|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
272-674 |
3.25e-70 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 231.56 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 272 TGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarsykhsavteaaaqqmnegqekekgfvcsrhsgl 351
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 352 ssglsggaskgrNMELIQPREPSSPYSSLCHELHILFQVMWSGEW-ALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCEL 430
Cdd:pfam00443 31 ------------RISPLSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 431 LDKIQRELEttgtklpaliptsqRRLIEQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPeryqcsGKDAA 510
Cdd:pfam00443 99 LDGLHEDLN--------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIP------GDSAE 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 511 SQPCLVTDMLDKFTETEALEGKI-YMCDHCNSKrrkfssksvvfTEAQKQLMICHLPQVLRLHLKRFRWSgRNNREKIGV 589
Cdd:pfam00443 159 LKTASLQICFLQFSKLEELDDEEkYYCDKCGCK-----------QDAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNT 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 590 HVVFEETLNMEPYCCREtLNALRPECFLYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTME-EVRKAQ 668
Cdd:pfam00443 227 EVEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSS 304
|
....*.
gi 332205971 669 AYILFY 674
Cdd:pfam00443 305 AYILFY 310
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-675 |
5.64e-63 |
|
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: 213.00 E-value: 5.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkarSYKHSAVTEAaaqqmnegqekekgfvcsrhsgls 352
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL-----------------SDRHSCTCLS------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 353 sglsggaskgrnmeliqprepSSPYSSLCHELHILFQVMW-SGEWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELL 431
Cdd:cd02660 41 ---------------------CSPNSCLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLL 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 432 DKIQRELetTGTKLPALIPTSQRRLIEQvlnvvnnIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPERYQCSGKDAAS 511
Cdd:cd02660 100 DQLHTHY--GGDKNEANDESHCNCIIHQ-------TFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 512 ----QPCLvTDMLDKFTETEALEGKIYMCDHCNSKRrkfssksvvftEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKI 587
Cdd:cd02660 171 gvsgTPTL-SDCLDRFTRPEKLGDFAYKCSGCGSTQ-----------EATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 588 GVHVVFEETLNMEPYCCRET----LNALRPECFLYNLSAVVIHHGKgFGSGHYTAYCYNsEGGFWVHCNDSKLSMCTMEE 663
Cdd:cd02660 239 DTYVQFPLELNMTPYTSSSIgdtqDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEE 316
|
410
....*....|..
gi 332205971 664 VRKAQAYILFYT 675
Cdd:cd02660 317 VLKSQAYLLFYH 328
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
420-674 |
9.16e-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: 199.25 E-value: 9.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 420 QQDAQEFLCELLDKIQRELETTGTKlpaliptsqRRLIEQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFP 499
Cdd:cd02257 22 QQDAHEFLLFLLDKLHEELKKSSKR---------TSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 500 ERyqcsgkdaASQPCLVTDMLDKFTETEALEGKIymCDHCNSKRRkfssksvvfTEAQKQLMICHLPQVLRLHLKRFRWS 579
Cdd:cd02257 93 VK--------GLPQVSLEDCLEKFFKEEILEGDN--CYKCEKKKK---------QEATKRLKIKKLPPVLIIHLKRFSFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 580 GRNNREKIGVHVVFEETLNMEPYCCRETLNALRPE-CFLYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSM 658
Cdd:cd02257 154 EDGTKEKLNTKVSFPLELDLSPYLSEGEKDSDSDNgSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFNDDKVTE 233
|
250 260
....*....|....*....|.
gi 332205971 659 CTMEEV-----RKAQAYILFY 674
Cdd:cd02257 234 VSEEEVlefgsLSSSAYILFY 254
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-674 |
1.63e-52 |
|
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: 184.02 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 272 TGLRNLGNTCYMNSVLQVLSHllifrqcflkldlnqwlAVAASDKARSYKHSavteaaaqqmNEGQEKEKGFVCsrhsgl 351
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTH-----------------TPPLANYLLSREHS----------KDCCNEGFCMMC------ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 352 ssglsggaskgrnmeliqprepsspysslCHELHILfQVMWSGEWALVSPFamLHSVWRLI-PAFRGYAQQDAQEFLCEL 430
Cdd:cd02661 49 -----------------------------ALEAHVE-RALASSGPGSAPRI--FSSNLKQIsKHFRIGRQEDAHEFLRYL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 431 LDKIQRelettgTKLPALIPTSQRRLIEQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFperyqcsgKDAA 510
Cdd:cd02661 97 LDAMQK------ACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI--------KGAD 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 511 SqpclVTDMLDKFTETEALEGK-IYMCDHCNSKrrkfssksvvfTEAQKQLMICHLPQVLRLHLKRFrwsGRNNREKIGV 589
Cdd:cd02661 163 S----LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGKINK 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 590 HVVFEETLNMEPYCCRETLNALRpecflYNLSAVVIHHGKGFGSGHYTAYCYNSEgGFWVHCNDSKLSMCTMEEVRKAQA 669
Cdd:cd02661 225 QISFPETLDLSPYMSQPNDGPLK-----YKLYAVLVHSGFSPHSGHYYCYVKSSN-GKWYNMDDSKVSPVSIETVLSQKA 298
|
....*
gi 332205971 670 YILFY 674
Cdd:cd02661 299 YILFY 303
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
420-675 |
1.51e-47 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 167.85 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 420 QQDAQEFLCELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFP 499
Cdd:cd02674 22 QQDAQEFLLFLLDGLH--------------------------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 500 ERYQCSGKdaasqpCLVTDMLDKFTETEALEGKIYM-CDHCNSKRRkfssksvvfteAQKQLMICHLPQVLRLHLKRFRW 578
Cdd:cd02674 76 SGSGDAPK------VTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLKRFSF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 579 SGRNnREKIGVHVVFE-ETLNMEPYCcretLNALRPECFLYNLSAVVIHHGKGFGsGHYTAYCYNSEGGFWVHCNDSKLS 657
Cdd:cd02674 139 SRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDDSRVT 212
|
250
....*....|....*...
gi 332205971 658 MCTMEEVRKAQAYILFYT 675
Cdd:cd02674 213 KVSESSVVSSSAYILFYE 230
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
400-674 |
1.03e-42 |
|
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: 156.01 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 400 SPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQFLSQVTCL 479
Cdd:cd02667 31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLR--------------------------TFIDSIFGGELTSTIMCE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 480 ACDNKSDTIESFWDLSLefPEryqcsgKDAASQPCLVTDMLDKFTETEALEGK-IYMCDHCnskrrkfssksvvfTEAQK 558
Cdd:cd02667 85 SCGTVSLVYEPFLDLSL--PR------SDEIKSECSIESCLKQFTEVEILEGNnKFACENC--------------TKAKK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 559 QLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMEPYCCRETLNALRPECFLYNLSAVVIHHGkGFGSGHYTA 638
Cdd:cd02667 143 QYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDKSSVLYRLYGVVEHSG-TMRSGHYVA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 332205971 639 YCY------------------NSEG---GFWVHCNDSKLSMCTMEEVRKAQAYILFY 674
Cdd:cd02667 222 YVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-674 |
1.60e-42 |
|
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: 157.03 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWlavAASDKARSYkhsavteaAAQ-QMNEGQEKEKgfvcsrhsgl 351
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED---DDDNKSVPL--------ALQrLFLFLQLSES---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 352 ssglsggaskgrnmELIQPREPSSPYSslchelhilfqvMWsgewalvspfamlhsvWRLIPAFRgyaQQDAQEFLCELL 431
Cdd:cd02659 63 --------------PVKTTELTDKTRS------------FG----------------WDSLNTFE---QHDVQEFFRVLF 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 432 DKIQRELEttGTKLPALIptsqrrlieqvlnvvNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEfperyqcsGKDAAS 511
Cdd:cd02659 98 DKLEEKLK--GTGQEGLI---------------KNLFGGKLVNYIICKECPHESEREEYFLDLQVA--------VKGKKN 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 512 qpclVTDMLDKFTETEALEG-KIYMCDHCNSKRRkfssksvvfteAQKQLMICHLPQVLRLHLKRFRWSG-RNNREKIGV 589
Cdd:cd02659 153 ----LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKIND 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 590 HVVFEETLNMEPYCCR------ETLNALRPECFLYNLSAVVIHHGkGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEE 663
Cdd:cd02659 218 RFEFPLELDMEPYTEKglakkeGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPND 296
|
410 420 430
....*....|....*....|....*....|...
gi 332205971 664 VRKAQ----------------------AYILFY 674
Cdd:cd02659 297 AEEECfggeetqktydsgprafkrttnAYMLFY 329
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-657 |
5.81e-38 |
|
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: 144.10 E-value: 5.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKldlnqwlavaasdkarsykhsavteaaaqqmnegqekekgFVCSRHSGLs 352
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE----------------------------------------CNSTEDAEL- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 353 sglsggaskgRNMELIQPREPSSPysslCHELHILFQVMWSGEWALVSPFAmlhsvwrLIPAFR--GYAQQDAQEFLCEL 430
Cdd:cd02668 40 ----------KNMPPDKPHEPQTI----IDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLF 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 431 LDKIQRELETTGTKlpaliptsqrrlieQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFperyqcsgKDAA 510
Cdd:cd02668 99 LSLLEAKLSKSKNP--------------DLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL--------KGHK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 511 SqpclVTDMLDKFTETEALEG-KIYMCDHCNSKRRkfssksvvfteAQKQLMICHLPQVLRLHLKRF---RWSGRnnREK 586
Cdd:cd02668 157 T----LEECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTGA--KKK 219
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332205971 587 IGVHVVFEETLNMEPYCCRETLNAlrpecFLYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLS 657
Cdd:cd02668 220 LNASISFPEILDMGEYLAESDEGS-----YVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVE 285
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
377-675 |
1.83e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 142.06 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 377 YSSLCHELHILFQVMWSGE--WALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPALIPTSQR 454
Cdd:cd02663 20 FENLLTCLKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 455 RLIEQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPERYQcsgkdaasqpclVTDMLDKFTETEALEGK-I 533
Cdd:cd02663 100 NNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTS------------ITSCLRQFSATETLCGRnK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 534 YMCDHCNSKRrkfssksvvftEAQKQLMICHLPQVLRLHLKRFRWSGRNNR-EKIGVHVVFEETLNMepycCRETLNALR 612
Cdd:cd02663 168 FYCDECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFPLELRL----FNTTDDAEN 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332205971 613 PeCFLYNLSAVVIHHGKGFGSGHYTAYCYNSegGFWVHCNDSKLSMCTMEEVRK--------AQAYILFYT 675
Cdd:cd02663 233 P-DRLYELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFYQ 300
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-674 |
2.63e-29 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 119.13 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLnqwlavaasdkarsykhsavteaaaqqMNEGQEKEKGFVcsrhsgls 352
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNL---------------------------PRLGDSQSVMKK-------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 353 sglsggaskgrnmeliqprepsspysslchELHILFQVMWSGEWALVSPFAMLHSVWRliPAFRGYAQQDAQEFLCELLD 432
Cdd:cd02664 46 ------------------------------LQLLQAHLMHTQRRAEAPPDYFLEASRP--PWFTPGSQQDCSEYLRYLLD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 433 KIQRelettgtklpaliptsqrrLIEQVlnvvnniFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPeryqcsgkdaasq 512
Cdd:cd02664 94 RLHT-------------------LIEKM-------FGGKLSTTIRCLNCNSTSARTERFRDLDLSFP------------- 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 513 pcLVTDMLDKFTETEALEGK-IYMCDHCNSKRRkfssksvvfteAQKQLMICHLPQVLRLHLKRFRWS-GRNNREKIGVH 590
Cdd:cd02664 135 --SVQDLLNYFLSPEKLTGDnQYYCEKCASLQD-----------AEKEMKVTGAPEYLILTLLRFSYDqKTHVREKIMDN 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 591 VVFEETLNM----------EPYCCRETLNALRPEC----FLYNLSAVVIHHGKGFGSGHYtaYCY--------------- 641
Cdd:cd02664 202 VSINEVLSLpvrvesksseSPLEKKEEESGDDGELvtrqVHYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecp 279
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 332205971 642 -------NSEGGFWVHCNDSKLSMCTMEEV-------RKAQAYILFY 674
Cdd:cd02664 280 epkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
412-674 |
2.39e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 105.14 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 412 IPAFRGY-----AQQDAQEFLCELLDKIQRELEttgtklpaliptsqrrlieqvlnvvnNIFHGQFLSQVTCLACDNKSD 486
Cdd:cd02662 21 LPSLIEYleeflEQQDAHELFQVLLETLEQLLK--------------------------FPFDGLLASRIVCLQCGESSK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 487 -TIESFWDLSLEFPERYQCSGkdaasqpCLVTDMLDKFTETEALEGkiYMCDHCnskrrkfssksvvfteaqkQLMICHL 565
Cdd:cd02662 75 vRYESFTMLSLPVPNQSSGSG-------TTLEHCLDDFLSTEIIDD--YKCDRC-------------------QTVIVRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 566 PQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMepyccretlnalrpecFLYNLSAVVIHHGkGFGSGHYTAY------ 639
Cdd:cd02662 127 PQILCIHLSRSVFDGRGTSTKNSCKVSFPERLPK----------------VLYRLRAVVVHYG-SHSSGHYVCYrrkplf 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 332205971 640 --------------CYNSEGGFWVHCNDSKLSMCTMEEVR-KAQAYILFY 674
Cdd:cd02662 190 skdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-674 |
2.86e-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: 239136 [Multi-domain] Cd Length: 332 Bit Score: 107.29 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 269 PGVTGLRNLGNTCYMNSVLQVLshllifrqCFlkldlnqwlavaasdkARSYKHSAvteaaaqqmnegqekekGFVCSrh 348
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVL--------YF----------------CPGFKHGL-----------------KHLVS-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 349 sglssglsggaskgrnmeLIQPREPSSPYSSLCHELhilfqvmWSGEWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLC 428
Cdd:cd02671 59 ------------------LISSVEQLQSSFLLNPEK-------YNDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 429 ELLDKIQrelettgtklpaliptsqrrlieqvlNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPERYQCSGKD 508
Cdd:cd02671 114 CILGNIQ--------------------------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 509 AAS-QPCLVTDMLD------KFTETEALEGK-IYMCDHCNSkrrkfssksvvFTEAQKQLMICHLPQVLRLHLKRFRWSG 580
Cdd:cd02671 168 SSEiSPDPKTEMKTlkwaisQFASVERIVGEdKYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANG 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 581 RNNR-----EKIGVHVVFEETLNMEPYCCRETLNalrpecfLYNLSAVVIHHGKGFGSGHYTAYCYnseggfWVHCNDSK 655
Cdd:cd02671 237 SEFDcygglSKVNTPLLTPLKLSLEEWSTKPKND-------VYRLFAVVMHSGATISSGHYTAYVR------WLLFDDSE 303
|
410 420
....*....|....*....|....*...
gi 332205971 656 LSMCTMEEVRKAQA---------YILFY 674
Cdd:cd02671 304 VKVTEEKDFLEALSpntsststpYLLFY 331
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-674 |
1.77e-24 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 104.34 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLSHllifrqcflkldlnqwlavaasdkarsykhsavteaaaqqMNEGQEKEKGFVCSRhsgls 352
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRS----------------------------------------VPELRDALKNYNPAR----- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 353 sglsggaskgrnmeliqpREPSSPYSSLCHELHILFQVMWSGEWAlVSPFAMLHSVWRLIPAF------RGYAQQDAQEF 426
Cdd:cd02657 36 ------------------RGANQSSDNLTNALRDLFDTMDKKQEP-VPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEEC 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 427 LCELLDKIQRELEttgtklpalIPTSQRRLIEQvlnvvnnIFHGQFLSQVTCLACDN-KSDTIESFWDLSLefperyQCS 505
Cdd:cd02657 97 WSQLLSVLSQKLP---------GAGSKGSFIDQ-------LFGIELETKMKCTESPDeEEVSTESEYKLQC------HIS 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 506 GKDAASQpcLVTDMLDKFTETEalegkiymcdhcnskrRKFSSKSVVFTEAQKQLMICHLPQVLRLHLKRFRWSGR-NNR 584
Cdd:cd02657 155 ITTEVNY--LQDGLKKGLEEEI----------------EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDiQKK 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 585 EKIGVHVVFEETLNMEPYCCretlnalrpECFLYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEV 664
Cdd:cd02657 217 AKILRKVKFPFELDLYELCT---------PSGYYELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDI 287
|
410
....*....|....*..
gi 332205971 665 RKAQ-------AYILFY 674
Cdd:cd02657 288 LKLSgggdwhiAYILLY 304
|
|
| zf-UBP |
pfam02148 |
Zn-finger in ubiquitin-hydrolases and other protein; |
26-88 |
3.22e-21 |
|
Zn-finger in ubiquitin-hydrolases and other protein;
Pssm-ID: 460464 Cd Length: 63 Bit Score: 87.70 E-value: 3.22e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205971 26 CMVCNTTESIWACLSCSHVACGKYIQEHALKHFQESSHPVAFEVNDMYAFCYLCNDYVLNDNA 88
Cdd:pfam02148 1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPSL 63
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
273-674 |
4.34e-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: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVAasDKARSYKhSAVTEAAaqqmnegqekeKGFVCSRHsgls 352
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVV--DPANDLN-CQLIKLA-----------DGLLSGRY---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 353 sglsggaskgrnmelIQPREPSSPYSSlchelhilFQVmwsGewalVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLD 432
Cdd:cd02658 63 ---------------SKPASLKSENDP--------YQV---G----IKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 433 KIQRELETTGTKLPaliptsqrrlieqvlnvvNNIFhgQFLSQ--VTCLACDNKSDTIESFWDLSLEFPER---YQCSGK 507
Cdd:cd02658 113 KLDRESFKNLGLNP------------------NDLF--KFMIEdrLECLSCKKVKYTSELSEILSLPVPKDeatEKEEGE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 508 DAASQPCLVtDMLDKFTETEALEGKiymCDHCNSKrrkfssksvvfTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKI 587
Cdd:cd02658 173 LVYEPVPLE-DCLKAYFAPETIEDF---CSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQLLENWVPKKL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 588 GVHVVFEETLNMEPYccretlnalrpecflyNLSAVVIHHGKGFGSGHYTAYCY--NSEGGFWVHCNDSKLSMCTMEEVR 665
Cdd:cd02658 238 DVPIDVPEELGPGKY----------------ELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPEM 301
|
....*....
gi 332205971 666 KAQAYILFY 674
Cdd:cd02658 302 KKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
270-664 |
2.16e-18 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 90.31 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 270 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLdlnqwlavaasdkarsykhsavteaaaqqmnegqekekgfvcsrhs 349
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------------------------------------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 350 glssglsggaskgrnmeliqPREPSSPYSSLCHELHILFQVMWSGEWALVSPFAMLHSVWRlipAFRGYAQQDAQEFLCE 429
Cdd:COG5077 226 --------------------PTDHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWD---SDDSFMQHDIQEFNRV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 430 LLDKIQRELETTgtklpaliptsqrrlieQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLslefperyQCSGKDA 509
Cdd:COG5077 283 LQDNLEKSMRGT-----------------VVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDI--------QLNVKGM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 510 ASqpclVTDMLDKFTETEALEGKiymcdhcnskrRKFSSKSVVFTEAQKQLMICHLPQVLRLHLKRFRWS-GRNNREKIG 588
Cdd:COG5077 338 KN----LQESFRRYIQVETLDGD-----------NRYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDfERDMMVKIN 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205971 589 VHVVFEETLNMEPYCCRETLNALRPECfLYNLSAVVIHHGKgFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEV 664
Cdd:COG5077 403 DRYEFPLEIDLLPFLDRDADKSENSDA-VYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
493-677 |
1.29e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 87.25 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 493 DLSLEFPERYQCSGKD----AASQPCLVTDMLDKFTETEAL-EGKIYMCDHCNSKRrkfssksvvftEAQKQLMICHLPQ 567
Cdd:COG5560 650 EKRYLSLFSYDPLWTIreigAAERTITLQDCLNEFSKPEQLgLSDSWYCPGCKEFR-----------QASKQMELWRLPM 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 568 VLRLHLKRFRwSGRNNREKIGVHVVFEET-LNMEPYccreTLNALRPEcFLYNLSAVVIHHGkGFGSGHYTAYCYNSEGG 646
Cdd:COG5560 719 ILIIHLKRFS-SVRSFRDKIDDLVEYPIDdLDLSGV----EYMVDDPR-LIYDLYAVDNHYG-GLSGGHYTAYARNFANN 791
|
170 180 190
....*....|....*....|....*....|.
gi 332205971 647 FWVHCNDSKLSMCTMEEVRKAQAYILFYTQR 677
Cdd:COG5560 792 GWYLFDDSRITEVDPEDSVTSSAYVLFYRRK 822
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
273-676 |
1.35e-17 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 83.70 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 273 GLRNLGNTCYMNSVLQVLshllifrqcflKLDLNqwlavaasdkarsykhsAVTEAAAQQMNEGQEkekgfvcsrhsgls 352
Cdd:COG5533 1 GLPNLGNTCFMNSVLQIL-----------ALYLP-----------------KLDELLDDLSKELKV-------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 353 sglsggaskgrnmeLIQPREPSSPYSSLCHELHILFQVMWSGEWALVSPFAMlhsvwrlipafrgYAQQDAQEFLCELLD 432
Cdd:COG5533 39 --------------LKNVIRKPEPDLNQEEALKLFTALWSSKEHKVGWIPPM-------------GSQEDAHELLGKLLD 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 433 KIqrelettgtklpaliptsqrrlieqvlnvvNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPERyqcsgkdaasq 512
Cdd:COG5533 92 EL------------------------------KLDLVNSFTIRIFKTTKDKKKTSTGDWFDIIIELPDQ----------- 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 513 pclvTDMLDKFTETEALEGKIYMC-DHCNSKRRKFSSKSVVfTEAQKQLMICHLPQVLRLHLKRFRWSGRNnrEKIGVHV 591
Cdd:COG5533 131 ----TWVNNLKTLQEFIDNMEELVdDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLGGN--QKIDTEV 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 592 vfEETLNMePYCCRETLNaLRPEcFLYNLSAVVIHHGkGFGSGHYTAYCynSEGGFWVHCNDSKLSMCTMEEVRKA---Q 668
Cdd:COG5533 204 --DEKFEL-PVKHDQILN-IVKE-TYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINEkakN 275
|
....*...
gi 332205971 669 AYILFYTQ 676
Cdd:COG5533 276 AYLYFYER 283
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
270-499 |
1.76e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 80.70 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 270 GVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLkldlnqwlavaasdkARSYKhsavteaaaQQMNEgqEKEKGFVCSRhs 349
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL---------------SDEYE---------ESINE--ENPLGMHGSV-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 350 glssglsggaskgrnmeliqprepSSPYSSLCHELHilfqvmwSGEWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCE 429
Cdd:COG5560 316 ------------------------ASAYADLIKQLY-------DGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 430 LLDKIQREL----ETTGTKLPALIPTSQ---RRLIEQVL--------NVVNNIFHGQFLSQVTCLACDNKSDTIESFWDL 494
Cdd:COG5560 365 LLDGLHEDLnriiKKPYTSKPDLSPGDDvvvKKKAKECWwehlkrndSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDL 444
|
....*
gi 332205971 495 SLEFP 499
Cdd:COG5560 445 TLPLP 449
|
|
| ZnF_UBP |
smart00290 |
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger; |
26-71 |
8.77e-12 |
|
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
Pssm-ID: 197632 Cd Length: 50 Bit Score: 60.46 E-value: 8.77e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 332205971 26 CMVCNTTESIWACLSCSHVACGKYIQEHALKHFQESSHPVAFEVND 71
Cdd:smart00290 2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGT 47
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
272-674 |
1.13e-10 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 63.66 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 272 TGLRNLGNTCYMNSVLQVLSHLLIFRQcfLKLDLNQWLAVAASDKARSYKhsavteaaaqqmnEGQEKEkgfvcsrhsgl 351
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRD--LVLNFDESKAELASDYPTERR-------------IGGREV----------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 352 ssglsggaskgRNMELIQPREpsspyssLCHELHILFQVMWSGEWALVSPFAMLhsvwrlipAFRGYAQQDAQEFLCELL 431
Cdd:cd02666 56 -----------SRSELQRSNQ-------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTECIDNVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 432 DKIQRELETTGTklpALIPTSQRRLIEQVlNVVNNIFHGQFLSQVT-CLACDNKSDTIESFWDLSLEFPERYQCSGKDAA 510
Cdd:cd02666 110 FQLEVALEPISN---AFAGPDTEDDKEQS-DLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVDVGKKGREIVVL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 511 SQPCLVTDMLDKFTETEALEgkiymcdhcNSKRRKFSSKSVVFTEAQKQLmichlpqvlrlhlkrfrwSGRNNREKIGVH 590
Cdd:cd02666 186 LEPKDLYDALDRYFDYDSLT---------KLPQRSQVQAQLAQPLQRELI------------------SMDRYELPSSID 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 591 VVFE------ETLNMEPYCCRETLNALRPEC---------FLYNLSAVVIHHGKGfGSGHYTAYCYNSEGGFWVHCNDSK 655
Cdd:cd02666 239 DIDElireaiQSESSLVRQAQNELAELKHEIekqfddlksYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDET 317
|
410 420
....*....|....*....|....*
gi 332205971 656 LSMCTMEEV------RKAQAYILFY 674
Cdd:cd02666 318 VTVVPASEVflftlgNTATPYFLVY 342
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
269-674 |
1.17e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 61.18 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 269 PGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQwlavaasdkarsykhsavteaaaqqmNEGQEKekgfvcsrh 348
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYE--------------------------NIKDRK--------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 349 sglssglsggaskgrnmeliqprepsspySSLCHELHILFQVMWSGEW--ALVSPFAMLHSVWRLIPA-FRGYAQQDAQE 425
Cdd:cd02669 162 -----------------------------SELVKRLSELIRKIWNPRNfkGHVSPHELLQAVSKVSKKkFSITEQSDPVE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 426 FLCELLDKIQRELETTGTKLPaliptsqrrlieqvlNVVNNIFHG------QFLSQVT--------CLACDNKSDTIES- 490
Cdd:cd02669 213 FLSWLLNTLHKDLGGSKKPNS---------------SIIHDCFQGkvqietQKIKPHAeeegskdkFFKDSRVKKTSVSp 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 491 FWDLSLEFPER--YQcSGKDAASQP-CLVTDMLDKFTETEalegkiymCDHCNSKRRKFssksvvfteaqkqlMICHLPQ 567
Cdd:cd02669 278 FLLLTLDLPPPplFK-DGNEENIIPqVPLKQLLKKYDGKT--------ETELKDSLKRY--------------LISRLPK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 568 VLRLHLKRFRwsgRNN--REKIGVHVVFEETLNMEPYCCRETLNALrPECFLYNLSAVVIHHGKGFGSGHYTAYCYNSEG 645
Cdd:cd02669 335 YLIFHIKRFS---KNNffKEKNPTIVNFPIKNLDLSDYVHFDKPSL-NLSTKYNLVANIVHEGTPQEDGTWRVQLRHKST 410
|
410 420
....*....|....*....|....*....
gi 332205971 646 GFWVHCNDSKLSMCTMEEVRKAQAYILFY 674
Cdd:cd02669 411 NKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
405-674 |
6.69e-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: 54.07 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 405 LHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPAlIPTSQRRLieqvlNVVNnIFHGQFLSQVTCLACDNK 484
Cdd:cd02673 18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNRTNVPP-SNIEIKRL-----NPLE-AFKYTIESSYVCIGCSFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 485 SDTIESFWDLSLEFPEryqcsgkdaaSQPCLVTDMLDKFTETEALEGKiymCDHCNSKRRKFSSKSVVFteaqkqlmich 564
Cdd:cd02673 91 ENVSDVGNFLDVSMID----------NKLDIDELLISNFKTWSPIEKD---CSSCKCESAISSERIMTF----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 565 lPQVLRLHLKRFRWsgrnnREKIGVHVVFEEtLNMEPYCCRETLnalrpecflYNLSAVVIHHGKGFGSGHYTAYCYN-S 643
Cdd:cd02673 147 -PECLSINLKRYKL-----RIATSDYLKKNE-EIMKKYCGTDAK---------YSLVAVICHLGESPYDGHYIAYTKElY 210
|
250 260 270
....*....|....*....|....*....|....
gi 332205971 644 EGGFWVHCNDSKLSMCTMEEVRKA---QAYILFY 674
Cdd:cd02673 211 NGSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
420-674 |
1.26e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 52.95 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 420 QQDAQEFLCELLDKIQRELEttgtklpalIPTSQRRLIEQVLNVVNNIFHGQFLSQVTCLAcdNKSDTIESFWdlslEFP 499
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQ---------AAAEAISPGEKSKNPMVQLFYGTFLTEGVLEG--KPFCNCETFG----QYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 500 ERYQCSGKdaasqpclvtdmLDKFTETEALEGKIymcDHCNSKRRKFSSKSVVFTEaqkqlmichLPQVLRLHLKRFRWs 579
Cdd:cd02665 87 LQVNGYGN------------LHECLEAAMFEGEV---ELLPSDHSVKSGQERWFTE---------LPPVLTFELSRFEF- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205971 580 GRNNREKIGVHVVFEETLNMEPYccretlnalrpecflyNLSAVVIHHGKGfGSGHYTAYCYNSEGGFWVHCNDSKLSMC 659
Cdd:cd02665 142 NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQSRQEWEKYNDISVTES 204
|
250 260
....*....|....*....|...
gi 332205971 660 TMEEV--------RKAQAYILFY 674
Cdd:cd02665 205 SWEEVerdsfgggRNPSAYCLMY 227
|
|
| |
