|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
253-626 |
1.40e-59 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 201.90 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 253 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTehlfpkatngktqlsgkptnssatelslrndraeaceregfcw 332
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 333 ngrasisrsleliqnKEPSSKHISLCRELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 411
Cdd:pfam00443 38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 412 QQELESEGTTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERyhciekgfvPLNQ 491
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD---------SAEL 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 492 TECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 570
Cdd:pfam00443 160 KTASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 21361749 571 VVFDQVLTMEPYCCRDmLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGG 626
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENN 281
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-625 |
1.20e-50 |
|
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: 178.34 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLnldpSKTEHLFPKATNGKTQLSgkptnssatelslrndraeaCEREgfcwn 333
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL----SDRHSCTCLSCSPNSCLS--------------------CAMD----- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 grasisrslELIQNKepsskHISLCRELHtlfrvmwsgkwalvSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQ 413
Cdd:cd02660 53 ---------EIFQEF-----YYSGDRSPY--------------GPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 414 ELESEgttrrilipFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERYHCIEKGFVPLNQTE 493
Cdd:cd02660 105 HYGGD---------KNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 494 CLLTEMLAKFTETEALEGRIYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVF 573
Cdd:cd02660 176 PTLSDCLDRFTRPEKLGDFAYKCSGCGST-----------QEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQF 244
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 21361749 574 DQVLTMEPYC----CRDMLSSLDKETFAYDLSAVVMHHGKgFGSGHYTAYCYNTEG 625
Cdd:cd02660 245 PLELNMTPYTsssiGDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQGDG 299
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
395-626 |
8.30e-47 |
|
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: 165.73 E-value: 8.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 395 YDQQDAQEFLCELLHKVQQELESEgttrrilipFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLE 474
Cdd:cd02257 20 SEQQDAHEFLLFLLDKLHEELKKS---------SKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 475 FPERyhciekgfvplNQTECLLTEMLAKFTETEALEGriYACDQCNSKRrksnpkplvLSEARKQLMIYRLPQVLRLHLK 554
Cdd:cd02257 91 LPVK-----------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361749 555 RFRWSGRNHREKIGVHVVFDQVLTMEPYCCRD-MLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGG 626
Cdd:cd02257 149 RFSFNEDGTKEKLNTKVSFPLELDLSPYLSEGeKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDG 221
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
253-620 |
4.11e-41 |
|
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: 151.66 E-value: 4.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 253 TGLRNLGNTCYMNSILQVLSHlqkfrecflnldpskTEHLfpkatngktqlsgkptnsSATELSLRNDRAeaCEREGFCw 332
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH---------------TPPL------------------ANYLLSREHSKD--CCNEGFC- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 333 ngrasISRSLEliqnkepssKHISlcrelhtlfRVMWSGKWALVSPF--AMLHSVWsliPAFRGYDQQDAQEFLCELLHK 410
Cdd:cd02661 46 -----MMCALE---------AHVE---------RALASSGPGSAPRIfsSNLKQIS---KHFRIGRQEDAHEFLRYLLDA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 411 VQqelesegttRRILIPFSQRKLTKQVLK---VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfperyhcIEKGfv 487
Cdd:cd02661 100 MQ---------KACLDRFKKLKAVDPSSQettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD-------IKGA-- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 488 plnQTeclLTEMLAKFTETEALEGR-IYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFrwsGRNHREK 566
Cdd:cd02661 162 ---DS---LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGK 221
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 21361749 567 IGVHVVFDQVLTMEPYccrdmLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYC 620
Cdd:cd02661 222 INKQISFPETLDLSPY-----MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYV 270
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-619 |
1.81e-37 |
|
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: 140.60 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFlnldpsktehlfpkatngktqlSGKPTNssatelslrndraeaceregfcwn 333
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL----------------------SETPKE------------------------ 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 grasisrsleliqnkepsskhislcrelhtlfrvmwsgkwalvspfaMLHSVWSLIPAFRGYDQQDAQEFLCELLHKvqq 413
Cdd:cd02667 35 -----------------------------------------------LFSQVCRKAPQFKGYQQQDSHELLRYLLDG--- 64
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 414 elesegttrriLIPFsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfpeRYHCIEKgfvplnqtE 493
Cdd:cd02667 65 -----------LRTF------------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLP---RSDEIKS--------E 110
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 494 CLLTEMLAKFTETEALEGR-IYACDQCnskrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVV 572
Cdd:cd02667 111 CSIESCLKQFTEVEILEGNnKFACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVS 176
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 21361749 573 FDQVLTMEPYCCRDMLSSLDKETFAYDLSAVVMHHGkGFGSGHYTAY 619
Cdd:cd02667 177 FPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSG-TMRSGHYVAY 222
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-619 |
3.24e-35 |
|
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: 135.85 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEhlfpkatngktqlsgKPTNSSATELSLRndraeaceregFCWN 333
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDD---------------DDNKSVPLALQRL-----------FLFL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 GRASISRsleliQNKEPSSKHislcrelhtlfRVMWsgkWALVSPFamlhsvwslipafrgyDQQDAQEFLCELLHKVQQ 413
Cdd:cd02659 58 QLSESPV-----KTTELTDKT-----------RSFG---WDSLNTF----------------EQHDVQEFFRVLFDKLEE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 414 ELEseGTTRRilipfsqrkltkqvlKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFperyhcieKGFVPlnqte 493
Cdd:cd02659 103 KLK--GTGQE---------------GLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV--------KGKKN----- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 494 clLTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRFRWSG-RNHREKIGVHV 571
Cdd:cd02659 153 --LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKINDRF 219
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 21361749 572 VFDQVLTMEPYCCRDMLS------SLDKETFAYDLSAVVMHHGkGFGSGHYTAY 619
Cdd:cd02659 220 EFPLELDMEPYTEKGLAKkegdseKKDSESYIYELHGVLVHSG-DAHGGHYYSY 272
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
396-626 |
1.43e-34 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 130.87 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 396 DQQDAQEFLCELLhkvqQELESegttrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEF 475
Cdd:cd02674 21 DQQDAQEFLLFLL----DGLHS----------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 476 PERYHciekgfvplNQTECLLTEMLAKFTETEALEGRIYA-CDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLK 554
Cdd:cd02674 75 PSGSG---------DAPKVTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361749 555 RFRWSGRNhREKIGVHVVFD-QVLTMEPYCcrdmLSSLDKETFAYDLSAVVMHHGKGFGsGHYTAYCYNTEGG 626
Cdd:cd02674 135 RFSFSRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETN 201
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-626 |
4.28e-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: 239133 [Multi-domain] Cd Length: 324 Bit Score: 126.77 E-value: 4.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDpsktehlFPKATNGKTQLSGKPTNSSatelslrndraeaceregfcwn 333
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECN-------STEDAELKNMPPDKPHEPQ---------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 grasisrsleliqnkepsskhiSLCRELHTLFRVMWSGKWALVSPFAmlhsvwsLIPAFR--GYDQQDAQEFLCELLHKV 411
Cdd:cd02668 52 ----------------------TIIDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLFLSLL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 412 QQELESEgttrrilipfsqrkLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEfperyhciekgfvpLNQ 491
Cdd:cd02668 103 EAKLSKS--------------KNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ--------------LKG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 492 TECLlTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRF---RWSGrnHREKI 567
Cdd:cd02668 155 HKTL-EECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTG--AKKKL 220
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21361749 568 GVHVVFDQVLTMEPYCCRDmlsslDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGG 626
Cdd:cd02668 221 NASISFPEILDMGEYLAES-----DEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTG 274
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
361-620 |
1.27e-30 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 122.03 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 361 LHTLFRVMWSGK--WALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGTTRRILIPFSQRKLTKQVL 438
Cdd:cd02663 27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 439 KVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPEryhciekgfvplnqtECLLTEMLAKFTETEALEGR-IYACD 517
Cdd:cd02663 107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ---------------NTSITSCLRQFSATETLCGRnKFYCD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 518 QCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSGRNHR-EKIGVHVVFDqvLTMEPYCCRDMLSSLDKEtf 596
Cdd:cd02663 172 ECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP--LELRLFNTTDDAENPDRL-- 236
|
250 260
....*....|....*....|....
gi 21361749 597 aYDLSAVVMHHGKGFGSGHYTAYC 620
Cdd:cd02663 237 -YELVAVVVHIGGGPNHGHYVSIV 259
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-87 |
4.94e-24 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 95.41 E-value: 4.94e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361749 26 CLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
226-619 |
9.88e-22 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 96.89 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 226 PAALPTSRRVPAATLKLRRqpaMAPGVTGLRNLGNTCYMNSILQVLShlqkfrecflnldpsktehlfpkatngktqlsg 305
Cdd:cd02671 1 DQVVPAPQPSSATSCEKRE---NLLPFVGLNNLGNTCYLNSVLQVLY--------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 306 kptnssatelslrndraeaceregFCWNGRASISRSLELIQNKEpssKHISLCRELHTLFrvmwSGKWALVSPFAMLHSV 385
Cdd:cd02671 45 ------------------------FCPGFKHGLKHLVSLISSVE---QLQSSFLLNPEKY----NDELANQAPRRLLNAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 386 WSLIPAFRGYDQQDAQEFLCELLHKVQQELESegttrrilipfsqrkltkqvlkvvntIFHGQLLSQVTCISCNYKSNTI 465
Cdd:cd02671 94 REVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------DFQGQLVLRTRCLECETFTERR 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 466 EPFWDLSLEFPERYHCIEKGFVPLNQTECLLTEMLAKFTETEALEGRI-----YACDQCNSkrrksnpkplvLSEARKQL 540
Cdd:cd02671 148 EDFQDISVPVQESELSKSEESSEISPDPKTEMKTLKWAISQFASVERIvgedkYFCENCHH-----------YTEAERSL 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361749 541 MIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTMEPYCCRDMLSSLDKETfaYDLSAVVMHHGKGFGSGHYTAY 619
Cdd:cd02671 217 LFDKLPEVITIHLKCFAANGSEFDCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAY 293
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-626 |
1.85e-21 |
|
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: 96.02 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTehlfpkatnGKTQLSGKPTNSSATELSLRNDRAEAceregfcwn 333
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL---------GDSQSVMKKLQLLQAHLMHTQRRAEA--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 grasisrsleliqnkePSSKHISLCRElhtlfrvmwsgkwalvspfamlhsvwsliPAFRGYDQQDAQEFLCELLHKVQQ 413
Cdd:cd02664 63 ----------------PPDYFLEASRP-----------------------------PWFTPGSQQDCSEYLRYLLDRLHT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 414 elesegttrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPeryhciekgfvplnqte 493
Cdd:cd02664 98 --------------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 494 cLLTEMLAKFTETEALEG-RIYACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH-REKIGVHV 571
Cdd:cd02664 135 -SVQDLLNYFLSPEKLTGdNQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDQKTHvREKIMDNV 202
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361749 572 VFDQVLTM----------EPYCCRDMLSSLDKE----TFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGG 626
Cdd:cd02664 203 SINEVLSLpvrvesksseSPLEKKEEESGDDGElvtrQVHYRLYAVVVHSGYSSESGHYFTYARDQTDA 271
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-626 |
2.57e-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: 92.01 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSktehlfpkatngktqlsgkptnssatelslrndRAEACERegfcwn 333
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPA---------------------------------RRGANQS------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 grasisrsleliqnkepsskHISLCRELHTLFRVMwSGKWALVSPFAMLHSVWSLIPAF------RGYDQQDAQEFLCEL 407
Cdd:cd02657 42 --------------------SDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 408 LHKVQQELESEGTTRRilipfsqrkltkqvlkVVNTIFHGQLLSQVTCI-SCNYKSNTIEPFWDLSLefperyHCIEKGF 486
Cdd:cd02657 101 LSVLSQKLPGAGSKGS----------------FIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQC------HISITTE 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 487 VplnqtECLLTEMLAKFTETEALEGRIYACDQCNSKRRKsnpkplvlsearkqlmIYRLPQVLRLHLKRFRWSGR-NHRE 565
Cdd:cd02657 159 V-----NYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSR----------------ISRLPKYLTVQFVRFFWKRDiQKKA 217
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361749 566 KIGVHVVFDQVLTMEPYCCrdmlssldkETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGG 626
Cdd:cd02657 218 KILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDG 269
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
386-619 |
4.10e-20 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 89.73 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 386 WSLIPAFRGY-----DQQDAQEFLCELLHKVQQELESegttrriliPFsqrkltkqvlkvvntifHGQLLSQVTCISCNY 460
Cdd:cd02662 18 LASLPSLIEYleeflEQQDAHELFQVLLETLEQLLKF---------PF-----------------DGLLASRIVCLQCGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 461 KSN-TIEPFWDLSLEFPERyhciekgfvpLNQTECLLTEMLAKFTETEALEGriYACDQCnskrrksnpkplvlsearkQ 539
Cdd:cd02662 72 SSKvRYESFTMLSLPVPNQ----------SSGSGTTLEHCLDDFLSTEIIDD--YKCDRC-------------------Q 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 540 LMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTmepyccrdmlssldkeTFAYDLSAVVMHHGkGFGSGHYTAY 619
Cdd:cd02662 121 TVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP----------------KVLYRLRAVVVHYG-SHSSGHYVCY 183
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
254-619 |
4.73e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 88.53 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpsktEHLFPKATNGktqlsgkPTNSSATELS-LRNdraeacereGFCw 332
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL-----ENKFPSDVVD-------PANDLNCQLIkLAD---------GLL- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 333 NGRASISRSLELIQNkePSSKHISlcrelhtlfrvmwsgkwalvsPFaMLHSvwsLI----PAFRGYDQQDAQEFLCELL 408
Cdd:cd02658 59 SGRYSKPASLKSEND--PYQVGIK---------------------PS-MFKA---LIgkghPEFSTMRQQDALEFLLHLI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 409 HKVQQELESEGTTRrilipfsqrkltkqvlkvVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPER----YHCIEK 484
Cdd:cd02658 112 DKLDRESFKNLGLN------------------PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeateKEEGEL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 485 GFVPLNQTEClltemLAKFTETEALEgriYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFR----WSG 560
Cdd:cd02658 174 VYEPVPLEDC-----LKAYFAPETIE---DFCSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQllenWVP 234
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 21361749 561 RnhreKIGVHVVFDQVLTMEPyccrdmlssldketfaYDLSAVVMHHGKGFGSGHYTAY 619
Cdd:cd02658 235 K----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAH 273
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
251-539 |
5.69e-18 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 88.02 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 251 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLnldpsktehlfpkatngktqlsgkptnssatelslrndraeaceregf 330
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------------------------------ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 331 cwngrasiSRSLELIQNKE-PSSKHISLCRELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLH 409
Cdd:COG5560 296 --------SDEYEESINEEnPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLD 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 410 KVQQEL----ESEGTTRRILIPFSQRKL-----------TKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLE 474
Cdd:COG5560 368 GLHEDLnriiKKPYTSKPDLSPGDDVVVkkkakecwwehLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLP 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 475 FPERY---HCIEkgFVPLNQTECLL--------TEMLAKFTETEALE----GRIYACD-QCNSKRRKSNPKPLVLSEARK 538
Cdd:COG5560 448 LPVSMvwkHTIV--VFPESGRRQPLkieldassTIRGLKKLVDAEYGklgcFEIKVMCiYYGGNYNMLEPADKVLLQDIP 525
|
.
gi 21361749 539 Q 539
Cdd:COG5560 526 Q 526
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
26-72 |
2.19e-15 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 70.47 E-value: 2.19e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 21361749 26 CLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDL 72
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQ 48
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
251-619 |
5.08e-15 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 79.14 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 251 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpsktehlfpkatngktqlsgkPTNSSatelslrndraeaceregf 330
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI----------------------PTDHP------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 331 cwNGRASISRSLEliqnkepsskhislcrelhTLFRVMWSGKwalvSPFAMLHSVWSLI-PAFRGYDQQDAQEFlcellh 409
Cdd:COG5077 231 --RGRDSVALALQ-------------------RLFYNLQTGE----EPVDTTELTRSFGwDSDDSFMQHDIQEF------ 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 410 kvqqelesegttRRILIPFSQRKLTKQVLK-VVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFperyhcieKGFVP 488
Cdd:COG5077 280 ------------NRVLQDNLEKSMRGTVVEnALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--------KGMKN 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 489 LNqteclltEMLAKFTETEALEG-RIYACDQCNskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWS-GRNHREK 566
Cdd:COG5077 340 LQ-------ESFRRYIQVETLDGdNRYNAEKHG------------LQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMVK 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 21361749 567 IGVHVVFDQVLTMEPYCCRDMLSSLDKEtFAYDLSAVVMHHGKgFGSGHYTAY 619
Cdd:COG5077 401 INDRYEFPLEIDLLPFLDRDADKSENSD-AVYVLYGVLVHSGD-LHEGHYYAL 451
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
254-619 |
4.57e-13 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 70.22 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 254 GLRNLGNTCYMNSILQVLShlqkfrecfLNLdpsktehlfPKATNGKTQLSGkptnssatelSLRNdraeaceregfcwn 333
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILA---------LYL---------PKLDELLDDLSK----------ELKV-------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 334 grasisrsleLIQNKEPSSKHISLCRELHtLFRVMWSGKwalvspfamLHSVWSLIPAfrgYDQQDAQEFLCELLHKVQQ 413
Cdd:COG5533 39 ----------LKNVIRKPEPDLNQEEALK-LFTALWSSK---------EHKVGWIPPM---GSQEDAHELLGKLLDELKL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 414 ELESEGtTRRILIPFSqrkltkqvlkvvntifhgqllsqvtciscNYKSNTIEPFWDLSLEFPERyhcieKGFVPLNQTE 493
Cdd:COG5533 96 DLVNSF-TIRIFKTTK-----------------------------DKKKTSTGDWFDIIIELPDQ-----TWVNNLKTLQ 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 494 CLLTEMLAKFTetealegriyacDQCNSKrRKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHR------EKI 567
Cdd:COG5533 141 EFIDNMEELVD------------DETGVK-AKENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEKF 207
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 21361749 568 GVHVVFDQvltmepyccrdmlSSLDKETFAYDLSAVVMHHGkGFGSGHYTAY 619
Cdd:COG5533 208 ELPVKHDQ-------------ILNIVKETYYDLVGFVLHQG-SLEGGHYIAY 245
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
250-623 |
9.98e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 67.34 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 250 PGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEhlfpkaTNGKTQLsgkptnssatelslrndraeacereg 329
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENI------KDRKSEL-------------------------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 330 fcwngrasISRSLELIqnkepssKHISLCRelhtLFRvmwsgkwALVSPFAMLH--SVWSLIPaFRGYDQQDAQEFLCEL 407
Cdd:cd02669 165 --------VKRLSELI-------RKIWNPR----NFK-------GHVSPHELLQavSKVSKKK-FSITEQSDPVEFLSWL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 408 LHKVQQELESEGTTRRILIPFS-QRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIePFWDLSLEFPER---YHCIE 483
Cdd:cd02669 218 LNTLHKDLGGSKKPNSSIIHDCfQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPPplfKDGNE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 484 KGFVPlnQTecLLTEMLAKFTETEALEgriyacdqcnskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRwsgRNH 563
Cdd:cd02669 297 ENIIP--QV--PLKQLLKKYDGKTETE----------------------LKDSLKRYLISRLPKYLIFHIKRFS---KNN 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361749 564 --REKIGVHVVFDQVLTMEPYCCRDMLSSLDKETfAYDLSAVVMHHGKGFGSGHYTAYCYNT 623
Cdd:cd02669 348 ffKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLST-KYNLVANIVHEGTPQEDGTWRVQLRHK 408
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
253-626 |
4.01e-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: 239131 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 253 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEhlfpkatngktqlsgkPTNSSATElslrndraeacEREGfcw 332
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAE----------------LASDYPTE-----------RRIG--- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 333 nGRAsISRSLELIQNKepsskhisLCRELHTLFRVMWSGKWALVSPFAMLhsvwslipAFRGYDQQDAQeflcELLHKVQ 412
Cdd:cd02666 52 -GRE-VSRSELQRSNQ--------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVT----ECIDNVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 413 QELESEGTTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVT-CISCNYKSNTIEPFWDLSLEFPeryhCIEKGFVPLNQ 491
Cdd:cd02666 110 FQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVD----VGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 492 TE-CLLTEMLAKFTETEALE-GRIYACDQCN----------SKRRKSNPKPL-VLSEARKQLMIYRLPQVLRLhlkrfRW 558
Cdd:cd02666 186 LEpKDLYDALDRYFDYDSLTkLPQRSQVQAQlaqplqreliSMDRYELPSSIdDIDELIREAIQSESSLVRQA-----QN 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361749 559 SGRNHREKIgvHVVFDqvltmepyccrdmlsslDKETFAYDLSAVVMHHGKGfGSGHYTAYCYNTEGG 626
Cdd:cd02666 261 ELAELKHEI--EKQFD-----------------DLKSYGYRLHAVFIHRGEA-SSGHYWVYIKDFEEN 308
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
382-632 |
1.59e-08 |
|
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: 56.00 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 382 LHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEgTTRRILIPFSQRKLTK-QVLKV-VNTIFhgqllsqvTCISCN 459
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVN-RTNVPPSNIEIKRLNPlEAFKYtIESSY--------VCIGCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 460 YKSNTIEPFWDLSLEFPERYHCIEKgfvplnqtecLLTEMLAKFTETEALegriyaCDQCNSKRRKSNPKplvlsearkq 539
Cdd:cd02673 89 FEENVSDVGNFLDVSMIDNKLDIDE----------LLISNFKTWSPIEKD------CSSCKCESAISSER---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361749 540 lmIYRLPQVLRLHLKRFRWsgrnhREKIGVHVVfDQVLTMEPYCcrdmlSSLDKetfaYDLSAVVMHHGKGFGSGHYTAY 619
Cdd:cd02673 143 --IMTFPECLSINLKRYKL-----RIATSDYLK-KNEEIMKKYC-----GTDAK----YSLVAVICHLGESPYDGHYIAY 205
|
250
....*....|...
gi 21361749 620 CYNTEGGACALLC 632
Cdd:cd02673 206 TKELYNGSSWLYC 218
|
|
| |
