|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
587-935 |
1.57e-157 |
|
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: 489.46 E-value: 1.57e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 587 RFVGLTNLGATCYLASTIQQLYMIPEARQAIFT---AKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPfcKTYTMDK 663
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTD--KTRSFGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 664 QPLNTGEQKDMTEFFTDLITKIEEMSP--ELKNTVKSLFGGVITNNVVSLDCEHVSqtAEEFYTVRCQVADM--KNIYES 739
Cdd:cd02659 79 DSLNTFEQHDVQEFFRVLFDKLEEKLKgtGQEGLIKNLFGGKLVNYIICKECPHES--EREEYFLDLQVAVKgkKNLEES 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 740 LDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLM 819
Cdd:cd02659 157 LDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 820 GkndrkegfKEDGEYLKETESYEYDLIGVTVHTGTADGGHYYSFIRDIVnphaykNNKWYLFNDAEVKPFDSTQLASECF 899
Cdd:cd02659 237 K--------KEGDSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPNDAEEECF 302
|
330 340 350
....*....|....*....|....*....|....*.
gi 733876222 900 GGEMTTKTYDSVtdkfmDFSFEKTHSAYMLFYKRME 935
Cdd:cd02659 303 GGEETQKTYDSG-----PRAFKRTTNAYMLFYERKS 333
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
589-931 |
1.21e-61 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 214.23 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 589 VGLTNLGATCYLASTIQQLYMIPEARQAIF----TAKYSEDMKHKTTLLELQKMFTYL-MESECKAYNPRPFCKTYTMDK 663
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLrispLSEDSRYNKDINLLCALRDLFKALqKNSKSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 664 QPLNTGEQKDMTEFFTDLITKIEE-MSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKN--- 735
Cdd:pfam00443 81 PDFSGYKQQDAQEFLLFLLDGLHEdLNGnhstENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAelk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 736 ---IYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPLRLDMTP 812
Cdd:pfam00443 161 tasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 813 YTedflmgkndrkegfkEDGEYLKETESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPfdst 892
Cdd:pfam00443 239 YL---------------AEELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIK------AYENNRWYKFDDEKVTE---- 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 733876222 893 qlasecfggemttktydsVTDKFMdfsfEKTHSAYMLFY 931
Cdd:pfam00443 294 ------------------VDEETA----VLSSSAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
590-932 |
9.83e-56 |
|
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: 195.01 E-value: 9.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMipearqaiftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplntg 669
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 670 EQKDMTEFFTDLITKIEEM----------SPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KN 735
Cdd:cd02257 21 EQQDAHEFLLFLLDKLHEElkksskrtsdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKglpqVS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 736 IYESLDEVTIKDTLEGDNMYTCSHCgKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDMTPYTE 815
Cdd:cd02257 101 LEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 816 DFLMGKNDrkegfkedgeylkETESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphayKNNKWYLFNDAEVKPfdstql 894
Cdd:cd02257 179 EGEKDSDS-------------DNGSYKYELVAVVVHSGTsADSGHYVAYVKDP------SDGKWYKFNDDKVTE------ 233
|
330 340 350
....*....|....*....|....*....|....*...
gi 733876222 895 asecfggemttktydsVTDKFMDFSFEKTHSAYMLFYK 932
Cdd:cd02257 234 ----------------VSEEEVLEFGSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-932 |
4.04e-55 |
|
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: 196.10 E-value: 4.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPEARQAIFTAKYSEDMKHK-----------TTLLELQKMFTYLMESECKAYNPRPFCKT 658
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKnmppdkphepqTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 659 YTmdkqpLNTGEQKDMTEFFTDLITKIE-----EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM 733
Cdd:cd02668 81 LG-----LDTGQQQDAQEFSKLFLSLLEaklskSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 734 KNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPY 813
Cdd:cd02668 156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 814 TEdflmgknDRKEGFkedgeylketesYEYDLIGVTVHTGT-ADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDST 892
Cdd:cd02668 236 LA-------ESDEGS------------YVYELSGVLIHQGVsAYSGHYIAHIKD------EQTGEWYKFNDEDVEEMPGK 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 733876222 893 QLasECFGGEMTTKTYDSVTDKfmdfSFEKTHSAYMLFYK 932
Cdd:cd02668 291 PL--KLGNSEDPAKPRKSEIKK----GTHSSRTAYMLVYK 324
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-931 |
2.10e-40 |
|
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: 152.82 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPEARQAIFTAKYSEDMKHKT--TLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLN 667
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGfcMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 668 TGEQKDMTEFFTDLITKIE-----------EMSPELKNT--VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK 734
Cdd:cd02661 83 IGRQEDAHEFLRYLLDAMQkacldrfkklkAVDPSSQETtlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 735 NIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMmkEKVNTHFSFPLRLDMTPYt 814
Cdd:cd02661 163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNF--RG--GKINKQISFPETLDLSPY- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 815 edfLMGKNDrkegfkedgeylketESYEYDLIGVTVHTGT-ADGGHYYSFIRDIvnphaykNNKWYLFNDAEVKPFDSTQ 893
Cdd:cd02661 238 ---MSQPND---------------GPLKYKLYAVLVHSGFsPHSGHYYCYVKSS-------NGKWYNMDDSKVSPVSIET 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 733876222 894 LASEcfggemttktydsvtdkfmdfsfekthSAYMLFY 931
Cdd:cd02661 293 VLSQ---------------------------KAYILFY 303
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
574-939 |
3.82e-36 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 150.79 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 574 WDYWPHDDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAIFTAKYSEDMKHKTTLLELQKMFtYLMESECKAYNPR 653
Cdd:COG5077 179 WHSFLNYNSKKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLF-YNLQTGEEPVDTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 654 PFCKTYTMDKqpLNTGEQKDMTEFFTDLITKIEE--MSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA 731
Cdd:COG5077 258 ELTRSFGWDS--DDSFMQHDIQEFNRVLQDNLEKsmRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 732 DMKNIYESLDEVTIKDTLEGDNMYTCSHCGkKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMT 811
Cdd:COG5077 336 GMKNLQESFRRYIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 812 PytedFLMGKNDRkegfkedgeylKETESYEYDLIGVTVHTGTADGGHYYSFIRdivnphAYKNNKWYLFNDAEVKPFDS 891
Cdd:COG5077 415 P----FLDRDADK-----------SENSDAVYVLYGVLVHSGDLHEGHYYALLK------PEKDGRWYKFDDTRVTRATE 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 733876222 892 TQLASECFGGEMTTKtydsvtDKFMDFS-FEKTHSAYMLFYKRMELEEE 939
Cdd:COG5077 474 KEVLEENFGGDHPYK------DKIRDHSgIKRFMSAYMLVYLRKSMLDD 516
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-899 |
1.42e-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: 239125 [Multi-domain] Cd Length: 328 Bit Score: 136.35 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPEARQAIFTAKYSEDMKHKTTLL----ELQKMFTYLMESEckayNPRPFCKTYTM---- 661
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNSclscAMDEIFQEFYYSG----DRSPYGPINLLylsw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 662 -DKQPLNTGEQKDMTEFFTDLITKIEEMS---PELKNTVKS-------LFGGVITNNVVSLDCEHVSQTAEEF------- 723
Cdd:cd02660 78 kHSRNLAGYSQQDAHEFFQFLLDQLHTHYggdKNEANDESHcnciihqTFSGSLQSSVTCQRCGGVSTTVDPFldlsldi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 724 --------YTVRCQVADMKNIYESLDEVTIKDTLeGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMvTMMK 795
Cdd:cd02660 158 pnkstpswALGESGVSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSL-NKTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 796 EKVNTHFSFPLRLDMTPYTEDflmGKNDRKEGFKEDGeylketeSYEYDLIGVTVHTGTADGGHYYSFIRdivnphaYKN 875
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYTSS---SIGDTQDSNSLDP-------DYTYDLFAVVVHKGTLDTGHYTAYCR-------QGD 298
|
330 340
....*....|....*....|....*
gi 733876222 876 NKWYLFNDAEVKPFDSTQ-LASECF 899
Cdd:cd02660 299 GQWFKFDDAMITRVSEEEvLKSQAY 323
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-932 |
1.25e-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: 239139 [Multi-domain] Cd Length: 230 Bit Score: 122.01 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLymipearqaiftakysedmkhkttllelqkmftylmeseckaynprpfcktytmdkqplnTG 669
Cdd:cd02674 1 GLRNLGNTCYMNSILQCL------------------------------------------------------------SA 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 670 EQKDMTEFFTDLITKIEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMK------NIYESLDEV 743
Cdd:cd02674 21 DQQDAQEFLLFLLDGLHSI-------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSgdapkvTLEDCLRLF 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 744 TIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPLR-LDMTPYTEDflmgkN 822
Cdd:cd02674 94 TKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR--FSFSRGSTRKLTTPVTFPLNdLDLTPYVDT-----R 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 823 DRKEGFKedgeylketesyeYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSTQLASEcfgge 902
Cdd:cd02674 167 SFTGPFK-------------YDLYAVVNHYGSLNGGHYTAYCKN------NETNDWYKFDDSRVTKVSESSVVSS----- 222
|
330 340 350
....*....|....*....|....*....|
gi 733876222 903 mttktydsvtdkfmdfsfekthSAYMLFYK 932
Cdd:cd02674 223 ----------------------SAYILFYE 230
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-932 |
3.64e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 114.90 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPEARQAIFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNP--------RPfcktytm 661
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPpdyfleasRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 662 dkQPLNTGEQKDMTEFFTDLITKieemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVR---CQVADMKNIYE 738
Cdd:cd02664 74 --PWFTPGSQQDCSEYLRYLLDR-------LHTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDlsfPSVQDLLNYFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 739 SldevtiKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFL 818
Cdd:cd02664 145 S------PEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLPVRVESKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 819 MGKNDRKEGFKEDGEYLKETESYEYDLIGVTVHTGTA-DGGHYYSFIRDIVN----------PHAYKNNK----WYLFND 883
Cdd:cd02664 219 SESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSsESGHYFTYARDQTDadstgqecpePKDAEENDesknWYLFND 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 733876222 884 AEVkpfdstqlaSECfggemTTKTYDSVTdkfmdfSFEKTHSAYMLFYK 932
Cdd:cd02664 299 SRV---------TFS-----SFESVQNVT------SRFPKDTPYILFYE 327
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-932 |
2.30e-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: 105.88 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPEARQAI--FTAKYSEDMKHKTTLL-ELQKMFTyLMESECKAYNPRPFCKTYTM----- 661
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQSSDNLTnALRDLFD-TMDKKQEPVPPIEFLQLLRMafpqf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 662 -DKQPLNTGEQKDMTEFFTDLITKIE---EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQ-TAEEFYTVRCQVaDMKNI 736
Cdd:cd02657 80 aEKQNQGGYAQQDAEECWSQLLSVLSqklPGAGSKGSFIDQLFGIELETKMKCTESPDEEEvSTESEYKLQCHI-SITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 737 YESLDEvTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTpyteD 816
Cdd:cd02657 159 VNYLQD-GLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLY----E 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 817 FLmgkndrkegfkedgeylkeTESYEYDLIGVTVHTG-TADGGHYYSFIRDivnphaYKNNKWYLFNDA---EVKPFDST 892
Cdd:cd02657 234 LC-------------------TPSGYYELVAVITHQGrSADSGHYVAWVRR------KNDGKWIKFDDDkvsEVTEEDIL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 733876222 893 QLASecfGGEmttktydsvtdkfmdfsfekTHSAYMLFYK 932
Cdd:cd02657 289 KLSG---GGD--------------------WHIAYILLYK 305
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-866 |
1.37e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 102.85 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPEARQAIftakySEDMKhkttllelqKMFtylmeSECKAYNPRpfcktytmdkqpLNTG 669
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELL-----SETPK---------ELF-----SQVCRKAPQ------------FKGY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 670 EQKDMTEFFTDLITKieemspeLKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADM----KNIYESLDEVTI 745
Cdd:cd02667 50 QQQDSHELLRYLLDG-------LRTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEikseCSIESCLKQFTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 746 KDTLEGDNMYTCSHCgkkVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKeKVNTHFSFPLRLDMTPytedFLMGKNDRK 825
Cdd:cd02667 123 VEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAP----FCDPKCNSS 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 733876222 826 EgfkedgeylkETESYEYDLIGVTVHTGTADGGHYYSFIRD 866
Cdd:cd02667 195 E----------DKSSVLYRLYGVVEHSGTMRSGHYVAYVKV 225
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-932 |
1.84e-23 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 103.16 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYmipearqaiftakysedmkHKTTLLELQKMFTYLMESECK--AYNPRPFCKTYTMDKQPLN 667
Cdd:cd02663 1 GLENFGNTCYCNSVLQALY-------------------FENLLTCLKDLFESISEQKKRtgVISPKKFITRLKRENELFD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 668 TGEQKDMTEFFTDLITKI------------------EEMSPELKNT-VKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRC 728
Cdd:cd02663 62 NYMHQDAHEFLNFLLNEIaeildaerkaekanrklnNNNNAEPQPTwVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 729 QVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRL 808
Cdd:cd02663 142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 809 DMTPYTEDflmgkndrkegfKEDGEYLketesyeYDLIGVTVHTG-TADGGHYYSFIRdivnphayKNNKWYLFNDAEVK 887
Cdd:cd02663 222 RLFNTTDD------------AENPDRL-------YELVAVVVHIGgGPNHGHYVSIVK--------SHGGWLLFDDETVE 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 733876222 888 PFDSTQLAsECFGGEMTTKTydsvtdkfmdfsfekthsAYMLFYK 932
Cdd:cd02663 275 KIDENAVE-EFFGDSPNQAT------------------AYVLFYQ 300
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-886 |
4.42e-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: 239123 [Multi-domain] Cd Length: 311 Bit Score: 99.32 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPE--ARQAIFTAKYSEDMKHKTTLLELQ--KMFT------YLMESECKAYN-------- 651
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSfqWRYDDLENKFPSDVVDPANDLNCQliKLADgllsgrYSKPASLKSENdpyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 652 PRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKIE-EMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQV 730
Cdd:cd02658 81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDrESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 731 ADMKNIYESLDE-----VTIKDTLEG-----DNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvtmmKEKVnt 800
Cdd:cd02658 161 PKDEATEKEEGElvyepVPLEDCLKAyfapeTIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLL-----ENWV-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 801 hfsfPLRLDMTPYTEDFLMGKNdrkegfkedgeylketesyeYDLIGVTVHTGT-ADGGHYYSFIRDIVNPhaykNNKWY 879
Cdd:cd02658 234 ----PKKLDVPIDVPEELGPGK--------------------YELIAFISHKGTsVHSGHYVAHIKKEIDG----EGKWV 285
|
....*..
gi 733876222 880 LFNDAEV 886
Cdd:cd02658 286 LFNDEKV 292
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
590-933 |
1.64e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 82.16 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQL-YMIPEARQAI---------FTAKYSEDMKHKTtLLELQKMFTYLMESECKAYNPRPfckty 659
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLddlskelkvLKNVIRKPEPDLN-QEEALKLFTALWSSKEHKVGWIP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 660 tmdkqplNTGEQKDMTEFFTDLItkiEEMSPELKNTVKSLFGGVITNNVVSLDCE----HVS----QTAEEFYTVRCQVA 731
Cdd:COG5533 75 -------PMGSQEDAHELLGKLL---DELKLDLVNSFTIRIFKTTKDKKKTSTGDwfdiIIElpdqTWVNNLKTLQEFID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 732 DMKniYESLDEVTIKdtlEGDNMytcshcGKKVRA--EKRACFKKLPRILSFNTMRYTF-NMVTMMKEKVNTHFSFPLRL 808
Cdd:COG5533 145 NME--ELVDDETGVK---AKENE------ELEVQAkqEYEVSFVKLPKILTIQLKRFANlGGNQKIDTEVDEKFELPVKH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 809 DMTpytedflmgKNDRKEGFkedgeylketesyeYDLIGVTVHTGTADGGHYYSFIRdivnphayKNNKWYLFNDAEVKP 888
Cdd:COG5533 214 DQI---------LNIVKETY--------------YDLVGFVLHQGSLEGGHYIAYVK--------KGGKWEKANDSDVTP 262
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 733876222 889 FDSTqlasecfgGEMTtktydsvtdkfmdfsfEKTHSAYMLFYKR 933
Cdd:COG5533 263 VSEE--------EAIN----------------EKAKNAYLYFYER 283
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
588-887 |
1.84e-16 |
|
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: 83.02 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 588 FVGLTNLGATCYLASTIQQLYMIPearqaiftaKYSEDMKHKTTLL----ELQKMFTYLME---SECKAYNPRPFCKTyT 660
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCP---------GFKHGLKHLVSLIssveQLQSSFLLNPEkynDELANQAPRRLLNA-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 661 MDKQPLNTG-EQKDMTEFFTDLITKIEEMspelkntVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVA-DMKNIYE 738
Cdd:cd02671 94 REVNPMYEGyLQHDAQEVLQCILGNIQEL-------VEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQeSELSKSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 739 SLDEVTIKDTLE------------------GDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMK----E 796
Cdd:cd02671 167 ESSEISPDPKTEmktlkwaisqfasverivGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCygglS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 797 KVNTHFSFPLRLDMTPYTEdflmgKNDRkegfkedgeylketesYEYDLIGVTVHTG-TADGGHYYSFIRdivnphaykn 875
Cdd:cd02671 247 KVNTPLLTPLKLSLEEWST-----KPKN----------------DVYRLFAVVMHSGaTISSGHYTAYVR---------- 295
|
330
....*....|..
gi 733876222 876 nkWYLFNDAEVK 887
Cdd:cd02671 296 --WLLFDDSEVK 305
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
589-883 |
4.30e-16 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 81.55 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 589 VGLTNLGATCYLASTIQQLYMIPEARQ-AIFTAKySEDMKHKTTLLELQKMFTYLMESE---CKAYNprpFCKTYT---- 660
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLA-TECLKEHCLLCELGFLFDMLEKAKgknCQASN---FLRALSsipe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 661 ------MDKQPLNTGEQKDMT------EFFTDLITKIEEMSP----ELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFY 724
Cdd:pfam13423 77 asalglLDEDRETNSAISLSSliqsfnRFLLDQLSSEENSTPpnpsPAESPLEQLFGIDAETTIRCSNCGHESVRESSTH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 725 TVRCQVADMKNIYESLDEVT-----IKDTLEGDNMY--TCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVtmmKEK 797
Cdd:pfam13423 157 VLDLIYPRKPSSNNKKPPNQtfssiLKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWR---QLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 798 VNTHFsFPLRLDMTpytedflmgKNDRKEGfkedgeylkETESYEYDLIGVTVHTGTADG-GHYYSFIR-DIVNPHAYKN 875
Cdd:pfam13423 234 KTPGW-LPPEIGLT---------LSDDLQG---------DNEIVKYELRGVVVHIGDSGTsGHLVSFVKvADSELEDPTE 294
|
....*...
gi 733876222 876 NKWYLFND 883
Cdd:pfam13423 295 SQWYLFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
588-887 |
2.25e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 68.50 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 588 FVGLTNLGATCYLASTIQQLYMIPEARQaiFTAKYSEDMKHKTTLLELQKMFTYLMEsecKAYNPRPFcKTY-------- 659
Cdd:cd02669 119 FVGLNNIKNNDYANVIIQALSHVKPIRN--FFLLYENYENIKDRKSELVKRLSELIR---KIWNPRNF-KGHvsphellq 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 660 ---TMDKQPLNTGEQKDMTEFFTDLITKI----EEMSPELKNTVKSLFGGVITN-----NVVSLDCEHVSQTAEEFYTVr 727
Cdd:cd02669 193 avsKVSKKKFSITEQSDPVEFLSWLLNTLhkdlGGSKKPNSSIIHDCFQGKVQIetqkiKPHAEEEGSKDKFFKDSRVK- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 728 cQVADMKNIYESLD-----------------EVTIKDTLEGDNMYTCSHCGKKVraeKRACFKKLPRILSFNTMRYTFNm 790
Cdd:cd02669 272 -KTSVSPFLLLTLDlpppplfkdgneeniipQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSKN- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 791 vTMMKEKVNTHFSFPLR-LDMTPYTEDflmgkndrkegfkedgEYLKETESYEYDLIGVTVHTGT-ADGGHYYSFIRDiv 868
Cdd:cd02669 347 -NFFKEKNPTIVNFPIKnLDLSDYVHF----------------DKPSLNLSTKYNLVANIVHEGTpQEDGTWRVQLRH-- 407
|
330
....*....|....*....
gi 733876222 869 nphaYKNNKWYLFNDAEVK 887
Cdd:cd02669 408 ----KSTNKWFEIQDLNVK 422
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-901 |
3.43e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 65.27 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYmipearqaiftaKYSEDMKHKTTLLelqkmFTYLMES-ECKAYNPRPfcktytmDKQPLNt 668
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF------------SQQQDVSEFTHLL-----LDWLEDAfQAAAEAISP-------GEKSKN- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 669 geqkDMTEFFTdlitkieemspELKNTVKSLFGGVITNNvvsldcehvsqtaEEFYTVRCQVADMKNIYESLDEVTIKDT 748
Cdd:cd02665 56 ----PMVQLFY-----------GTFLTEGVLEGKPFCNC-------------ETFGQYPLQVNGYGNLHECLEAAMFEGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 749 LEGDnmytcsHCGKKVRAEKRACFKKLPRILSFNTMRYTFNmvTMMKEKVNTHFSFPlrldmtpytedflmgkndrkegf 828
Cdd:cd02665 108 VELL------PSDHSVKSGQERWFTELPPVLTFELSRFEFN--QGRPEKIHDKLEFP----------------------- 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733876222 829 kedgeylKETESYEYDLIGVTVHTGTADGGHYYSFIRDivNPHayknNKWYLFNDAEVKPFDSTQLASECFGG 901
Cdd:cd02665 157 -------QIIQQVPYELHAVLVHEGQANAGHYWAYIYK--QSR----QEWEKYNDISVTESSWEEVERDSFGG 216
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
677-933 |
1.17e-10 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 67.22 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 677 FFTDLITKIEemSPELKNTVKSlfGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYES--------LDEVTIKDT 748
Cdd:COG5560 614 SWLKLETEID--TKREEQVEEE--GQMNFNDAVVISCEWEEKRYLSLFSYDPLWTIREIGAAErtitlqdcLNEFSKPEQ 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 749 LEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRytFNMVTMMKEKVNTHFSFPLrldmtpytEDFLMgknDRKEGF 828
Cdd:COG5560 690 LGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKR--FSSVRSFRDKIDDLVEYPI--------DDLDL---SGVEYM 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 829 KEDGEYLketesyeYDLIGVTVHTGTADGGHYYSFIRDivnphaYKNNKWYLFNDAEVKPFDSTqlasecfggemttkty 908
Cdd:COG5560 757 VDDPRLI-------YDLYAVDNHYGGLSGGHYTAYARN------FANNGWYLFDDSRITEVDPE---------------- 807
|
250 260
....*....|....*....|....*
gi 733876222 909 DSVTDkfmdfsfekthSAYMLFYKR 933
Cdd:COG5560 808 DSVTS-----------SAYVLFYRR 821
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
1054-1387 |
4.67e-10 |
|
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.
Pssm-ID: 463438 Cd Length: 407 Bit Score: 64.24 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 1054 QILIKCPNQIVRQMFQRLCIHVIQRLrpvHAHLYLQPGIEDCSDDMDGPVEDigSRSCVTRFVKTLLSIMEHgVKPHSKH 1133
Cdd:pfam12030 6 ELLLRNPDAEVRSAFGKLIVFALHKL---KELYGLPDGPCDPDDLEEEWRSL--SDSVLEAVVALLDHLWKE-FHTHLRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 1134 LTEYFAFLYEFAKMGEEESQFLLS---LQAISTMVHFYMGTKGPENPQ-VEVLSEEegeeeeeeedilslaeEKYRPAAL 1209
Cdd:pfam12030 80 WDEYFGLLLSYANLGPREVAQLLDlgfLLKCLEIIAADEGDGPPLKYQyARMLRLV----------------EKRRPPSY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 1210 EKMIALIALLVEQ---SRSERHLTLSQNDMAALTGGKGFPF------LFQH-------------IRDGINIRQTCNLIFS 1267
Cdd:pfam12030 144 EKLIQLLSVLLRCcdlSLPPQSINEGAEPLPNSLPDGPFPLtseeadLLRPlgrtngsifvkklLEIDQNPEATRKILRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 1268 LCRYNNRLAEHIVSMLFTSIAK-LTPEAANPFFKLLTMLMEFAGGPPgmppfasyilqRIWEVIEYNPSQC--------- 1337
Cdd:pfam12030 224 LLWENPELSDSILKTLLWGIRGaPAHLLRDPFLRAAIVFCEDSWQAH-----------RIHNLIDHVAKQAdslnntegr 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 1338 --LDWL--AVQTPRNKL------AHSWVLQNMENWVErFLLAHNYPRVRTSAAYLLVSLI 1387
Cdd:pfam12030 293 afLHFFkrAYQCINCRLgfdkewFASQVLENIPDWAP-PLLSYPDSNVRSETEDFLQEEL 351
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
590-931 |
9.23e-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: 239127 [Multi-domain] Cd Length: 240 Bit Score: 55.45 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 590 GLTNLGATCYLASTIQQLYMIPearqaiftakysedmkhkttllelqkmftYLMEseckaynprpFCKTYTmdkqplntg 669
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLP-----------------------------SLIE----------YLEEFL--------- 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 670 EQKDMTEFFTDLITKIEemspelkNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEvtiKDTL 749
Cdd:cd02662 33 EQQDAHELFQVLLETLE-------QLLKFPFDGLLASRIVCLQCGESSKVRYESFTMLSLPVPNQSSGSGTTL---EHCL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 750 EGDNM------YTCSHCgkkvraekRACFKKLPRILSFNTMRYTFNMvTMMKEKVNTHFSFPLRLDmtpytedflmgknd 823
Cdd:cd02662 103 DDFLSteiiddYKCDRC--------QTVIVRLPQILCIHLSRSVFDG-RGTSTKNSCKVSFPERLP-------------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 824 rkegfkedgeylketeSYEYDLIGVTVHTGTADGGHYYSFIR-----------DIVNPHAYKN---NKWYLFNDAEVKpf 889
Cdd:cd02662 160 ----------------KVLYRLRAVVVHYGSHSSGHYVCYRRkplfskdkepgSFVRMREGPSstsHPWWRISDTTVK-- 221
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 733876222 890 dstqlasECfggemttKTYDSVTDKfmdfsfekthSAYMLFY 931
Cdd:cd02662 222 -------EV-------SESEVLEQK----------SAYMLFY 239
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
589-886 |
4.97e-06 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 589 VGLTNLGATCYLASTIQQLYMIPEARQAIFTAKYS----EDMKHKTTLL------------------ELQKMFTYLMESE 646
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaelASDYPTERRIggrevsrselqrsnqfvyELRSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 647 CKAYNPRPFCKTYTMDKQplNTGEQKDMTEFFTDLITKIEEMSP---------ELKNTVKSLFGG--------VITNNVV 709
Cdd:cd02666 82 TRSVTPSKELAYLALRQQ--DVTECIDNVLFQLEVALEPISNAFagpdteddkEQSDLIKRLFSGktkqqlvpESMGNQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 710 SLDC--EHVSQTA----EEFYTVRCQvADMKNIYESLDEVTIKDTLEgdnmytcshcgkKVRAEKRacfkkLPRILSFNT 783
Cdd:cd02666 160 SVRTktERFLSLLvdvgKKGREIVVL-LEPKDLYDALDRYFDYDSLT------------KLPQRSQ-----VQAQLAQPL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 784 MRYTFNMVTM-MKEKVNTHFSFpLRLDMTPYTEDFLMGKNDRKEGFKEDGEYLKETESYEYDLIGVTVHTGTADGGHYYS 862
Cdd:cd02666 222 QRELISMDRYeLPSSIDDIDEL-IREAIQSESSLVRQAQNELAELKHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWV 300
|
330 340
....*....|....*....|....
gi 733876222 863 FIRDivnphaYKNNKWYLFNDAEV 886
Cdd:cd02666 301 YIKD------FEENVWRKYNDETV 318
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
670-932 |
5.19e-05 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 47.14 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 670 EQKDMTEFFTDLITKIEEMSPELKntvkslfggvitnnvvsLDCEHVSQTAEEfytvrcqvaDMKNIYESLDEVTIKDTl 749
Cdd:cd02670 22 EQQDPEEFFNFITDKLLMPLLEPK-----------------VDIIHGGKKDQD---------DDKLVNERLLQIPVPDD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 750 EGDNMYTCSHCGKkvRAEKRACFKKLPRILSFNTMRYTfnMVTMMKEKVNTHFSFPLRLDMTPYTED--FLMGKNDRKEG 827
Cdd:cd02670 75 DDGGGITLEQCLE--QYFNNSVFAKAPSCLIICLKRYG--KTEGKAQKMFKKILIPDEIDIPDFVADdpRACSKCQLECR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 828 -FKEDGEYLKETESYEYDLIGVTVHTGTA-DGGHYYSFIR-----DIVNPHAYKNNKWYLFndaevkpfDSTQLASECFG 900
Cdd:cd02670 151 vCYDDKDFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVRygsysLTETDNEAYNAQWVFF--------DDMADRDGVSN 222
|
250 260 270
....*....|....*....|....*....|..
gi 733876222 901 GemttktyDSVTDKFmdfsfeKTHSAYMLFYK 932
Cdd:cd02670 223 G-------FNIPAAR------LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
765-890 |
1.21e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 43.27 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733876222 765 RAEKRACFKKLPRILSFNTMRYtfNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLMGKN--------DRKEGFKEDGEYlk 836
Cdd:cd02672 134 KAWCDTCCKYQPLEQTTSIRHL--PDILLLVLVINLSVTNGEFDDINVVLPSGKVMQNkvspkaidHDKLVKNRGQES-- 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 733876222 837 eteSYEYDLIGVTVHTGTAD-GGHYYSFIRDIvnPHAYKNNKWYLFNDAEVKPFD 890
Cdd:cd02672 210 ---IYKYELVGYVCEINDSSrGQHNVVFVIKV--NEESTHGRWYLFNDFLVTPVS 259
|
|
| |
