSLVQSLYMTPEFRNAMYDweyvqqpahIKEQRKKAEQSIPCQLQKLFLLLQTSeNDSLETKDLTQS 166
Cdd:COG5077 193 YVGLRNQGATCYMNSLLQSLFFIAKFRKDVYG---------IPTDHPRGRDSVALALQRLFYNLQTG-EEPVDTTELTRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 167 FGWTSNEAYDQHDVQELCRLMFDALEHKWKGTEHEKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKPFgaiha 246
Cdd:COG5077 263 FGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGM----- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 247 yKSVEEALTAFVQPELLDGSNQYMCENcKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVLDLND 326
Cdd:COG5077 338 -KNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLP 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 327 YVNKEkrsttssawqqigKNKSENEeddmelgspnpkrctpgvqspnryqgsenvcvgqpidhaavddivktsgDNVYEL 406
Cdd:COG5077 416 FLDRD-------------ADKSENS-------------------------------------------------DAVYVL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 407 FSVMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEI-EKSFGG----HPSGWN----QSNTNAYMLMYRRIDP 477
Cdd:COG5077 434 YGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVlEENFGGdhpyKDKIRDhsgiKRFMSAYMLVYLRKSM 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 478 KRN-ARFILSNQLPQHIKD--SQEKWKRLEREAEDERLRKLSLIQVYVTINYPFPSVVTLPDKKQLDltpqkyqiaEDFG 554
Cdd:COG5077 514 LDDlLNPVAAVDIPPHVEEvlSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFDYPDFSSEL---------NDSG 584
|
490 500 510
....*....|....*....|....*....|
gi 32563999 555 EYKTEISREMPIKNVFNHAFEFFNERARAY 584
Cdd:COG5077 585 LAQFVIKRGAKISDLRNNIAEHLNTPQSLY 614
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
89-473 |
2.46e-59 |
|
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: 204.64 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMtpefrnamydweyvqqpahikeqrkkaeqsipcqlqklflllqtsendsletkdltqsfg 168
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 169 wtsneayDQHDVQELCRLMFDALEHKWKG--------TEHEKLIQDLYRGTMEDFVACLKCGRESVKTD--YFLDLPLAV 238
Cdd:cd02257 21 -------EQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESVSTEpeLFLSLPLPV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 239 KPFGaihaYKSVEEALTAFVQPELLDGSNQYMCEnCKSKQDAHKGLRITQFPYLLTIQLKRFDFDyNTMHRIKLNDKMTF 318
Cdd:cd02257 94 KGLP----QVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSF 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 319 PDVLDLNDYVNKEKrsttssawqqigknkseneeddmelgspnpkrctpgvqspnryqgsenvcvgqpidhaavDDIVKT 398
Cdd:cd02257 168 PLELDLSPYLSEGE------------------------------------------------------------KDSDSD 187
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563999 399 SGDNVYELFSVMVHSGNAA-GGHYFAYIKNLDQDRWYVFNDTRVDFATPLEIEKSFGghpsgwnqSNTNAYMLMYR 473
Cdd:cd02257 188 NGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEFGS--------LSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-473 |
4.53e-56 |
|
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: 198.03 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEYVQQPAH--IKEQRKKAEQSIPCQLQKLFLLLQTSENDSLETKDLTQS 166
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELknMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 167 FGwTSNEayDQHDVQELCRLMFDALE---HKWKGTEHEKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKPFga 243
Cdd:cd02668 81 LG-LDTG--QQQDAQEFSKLFLSLLEaklSKSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 244 ihayKSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVLD 323
Cdd:cd02668 156 ----KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 324 LNDYvnkekrsttssawqqigknkseneeddmelgspnpkrctpgvqspnryqgsenvCVGQPidhaavddivktSGDNV 403
Cdd:cd02668 232 MGEY------------------------------------------------------LAESD------------EGSYV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 404 YELFSVMVHSGNAA-GGHYFAYIKNLDQDRWYVFNDTRVDFATPLEIEK---------SFGGHPSGWnQSNTNAYMLMYR 473
Cdd:cd02668 246 YELSGVLIHQGVSAySGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLgnsedpakpRKSEIKKGT-HSSRTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-472 |
3.08e-44 |
|
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: 162.83 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEYVQQPAHIK-----EQRKKAEQSIPCQLQKLFLLLQTSEndsleTKDL 163
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcmmcALEAHVERALASSGPGSAPRIFSSN-----LKQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 164 TQSFGwtsneAYDQHDVQELCRLMFDALE------HKWKGTEHEK-----LIQDLYRGTMEDFVACLKCGRESVKTDYFL 232
Cdd:cd02661 78 SKHFR-----IGRQEDAHEFLRYLLDAMQkacldrFKKLKAVDPSsqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 233 DLPLAvkpfgaIHAYKSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFdyNTMHriKL 312
Cdd:cd02661 153 DLSLD------IKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSN--FRGG--KI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 313 NDKMTFPDVLDLNDYVnkekrsttssawqqigknkseneeddmelgspnpkrctpgvqspnrYQGSENVCvgqpidhaav 392
Cdd:cd02661 223 NKQISFPETLDLSPYM----------------------------------------------SQPNDGPL---------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 393 ddivktsgdnVYELFSVMVHSG-NAAGGHYFAYIKNlDQDRWYVFNDTRVdfaTPLEIEKSFgghpsgwnqsNTNAYMLM 471
Cdd:cd02661 247 ----------KYKLYAVLVHSGfSPHSGHYYCYVKS-SNGKWYNMDDSKV---SPVSIETVL----------SQKAYILF 302
|
.
gi 32563999 472 Y 472
Cdd:cd02661 303 Y 303
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-473 |
3.99e-39 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 148.79 E-value: 3.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNamydweyvqQPAHIKEQRKKAEQSIPCQLQKLFLLLQTSENDSLETKD--LTQS 166
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRR---------QVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPDyfLEAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 167 FGWTSNEAYdQHDVQELCRLMFDALEhkwkgteheKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKpfgaiha 246
Cdd:cd02664 72 RPPWFTPGS-QQDCSEYLRYLLDRLH---------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 247 ykSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVLDLNd 326
Cdd:cd02664 135 --SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLP- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 327 yVNKEKRSTTSSawqqigknkseNEEDDMElgspnpkrctpgvqspnryQGSENVCVGQPIdhaavddivktsgdnVYEL 406
Cdd:cd02664 212 -VRVESKSSESP-----------LEKKEEE-------------------SGDDGELVTRQV---------------HYRL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 407 FSVMVHSGNAA-GGHYFAYIKNL--------------------DQDRWYVFNDTRVDFATPLEIEK--SFGGHpsgwnqs 463
Cdd:cd02664 246 YAVVVHSGYSSeSGHYFTYARDQtdadstgqecpepkdaeendESKNWYLFNDSRVTFSSFESVQNvtSRFPK------- 318
|
410
....*....|
gi 32563999 464 NTnAYMLMYR 473
Cdd:cd02664 319 DT-PYILFYE 327
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-473 |
5.22e-39 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 145.51 E-value: 5.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 176 DQHDVQELCRLMFDALEhkwkgteheKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVkPFGAIHAYK-SVEEAL 254
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI-PSGSGDAPKvTLEDCL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 255 TAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMhrIKLNDKMTFPDV-LDLNDYVnkekr 333
Cdd:cd02674 91 RLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPLNdLDLTPYV----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 334 sttssawqqigknkseneeddMELGSPNPKRctpgvqspnryqgsenvcvgqpidhaavddivktsgdnvYELFSVMVHS 413
Cdd:cd02674 164 ---------------------DTRSFTGPFK---------------------------------------YDLYAVVNHY 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 414 GNAAGGHYFAYIKNLDQDRWYVFNDTRVdfaTPLEIEksfgghpsgwNQSNTNAYMLMYR 473
Cdd:cd02674 184 GSLNGGHYTAYCKNNETNDWYKFDDSRV---TKVSES----------SVVSSSAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-472 |
9.58e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 127.49 E-value: 9.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEYvQQPAHIKEQRKkaeqSIPCQLQKLFLLLQTSENdsletkdlTQSFG 168
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRH-SCTCLSCSPNS----CLSCAMDEIFQEFYYSGD--------RSPYG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 169 --------WTSN---EAYDQHDVQELCRLMFDALE------HKWKGTEHEK--LIQDLYRGTMEDFVACLKCGRESVKTD 229
Cdd:cd02660 69 pinllylsWKHSrnlAGYSQQDAHEFFQFLLDQLHthyggdKNEANDESHCncIIHQTFSGSLQSSVTCQRCGGVSTTVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 230 YFLDLPLAVKP-------FGAIH--AYKSVEEALTAFVQPELLdGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRF 300
Cdd:cd02660 149 PFLDLSLDIPNkstpswaLGESGvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 301 DFDYNTMHRiKLNDKMTFPDVLDLNDYvnkekrsTTSSawqqIGKNKSENEEDdmelgspnpkrctpgvqspnryqgsen 380
Cdd:cd02660 228 EHSLNKTSR-KIDTYVQFPLELNMTPY-------TSSS----IGDTQDSNSLD--------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 381 vcvgqpidhaavddivktsGDNVYELFSVMVHSGNAAGGHYFAYIKNLDqDRWYVFNDTRVdfaTPLEIEKSFGghpsgw 460
Cdd:cd02660 269 -------------------PDYTYDLFAVVVHKGTLDTGHYTAYCRQGD-GQWFKFDDAMI---TRVSEEEVLK------ 319
|
410
....*....|..
gi 32563999 461 nqsnTNAYMLMY 472
Cdd:cd02660 320 ----SQAYLLFY 327
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-473 |
4.78e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 115.18 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRnamydweyvqqpAHIKEQ--------RKKAEQSIpcqlqklflllqtsendslet 160
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALR------------ELLSETpkelfsqvCRKAPQFK--------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 161 kdltqsfgwtsneAYDQHDVQELCRLMFDALEhkwkgteheKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKP 240
Cdd:cd02667 48 -------------GYQQQDSHELLRYLLDGLR---------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 241 FgaIHAYKSVEEALTAFVQPELLDGSNQYMCENCkskQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRiKLNDKMTFPD 320
Cdd:cd02667 106 E--IKSECSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 321 VLDLNDYvnkekrsttssawqqigknkseneeddmelgspnpkrCTPGVQSPnryQGSENVcvgqpidhaavddivktsg 400
Cdd:cd02667 180 ILDLAPF-------------------------------------CDPKCNSS---EDKSSV------------------- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 401 dnVYELFSVMVHSGNAAGGHYFAYIK---------------------NLDQDRWYVFNDTRVDFATPLEIEKSfgghpsg 459
Cdd:cd02667 201 --LYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltkskpaadeaGPGSGQWYYISDSDVREVSLEEVLKS------- 271
|
410
....*....|....
gi 32563999 460 wnqsntNAYMLMYR 473
Cdd:cd02667 272 ------EAYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-472 |
2.96e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 107.78 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYmtpeFRNAMY---DWEYVqqpahIKEQRKKAEQSIPcqlqKLFLLLQTSEN---DSLETKD 162
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY----FENLLTclkDLFES-----ISEQKKRTGVISP----KKFITRLKRENelfDNYMHQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 163 LTQSFGWTSNEAYDQHDVQELCRLMFDALEHKWKGTEHEKLIQDLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKPfg 242
Cdd:cd02663 68 AHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 243 aihaYKSVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVL 322
Cdd:cd02663 146 ----NTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 323 DLndyvnkekrsttssawqqigKNKSENEEDDmelgspnpkrctpgvqspnryqgsenvcvgqpidhaavddivktsgDN 402
Cdd:cd02663 222 RL--------------------FNTTDDAENP----------------------------------------------DR 235
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32563999 403 VYELFSVMVHSGNAAG-GHYFAYIKNldQDRWYVFNDTRVDFATPLEIEKSFGGHPsgwnqSNTNAYMLMY 472
Cdd:cd02663 236 LYELVAVVVHIGGGPNhGHYVSIVKS--HGGWLLFDDETVEKIDENAVEEFFGDSP-----NQATAYVLFY 299
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-473 |
1.18e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 94.32 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNAMydweyvqqpahikeqrkKAEQSIPCQLQKLFLLLQTSENDSLETKDLTQS-- 166
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDAL-----------------KNYNPARRGANQSSDNLTNALRDLFDTMDKKQEpv 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 167 ---------------FGWTSNEA-YDQHDVQELCRLMFDALEHKWKG-TEHEKLIQDLYRGTMEDFVACLKCGRESVKT- 228
Cdd:cd02657 64 ppieflqllrmafpqFAEKQNQGgYAQQDAEECWSQLLSVLSQKLPGaGSKGSFIDQLFGIELETKMKCTESPDEEEVSt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 229 --DYFLDLPLAVKpfgaihayksveeALTAFVQPELLDGSNQYMCENCKSKQ-DA--HKGLRITQFPYLLTIQLKRFDFD 303
Cdd:cd02657 144 esEYKLQCHISIT-------------TEVNYLQDGLKKGLEEEIEKHSPTLGrDAiyTKTSRISRLPKYLTVQFVRFFWK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 304 YNTMHRIKLNDKMTFPDVLDLNDYvnkekrsttssawqqigknkseneeddmelgspnpkrCTPgvqspnryqgsenvcv 383
Cdd:cd02657 211 RDIQKKAKILRKVKFPFELDLYEL-------------------------------------CTP---------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 384 gqpidhaavddivktSGdnVYELFSVMVHSG-NAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEIEKSFGGHPSgwnq 462
Cdd:cd02657 238 ---------------SG--YYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLSGGGDW---- 296
|
410
....*....|.
gi 32563999 463 snTNAYMLMYR 473
Cdd:cd02657 297 --HIAYILLYK 305
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
63-473 |
1.60e-19 |
|
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: 91.49 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 63 ASSSSPANVANNQYAIPvdenghrYVGLVNQAMTCYLNSLVQSLYMTPEFRNAMydwEYVQQPAHIKEQRKKAEQSIPcq 142
Cdd:cd02671 7 PQPSSATSCEKRENLLP-------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGL---KHLVSLISSVEQLQSSFLLNP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 143 LQKLFLLLQTSENDSLET-KDLTQSFgwtsnEAYDQHDVQELCRLMFDALEhkwkgteheKLIQDLYRGTMEDFVACLKC 221
Cdd:cd02671 75 EKYNDELANQAPRRLLNAlREVNPMY-----EGYLQHDAQEVLQCILGNIQ---------ELVEKDFQGQLVLRTRCLEC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 222 GRESVKTDYFLDLPLAVKPFGAIHAYKSVE-------------EALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQ 288
Cdd:cd02671 141 ETFTERREDFQDISVPVQESELSKSEESSEispdpktemktlkWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 289 FPYLLTIQLKRFDFDYNTMHRI----KLNDKMTFPDVLDLNDYVNKEKRsttssawqqigknkseneeddmelgspnpkr 364
Cdd:cd02671 221 LPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLEEWSTKPKN------------------------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 365 ctpgvqspnryqgsenvcvgqpidhaavddivktsgdNVYELFSVMVHSG-NAAGGHYFAYIknldqdRWYVFNDTRVDF 443
Cdd:cd02671 270 -------------------------------------DVYRLFAVVMHSGaTISSGHYTAYV------RWLLFDDSEVKV 306
|
410 420 430
....*....|....*....|....*....|
gi 32563999 444 ATPLEIEKSFgghpSGWNQSNTNAYMLMYR 473
Cdd:cd02671 307 TEEKDFLEAL----SPNTSSTSTPYLLFYK 332
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-473 |
3.93e-17 |
|
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: 83.91 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEYVQQPA------HIKEQRKK---AEQSIPCQLQKLFLLLQTSENDSLE 159
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvdpanDLNCQLIKladGLLSGRYSKPASLKSENDPYQVGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 160 TKDLTQSFGwTSNEAYD---QHDVQELCRLMFDALEHKWKgTEHEKLIQDLYRGTMEDFVACLKCGR--ESVKTDYFLDL 234
Cdd:cd02658 81 PSMFKALIG-KGHPEFStmrQQDALEFLLHLIDKLDRESF-KNLGLNPNDLFKFMIEDRLECLSCKKvkYTSELSEILSL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 235 PL-----AVKPFGAIhAYKSV--EEALTAFVQPELLDgsnqYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDF--DYN 305
Cdd:cd02658 159 PVpkdeaTEKEEGEL-VYEPVplEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 306 TMhriKLNDKMTFPDVLDlndyvnkekrsttssawqqIGKnkseneeddmelgspnpkrctpgvqspnryqgsenvcvgq 385
Cdd:cd02658 234 PK---KLDVPIDVPEELG-------------------PGK---------------------------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 386 pidhaavddivktsgdnvYELFSVMVHSGNAA-GGHYFAYIKNL--DQDRWYVFNDTRVDFATPLEIEKsfgghpsgwnq 462
Cdd:cd02658 252 ------------------YELIAFISHKGTSVhSGHYVAHIKKEidGEGKWVLFNDEKVVASQDPPEMK----------- 302
|
410
....*....|.
gi 32563999 463 snTNAYMLMYR 473
Cdd:cd02658 303 --KLGYIYFYQ 311
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
89-327 |
7.53e-14 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 72.78 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRnamydwEYVqqpahikeqrkkaeqsipcqlqklflllqtsendsletkdltqsfg 168
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLI------EYL---------------------------------------------- 28
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 169 wtsNEAYDQHDVQELCRLMFDALEHKWKGtehekliqdLYRGTMEDFVACLKCGRES-VKTDYFLDLPLAVkPFGAIHAY 247
Cdd:cd02662 29 ---EEFLEQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPV-PNQSSGSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 248 KSVEEALTAFVQPELLDGsnqYMCENCKSKqdahkglrITQFPYLLTIQLKRFDFDYNTMHRiKLNDKMTFPDVLDLNDY 327
Cdd:cd02662 96 TTLEHCLDDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRGTST-KNSCKVSFPERLPKVLY 163
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
249-474 |
1.11e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 76.08 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 249 SVEEALTAFVQPELLDGSNQYMCENCKSKQDAHKGLRITQFPYLLTIQLKRFDFDYNTmhRIKLNDKMTFP-DVLDLNDY 327
Cdd:COG5560 676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGV 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 328 vnkekrsttssawqqigknksENEEDDMELGspnpkrctpgvqspnryqgsenvcvgqpidhaavddivktsgdnvYELF 407
Cdd:COG5560 754 ---------------------EYMVDDPRLI---------------------------------------------YDLY 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32563999 408 SVMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEIEKSfgghpsgwnqsntNAYMLMYRR 474
Cdd:COG5560 768 AVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTS-------------SAYVLFYRR 821
|
|
| USP47_C |
pfam19718 |
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ... |
1159-1318 |
5.53e-13 |
|
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of Ubiquitin carboxyl-terminal hydrolase 47 (USP47), a ubiquitin-specific protease involved in deubiquitinating of monoubiquitinated DNA polymerase beta (Polbeta), being required for its stability and, therefore, plays a role in DNA base excision repair (BER). The C-terminal domains in USPs mediate protein- protein interactions.
Pssm-ID: 466158 Cd Length: 240 Bit Score: 70.17 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 1159 SHLYLQIITDEAMIGKPGE-PIMVRRFRPSTVEVNPTHEVLVDanaENPVVSFVEALSKISGIPVERLAITDLKefnwQK 1237
Cdd:pfam19718 83 WEMYVEPLKGPEKKKHTTQlQVYVRRWHPSQCSVDPFEEIILD---NRTPKELKEKLSELSGVPVEYIYIAKGK----GS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 1238 WPYLKSRLDmLENKVNFTKDLQVTYPLPREFLDKvgSRVLYYKDSDEEAKVLSEDERKQIKIKEN------GQSANANRR 1311
Cdd:pfam19718 156 FPCEISVLD-IENELEWNSITSSLSSYPLYLYED--GHVIYYKDNRETMKELTDEERSEIQQKENarltkiSERSSYSPR 232
|
....*..
gi 32563999 1312 KERPLRI 1318
Cdd:pfam19718 233 KERALKI 239
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
177-472 |
4.38e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 64.12 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 177 QHDVQELCRLMFDALEHKWKGTEH-----EKLIQDLYRGTMEDFVA-CLKCGRESVKTDYFLDLPLAVKPFGAIHayksv 250
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEaispgEKSKNPMVQLFYGTFLTeGVLEGKPFCNCETFGQYPLQVNGYGNLH----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 251 eEALTAfvqpELLDGSnqymCENCKSKQDAHKGLR--ITQFPYLLTIQLKRFDFdyNTMHRIKLNDKMTFPDVLDlndyv 328
Cdd:cd02665 97 -ECLEA----AMFEGE----VELLPSDHSVKSGQErwFTELPPVLTFELSRFEF--NQGRPEKIHDKLEFPQIIQ----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 329 nkekrsttssawqqigknkseneeddmelgspnpkrctpgvQSPnryqgsenvcvgqpidhaavddivktsgdnvYELFS 408
Cdd:cd02665 161 -----------------------------------------QVP-------------------------------YELHA 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32563999 409 VMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEIEK-SFGGHpsgwnqSNTNAYMLMY 472
Cdd:cd02665 169 VLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERdSFGGG------RNPSAYCLMY 227
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
89-475 |
3.46e-09 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 59.43 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSL-YMTPEFRNAMydweyVQQPAHIKEQRKKAEQSIPCQLQKLFLLLQTSENDSLETKdltqsF 167
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELL-----DDLSKELKVLKNVIRKPEPDLNQEEALKLFTALWSSKEHK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 168 GWTSNeAYDQHDVQELCRLMFDALEhkwkgteheklIQDLYRGTMEDFvaclKCGRESVKTDYfldlplavKPFGAIH-- 245
Cdd:COG5533 71 GWIPP-MGSQEDAHELLGKLLDELK-----------LDLVNSFTIRIF----KTTKDKKKTST--------GDWFDIIie 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 246 -AYKSVEEALTAFvqPELLDGSNQYMCENCKSKQDAHKGLRI----------TQFPYLLTIQLKRFDFDyNTMHRIKlnd 314
Cdd:COG5533 127 lPDQTWVNNLKTL--QEFIDNMEELVDDETGVKAKENEELEVqakqeyevsfVKLPKILTIQLKRFANL-GGNQKID--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 315 kmtfpdvldlndyvnkekrsttssawqqigknKSENEEDDMelgspnpkrctpgvqspnryqgsenvcvgqPIDHAAVDD 394
Cdd:COG5533 201 --------------------------------TEVDEKFEL------------------------------PVKHDQILN 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 395 IVKTSgdnVYELFSVMVHSGNAAGGHYFAYIKNLDQdrWYVFNDTRVdfaTPLEIEKSFgghpsgwNQSNTNAYMLMYRR 474
Cdd:COG5533 219 IVKET---YYDLVGFVLHQGSLEGGHYIAYVKKGGK--WEKANDSDV---TPVSEEEAI-------NEKAKNAYLYFYER 283
|
.
gi 32563999 475 I 475
Cdd:COG5533 284 I 284
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
88-449 |
3.80e-09 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 60.20 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 88 VGLVNQAMTCYLNSLVQSLYMTPEFRNAM--YDWEYVQQPAHIKEQRKKAEQSIPCQLQKLFLLLQ-----------TSE 154
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnFDESKAELASDYPTERRIGGREVSRSELQRSNQFVyelrslfndliHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 155 NDSLE-TKDLTqsfgwtsNEAYDQHDVQELCRLMFDALEHKWK-------------GTEHEKLIQDLYRG-TMEDFVACL 219
Cdd:cd02666 82 TRSVTpSKELA-------YLALRQQDVTECIDNVLFQLEVALEpisnafagpdtedDKEQSDLIKRLFSGkTKQQLVPES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 220 KCGRESV--KTDYFLDLPlavkpfgaIHAYKSVEEALTAFVQPELLDGSNQYMcenckskqdahKGLRITQFPYLLTIQL 297
Cdd:cd02666 155 MGNQPSVrtKTERFLSLL--------VDVGKKGREIVVLLEPKDLYDALDRYF-----------DYDSLTKLPQRSQVQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 298 KrfdfdyntmhriklNDKMTFPDVLDLNDYVNKEKRSTTSSAWQQ-IGKNKSENEEDDMELGSPNPKRctpgvqspnryq 376
Cdd:cd02666 216 Q--------------LAQPLQRELISMDRYELPSSIDDIDELIREaIQSESSLVRQAQNELAELKHEI------------ 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32563999 377 gsenvcvgqpidhAAVDDIVKtsgDNVYELFSVMVHSGNAAGGHYFAYIKNLDQDRWYVFNDTRVDFATPLEI 449
Cdd:cd02666 270 -------------EKQFDDLK---SYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
88-441 |
3.95e-08 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 56.51 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 88 VGLVNQAMTCYLNSLVQSLYMTPEFRN-AMydweyvqqpAHIKE--QRK---------------KAEqSIPCQlqklfll 149
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlAL---------SHLATecLKEhcllcelgflfdmleKAK-GKNCQ------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 150 lqtSEN--DSLETKDLTQSFG-------WTSNEAYdQHDVQELCRLMFDALEHKWKGTEH-----EKLIQDLYRGTMEDF 215
Cdd:pfam13423 64 ---ASNflRALSSIPEASALGlldedreTNSAISL-SSLIQSFNRFLLDQLSSEENSTPPnpspaESPLEQLFGIDAETT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 216 VACLKCGRESVKTD--YFLDL--PLAVKPFGAIHAYKSVEEALTAFVQPELldgSNQYMCENCKSKQDAHKGLRITQFPY 291
Cdd:pfam13423 140 IRCSNCGHESVRESstHVLDLiyPRKPSSNNKKPPNQTFSSILKSSLERET---TTKAWCEKCKRYQPLESRRTVRNLPP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 292 LLTIqlkrfdfdyNTMhriklndkmtfpdvldlndyvnkekrsTTSSAWQQIGKNKSeneeddmELgspnPKRctpgvqs 371
Cdd:pfam13423 217 VLSL---------NAA---------------------------LTNEEWRQLWKTPG-------WL----PPE------- 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32563999 372 pnryqgsenvcvgqpIDHAAVDDIVKTSGDNVYELFSVMVHSGNAAG-GHYFAYIK-------NLDQDRWYVFNDTRV 441
Cdd:pfam13423 243 ---------------IGLTLSDDLQGDNEIVKYELRGVVVHIGDSGTsGHLVSFVKvadseleDPTESQWYLFNDFLV 305
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
89-239 |
2.09e-04 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 45.64 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 89 GLVNQAMTCYLNSLVQSLYMTPEFRNAMYDWEYVQQpahIKEQRKKA-EQSIPCQLQKLFLLLQTSENDSLETKDLTQSF 167
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEES---INEENPLGmHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 168 G--WTSNEAYDQHDVQELCRLMFDAL----------------------EHKWKGTEHEK----------LIQDLYRGTME 213
Cdd:COG5560 344 GsfNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytskpdlspgdDVVVKKKAKECwwehlkrndsIITDLFQGMYK 423
|
170 180
....*....|....*....|....*...
gi 32563999 214 DFVACLKCGRESVKTDYFLD--LPLAVK 239
Cdd:COG5560 424 STLTCPGCGSVSITFDPFMDltLPLPVS 451
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
369-438 |
6.19e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 40.19 E-value: 6.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32563999 369 VQSPNRYQGSENVCVGQP-IDHAAVDDIVKTSGDNVYELFSVMVH-SGNAAGGHYFAYI----KNLDQDRWYVFND 438
Cdd:cd02672 177 INVVLPSGKVMQNKVSPKaIDHDKLVKNRGQESIYKYELVGYVCEiNDSSRGQHNVVFVikvnEESTHGRWYLFND 252
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
176-327 |
8.66e-03 |
|
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: 39.43 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 176 DQHDVQELCRLMFDAL------EHKWKGTEHEKLIQ----DLYRGTMEDFVACLKCGRESVKTDYFLDLPLAVKPfgaiH 245
Cdd:cd02673 32 DQQDAHEFLLTLLEAIddimqvNRTNVPPSNIEIKRlnplEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID----N 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32563999 246 AYKSVEEALTAFVQPElldgSNQYMCENCKSkQDAHKGLRITQFPYLLTIQLKRFDFDYNTMHRIKLNDKMTFPDVLDLN 325
Cdd:cd02673 108 KLDIDELLISNFKTWS----PIEKDCSSCKC-ESAISSERIMTFPECLSINLKRYKLRIATSDYLKKNEEIMKKYCGTDA 182
|
..
gi 32563999 326 DY 327
Cdd:cd02673 183 KY 184
|
|
| |
