|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-452 |
8.26e-45 |
|
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: 157.53 E-value: 8.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 46 GLSNAANDCFINSVLQALAGLPDLRIYLIREThrrkldgpevyevdpgrlntdnssvtpgkleglqqgvltyglkdvlda 125
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEFL------------------------------------------------ 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 126 lnerpiykktispqpfirslerafgtrisrQQQDAQEFLQIVTERLCDEYhagskarrqalkrginvangdtaserskii 205
Cdd:cd02662 33 ------------------------------EQQDAHELFQVLLETLEQLL------------------------------ 52
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 206 eqfgtapaaasdsntieeeeedddededkppvdedGFPFEGKIESQIECETCHFKPKPSVSTFVTLTLNVPQ---VSSTS 282
Cdd:cd02662 53 -----------------------------------KFPFDGLLASRIVCLQCGESSKVRYESFTMLSLPVPNqssGSGTT 97
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 283 LNACFDGMLKVESIDDFKCERCRLEhalrskdhelsqatdvevreriqsdivkirhametdpenppkdvelpdskqspkr 362
Cdd:cd02662 98 LEHCLDDFLSTEIIDDYKCDRCQTV------------------------------------------------------- 122
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 363 risrhmyISQFPKVLAIHLSRSVYAIGSASTKNLAKVSFPETLPlggllhRKNYKLLGAVTHKGSHNSGHYEAFRRQVQP 442
Cdd:cd02662 123 -------IVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP------KVLYRLRAVVVHYGSHSSGHYVCYRRKPLF 189
|
410
....*....|
gi 160702019 443 LPFSTPVSFG 452
Cdd:cd02662 190 SKDKEPGSFV 199
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
45-439 |
1.51e-30 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 120.63 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 45 VGLSNAANDCFINSVLQALAGLPDLRIYLIRETHRRKLDGPEvyevdpgrlntdnssvtpgkleglQQGVLTYGLKDVLD 124
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYN------------------------KDINLLCALRDLFK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 125 ALNERpIYKKTISPQPFIRSLERAFGTRISRQQQDAQEFLQIVTERLcdeyHAGSkarrqalkrginvaNGDTASERSKI 204
Cdd:pfam00443 57 ALQKN-SKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL----HEDL--------------NGNHSTENESL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 205 IEQFgtapaaasdsntieeeeedddededkppvdedgfpFEGKIESQIECETCHFKPKPSVsTFVTLTLNVPQVSSTSLN 284
Cdd:pfam00443 118 ITDL-----------------------------------FRGQLKSRLKCLSCGEVSETFE-PFSDLSLPIPGDSAELKT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 285 ACFDGMLKVESI-------DDFKCERCrlehalrskdHELSQATdvevreriqsdivkirhametdpenppkdvelpdsk 357
Cdd:pfam00443 162 ASLQICFLQFSKleelddeEKYYCDKC----------GCKQDAI------------------------------------ 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 358 qspkrrisRHMYISQFPKVLAIHLSRSVYAiGSASTKNLAKVSFPETLPLGGLL---------HRKNYKLLGAVTHKGSH 428
Cdd:pfam00443 196 --------KQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTEVEFPLELDLSRYLaeelkpktnNLQDYRLVAVVVHSGSL 266
|
410
....*....|.
gi 160702019 429 NSGHYEAFRRQ 439
Cdd:pfam00443 267 SSGHYIAYIKA 277
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
153-439 |
1.86e-27 |
|
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: 110.65 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 153 ISRQQQDAQEFLQIVTERLCDEYHAGSKarrqalkrginvaNGDTASERSKIIEQfgtapaaasdsntieeeeedddede 232
Cdd:cd02257 18 LFSEQQDAHEFLLFLLDKLHEELKKSSK-------------RTSDSSSLKSLIHD------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 233 dkppvdedgfPFEGKIESQIECETCHF-KPKPSVSTFVTLTLNVPQVSSTSLNACFDGMLKVESIDDFKCERCrlehalr 311
Cdd:cd02257 60 ----------LFGGKLESTIVCLECGHeSVSTEPELFLSLPLPVKGLPQVSLEDCLEKFFKEEILEGDNCYKC------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 312 skdhelsqatdvevreriqsdivkirhametdpenppkdvelpdsKQSPKRRISRHMYISQFPKVLAIHLSRSVYAIGSA 391
Cdd:cd02257 123 ---------------------------------------------EKKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGT 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 392 STKNLAKVSFPETLPL-----------GGLLHRKNYKLLGAVTHKGSH-NSGHYEAFRRQ 439
Cdd:cd02257 158 KEKLNTKVSFPLELDLspylsegekdsDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKD 217
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
244-436 |
9.90e-18 |
|
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: 82.34 E-value: 9.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 244 FEGKIESQIECETCHfkpKPSVS--TFVTLTLNVPQVSST----SLNACFDGMLKVESIDDFKCERCrlehalrskdhel 317
Cdd:cd02674 44 FQGQLKSRLTCLTCG---KTSTTfePFTYLSLPIPSGSGDapkvTLEDCLRLFTKEETLDGDNAWKC------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 318 sqatdvevreriqsdivkirhametdpenppkdvelpdSKQSPKRRISRHMYISQFPKVLAIHLSRSVYAIGSAStKNLA 397
Cdd:cd02674 108 --------------------------------------PKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTR-KLTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 160702019 398 KVSFP-------ETLPLGGLLHRKNYKLLGAVTHKGSHNSGHYEAF 436
Cdd:cd02674 149 PVTFPlndldltPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAY 194
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-436 |
1.43e-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: 239126 [Multi-domain] Cd Length: 304 Bit Score: 74.23 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 46 GLSNAANDCFINSVLQALAGLPDLRIYLIRETHRRKLDGPEvyevdpgrlntdnssvtPGKLEGLQQGVLTYglkdvlda 125
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEG-----------------FCMMCALEAHVERA-------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 126 lneRPIYKKTISPQPFIRSLERAFGT-RISRqQQDAQEFLQIVTERLcdeyhagskaRRQALKRGINVANGDTASERSKI 204
Cdd:cd02661 58 ---LASSGPGSAPRIFSSNLKQISKHfRIGR-QEDAHEFLRYLLDAM----------QKACLDRFKKLKAVDPSSQETTL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 205 IEQ-FGtapaaasdsntieeeeedddededkppvdedgfpfeGKIESQIECETCHfkpKPSVST--FVTLTLNVPQVSst 281
Cdd:cd02661 124 VQQiFG------------------------------------GYLRSQVKCLNCK---HVSNTYdpFLDLSLDIKGAD-- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 282 SLNACFDGMLKVESIDD---FKCERCRlehalrskdhELSQAtdvevreriqsdivkirhametdpenppkdvelpdSKQ 358
Cdd:cd02661 163 SLEDALEQFTKPEQLDGenkYKCERCK----------KKVKA-----------------------------------SKQ 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 359 spkrrisrhMYISQFPKVLAIHLSRSVYAIGSASTKnlaKVSFPETLPLGGLLHRKN-----YKLLGAVTHKG-SHNSGH 432
Cdd:cd02661 198 ---------LTIHRAPNVLTIHLKRFSNFRGGKINK---QISFPETLDLSPYMSQPNdgplkYKLYAVLVHSGfSPHSGH 265
|
....
gi 160702019 433 YEAF 436
Cdd:cd02661 266 YYCY 269
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-433 |
3.12e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 67.33 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 46 GLSNAANDCFINSVLQALaglpdlriylirethrrkldgpeVYEVdpgrlntdnssvtpgkleglqqgvLTYGLKDVLDA 125
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL-----------------------YFEN------------------------LLTCLKDLFES 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 126 LNERPIYKKTISPQPFIRSLERAFGTRISRQQQDAQEFLQIVTERLCDEYhagsKARRQALKRGINVANGDTASERSKII 205
Cdd:cd02663 34 ISEQKKRTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEIL----DAERKAEKANRKLNNNNNAEPQPTWV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 206 EQFgtapaaasdsntieeeeedddededkppvdedgfpFEGKIESQIECETCHfkpkpSVS----TFVTLTLNVPQvsST 281
Cdd:cd02663 110 HEI-----------------------------------FQGILTNETRCLTCE-----TVSsrdeTFLDLSIDVEQ--NT 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 282 SLNACFDGMLKVE---SIDDFKCERCRlehalrskdhelsqatdvevreriqsdivkirhametdpenppkdvelpdSKQ 358
Cdd:cd02663 148 SITSCLRQFSATEtlcGRNKFYCDECC--------------------------------------------------SLQ 177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 359 SPKRRisrhMYISQFPKVLAIHLSRSVYA-IGSASTKNLAKVSFPETLPLGGLLHR-----KNYKLLGAVTHKGSH-NSG 431
Cdd:cd02663 178 EAEKR----MKIKKLPKILALHLKRFKYDeQLNRYIKLFYRVVFPLELRLFNTTDDaenpdRLYELVAVVVHIGGGpNHG 253
|
..
gi 160702019 432 HY 433
Cdd:cd02663 254 HY 255
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-439 |
5.01e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 67.01 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 46 GLSNAANDCFINSVLQALAGLPDLRIYLIRETHRRKLDGPEVYevdpgrlntdnssvtpgkleglqqGVLTYGLKDVLDA 125
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPN------------------------SCLSCAMDEIFQE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 126 LNerpiYKKTISPQPFIRSLERAFgtRISR-----QQQDAQEFLQIvterLCDEYHagskarrQALKRGINVANgdTASE 200
Cdd:cd02660 58 FY----YSGDRSPYGPINLLYLSW--KHSRnlagySQQDAHEFFQF----LLDQLH-------THYGGDKNEAN--DESH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 201 RSKIIEQFgtapaaasdsntieeeeedddededkppvdedgfpFEGKIESQIECETCHFKPKpSVSTFVTLTLNVP---- 276
Cdd:cd02660 119 CNCIIHQT-----------------------------------FSGSLQSSVTCQRCGGVST-TVDPFLDLSLDIPnkst 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 277 ---------QVSSTSLNACFDGMLKVESIDDF--KCERCrlehalrskdhelsqatdvevreriqsdivkirhametdpe 345
Cdd:cd02660 163 pswalgesgVSGTPTLSDCLDRFTRPEKLGDFayKCSGC----------------------------------------- 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 346 nppkdvelpDSKQSPKRRISrhmyISQFPKVLAIHLSRSVYAIGSASTKNLAKVSFPETL-------PLGGLLHRKN--- 415
Cdd:cd02660 202 ---------GSTQEATKQLS----IKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQFPLELnmtpytsSSIGDTQDSNsld 268
|
410 420
....*....|....*....|....*...
gi 160702019 416 ----YKLLGAVTHKGSHNSGHYEAFRRQ 439
Cdd:cd02660 269 pdytYDLFAVVVHKGTLDTGHYTAYCRQ 296
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-439 |
8.51e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 63.11 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 46 GLSNAANDCFINSVLQALAGLPDLRI-YLIRETHrrkldgpevYEVDPGRLNTD-NSSVTpgKL-EGLQQGvlTYGLKDV 122
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWrYDDLENK---------FPSDVVDPANDlNCQLI--KLaDGLLSG--RYSKPAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 123 LDalNERPIYKKTISPQPFIRSLERA---FGTRisrQQQDAQEFLQIVTERLcdeyhagSKARRQALKRGINvangdtas 199
Cdd:cd02658 68 LK--SENDPYQVGIKPSMFKALIGKGhpeFSTM---RQQDALEFLLHLIDKL-------DRESFKNLGLNPN-------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 200 erskiieqfgtapaaasdsntieeeeedddededkppvdeDGFPFegKIESQIECETCHfKPKPSVSTFVTLTLNVPQV- 278
Cdd:cd02658 128 ----------------------------------------DLFKF--MIEDRLECLSCK-KVKYTSELSEILSLPVPKDe 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 279 -----------SSTSLNACFDGMLKVESIDDFKCERCRLEHALRSKdhelsqatdvevreriqsdivkirhAMETdpenp 347
Cdd:cd02658 165 atekeegelvyEPVPLEDCLKAYFAPETIEDFCSTCKEKTTATKTT-------------------------GFKT----- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 348 pkdvelpdskqspkrrisrhmyisqFPKVLAIHLSRSVYAIGSASTKNLAKVSFPETLPLGgllhrkNYKLLGAVTHKG- 426
Cdd:cd02658 215 -------------------------FPDYLVINMKRFQLLENWVPKKLDVPIDVPEELGPG------KYELIAFISHKGt 263
|
410
....*....|...
gi 160702019 427 SHNSGHYEAFRRQ 439
Cdd:cd02658 264 SVHSGHYVAHIKK 276
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
45-436 |
1.00e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 63.05 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 45 VGLSNAANDCFINSVLQALAGLPDLRIYlirethrrkldgpeVYEVDPGRLNTDNSSVtPGKLEgLQQGVLTYGLKDVld 124
Cdd:cd02659 3 VGLKNQGATCYMNSLLQQLYMTPEFRNA--------------VYSIPPTEDDDDNKSV-PLALQ-RLFLFLQLSESPV-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 125 alnerpiykKTISPQPFIRSleraFGTRI--SRQQQDAQEFLQIvterLCDEYHAGSKarrqalkrginvangdtASERS 202
Cdd:cd02659 65 ---------KTTELTDKTRS----FGWDSlnTFEQHDVQEFFRV----LFDKLEEKLK-----------------GTGQE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 203 KIIEQFgtapaaasdsntieeeeedddededkppvdedgfpFEGKIESQIECETCHFKPKPsVSTFVTLTLNVPQVSstS 282
Cdd:cd02659 111 GLIKNL-----------------------------------FGGKLVNYIICKECPHESER-EEYFLDLQVAVKGKK--N 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 283 LNACFDGMLKVESIDD---FKCERCrlehalrskdhelsqatdvevreriqsdivkirhametdpenppkdvelpDSKQS 359
Cdd:cd02659 153 LEESLDAYVQGETLEGdnkYFCEKC--------------------------------------------------GKKVD 182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 360 PKRRISrhmyISQFPKVLAIHLSRSVYAIGS-ASTKNLAKVSFPETL-----------PLGGLLHRK-----NYKLLGAV 422
Cdd:cd02659 183 AEKGVC----FKKLPPVLTLQLKRFEFDFETmMRIKINDRFEFPLELdmepytekglaKKEGDSEKKdsesyIYELHGVL 258
|
410
....*....|....
gi 160702019 423 THKGSHNSGHYEAF 436
Cdd:cd02659 259 VHSGDAHGGHYYSY 272
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
368-438 |
1.50e-07 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 52.77 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 368 MYISQFPKVLAIHLSRSVYAIGSASTKNLAKVSFPETLPLGGLLHRKN----------YKLLGAVTHKGSHNSGHYEAFR 437
Cdd:cd02667 144 YLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCnssedkssvlYRLYGVVEHSGTMRSGHYVAYV 223
|
.
gi 160702019 438 R 438
Cdd:cd02667 224 K 224
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
46-438 |
7.80e-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: 239129 [Multi-domain] Cd Length: 327 Bit Score: 47.87 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 46 GLSNAANDCFINSVLQALAGLPDLRIYLIRETHRRKldgpevyevdpgrlntdNSSVTPGKLEGLQQGVLTYGlkdvlDA 125
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL-----------------GDSQSVMKKLQLLQAHLMHT-----QR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 126 LNERPIYK--KTISPQPFirslerafgtrISRQQQDAQEFLQIVTERLcdeyhagskarrqalkrginvangDTASERSk 203
Cdd:cd02664 59 RAEAPPDYflEASRPPWF-----------TPGSQQDCSEYLRYLLDRL------------------------HTLIEKM- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 204 iieqfgtapaaasdsntieeeeedddededkppvdedgfpFEGKIESQIECETCHFKPKpSVSTFVTLTLNVPQVssTSL 283
Cdd:cd02664 103 ----------------------------------------FGGKLSTTIRCLNCNSTSA-RTERFRDLDLSFPSV--QDL 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 284 NACFDGMLKVESIDDFKCERCR-LEHALRSKD-----HEL---------SQATdvEVRERIQsDIVKIrhametdpenpP 348
Cdd:cd02664 140 LNYFLSPEKLTGDNQYYCEKCAsLQDAEKEMKvtgapEYLiltllrfsyDQKT--HVREKIM-DNVSI-----------N 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 349 KDVELPdskqspkrrisrhmyisqfpkvlaihlsrsVYAIGSASTKNLAKVSFPETLPLGGLLHRKNYKLLGAVTHKG-S 427
Cdd:cd02664 206 EVLSLP------------------------------VRVESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGyS 255
|
410
....*....|.
gi 160702019 428 HNSGHYEAFRR 438
Cdd:cd02664 256 SESGHYFTYAR 266
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
350-436 |
1.52e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 40.23 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 350 DVELPDSKQSPKRRiSRHMYiSQFPKVLAIHLSRSVYAIGSAStKNLAKVSFPETLplggllHRKNYKLLGAVTHKGSHN 429
Cdd:cd02665 107 EVELLPSDHSVKSG-QERWF-TELPPVLTFELSRFEFNQGRPE-KIHDKLEFPQII------QQVPYELHAVLVHEGQAN 177
|
....*..
gi 160702019 430 SGHYEAF 436
Cdd:cd02665 178 AGHYWAY 184
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
291-438 |
2.46e-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: 39.82 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160702019 291 LKVESIddFKCERCrlehalrsKDHELSQATDVEVRERIQSDIVKIRHAMETdPENPPKDVELPDSKQSPKRRISRHMyI 370
Cdd:cd02673 76 YTIESS--YVCIGC--------SFEENVSDVGNFLDVSMIDNKLDIDELLIS-NFKTWSPIEKDCSSCKCESAISSER-I 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160702019 371 SQFPKVLAIHLSRSV--YAIGSASTKN-LAKVSFPETLPlggllhrkNYKLLGAVTHKG-SHNSGHYEAFRR 438
Cdd:cd02673 144 MTFPECLSINLKRYKlrIATSDYLKKNeEIMKKYCGTDA--------KYSLVAVICHLGeSPYDGHYIAYTK 207
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
368-439 |
2.76e-03 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 39.79 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160702019 368 MYISQFPKVLAIHLSRSVYAIGSASTKNlaKVSFPETLPLG---GLLHRKN--YKLLGAVTHKGSHNSGHYEAFRRQ 439
Cdd:COG5533 174 VSFVKLPKILTIQLKRFANLGGNQKIDT--EVDEKFELPVKhdqILNIVKEtyYDLVGFVLHQGSLEGGHYIAYVKK 248
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